ENTRY
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2.59k
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stringlengths
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196
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stringlengths
6
7.19k
PATHWAY
stringlengths
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908
FUNCTION_CC
stringlengths
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15.4k
DOMAIN_CC
stringlengths
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6.72k
PROTEIN_FAMILIES
stringlengths
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237
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stringlengths
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286
A0A009IHW8
reviewed
ABTIR_ACIB9
2' cyclic ADP-D-ribose synthase AbTIR (2'cADPR synthase AbTIR) (EC 3.2.2.-) (NAD(+) hydrolase AbTIR) (EC 3.2.2.6) (TIR domain-containing protein in A.baumannii) (AbTIR)
J512_3302
Acinetobacter baumannii (strain 1295743)
null
null
FUNCTION: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide (PubMed:29395922). In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed 2'cADPR (v-cADPR) (PubMed:29395922, PubMed:36048923). Cleaves NADP(+), but does not cyclize the product (PubMed:36048923). {ECO:0000269|PubMed:29395922, ECO:0000269|PubMed:36048923}.
DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity (Probable). The TIR domain alone is active and produces cADPR (residues 134-267) (PubMed:36048923). {ECO:0000255|PROSITE-ProRule:PRU00204, ECO:0000269|PubMed:36048923, ECO:0000305|PubMed:36048923}.
null
null
J512_3302
null
A0A023I7E1
reviewed
ENG1_RHIMI
Glucan endo-1,3-beta-D-glucosidase 1 (Endo-1,3-beta-glucanase 1) (EC 3.2.1.39) (Laminarinase) (RmLam81A)
ENG1 LAM81A
Rhizomucor miehei
null
null
FUNCTION: Cleaves internal linkages in 1,3-beta-glucan. {ECO:0000269|PubMed:34801773}.
null
Glycosyl hydrolase 81 family
ENG1
null
LAM81A
A0A024B7W1
reviewed
POLG_ZIKVF
Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]
null
Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013) (ZIKV)
null
null
FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of the mature virus particle (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins (By similarity). Can migrate to the cell nucleus where it modulates host functions (By similarity). Inhibits the integrated stress response (ISR) in the infected cell (PubMed:28592527). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:28592527}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion. Contributes to fetal microcephaly in humans. Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptors and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HAVCR1 in a cell-type specific manner (By similarity). In addition, host NCAM1 can also be used as entry receptor (By similarity). Interaction with host HSPA5 plays an important role in the early stages of infection as well (By similarity). Envelope protein is synthesized in the endoplasmic reticulum and forms a heterodimer with protein prM. The heterodimer plays a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes the dissociation of PrM-E heterodimers and formation of E homodimers. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion (By similarity). {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 1]: Plays a role in the inhibition of host RLR-induced interferon-beta activation by targeting TANK-binding kinase 1/TBK1. In addition, recruits the host deubiquitinase USP8 to cleave 'Lys-11'-linked polyubiquitin chains from caspase-1/CASP1 thus inhibiting its proteasomal degradation. In turn, stabilized CASP1 promotes cleavage of cGAS, which inhibits its ability to recognize mitochondrial DNA release and initiate type I interferon signaling. {ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that recruits genomic RNA, the structural protein prM/E complex, and the NS2B/NS3 protease complex to the virion assembly site and orchestrates virus morphogenesis (By similarity). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). May disrupt adherens junction formation and thereby impair proliferation of radial cells in the host cortex (By similarity). {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. {ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). Inhibits the integrated stress response (ISR) in the infected cell by blocking stress granules assembly (PubMed:28592527). Disrupts host centrosome organization in a CEP63-dependent manner to degrade host TBK1 and inhibits innate immune response (PubMed:35793002). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:28592527, ECO:0000269|PubMed:35793002}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Cooperatively with NS4B suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). By inhibiting host ANKLE2 functions, may cause defects in brain development, such as microcephaly (PubMed:30550790). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). Inhibits the integrated stress response (ISR) in the infected cell by blocking stress granules assembly (PubMed:28592527). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440, ECO:0000269|PubMed:28592527, ECO:0000269|PubMed:30550790}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place (By similarity). Also plays a role in the inhibition of host RLR-induced interferon-beta production at TANK-binding kinase 1/TBK1 level (By similarity). Cooperatively with NS4A suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:30951555). Methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Once sufficient NS5 is expressed, binds to the cap-proximal structure and inhibits further translation of the viral genome (By similarity). Besides its role in RNA genome replication, also prevents the establishment of a cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Mechanistically, interferes with host kinases TBK1 and IKKE upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I pathway (By similarity). Antagonizes also type I interferon signaling by targeting STAT2 for degradation by the proteasome thereby preventing activation of JAK-STAT signaling pathway (By similarity). Within the host nucleus, disrupts host SUMO1 and STAT2 co-localization with PML, resulting in PML degradation (PubMed:32699085). May also reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (PubMed:30550790). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:30550790, ECO:0000269|PubMed:30951555, ECO:0000269|PubMed:32699085}.
DOMAIN: [Small envelope protein M]: The transmembrane domain contains an endoplasmic reticulum retention signal. {ECO:0000250|UniProtKB:P17763}.; DOMAIN: [Envelope protein E]: The transmembrane domain contains an endoplasmic reticulum retention signal. {ECO:0000250|UniProtKB:P17763}.; DOMAIN: [Capsid protein C]: The disordered region at the N-terminus may be involved in lipid-droplet binding. {ECO:0000250|UniProtKB:P12823}.; DOMAIN: [Serine protease subunit NS2B]: The central disordered region transitions to ordered by binding to NS3. {ECO:0000250|UniProtKB:Q32ZE1}.; DOMAIN: [RNA-directed RNA polymerase NS5]: Comprises a methyltransferase (MTase) in the N-terminal region and an RNA-dependent RNA polymerase in the C-terminal region. {ECO:0000250|UniProtKB:Q32ZE1}.
Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family
null
null
null
A0A024SC78
reviewed
CUTI1_HYPJR
Cutinase (EC 3.1.1.74)
M419DRAFT_76732
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
null
null
FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:25219509). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:25219509). {ECO:0000269|PubMed:25219509}.
DOMAIN: In contract to classical cutinases, possesses a lid formed by two N-terminal helices which covers its active site (PubMed:25219509). The lid opens in the presence of surfactants to uncover the catalytic crevice, allowing enzyme activity and inhibition (PubMed:25219509). {ECO:0000269|PubMed:25219509}.
Cutinase family
null
M419DRAFT_76732
null
A0A024SH76
reviewed
GUX2_HYPJR
Exoglucanase 2 (EC 3.2.1.91) (1,4-beta-cellobiohydrolase) (Cellobiohydrolase 6A) (Cel6A) (Exocellobiohydrolase II) (CBHII) (Exoglucanase II)
cbh2 M419DRAFT_122470
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
null
null
FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units. {ECO:0000250|UniProtKB:P07987}.
DOMAIN: The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence. {ECO:0000250|UniProtKB:P07987}.
Glycosyl hydrolase 6 (cellulase B) family
cbh2
M419DRAFT_122470
null
A0A026W182
reviewed
ORCO_OOCBI
Odorant receptor coreceptor
Orco X777_12371
Ooceraea biroi (Clonal raider ant) (Cerapachys biroi)
null
null
FUNCTION: Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). Obligate coreceptor of all odorant receptors (By similarity). Orco is a universal and integral part of the functional odorant receptor, involved in the dendritic localization of other olfactory receptors. Can form functional ion channels in the absence of an odor-binding odorant receptor (By similarity). Plays a central role in the perception of olfactory stimuli in ants and is essential for ant social organization (PubMed:28802042). Required for pheromone sensing (PubMed:28802042). Also required for the development and maintenance of odorant receptor neurons (ORNs) and of antennal lobe glomeruli (PubMed:28802042). {ECO:0000250|UniProtKB:Q7QCC7, ECO:0000269|PubMed:28802042}.
null
Insect chemoreceptor superfamily, Heteromeric odorant receptor channel (TC 1.A.69) family, Orco subfamily
Orco
X777_12371
null
A0A044RE18
reviewed
BLI_ONCVO
Endoprotease bli (EC 3.4.21.75) (Blisterase)
Bli
Onchocerca volvulus
null
null
FUNCTION: Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif. {ECO:0000269|PubMed:12855702}.
null
Peptidase S8 family, Furin subfamily
Bli
null
null
A0A059TC02
reviewed
CCR1_PETHY
Cinnamoyl-CoA reductase 1 (Ph-CCR1) (EC 1.2.1.44) (Coniferylaldehyde synthase) (Coumaroyl-CoA reductase) (Feruloyl-CoA reductase) (Sinapoyl-CoA reductase)
CCR1
Petunia hybrida (Petunia)
null
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}.
FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:24985707). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:24985707, PubMed:25217505). Mediates the conversion of feruloyl CoA to coniferylaldehyde (PubMed:24985707, PubMed:25217505). Also active toward p-coumaroyl-CoA and sinapoyl-CoA (PubMed:24985707, PubMed:25217505). Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (PubMed:24985707). {ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}.
null
NAD(P)-dependent epimerase/dehydratase family, Dihydroflavonol-4-reductase subfamily
CCR1
null
null
A0A060A682
reviewed
HAP2_TETTH
Hapless 2 (Generative cell specific-1)
HAP2 GCS1
Tetrahymena thermophila
null
null
FUNCTION: During fertilization, required for the formation of intercellular membrane pores and subsequent exchange of gametic pronuclei between cells. Probably initiates the formation of intercellular membrane pores by inserting part of its extracellular domain into the cell membrane of the adjoining cell in the mating pair. Mating requires the presence of HAP2 on at least one of the two cells. Mating efficiency is high when HAP2 is present on both cells, and is strongly reduced when HAP2 is present on only one of the two cells. {ECO:0000269|PubMed:25155508, ECO:0000269|PubMed:28238660}.
DOMAIN: The region that is important for membrane fusion binds to lipids and can insert itself into lipid membranes. It is unstructured in an aqueous environment and assumes a more ordered, beta-stranded conformation in the presence of lipid membranes. {ECO:0000269|PubMed:28238660}.
HAP2/GCS1 family
HAP2
null
GCS1
A0A061ACU2
reviewed
PIEZ1_CAEEL
Piezo-type mechanosensitive ion channel component 1
pezo-1 C10C5.1
Caenorhabditis elegans
null
null
FUNCTION: Pore-forming subunit of a mechanosensitive non-specific cation channel (By similarity). Generates currents characterized by a linear current-voltage relationship (By similarity). Plays a role in reproduction by positively regulating inter-tissue signaling to promote oocyte maturation, ovulation and fertilization, and sperm navigation from and to the spermatheca (PubMed:32490809). May play a role in regulating cytosolic and endoplasmic reticulum calcium ion release (PubMed:32490809). {ECO:0000250|UniProtKB:Q92508, ECO:0000269|PubMed:32490809}.
null
PIEZO (TC 1.A.75) family
pezo-1
C10C5.1
null
A0A061I403
reviewed
FICD_CRIGR
Protein adenylyltransferase FICD (EC 2.7.7.108) (AMPylator FICD) (De-AMPylase FICD) (EC 3.1.4.-) (FIC domain-containing protein) (Huntingtin-interacting protein E)
FICD HYPE H671_4g11989 I79_014982
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
null
null
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (PubMed:27918543). The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (PubMed:27918543). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (PubMed:27918543). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (PubMed:26673894, PubMed:27918543, PubMed:29064368). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (PubMed:27918543). Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (By similarity). {ECO:0000250|UniProtKB:Q9BVA6, ECO:0000269|PubMed:26673894, ECO:0000269|PubMed:27918543, ECO:0000269|PubMed:29064368}.
DOMAIN: The fido domain mediates the adenylyltransferase activity. {ECO:0000250|UniProtKB:Q9BVA6}.
Fic family
FICD
H671_4g11989 I79_014982
HYPE
A0A067CMC7
reviewed
HTP3_SAPPC
Endonuclease Htp3 (EC 3.1.31.-) (Host targeting protein 3) (RxLR effector protein Htp3)
HTP3 SPRG_03573
Saprolegnia parasitica (strain CBS 223.65)
null
null
FUNCTION: Effector involved in the disease saprolegniosis in salmonids and other freshwater fish, resulting in considerable economic losses in aquaculture (PubMed:29904064). Within the host fish cells, Htp3 is released from vesicles into host cytosol where it degrades nucleic acids (PubMed:29904064). {ECO:0000269|PubMed:29904064}.
DOMAIN: The conserved RxLR motif does not seem to be involved in self-translocation into fish cells. {ECO:0000269|PubMed:29904064}.; DOMAIN: The C-terminus (residues 200 to 211) is predicted to form a short helix with charged amino acids and is required for the self-translocation into fish cells. {ECO:0000269|PubMed:29904064}.
RxLR effector family; LCL3 family
HTP3
SPRG_03573
null
A0A067XGX8
reviewed
AROG2_PETHY
Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 2) (DAHP synthase 2) (PhDAHP2) (Phospho-2-keto-3-deoxyheptonate aldolase 2)
DAHP2 DHS2
Petunia hybrida (Petunia)
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}.
FUNCTION: Involved in the production of volatile organic compounds (VOCs) (PubMed:24815009). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity). {ECO:0000250|UniProtKB:O53512, ECO:0000269|PubMed:24815009}.
null
Class-II DAHP synthase family
DAHP2
null
DHS2
A0A067XH53
reviewed
AROG1_PETHY
Phospho-2-dehydro-3-deoxyheptonate aldolase 1, chloroplastic (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 1) (DAHP synthase 1) (PhDAHP1) (Phospho-2-keto-3-deoxyheptonate aldolase 1)
DAHP1 DAHPS DHS1
Petunia hybrida (Petunia)
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}.
FUNCTION: Involved in the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26), scent attracting pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta) (PubMed:24815009). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity). {ECO:0000250|UniProtKB:O53512, ECO:0000269|PubMed:24815009}.
null
Class-II DAHP synthase family
DAHP1
null
DAHPS DHS1
A0A067XR63
reviewed
XTH7_DIOKA
Xyloglucan endotransglucosylase protein 7 (XET protein 7) (EC 2.4.1.207) (DkXTH7) (Xyloglucan endotransglucosylase/hydrolase protein 7) (XTH protein 7)
XTH7
Diospyros kaki (Kaki persimmon) (Diospyros chinensis)
null
null
FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall assembly and synthesis in fast growing tissues and in the maintenance of firmness in mature fruits. {ECO:0000269|PubMed:27242828}.
null
Glycosyl hydrolase 16 family, XTH group 2 subfamily
XTH7
null
null
A0A067XRK9
reviewed
XTH6_DIOKA
Xyloglucan endotransglucosylase protein 6 (XET protein 6) (EC 2.4.1.207) (DkXTH6) (Xyloglucan endotransglucosylase/hydrolase protein 6) (XTH protein 6)
XTH6
Diospyros kaki (Kaki persimmon) (Diospyros chinensis)
null
null
FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall restructuring during postharvest fruit softening. {ECO:0000269|PubMed:27242828}.
null
Glycosyl hydrolase 16 family, XTH group 1 subfamily
XTH6
null
null
A0A067YMX8
reviewed
XTH8_DIOKA
Xyloglucan endotransglucosylase protein 8 (XET protein 8) (EC 2.4.1.207) (DkXTH8) (Xyloglucan endotransglucosylase/hydrolase protein 8) (XTH protein 8)
XTH8
Diospyros kaki (Kaki persimmon) (Diospyros chinensis)
null
null
FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Overexpression in Arabidopsis transgenic plants causes accelerated dark-induced leaf senescence and higher lipid peroxidation of the leaf cells. Overexpression in transgenic tomato plants promotes fruit ripening and softening. Probably involved in cell wall restructuring during postharvest fruit softening. {ECO:0000269|PubMed:27966647}.
null
Glycosyl hydrolase 16 family, XTH group 2 subfamily
XTH8
null
null
A0A068B6Q6
reviewed
CA18_CONBE
Conotoxin Bt1.8
null
Conus betulinus (Beech cone)
null
null
FUNCTION: Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. This toxin inhibits mammalian alpha-3-beta-2/CHRNA3-CHRNB2 nAChR (IC(50)=9.4 nM (rat), IC(50)=8.8 nM (human)), as well as the subunit chimera alpha-6/alpha-3-beta-2-beta-3 nAChR (CHRNA6/CHRNA3-CHRNB2-CHRNB3)(IC(50)=2.1 nM (rat), IC(50)=1.7 nM (human)). Binds to rat alpha-6/alpha-3-beta-2-beta-3 more rapidly than to alpha-3-beta-2, and dissociates more rapidly from alpha-3-beta-2 than from alpha-6/alpha-3-beta-2-beta-3. {ECO:0000269|PubMed:34008858}.
DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern. {ECO:0000305}.
Conotoxin A superfamily
null
null
null
A0A068J840
reviewed
UGT1_PANGI
UDP-glycosyltransferase 1 (UGTPg1) (EC 2.4.1.363)
UGT1
Panax ginseng (Korean ginseng)
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305}.
FUNCTION: Component of the dammarane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway (PubMed:26032089, PubMed:29378087). Glycosyltransferase that catalyzes the biosynthesis of ginsenoside F1 from protopanaxatriol (PPT) (PubMed:26032089). Triggers C20-OH glycosylation of ginsenoside Rg3 to produce ginsenoside Rd (PubMed:26032089). Mediates the conversion of protopanaxadiol (PPD) to the ginsenoside compound K (PubMed:24603359, PubMed:26032089). catalyzes the production of 20S-O-beta-(D-glucosyl)-dammarenediol II form dammarenediol II (DM) (PubMed:24603359). {ECO:0000269|PubMed:24603359, ECO:0000269|PubMed:26032089, ECO:0000303|PubMed:29378087}.
null
UDP-glycosyltransferase family
UGT1
null
null
A0A068Q5Q5
reviewed
DEPOL_BPKNT
Depolymerase, capsule K1-specific (EC 4.-.-.-) (Gene product 34) (gp34) (K1-ORF34 protein) (Probable tail spike protein)
ORF34
Klebsiella phage NTUH-K2044-K1-1 (Bacteriophage NTUH-K2044-K1-1)
null
null
FUNCTION: Functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides (PubMed:35130876). Displays a lyase activity that specifically degrades the K1-type polysaccharides of Klebsiella pneumoniae capsule (PubMed:25001459, PubMed:35130876). {ECO:0000269|PubMed:25001459, ECO:0000269|PubMed:35130876}.
null
K1-specific depolymerase family
null
ORF34
null
A0A072ULZ1
reviewed
GLB12_MEDTR
Anaerobic nitrite reductase Glb1-2 (EC 1.7.2.-) (Non-symbiotic hemoglobin 1-2) (MtGlb1-2) (Phytoglobin 1.2) (Phytogb1.2)
Glb1-2 MTR_4g068870 Medtr4g068870 MtrunA17_Chr4g0034311
Medicago truncatula (Barrel medic) (Medicago tribuloides)
null
null
FUNCTION: Phytoglobin that regulates the fine tuning of nitric oxide (NO) concentration in the cytosol in response to sudden changes in O(2) availability, and performs both symbiotic and nonsymbiotic functions (PubMed:33329665). Exhibits NO dioxygenase activity in the presence of O(2) but nitrite reductase (NiR) activity in the absence of O(2) (e.g. during flooding or in waterlogged soil) (PubMed:33329665). May not function as an oxygen storage or transport protein (By similarity). Extremely reactive toward the physiological ligands O(2), nitric oxide (NO), and nitrite with a very high affinity for O(2) through an hexacoordinate heme iron because of a very low dissociation constant (PubMed:33329665). {ECO:0000250|UniProtKB:O04986, ECO:0000269|PubMed:33329665}.; FUNCTION: [Isoform 2]: Very high affinity for O(2) through two hexacoordinate heme irons (PubMed:33329665). Extremely reactive toward the physiological ligands O(2), nitric oxide (NO), and nitrite (PubMed:33329665). {ECO:0000269|PubMed:33329665}.; FUNCTION: [Isoform 4]: Very high affinity for O(2) through a single hexacoordinate heme iron (PubMed:33329665). Extremely reactive toward the physiological ligands O(2), nitric oxide (NO), and nitrite (PubMed:33329665). {ECO:0000269|PubMed:33329665}.
null
Plant globin family
Glb1-2
MtrunA17_Chr4g0034311
null
A0A072UR65
reviewed
CHT5B_MEDTR
Class V chitinase CHIT5b (MtCHIT5b) (EC 3.2.1.14)
CHIT5B MTR_4g117000
Medicago truncatula (Barrel medic) (Medicago tribuloides)
null
PATHWAY: Glycan degradation; chitin degradation. {ECO:0000305}.
FUNCTION: Possesses chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5 (PubMed:27383628). Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3 molecules (PubMed:27383628). Has the capacity to reduce hyphal growth of the fungus Trichoderma viride in an agar-plate bioassay (PubMed:27383628). {ECO:0000269|PubMed:27383628}.
null
Glycosyl hydrolase 18 family, Chitinase class V subfamily
CHIT5B
null
null
A0A072VDF2
reviewed
CCR1_MEDTR
Cinnamoyl-CoA reductase 1 (Mt-CCR1) (EC 1.2.1.44) (Caffeoyl-CoA reductase) (EC 1.2.1.-) (Coumaroyl-CoA reductase) (Feruloyl-CoA reductase) (Sinapoyl-CoA reductase)
CCR1 MTR_2g104960 MtrunA17_Chr2g0333781
Medicago truncatula (Barrel medic) (Medicago tribuloides)
null
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000250|UniProtKB:A0A059TC02}.
FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:20876124). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:20876124). Mediates the conversion of feruloyl-CoA to coniferylaldehyde (PubMed:20876124). Also active, with a lower efficiency, toward coumaroyl-CoA, caffeoyl CoA and sinapoyl-CoA (PubMed:20876124). Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity). {ECO:0000250|UniProtKB:A0A059TC02, ECO:0000269|PubMed:20876124}.
null
NAD(P)-dependent epimerase/dehydratase family, Dihydroflavonol-4-reductase subfamily
CCR1
MtrunA17_Chr2g0333781
null
A0A075BSX9
reviewed
HLNO_SHIS7
(S)-6-hydroxynicotine oxidase ((S)-6HN oxidase) (EC 1.5.3.5) (6-hydroxy-L-nicotine oxidase) (6-HLNO) (L-hydroxynicotine oxidase) (LHNO)
nctB shn_30305
Shinella sp. (strain HZN7)
null
PATHWAY: Alkaloid degradation; nicotine degradation; 6-hydroxypseudooxynicotine from nicotine (S-isomer route): step 2/2. {ECO:0000305}.
FUNCTION: Involved in the degradation of L-nicotine (PubMed:25002425). Catalyzes the oxidation of (S)-6-hydroxynicotine (6-hydroxy-L-nicotine) to 6-hydroxypseudooxynicotine (PubMed:25002425). Oxidation of the pyrrolidine ring of (S)-6-hydroxynicotine leads to the formation of the optically inactive 6-hydroxy-N-methylmyosmine, which hydrolyzes spontaneously to 6-hydroxypseudooxynicotine (PubMed:25002425). Acts with absolute stereospecificity on the L-form of 6-hydroxynicotine (PubMed:25002425). Also involved in the degradation of nornicotine, and catalyzes the oxidation of 6-hydroxynornicotine to 6-hydroxymyosmine, which hydrolyzes to 6-hydroxypseudooxynornicotine (PubMed:27568381). In vitro, converts (S)-nicotine into N-methylmyosmine, which spontaneously hydrolyzes spontaneously into pseudooxynicotine, but catalytic efficiency is about 1900-fold higher with (S)-6-hydroxynicotine (PubMed:25002425). {ECO:0000269|PubMed:25002425, ECO:0000269|PubMed:27568381}.
null
Flavin monoamine oxidase family
nctB
shn_30305
null
A0A075D5I4
reviewed
PINMT_RAUSE
Picrinine-N-methytransferase (RsPiNMT) (EC 2.1.1.-) (Gamma-tocopherol-like methyltransferase PiNMT) (RsTLMT)
PiNMT Rs8692
Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
null
PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. {ECO:0000269|PubMed:26848097}.
FUNCTION: S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline (PubMed:26848097). Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine) (PubMed:26848097). Accepts also, with low efficiency, 21-hydroxycyclolochnericine and norajmaline as substrates (PubMed:26848097). {ECO:0000269|PubMed:26848097}.
null
Class I-like SAM-binding methyltransferase superfamily, gTMT family
PiNMT
null
Rs8692
A0A075D657
reviewed
PINMT_VINMI
Picrinine-N-methytransferase (VmPiNMT) (EC 2.1.1.-) (Gamma-tocopherol-like methyltransferase PiNMT) (VmTLMT)
PiNMT Vm130
Vinca minor (Common periwinkle)
null
PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. {ECO:0000269|PubMed:26848097}.
FUNCTION: S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline (PubMed:26848097). Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine) (PubMed:26848097). Accepts also, with low efficiency, 21-hydroxycyclolochnericine and norajmaline as substrates (PubMed:26848097). {ECO:0000269|PubMed:26848097}.
null
Class I-like SAM-binding methyltransferase superfamily, gTMT family
PiNMT
null
Vm130
A0A075F7E9
reviewed
LERK1_ORYSI
G-type lectin S-receptor-like serine/threonine-protein kinase LECRK1 (OsLecRK1) (EC 2.7.11.1) (OsRLCK134)
LECRK1 LECRK OsI_14840
Oryza sativa subsp. indica (Rice)
null
null
FUNCTION: Involved in innate immunity. Required for the expression of defense-related genes PR1A, LOX2 and CHS1 upon biotic stresses. Required for basal resistance to the fungal blast (M.grisea), bacterial blight (O.oryzae pv. oryzae, Xoo) and the herbivorous insect brown planthopper (N.lugens, BPH). May be involved in several defense signaling pathways. Involved in the promotion of seed germination. Required for the expression of alpha-amylase genes during seed germination (PubMed:15685292). Involved in resistance against the brown planthopper (BPH). Member of the BPH3 (BPH resistance locus 3) cluster which contains LECRK1, LECRK2 and LECRK3 (PubMed:25485617). {ECO:0000269|PubMed:15685292, ECO:0000269|PubMed:25485617}.
null
Protein kinase superfamily, Ser/Thr protein kinase family
LECRK1
OsI_14840
LECRK
A0A075F932
reviewed
SYT1_ANSCY
Synaptotagmin-1 (Synaptotagmin I) (SytI)
SYT1
Anser cygnoides (Swan goose)
null
null
FUNCTION: Calcium sensor that participates in triggering neurotransmitter release at the synapse (By similarity). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. May play a role in dendrite formation by melanocytes (By similarity). May play a role in regulating the secretion of hormones relevant to the reproduction and egg-laying of female geese (PubMed:25146222). {ECO:0000250|UniProtKB:P21579, ECO:0000250|UniProtKB:P46096, ECO:0000269|PubMed:25146222}.
DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid binding. {ECO:0000250|UniProtKB:P21707}.; DOMAIN: The second C2 domain mediates interaction with SV2A and probably with STN2. {ECO:0000250|UniProtKB:P21707}.
Synaptotagmin family
SYT1
null
null
A0A075FBG7
reviewed
ELS_MARVU
9,13-epoxylabda-14-ene synthase, chloroplastic (EC 4.2.3.189) (Manoyl oxide synthase) (EC 4.2.3.190) (Miltiradiene synthase) (EC 4.2.3.131)
ELS
Marrubium vulgare (White horehound)
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:24990389}.
FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including marrubiin and other labdane-related furanoid diterpenoids with potential applications as anti-diabetics, analgesics or vasorelaxants (Probable). Terpene synthase the catalyzes the conversion of peregrinol diphosphate to 9,13(R)-epoxy-labd-14-ene, from (+)-copalyl diphosphate ((+)-CPP) to miltiradiene and from 8-hydroxycopalyl diphosphate (LPP, labda-13-en-8-ol diphosphate) to manoyl oxide (PubMed:24990389). {ECO:0000269|PubMed:24990389, ECO:0000305|PubMed:24990389}.
DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+). {ECO:0000250|UniProtKB:G8GJ94}.
Terpene synthase family
ELS
null
null
A0A075QQ08
reviewed
IF4E1_TOBAC
Eukaryotic translation initiation factor 4E-1 (NteIF4E1) (eIF4E-1) (Eukaryotic translation initiation factor 4E2-T) (eIF4E2-T) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)
eIF4E EIF4E2-T T015277 LOC107829212
Nicotiana tabacum (Common tobacco)
null
null
FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:15988567). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (PubMed:15988567). Key component of recessive resistance to potyviruses (Ref.2). {ECO:0000269|PubMed:15988567, ECO:0000269|Ref.2}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection (e.g. potato virus Y (PVY) and pepper mottle virus (PepMoV)) by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|Ref.2}.
null
Eukaryotic initiation factor 4E family
eIF4E
LOC107829212
EIF4E2-T T015277
A0A075TJ05
reviewed
OTASE_ASPNG
Ochratoxinase (OTase) (EC 3.4.17.-) (Amidohydrolase 2) (Amidase 2) (Carboxypeptidase Am2)
Am2
Aspergillus niger
null
null
FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products (PubMed:24947135). {ECO:0000269|PubMed:24947135, ECO:0000269|PubMed:33647354}.
DOMAIN: Each subunit of the homooctameric enzyme folds into a two-domain structure characteristic of a metal dependent amidohydrolase, with a twisted TIM (triosephosphateisomerase)-barrel and a smaller beta-sandwich domain. {ECO:0000269|PubMed:24947135}.
Metallo-dependent hydrolases superfamily, Ochratoxinase amidase 2 family
Am2
null
null
A0A075TMP0
reviewed
PATD_PENEN
Alcohol dehydrogenase patD (EC 1.1.1.-) (Patulin biosynthesis cluster protein D)
patD PEX2_082780
Penicillium expansum (Blue mold rot fungus)
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
FUNCTION: Alcohol dehydrogenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatD catalyzes the conversion of neopatulin into E-ascladiol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.
null
Zinc-containing alcohol dehydrogenase family
patD
PEX2_082780
null
A0A075TMP8
reviewed
PATI_PENEN
Cytochrome P450 monooxygenase patI (EC 1.-.-.-) (Patulin biosynthesis cluster protein I) (m-hydroxybenzyl alcohol hydroxylase)
patI PEX2_082860
Penicillium expansum (Blue mold rot fungus)
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatI catalyzes the conversion of m-hydroxybenzyl alcohol into gentisyl alcohol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.
null
Cytochrome P450 family
patI
PEX2_082860
null
A0A075TR33
reviewed
PATO_PENEN
FAD-linked oxidoreductase patO (EC 1.-.-.-) (Patulin biosynthesis cluster protein O)
patO PEX2_082840
Penicillium expansum (Blue mold rot fungus)
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatO acts with patJ in the vacuole to convert gentisyl alcohol to isoepoxydon (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.
null
Oxygen-dependent FAD-linked oxidoreductase family
patO
PEX2_082840
null
A0A075TR41
reviewed
PATJ_PENEN
Probable oxidoreductase patJ (EC 1.-.-.-) (Patulin biosynthesis cluster protein J)
patJ PEX2_082870
Penicillium expansum (Blue mold rot fungus)
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
FUNCTION: Probable oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatJ acts with patO in the vacuole to convert gentisyl alcohol to isoepoxydon (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.
null
Oxidoreductase OpS7 family
patJ
PEX2_082870
null
A0A075TRC0
reviewed
PATK_PENEN
6-methylsalicylic acid synthase (6MSAS) (EC 2.3.1.165) (Non-reducing polyketide synthase patK) (Patulin biosynthesis cluster protein K)
patK PEX2_082880
Penicillium expansum (Blue mold rot fungus)
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
FUNCTION: 6-methylsalicylic acid synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886, PubMed:35339702). PatK catalyzes the first step of the pathway which is the synthesis of 6-methylsalicylic acid via condensation of 1 acetate and 3 malonate units (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000269|PubMed:35339702, ECO:0000305|PubMed:30680886}.
DOMAIN: Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm. {ECO:0000250|UniProtKB:Q5B0D0}.
null
patK
PEX2_082880
null
A0A075TRK9
reviewed
PATE_PENEN
Patulin synthase (EC 1.1.-.-) (Dehydrogenase patE) (Patulin biosynthesis cluster protein E)
patE PEX2_082770
Penicillium expansum (Blue mold rot fungus)
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
FUNCTION: Patulin synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatE catalyzes the last step of the pathway which is the conversion of E-ascladiol to patulin (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.
null
GMC oxidoreductase family
patE
PEX2_082770
null
A0A075TRL5
reviewed
PATH_PENEN
Cytochrome P450 monooxygenase patH (EC 1.-.-.-) (Patulin biosynthesis cluster protein H) (m-cresol hydrolase)
patH PEX2_082740
Penicillium expansum (Blue mold rot fungus)
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatH catalyzes the conversion of m-cresol into m-hydroxybenzyl alcohol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.
null
Cytochrome P450 family
patH
PEX2_082740
null
A0A075TXZ1
reviewed
PATG_PENEN
6-methylsalicylic acid decarboxylase (EC 4.1.1.52) (Patulin biosynthesis cluster protein G)
patG PEX2_082750
Penicillium expansum (Blue mold rot fungus)
null
PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.
FUNCTION: 6-methylsalicylic acid decarboxylase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatG catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.
null
Metallo-dependent hydrolases superfamily, ACMSD family
patG
PEX2_082750
null
A0A076FFM5
reviewed
F8H1_OCIBA
Flavonoid 8-hydroxylase 1, chloroplastic (ObF8H-1) (EC 1.14.15.-)
F8H-1
Ocimum basilicum (Sweet basil)
null
PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}.
FUNCTION: Rieske-type, PAO-family oxygenase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects (PubMed:25139498). Catalyzes the 8-hydroxylation of salvigenin (SALV) to produce 8-hydroxysalvigenin (8-OH-SALV) (PubMed:25139498). Can also use cirsimaritin (CIRM) as substrate with low efficiency (PubMed:25139498). {ECO:0000269|PubMed:25139498}.
null
null
F8H-1
null
null
A0A078CGE6
reviewed
M3KE1_BRANA
MAP3K epsilon protein kinase 1 (BnM3KE1) (EC 2.7.11.1)
M3KE1 BnaA03g30290D GSBRNA2T00111755001
Brassica napus (Rape)
null
null
FUNCTION: Serine/threonine-protein kinase involved in the spatial and temporal control system organizing cortical activities in mitotic and postmitotic cells (PubMed:11489177). Required for the normal functioning of the plasma membrane in developing pollen. Involved in the regulation of cell expansion and embryo development (By similarity). {ECO:0000250|UniProtKB:Q9LJD8, ECO:0000269|PubMed:11489177}.
null
Protein kinase superfamily, Ser/Thr protein kinase family
M3KE1
BnaA03g30290D GSBRNA2T00111755001
null
A0A087WPF7
reviewed
AUTS2_MOUSE
Autism susceptibility gene 2 protein homolog
Auts2 Kiaa0442
Mus musculus (Mouse)
B2RWS6; Q61985; Q99K48; Q9CQJ4
null
FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The PRC1-like complex that contains PCGF5, RNF2, CSNK2B, RYBP and AUTS2 has decreased histone H2A ubiquitination activity, due to the phosphorylation of RNF2 by CSNK2B. As a consequence, the complex mediates transcriptional activation (By similarity). In the cytoplasm, plays a role in axon and dendrite elongation and in neuronal migration during embryonic brain development. Promotes reorganization of the actin cytoskeleton, lamellipodia formation and neurite elongation via its interaction with RAC guanine nucleotide exchange factors, which then leads to the activation of RAC1 (PubMed:25533347). {ECO:0000250|UniProtKB:Q8WXX7, ECO:0000269|PubMed:25533347}.
DOMAIN: The Pro-rich region is important for the interaction with RAC guanine nucleotide exchange factors and the subsequent activation of RAC1, which then promotes lamellipodia formation. {ECO:0000269|PubMed:25533347}.
AUTS2 family
Auts2
null
Kiaa0442
A0A087X1C5
reviewed
CP2D7_HUMAN
Putative cytochrome P450 2D7 (EC 1.14.14.1)
CYP2D7
Homo sapiens (Human)
null
null
FUNCTION: May be responsible for the metabolism of many drugs and environmental chemicals that it oxidizes. It may be involved in the metabolism of codeine to morphine (PubMed:15051713). However, another study could not confirm it (PubMed:18838503). {ECO:0000269|PubMed:15051713, ECO:0000269|PubMed:18838503}.
null
Cytochrome P450 family
CYP2D7
null
null
A0A088MIT0
reviewed
BRKP2_PHYNA
Bradykinin-related peptides [Cleaved into: Nattererimorphin; [Val1,Thr6]-bradykinyl-Ser,Pro,Ala; Bradykinin; Des-Arg9-bradykinin; [Hyp3]-bradykinyl-Val,Asp]
BBN
Physalaemus nattereri (Cuyaba dwarf frog) (Eupemphix nattereri)
null
null
FUNCTION: [[Val1,Thr6]-bradykinyl-Ser,Pro,Ala]: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB). {ECO:0000250|UniProtKB:P84899}.; FUNCTION: [Bradykinin]: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB). {ECO:0000250|UniProtKB:L0PIN3}.; FUNCTION: [Des-Arg9-bradykinin]: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB). {ECO:0000250|UniProtKB:L0PIN3}.; FUNCTION: [[Hyp3]-bradykinyl-Val,Asp]: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB). {ECO:0000250|UniProtKB:L0PIN3}.
null
Frog skin active peptide (FSAP) family, Bradykinin-related peptide subfamily
BBN
null
null
A0A088MLT8
reviewed
IQIP1_MOUSE
IQCJ-SCHIP1 readthrough transcript protein
Iqcj-Schip1 Iqschfp Schip1
Mus musculus (Mouse)
null
null
FUNCTION: May play a role in action potential conduction in myelinated cells through the organization of molecular complexes at nodes of Ranvier and axon initial segments (PubMed:25950943, PubMed:25953347, PubMed:27979964). May also play a role in axon outgrowth and guidance (PubMed:25953347). {ECO:0000269|PubMed:25950943, ECO:0000269|PubMed:25953347, ECO:0000269|PubMed:27979964}.
null
null
Iqcj-Schip1
null
Iqschfp Schip1
A0A089QRB9
reviewed
MSL3_MYCTU
Mycolipanoate synthase (EC 2.3.1.252) (Mycocerosic acid synthase-like polyketide synthase) (MAS-like PKS) (Mycolipanoic/mycolipenic acids synthase-like polyketide synthase)
msl3 pks3 pks4 Rv1180/Rv1181
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
null
PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305|PubMed:12207710}.
FUNCTION: Polyketide synthase involved in the biosynthesis of methyl-branched fatty acids such as mycolipanoic, mycolipenic (phthienoic) and mycolipodienoic acids required for the synthesis of a major class of polyacylated trehaloses. Catalyzes the elongation of CoA esters of long-chain fatty acids by incorporation of three methylmalonyl (but not malonyl) residues, to form trimethyl-branched fatty-acids. {ECO:0000269|PubMed:12207710}.
null
null
msl3
null
pks3 pks4
A0A095AMW7
reviewed
MLES_LEUME
Malolactic enzyme (MLE) (EC 4.1.1.101)
mleS LH61_04880
Leuconostoc mesenteroides
null
null
FUNCTION: Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate. {ECO:0000269|PubMed:16345941}.
null
Malic enzymes family
mleS
LH61_04880
null
A0A095C6S0
reviewed
OXDA2_CRYD2
D-amino-acid oxidase 2 (DAAO) (DAMOX) (DAO) (EC 1.4.3.3) (CgDAO2)
DAO2 CNBG_2060
Cryptococcus deuterogattii (strain R265) (Cryptococcus gattii VGII (strain R265))
null
null
FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:26132227). Enables the organism to utilize D-amino acids as a source of nutrients (PubMed:26132227). Enables the organism to utilize D-alanine, D-cysteine, D-histidine, D-leucine, D-methionine, D-phenylalanine, D-proline, D-serine, D-threonine, D-aspartate and D-valine as a nitrogen source and may also contribute to utlization of D-tryptophan, D-tyrosine and D-asparagine as a nitrogen source (PubMed:26132227). Protects the organism from the toxicity of D-amino acids, including from D-alanine (PubMed:26132227). May play a role in its interaction with the host (PubMed:26132227). {ECO:0000269|PubMed:26132227}.
null
DAMOX/DASOX family
DAO2
CNBG_2060
null
A0A096MJN4
reviewed
SEPT4_RAT
Septin-4 (Apoptosis-related protein in the TGF-beta signaling pathway) (Arts) (Bradeion beta) (Brain protein H5) (CE5B3 beta) (Cell division control-related protein 2) (hCDCREL-2) (Peanut-like protein 2)
Septin4 Arts Bh5 Gm11492 Pnut12 Sep4 Sept4
Rattus norvegicus (Rat)
null
null
FUNCTION: Filament-forming cytoskeletal GTPase. Pro-apoptotic protein involved in LGR5-positive intestinal stem cell and Paneth cell expansion in the intestines, via its interaction with XIAP (By similarity). May also play a role in the regulation of cell fate in the intestine (By similarity). Positive regulator of apoptosis involved in hematopoietic stem cell homeostasis; via its interaction with XIAP (By similarity). Negative regulator of repair and hair follicle regeneration in response to injury, due to inhibition of hair follicle stem cell proliferation, potentially via its interaction with XIAP (By similarity). Plays an important role in male fertility and sperm motility (By similarity). During spermiogenesis, essential for the establishment of the annulus (a fibrous ring structure connecting the midpiece and the principal piece of the sperm flagellum) which is a requisite for the structural and mechanical integrity of the sperm (By similarity). Involved in the migration of cortical neurons and the formation of neuron leading processes during embryonic development (By similarity). Required for dopaminergic metabolism in presynaptic autoreceptors; potentially via activity as a presynaptic scaffold protein (By similarity). {ECO:0000250|UniProtKB:P28661}.
null
TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family
Septin4
null
Arts Bh5 Gm11492 Pnut12 Sep4 Sept4
A0A096MJY4
reviewed
MEF2C_RAT
Myocyte-specific enhancer factor 2C (Myocyte enhancer factor 2C)
Mef2c
Rattus norvegicus (Rat)
null
null
FUNCTION: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes (PubMed:15862299). Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture (By similarity). {ECO:0000250|UniProtKB:Q8CFN5, ECO:0000269|PubMed:15862299}.
DOMAIN: The beta domain is required for enhancement of transcriptional activity. {ECO:0000250}.
MEF2 family
Mef2c
null
null
A0A096MK47
reviewed
MLIP_RAT
Muscular LMNA-interacting protein (Cardiac Isl1-interacting protein) (CIP)
Mlip Cip
Rattus norvegicus (Rat)
null
null
FUNCTION: Required for myoblast differentiation into myotubes, possibly acting as a transcriptional regulator of the myogenic program (By similarity). Required for cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays a role in the protection against cardiac hypertrophy (PubMed:22343712, PubMed:26436652). Binds chromatin (By similarity). May act as a transcriptional cofactor for ISL1, repressing its transcriptional activity (By similarity). May also repress MYOCD transcriptional activity (By similarity). {ECO:0000250|UniProtKB:Q5FW52, ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26436652}.
null
null
Mlip
null
Cip
A0A096P8D3
reviewed
IDH_OSTTA
Isocitrate dehydrogenase (NAD(+)), mitochondrial (OtIDH) (EC 1.1.1.41)
IDH Ot_13g02940 BE221DRAFT_192402
Ostreococcus tauri
null
null
FUNCTION: Performs an essential role in the oxidative function of the tricarboxylic acid cycle and respiration (Probable). Catalyzes the decarboxylation of isocitrate to produce 2-oxoglutarate and generate NADH to provide electrons for energy production (Probable). {ECO:0000305|PubMed:25724193}.
null
Isocitrate and isopropylmalate dehydrogenases family
IDH
BE221DRAFT_192402
null
A0A097PTA8
reviewed
DEFCO_COPCI
Fungal defensin copsin
null
Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
null
null
FUNCTION: Antimicrobial peptide that acts against Gram-positive bacteria (Listeria spp., Enterococcus spp., B.subtilis, B.anthracis, P.aeruginosa) (PubMed:25342741, PubMed:28825809). Is not active against Gram-negative bacteria (PubMed:25342741). It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio), probably anchoring lipid II to the membrane, thus inhibiting cell wall synthesis (PubMed:25342741, PubMed:28825809). The interaction with lipid II involves the third position of the pentapeptide (PubMed:25342741). Shows bactericidal activity at about 2-fold minimal inhibitory concentrations (MIC), but does not form pore across the membrane (PubMed:25342741). {ECO:0000269|PubMed:25342741, ECO:0000269|PubMed:28825809}.
null
Invertebrate defensin family
null
null
null
A0A0A0LLY1
reviewed
SRBP1_CUCSA
Small RNA binding protein 1 (CsSRBP1)
SRBP1 Csa_2G247040
Cucumis sativus (Cucumber)
null
null
FUNCTION: Possibly has a role in RNA transcription or processing during stress (By similarity). Binds sequence non-specifically to RNAs and DNAs (By similarity). Mediates cell-to-cell trafficking of RNA interference (RNAi) signals (small RNAs (sRNA), e.g. small interfering RNA (siRNA) and microRNA (miRNA)) which regulate growth and development, as well as responses to environmental inputs, including pathogen attack; can compromise zucchini yellow mosaic virus (ZYMV) and tobacco rattle virus (TRV) infections at the early stage (PubMed:31812689). {ECO:0000250|UniProtKB:Q9LIS2, ECO:0000269|PubMed:31812689}.
DOMAIN: The glycine-rich (GR) domain is necessary and sufficient for cell-to-cell movement and to interefere with zucchini yellow mosaic virus (ZYMV) infection. {ECO:0000269|PubMed:31812689}.
GR-RBP family
SRBP1
Csa_2G247040
null
A0A0A1C3I2
reviewed
HMGR1_PANGI
3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG-CoA reductase 1) (Hydroxymethylglutaryl-CoA reductase) (PgHMGR1) (EC 1.1.1.34)
HMGR1 HMGR
Panax ginseng (Korean ginseng)
null
PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. {ECO:0000305}.
FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:24569845, PubMed:29378087). Promotes triterpenes accumulation in roots (PubMed:24569845). {ECO:0000250|UniProtKB:P14891, ECO:0000269|PubMed:24569845, ECO:0000303|PubMed:29378087}.
null
HMG-CoA reductase family
HMGR1
null
HMGR
A0A0A1C930
reviewed
HMR2A_PANGI
3-hydroxy-3-methylglutaryl coenzyme A reductase 2-A (HMG-CoA reductase 2) (Hydroxymethylglutaryl-CoA reductase) (PgHMGR2) (EC 1.1.1.34)
HMGR2
Panax ginseng (Korean ginseng)
null
PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. {ECO:0000305}.
FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:24569845, PubMed:29378087). {ECO:0000250|UniProtKB:P14891, ECO:0000269|PubMed:24569845, ECO:0000303|PubMed:29378087}.
null
HMG-CoA reductase family
HMGR2
null
null
A0A0A1H8I4
reviewed
AIS_PSESP
Aconitate isomerase (AI) (EC 5.3.3.7)
ais
Pseudomonas sp
null
null
FUNCTION: Involved in assimilation of trans-aconitic acid. Preference for cis-aconitic acid is 14-fold higher than for trans-aconitic acid. Not active on intermediates of tricarboxylic acid (TCA) cycle including citric acid, succinic acid, fumaric acid, and 2-oxoglutaric acid or on other dicarboxilic acids including itaconic acid, formic acid, citraconic acid or maleic acid. {ECO:0000269|PubMed:26293748}.
null
null
ais
null
null
A0A0A1HA03
reviewed
708C1_FAGES
UDP-glycosyltransferase 708C1 (EC 2.4.1.360) (C-glucosyltransferase a) (FeCGTa) (UDP-glucose:2-hydroxyflavanone C-glucosyltransferase)
UGT708C1 CGTa
Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum)
null
null
FUNCTION: UDP-glucose-dependent glucosyltransferase catalyzing the C-glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin, 2-hydroxyeriodictyol and 2-hydroxypinocembrin) and phloretin (PubMed:25142187). No activity with flavanones, flavones or flavonols (PubMed:25142187). Exhibits C-glycosylation activity toward 2',4',6'-trihydroxyacetophenone and phloretin using UDP-glucose as sugar donor (PubMed:32699169). Can use UDP-galactose as sugar donor, but catalytic efficiency is 14-fold lower toward UDP-galactose than toward UDP-glucose (PubMed:32699169). {ECO:0000269|PubMed:25142187, ECO:0000269|PubMed:32699169}.
null
UDP-glycosyltransferase family
UGT708C1
null
CGTa
A0A0A1I6E7
reviewed
NDB4S_ANDCR
Antimicrobial peptide AcrAP1
null
Androctonus crassicauda (Arabian fat-tailed scorpion)
null
null
FUNCTION: Has antimicrobial activity against the Gram-positive bacteria S.aureus (MIC=8 uM) and the yeast C.albicans (MIC=16 uM). Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Minimum bactericidal concentrations have also been tested against S.aureus and is four-fold higher (MBC=32 uM). {ECO:0000269|PubMed:25332684}.
null
Non-disulfide-bridged peptide (NDBP) superfamily, Short antimicrobial peptide (group 4) family
null
null
null
A0A0A1I6N9
reviewed
NDB4T_ANDCR
Antimicrobial peptide AcrAP2
null
Androctonus crassicauda (Arabian fat-tailed scorpion)
null
null
FUNCTION: Has antimicrobial activity against the Gram-positive bacteria S.aureus (MIC=8 uM) and the yeast C.albicans (MIC=16 uM). Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Minimum bactericidal concentrations have also been tested against S.aureus and is four-fold higher (MBC=32 uM). {ECO:0000269|PubMed:25332684}.
null
Non-disulfide-bridged peptide (NDBP) superfamily, Short antimicrobial peptide (group 4) family
null
null
null
A0A0A6ZFY4
reviewed
UGT29_PANGI
UDP-glucosyltransferase 29 (UGTPg29) (EC 2.4.1.365) (UDP-glucosyltransferase 94B1) (PgUGT94B1) (UDP-glucosyltransferase 94Q2) (PgUGT94Q2)
UGT29 UGT94B1 UGT94Q2
Panax ginseng (Korean ginseng)
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305}.
FUNCTION: Component of the dammarane-type triterpene saponins (e.g. PPD-type ginsenosides or panaxosides) biosynthetic pathway (PubMed:25320211, PubMed:25769286, PubMed:27746309, PubMed:29378087). Glycosyltransferase that catalyzes the conversion of ginsenoside Rh2 to ginsenoside Rg3 (PubMed:25320211, PubMed:25769286, PubMed:27746309). Triggers the biosynthesis of ginsenoside Rd from ginsenoside F2 (PubMed:25320211). {ECO:0000269|PubMed:25320211, ECO:0000269|PubMed:25769286, ECO:0000269|PubMed:27746309, ECO:0000303|PubMed:29378087}.
null
UDP-glycosyltransferase family
UGT29
null
UGT94B1 UGT94Q2
A0A0A7EPL0
reviewed
PIAL1_ARATH
E4 SUMO-protein ligase PIAL1 (EC 2.3.2.-) (Protein EMBRYO DEFECTIVE 3001) (Protein INHIBITOR OF ACTIVATED STAT-LIKE 1)
PIAL1 EMB3001 At1g08910 F7G19.21
Arabidopsis thaliana (Mouse-ear cress)
null
PATHWAY: Protein modification; protein sumoylation. {ECO:0000269|PubMed:25415977}.
FUNCTION: Together with MOM1 and PIAL2, regulates transcriptional gene silencing (TGS) independently of changes in DNA methylation (PubMed:27113777). E4-type SUMO ligase that promotes SUMO chain formation in a SCE1-dependent manner and thus contributes to a pathway for proteolytic removal of sumoylation substrates (PubMed:25415977). Involved in stress responses (e.g. osmotic, salt and abscisic acid ABA) and sulfur metabolism (PubMed:25415977). {ECO:0000269|PubMed:25415977, ECO:0000269|PubMed:27113777}.
null
PIAL protein ligase family
PIAL1
F7G19.21
EMB3001
A0A0A7EQR3
reviewed
GCE_CERUI
4-O-methyl-glucuronoyl methylesterase (EC 3.1.1.117) (Glucuronoyl esterase) (GE)
null
Cerrena unicolor (Canker rot fungus) (Daedalea unicolor)
null
null
FUNCTION: Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin (PubMed:25425346, PubMed:26712478). {ECO:0000269|PubMed:25425346, ECO:0000269|PubMed:26712478}.
null
Carbohydrate esterase 15 (CE15) family
null
null
null
A0A0A7GEY4
reviewed
GGPPS_GEOAI
Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
GACE_1337
Geoglobus acetivorans
null
PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000305}.; PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000305}.; PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000305}.
FUNCTION: Catalyzes the addition of 3 molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl pyrophosphate (GGPP). Catalyzes the synthesis of geranylgeranyl pyrophosphate as a major product and of farnesyl pyrophosphate in smaller amounts. {ECO:0000269|PubMed:30062607}.
null
FPP/GGPP synthase family
null
GACE_1337
null
A0A0A7HFE1
reviewed
CAS10_STRTR
CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) (ssDNase Cas10) (EC 3.1.-.-) (Cyclic oligoadenylate synthase) (EC 2.7.7.-) (StCas10)
cas10 csm1
Streptococcus thermophilus
null
null
FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host this Csm effector complex restricts ssRNA phage MS2, suggesting it may target RNA viruses in vivo. {ECO:0000269|PubMed:25458845}.; FUNCTION: Csm functions as a non-specific ssDNase. Base-pairing between crRNA and target RNA to form a ternary Csm complex activates a ssDNase activity; target RNA cleavage suppresses the ssDNase, a temporal control that prevents uncontrolled DNA degradation. Viral RNA transcripts probably tether the Csm complex to the viral genome, recruiting Cas10 ssDNA activity which is able to degrade DNA in the transcription bubble, spatially controlling the DNase activity. {ECO:0000269|PubMed:27105119}.; FUNCTION: This subunit has a weak ssDNase activity that is dramatically activated by the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA). Target RNA and ssDNA are cleaved simultaneously, although RNase activity (of Csm3) is much faster. RNA cleavage by Csm3 is not required for ssDNase activity as Csm complex with inactive Csm3 still has ssDNase activity; however as the cleaved target RNA products dissociate away ssDNase activity decreases. Self-recognition, with subsequent repression of the ssDNase activity, occurs when the 5' handle of the crRNA bases pairs with the 3' flanking sequence of the target RNA (which would occur if the CRISPR locus were transcribed as an anti-pre-crRNA). This protein has low activity on dsDNA which is not stimulated by the Csm complex. {ECO:0000269|PubMed:27105119}.; FUNCTION: This subunit is a single-strand-specific deoxyribonuclease (ssDNase) which digests both linear and circular ssDNA; it has both exo- and endonuclease activity. {ECO:0000250|UniProtKB:B6YWB8}.; FUNCTION: When associated with the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic oligoadenylates (cOA) from ATP, producing cyclic triadenylate (cA3) up to cyclic hexaadenylate (cA6), which is the active cOA. The enzyme is also able to cyclize pppA3 up to pppA6. cOAs are second messengers that induce an antiviral state important for defense against invading nucleic acids. Synthesis of cOA can occur with AMP plus ATP, 2'dATP or 3'dATP (but no other nucleotides), and requires a free 3'-OH ribose moiety. {ECO:0000269|PubMed:28663439}.
DOMAIN: The N-terminal HD domain has ssDNase activity (PubMed:27105119). The C-terminal GGDEF domain has the cOA synthesis activity (PubMed:28663439). {ECO:0000269|PubMed:27105119, ECO:0000269|PubMed:28663439}.
CRISPR-associated Cas10/Csm1 family
cas10
null
csm1
A0A0A7HIF0
reviewed
CSM3_STRTR
CRISPR system Cms endoribonuclease Csm3 (Csm3 RNase) (EC 3.1.-.-) (CRISPR type III A-associated RAMP protein Csm3)
csm3
Streptococcus thermophilus
null
null
FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host this Csm effector complex restricts ssRNA phage MS2, suggesting it may target RNA viruses in vivo. {ECO:0000269|PubMed:25458845}.; FUNCTION: Csm functions as a non-specific ssDNase. Base-pairing between crRNA and target RNA to form a ternary Csm complex activates a ssDNase activity; target RNA cleavage suppresses the ssDNase, a temporal control that prevents uncontrolled DNA degradation. Viral RNA transcripts probably tether the Csm complex to the viral genome, recruiting Cas10 ssDNA activity which is able to degrade DNA in the transcription bubble, spatially controlling the DNase activity. {ECO:0000269|PubMed:27105119}.; FUNCTION: This subunit has the target ssRNA endonuclease activity; it cleaves multiple sites in the target RNA at 6 nucleotide intervals. The number of cleavage sites in the target RNA correlates with the number of Csm3 subunits in the Csm effector complex (PubMed:25458845). In the Csm complex target RNA and ssDNA are cleaved simultaneously, although RNase activity (of Csm3) is much faster. RNA cleavage by Csm3 is not required for ssDNase activity as Csm complex with inactive Csm3 still has ssDNase activity; however as the cleaved target RNA products dissociate away ssDNase activity decreases (PubMed:27105119). {ECO:0000269|PubMed:25458845, ECO:0000269|PubMed:27105119}.
null
CRISPR-associated Csm3 family
csm3
null
null
A0A0A7HIX6
reviewed
CSM6A_STRTR
CRISPR system endoribonuclease Csm6 (EC 3.1.-.-) (CRISPR type III-A associated protein Csm6-1)
csm6
Streptococcus thermophilus
null
null
FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host this Csm effector complex restricts ssRNA phage MS2, suggesting it may target RNA viruses in vivo. This protein is not part of the Csm complex. {ECO:0000269|PubMed:25458845}.; FUNCTION: Csm functions as a non-specific ssDNase. Base-pairing between crRNA and target RNA to form a ternary Csm complex activates a ssDNase activity; target RNA cleavage suppresses the ssDNase, a temporal control that prevents uncontrolled DNA degradation. Viral RNA transcripts probably tether the Csm complex to the viral genome, recruiting Cas10 ssDNA activity which is able to degrade DNA in the transcription bubble, spatially controlling the DNase activity. {ECO:0000269|PubMed:27105119}.; FUNCTION: A single-strand-specific endoribonuclease (ssRNase) that is approximately 1000-fold stimulated by cyclic oligoadenylate (cOA); although several species of cOA are synthesized by this organism only cyclic hexaadenylate (cA6) stimulates the ssRNase activity. Cleaves preferentially within GA or AA dinucleotides, although the presence of cA6 broadens the preference. Linear oligoadenylates do not activate the RNase. {ECO:0000269|PubMed:28663439}.
DOMAIN: The N-terminal CRISPR-associated Rossman fold (CARF) probably binds the cA6 effector. ssRNase activity resides in the C-terminal HEPN domain. {ECO:0000250|UniProtKB:Q53W17}.
CRISPR-associated Csm6 family
csm6
null
null
A0A0A8IDB7
reviewed
AA12_COPCI
Pyrroloquinoline quinone-dependent pyranose dehydrogenase (PDH) (EC 1.1.99.-) (AA12 family sugar dehydrogenase) (Pyrroloquinoline quinone-dependent sugar dehydrogenase) (SDH)
PDH SDH
Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
null
null
FUNCTION: Pyrroloquinoline quinone (PPQ)-dependent oxidoreductase that catalyzes the oxidation of various sugars including L-galactose, L-gulose, D-talose, D-arabinose, D-lyxose, L-fucose and D-glucosone (PubMed:25121592, PubMed:25679509, PubMed:27338639). Shows significant activity toward the reverse-chair conformation of pyranoses (PubMed:25679509). Shows little or no activity toward abundant sugars such as D-glucose, D-fructose, cellobiose, as well L-xylose and L-glucose (PubMed:25121592, PubMed:25679509). This enzyme is able to direct electrical communication with electrodes, without artificial electron mediators, thus allowing direct electron transfer (DET)-type bioelectrocatalysis (PubMed:27338639). Exhibits binding affinity for insoluble cellulose (PubMed:25679509). PDH does not oxidize cello-oligosaccharides but is able to activate the C-1-oxidizing Neurospora crassa LPMO9F and the C-4-oxidizing Neurospora crassa LPMO9C thanks to the electron-tranfer activity of the cytochrome domain and the localization of PDH in the vicinity of the LPMO substrates by the CBM1 domain (PubMed:29602785). {ECO:0000269|PubMed:25121592, ECO:0000269|PubMed:25679509, ECO:0000269|PubMed:27338639, ECO:0000269|PubMed:29602785}.
DOMAIN: PDH consists of three domains: an N-terminal cytochrome domain (found in AA8 family enzymes), a PQQ-dependent dehydrogenase domain in the middle of the sequence, and a C-terminal cellulose-binding domain classified as a member of the family 1 carbohydrate-binding module (CBM1). {ECO:0000305|PubMed:25121592}.; DOMAIN: The N-terminal cytochrome domain has an electron transfer function, i.e., intra- and inter-molecular electron transfer between the cytochrome domain and the catalytic domain and also Fe (III)-reducing ability (PubMed:25679509, PubMed:27338639). This function is essential to activate lytic polysaccharide monooxygenases (LPMOs) at the cell wall (PubMed:29602785). {ECO:0000269|PubMed:25679509, ECO:0000269|PubMed:27338639, ECO:0000269|PubMed:29602785}.; DOMAIN: The CBM1 domain binds cellulose and is essential to localize the electron transfer activity in the vicinity of the substrate of lytic polysaccharide monooxygenases (LPMOs) to activate them. {ECO:0000269|PubMed:29602785}.
Sugar dehydrogenase AA12 family
PDH
null
SDH
A0A0B0QJR1
reviewed
HEPT_APHF2
tRNA nuclease HepT (EC 3.1.27.-) (Toxin HEPN) (tRNA nuclease HEPN)
hepT hepn OA07_26455
Aphanizomenon flos-aquae (strain 2012/KM1/D3)
null
null
FUNCTION: Toxic component of a type VII toxin-antitoxin (TA) system. Upon cloning in E.coli inhibits cell growth for several hours; eventually cells recover and start growing. Cleaves the last 4 nucleotides from the tRNA acceptor stem (shown in vitro with E.coli tRNA-Glu(UUC)); only cleaves intact tRNA. Has no activity on mRNA. Neutralized by coexpression with cognate antitoxin MntA, which is due to di-AMPylation of the RNase. {ECO:0000269|PubMed:33290744}.
null
HepT RNase toxin family
hepT
OA07_26455
hepn
A0A0B4J1F4
reviewed
ARRD4_MOUSE
Arrestin domain-containing protein 4
Arrdc4
Mus musculus (Mouse)
null
null
FUNCTION: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates (PubMed:27462458). Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) (By similarity). Through an ubiquitination-dependent mechanism also plays a role in the incorporation of SLC11A2 into extracellular vesicles (PubMed:27462458). May play a role in glucose uptake (By similarity). Participates in innate immune response by promoting IFIH1/MDA5 activation through interaction with TRIM65 (By similarity). {ECO:0000250|UniProtKB:Q8NCT1, ECO:0000269|PubMed:27462458}.
null
Arrestin family
Arrdc4
null
null
A0A0B4J1G0
reviewed
FCG3A_MOUSE
Low affinity immunoglobulin gamma Fc region receptor III-A (IgG Fc receptor III-A) (CD16-2) (FcgammaRIV) (CD antigen CD16a)
Fcgr4 Fcgr3a
Mus musculus (Mouse)
null
null
FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG) (PubMed:16039578). Binds with intermediate affinity to both IgG2a and IgG2b (PubMed:16039578, PubMed:17558411, PubMed:19795417). Can bind to IgG2a and IgG2b monomers (PubMed:18949059). Does not display binding to IgG1 or IgG3 (PubMed:16039578). Recognizes neutralizing virus-specific IgGs displayed on the cell surface of infected cells and triggers antibody-dependent cellular cytotoxicity (ADCC). Confers protection to lethal influenza virus infection (PubMed:24412922). On splenic dendritic cells, uptakes antigen immune complexes and efficiently divert them into MHC class I and II antigen presentation pathways to provide for superior priming of CD4-positive and CD8-positive T cell immune responses (PubMed:28389502). Mediates neutrophil activation by IgG complexes redundantly with FCGR2A (PubMed:18097064). Plays a role in promoting bone resorption by enhancing osteoclast differentiation following binding to IgG2a (PubMed:25824719). Also acts as a receptor for the Fc region of immunoglobulin epsilon (IgE) (PubMed:17558411, PubMed:18949059). Binds with low affinity to both the a and b allotypes of IgE (PubMed:18949059). Has also been shown to bind to IgE allotype a only but not to allotype b (PubMed:17558411). Binds aggregated IgE but not the monomeric form and bound monomeric IgG is readily displaced by IgE complexes (PubMed:18949059). Binding to IgE promotes macrophage-mediated phagocytosis, antigen presentation to T cells, production of pro-inflammatory cytokines and the late phase of cutaneous allergic reactions (PubMed:17558411, PubMed:18949059). Mediates enhanced ADCC in response to afucosylated IgGs (PubMed:34485821). {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:18097064, ECO:0000269|PubMed:18949059, ECO:0000269|PubMed:19795417, ECO:0000269|PubMed:24412922, ECO:0000269|PubMed:25824719, ECO:0000269|PubMed:28389502, ECO:0000269|PubMed:34485821}.
null
null
Fcgr4
null
Fcgr3a
A0A0B4J1N3
reviewed
GP15L_MOUSE
Protein GPR15LG (Protein GPR15 ligand) (Protein GPR15L)
Gpr15lg Gpr15l
Mus musculus (Mouse)
null
null
FUNCTION: Highly cationic protein that has multiple functions. Acts as a chemotactic factor that mediates lymphocytes recruitment to epithelia through binding and activation of the G-protein coupled receptor GPR15 (PubMed:28900043, PubMed:28936214). May be a tumor suppressor; together with SUSD2 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest (By similarity). May regulate keratinocyte proliferation. In addition, through activation of Mas-related G protein-coupled receptors (MRGPRs) contributes to pruritogenesis by activating itch-selective sensory neurons and mast cells degranulation (PubMed:35704588). {ECO:0000250|UniProtKB:Q6UWK7, ECO:0000269|PubMed:28900043, ECO:0000269|PubMed:28936214, ECO:0000269|PubMed:35704588}.; FUNCTION: Has antimicrobial activity against Gram-positive bacteria, including Staphylococcus aureus and Actinomyces spec., and Mycoplasma hominis and lentivirus. {ECO:0000250|UniProtKB:Q6UWK7}.
null
null
Gpr15lg
null
Gpr15l
A0A0B4J2F0
reviewed
PIOS1_HUMAN
Protein PIGBOS1 (PIGB opposite strand protein 1)
PIGBOS1
Homo sapiens (Human)
Q96S66
null
FUNCTION: Plays a role in regulation of the unfolded protein response triggered by endoplasmic reticulum (ER) stress resulting from the presence of unfolded proteins in the ER lumen. {ECO:0000269|PubMed:31653868}.
null
null
PIGBOS1
null
null
A0A0B4J2F2
reviewed
SIK1B_HUMAN
Putative serine/threonine-protein kinase SIK1B (EC 2.7.11.1) (Salt-inducible kinase 1B)
SIK1B
Homo sapiens (Human)
Q9BRT9; Q68G74; Q14696; P78337; Q9NRG1; P62072
null
FUNCTION: Probable serine/threonine-protein kinase. {ECO:0000250|UniProtKB:P57059}.
null
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, AMPK subfamily
SIK1B
null
null
A0A0B4K692
reviewed
NEP2_DROME
Neprilysin-2 (EC 3.4.24.11) [Cleaved into: Neprilysin-2, soluble form]
Nep2 CG9761
Drosophila melanogaster (Fruit fly)
null
null
FUNCTION: Metalloendoprotease which cleaves peptides such as tachykinin peptide TK-2 at the amino side of hydrophobic residues (PubMed:15554877, PubMed:17157960). Functions in female fertility, embryogenesis and memory formation (PubMed:24395329, PubMed:27629706). Required in females for normal patterns of egg laying, probably due to its function in sperm retention and preventing sperm displacement by rival ejaculates (PubMed:24395329). Also required for normal patterns of hatching due to its important role in early embryonic development (PubMed:24395329). Required in the dorsal paired medial neurons for the proper formation of middle-term memory (PubMed:27629706). Also required in the mushroom body neurons where it functions redundantly with neprilysins Nep3 and Nep4 in normal long-term memory formation (PubMed:27629706). {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960, ECO:0000269|PubMed:24395329, ECO:0000269|PubMed:27629706}.
null
Peptidase M13 family
Nep2
CG9761
null
A0A0B4K7J2
reviewed
RBP2_DROME
E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358)
Nup358 RanBP2 CG11856
Drosophila melanogaster (Fruit fly)
null
null
FUNCTION: E3 SUMO-protein ligase (By similarity). Component of the nuclear pore complex (NPC), a complex required for trafficking across the nuclear envelope (PubMed:17682050). Required for nuclear import of nuclear localization signal (NLS)-containing proteins in an importin alpha/importin beta-dependent manner, but also for the nuclear import of specific proteins such as phosphorylated Mad or the sesquiterpenoid juvenile hormone receptor Met as part of the juvenile hormone signal transduction pathway (PubMed:17682050, PubMed:27979731). Plays a role in nuclear mRNA export by recruiting the mRNA transport complex composed of Nxt1 and sbr/Nxf1 to the NPC (PubMed:14729961). Essential during germline development for transposon silencing and piRNA biogenesis probably by regulating piwi localization to the nucleus (PubMed:29735528). During oogenesis, required to form granules that modulate the biogenesis of annulate lamellae containing nuclear pore complex components (PubMed:31626769). {ECO:0000250|UniProtKB:P49792, ECO:0000269|PubMed:14729961, ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:27979731, ECO:0000269|PubMed:29735528, ECO:0000269|PubMed:31626769}.
DOMAIN: Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. {ECO:0000305}.
RanBP2 E3 ligase family
Nup358
CG11856
RanBP2
A0A0B4KEE4
reviewed
KOI_DROME
Klaroid protein
koi CG44154
Drosophila melanogaster (Fruit fly)
null
null
FUNCTION: Component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (By similarity). Is required to nuclear migration in eye and to anchor klar in the nuclear membrane (PubMed:18820457). {ECO:0000250|UniProtKB:O94901, ECO:0000269|PubMed:18820457}.
null
null
koi
CG44154
null
A0A0B4KGY6
reviewed
NOVA_DROME
RNA-binding protein Pasilla
ps l(3)10615 NOVA1 CG42670
Drosophila melanogaster (Fruit fly)
null
null
FUNCTION: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion (By similarity). Plays a role in long-term memory formation by processing the unspliced Orb2-isoform A (Orb2A) mRNA and thereby controlling Orb2A protein abundance (PubMed:28525754). {ECO:0000250|UniProtKB:Q9JKN6, ECO:0000269|PubMed:28525754}.
DOMAIN: The KH domain consists of approximately 70 amino acids and includes a conserved hydrophobic core, an invariant Gly-X-X-Gly motif, and an additional variable segment. The third KH domain (KH3) binds a hairpin RNA loop containing the 5'-UCAY-3' motif on targeted molecules. RNA binding by KH3 requires residues C-terminal to the KH domain. {ECO:0000250|UniProtKB:P51513}.
null
ps
CG42670
l(3)10615 NOVA1
A0A0B4LFY9
reviewed
STING_DROME
Stimulator of interferon genes protein homolog (dSTING) (dmSTING)
Sting CG1667
Drosophila melanogaster (Fruit fly)
null
null
FUNCTION: Facilitator of innate immune signaling that binds cyclic dinucleotides produced in response to infection by bacteria and/or viruses, and promotes the activation of the NF-kappa-B transcription factor Rel (Relish) (PubMed:29924997, PubMed:29934091, PubMed:30119996, PubMed:33262294, PubMed:34261127, PubMed:34261128). Recognizes and binds cyclic di-GMP (c-di-GMP), a cyclic dinucleotide messenger produced by bacteria such as L.monocytogenes, leading to activation of the peptidoglycan recognition protein (IMD) signaling pathway and activation of Rel (Relish) (PubMed:29924997). Innate immune response is triggered in response to double-stranded RNA from viruses delivered to the cytoplasm: Sting acts by specifically binding cyclic dinucleotides 3',2'-cGAMP and 2',3'-cGAMP produced by cGlr1 and cGlr2 in response to RNA virus in the cytosol (PubMed:34261127, PubMed:34261128). Has a strong preference for 3',2'-cGAMP compared to other cyclic dinucleotides such as 2',3'-cGAMP or 3'3'-c-di-GMP (PubMed:34261127). Upon binding to 3',2'-cGAMP, activates an antiviral immune response, leading to the activation of Rel (Relish) (PubMed:34261127, PubMed:34261128). Activated in brain in response to Zika virus infection, leading to autophagy (PubMed:29934091). {ECO:0000269|PubMed:29924997, ECO:0000269|PubMed:29934091, ECO:0000269|PubMed:30119996, ECO:0000269|PubMed:33262294, ECO:0000269|PubMed:34261127, ECO:0000269|PubMed:34261128}.
null
STING family
Sting
CG1667
null
A0A0B4U9L8
reviewed
VMF1_VIPAA
Zinc metalloproteinase-disintegrin-like protein F1 (EC 3.4.24.-) (Fibrinogenase 1) (Metalloproteinase F1) (P-IIIa metalloproteinase F1) (Snake venom metalloproteinase) (SVMP) (VaF1)
null
Vipera ammodytes ammodytes (Western sand viper)
null
null
FUNCTION: Zinc metalloprotease that has fibrinogenolytic activity. Does not have hemorrhagic activity in rats. Cleaves insulin B chain at '38-Ala-|-Leu-39' and '40-Tyr-|-Leu-41' bonds. Hydrolyzes only partially and weakly isolated extracellular matrix (ECM) bovine fibronectin and basal membrane (BM) protein human collagen IV in vitro. Murine laminin is not hydrolyzed, neither isolated nor in a solubilized BM preparation. Nidogen is hydrolyzed at '350-Ser-|-Phe-351' bond in a solubilized BM preparation. Hydrolyzes plasma proteins involved in blood coagulation in vitro. Has alpha-fibrinogenase activity cleaving human fibrinogen alpha chain at '432-Lys-|-Leu-433' bond, but does not cleave beta or gamma chains. Does not cleave fibrin. Hydrolyzes only partially bovine prothrombin at '200-Ser-|-Gly-201' bond, factor X (FX) heavy chain, and very slowly, FX light chain and plasminogen in vitro, without activating any of them. Has no effect in plasma thrombin generation. Does not inhibit platelet aggregation induced by collagen in vitro. May have a delayed pathological action as an anticoagulant in envenomed patients after they received serotherapy as it is not recognized by the venom antiserum. {ECO:0000269|PubMed:25549999}.
null
Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily
null
null
null
A0A0B5A051
reviewed
PT1L_HUMLU
2-acylphloroglucinol 4-prenyltransferase (EC 2.5.1.136) (Aromatic prenyltransferase PT1L) (Humulus lupulus prenyltransferase-1-like) (HlPT1L)
PT1L
Humulus lupulus (European hop)
null
PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30468448}.
FUNCTION: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the first prenylation step in the beta-bitter acid pathway (PubMed:25564559). Uses dimethylallyl diphosphate (DMAPP) as the prenyl donor (PubMed:25564559). {ECO:0000269|PubMed:25564559, ECO:0000305|PubMed:30468448}.
null
UbiA prenyltransferase family
PT1L
null
null
A0A0B5A886
reviewed
GP_SFTSV
Envelopment polyprotein (M polyprotein) [Cleaved into: Glycoprotein N (Gn) (Glycoprotein G1); Glycoprotein C (Gc) (Glycoprotein G2)]
GP
SFTS phlebovirus (isolate SFTSV/Human/China/HB29/2010) (Severe fever with thrombocytopenia virus)
null
null
FUNCTION: [Glycoprotein N]: Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (By similarity). Plays a role in the packaging of ribonucleoproteins and polymerase during virus assembly (PubMed:29467349). {ECO:0000250|UniProtKB:P09613, ECO:0000250|UniProtKB:P21401, ECO:0000250|UniProtKB:R4V2Q5, ECO:0000269|PubMed:29467349}.; FUNCTION: [Glycoprotein C]: Structural component of the virion that interacts with glycoprotein N (By similarity). Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (By similarity). {ECO:0000250|UniProtKB:P09613, ECO:0000250|UniProtKB:P21401, ECO:0000250|UniProtKB:R4V2Q5}.
DOMAIN: [Glycoprotein N]: Contains a Golgi retention signal on its C-terminus. The cytoplasmic tail specifically interacts with the ribonucleoproteins and is critical for genome packaging. {ECO:0000250|UniProtKB:P09613}.
Phlebovirus envelope glycoprotein family
GP
null
null
A0A0B5A8P4
reviewed
INS3A_CONGE
Con-Ins G3 (Insulin 3) [Cleaved into: Con-Ins G3 B chain; Con-Ins G3 A chain]
null
Conus geographus (Geography cone) (Nubecula geographus)
null
null
FUNCTION: This venom insulin, from a fish-hunting cone snail, facilitates prey capture by rapidly inducing hypoglycemic shock (PubMed:30747102). It is one of the smallest known insulin found in nature and lacks the C-terminal segment of the B chain that, in human insulin, mediates engagement of the insulin receptor (INSR) and assembly of the hormone's hexameric storage form (By similarity). Despite lacking this segment, it both binds and activates human insulin receptor (long isoform (HIR-B)) with a high potency (EC(50)=242 nM) (PubMed:30747102). In vivo, intraperitoneal injection of this peptide into zebrafish lowers blood glucose with a lower potency than human insulin (PubMed:30747102). In addition, when applied to water, this peptide reduces overall locomotor activity of zebrafish larvae, observed as a significant decrease in the percentage of time spent swimming and movement frequency (By similarity). When tested on a mouse model of diabetes, this insulin also lowers blood glucose with a 10-fold lower potency than human insulin (By similarity). {ECO:0000250|UniProtKB:A0A0B5AC95, ECO:0000269|PubMed:30747102}.
null
Insulin family
null
null
null
A0A0B5AC19
reviewed
NSS_SFTSV
Non-structural protein NS-S (NSs)
NSS
SFTS phlebovirus (isolate SFTSV/Human/China/HB29/2010) (Severe fever with thrombocytopenia virus)
O95786; Q14258
null
FUNCTION: Sequesters host STAT2 into viral inclusion bodies (Probable) (PubMed:29886262). Impairs IFN-stimulated phosphorylation and nuclear translocation of host STAT2, thereby suppressing type-I IFN antiviral signaling (Probable) (PubMed:28680969, PubMed:29886262). Sequesters host TRIM25, RIGI, TBK1/IKK complex components (TBK1, IKBKE/IKKE, and IRF3) and IRF7 into viral inclusion bodies, thereby inhibiting the IFN responses (Probable). Inhibits TRIM25-mediated ubiquitination of the RIGI (PubMed:32471869). The sequestration of IKBKE/IKKE, and IRF3 occurs via the interaction with TBK1 (PubMed:24335286). Sequestration and inhibition of host TBK1 probably participates to the cytokine storm induced by the virus (PubMed:33288641). Also inhibits the phosphorylation of host TBK1 (PubMed:28680969). Interacts with host TNIP2 and promotes TPL2-TNIP2-p105 complex formation leading to IL-10 induction (PubMed:30617349). By interacting with CDK1, induces host cell arrest at the G2/M transition to promote viral replication (PubMed:31852787). Requested for the formation of the viral cytoplasmic inclusion bodies (PubMed:24335286, PubMed:27226560). {ECO:0000269|PubMed:24335286, ECO:0000269|PubMed:27226560, ECO:0000269|PubMed:28680969, ECO:0000269|PubMed:29886262, ECO:0000269|PubMed:30617349, ECO:0000269|PubMed:31852787, ECO:0000269|PubMed:32471869, ECO:0000269|PubMed:33288641, ECO:0000305|PubMed:24478431, ECO:0000305|PubMed:24706939, ECO:0000305|PubMed:25631085, ECO:0000305|PubMed:30021900, ECO:0000305|PubMed:30598516}.
null
Bandavirus NS-S protein family
NSS
null
null
A0A0B5AC95
reviewed
INS1A_CONGE
Con-Ins G1a (Insulin 1) [Cleaved into: Con-Ins G1 B chain; Con-Ins G1a A chain]
null
Conus geographus (Geography cone) (Nubecula geographus)
null
null
FUNCTION: This venom insulin, from a fish-hunting cone snail, facilitates prey capture by rapidly inducing hypoglycemic shock (PubMed:25605914, PubMed:27617429). It is one of the smallest known insulin found in nature and lacks the C-terminal segment of the B chain that, in human insulin, mediates engagement of the insulin receptor (INSR) and assembly of the hormone's hexameric storage form (PubMed:27617429). Despite lacking this segment, it both binds and activates human insulin receptor (long isoform (HIR-B)) with a high potency (EC(50)=16.28 nM) (PubMed:27617429, PubMed:30747102). In vivo, intraperitoneal injection of this peptide into zebrafish lowers blood glucose with the same potency than human insulin (PubMed:25605914, PubMed:30747102). In addition, when applied to water, this peptide reduces overall locomotor activity of zebrafish larvae, observed as a significant decrease in the percentage of time spent swimming and movement frequency (PubMed:25605914). When tested on a mouse model of diabetes, this insulin also lowers blood glucose with a 10-fold lower potency than human insulin (PubMed:30747102). {ECO:0000269|PubMed:25605914, ECO:0000269|PubMed:27617429, ECO:0000269|PubMed:30747102}.
null
Insulin family
null
null
null
A0A0B5KYT4
reviewed
MPDE2_PENBR
Cytochrome P450 monooxygenase mpaDE' (EC 1.-.-.-) (Mycophenolic acid biosynthesis cluster protein DE')
mpaDE'
Penicillium brevicompactum
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31209052}.
FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (PubMed:31209052). MpaDE' is an endoplasmic reticulum-bound enzyme that catalyzes the conversion of 5-methylorsellinic acid (5MOA) into the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) (PubMed:31209052). MpaDE' first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB), and then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP (PubMed:31209052). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable) (PubMed:31209052). {ECO:0000269|PubMed:31209052, ECO:0000305|PubMed:31209052}.
null
Cytochrome P450 family
mpaDE'
null
null
A0A0B5LB55
reviewed
MPAH2_PENBR
Type I acyl-CoA thioesterase mpaH' (EC 3.1.1.-) (Mycophenolic acid biosynthesis cluster protein H')
mpaH'
Penicillium brevicompactum
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134}.
FUNCTION: Type I acyl-CoA thioesterase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (PubMed:31209052, PubMed:33843134). MpaH' acts as a peroxisomal acyl-CoA hydrolase that converts MPA-CoA into the final product MPA (PubMed:31209052, PubMed:33843134). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable) (PubMed:31209052). {ECO:0000269|PubMed:31209052, ECO:0000269|PubMed:33843134, ECO:0000305|PubMed:31209052}.
null
AB hydrolase superfamily, MpaH hydrolase family
mpaH'
null
null
A0A0B6CGH9
reviewed
F7ODM_OCIBA
Oxoglutarate-dependent flavonoid 7-O-demethylase 1 (ObF7ODM1) (2-oxoglutarate-dependent dioxygenase 1) (ObDIOX1) (8-hydroxysalvigenin 7-O-demethylase) (EC 1.14.13.-) (Gardenin B 7-O-demethylase) (EC 1.14.13.-)
F7ODM1 DIOX1
Ocimum basilicum (Sweet basil)
null
PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}.
FUNCTION: Oxoglutarate-dependent dioxygenase (2-ODD) acting as a flavonoid 7-O-demethylase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects (PubMed:25378691). Catalyzes the 7-O-demethylation of methoxylated flavones; mediates the conversion of 8-hydroxysalvigenin (8-OH-SALV) to pilosin (PIL) and of gardenin B (GARD B) to nevadensin (NEV) (PubMed:25378691). {ECO:0000269|PubMed:25378691}.
null
Iron/ascorbate-dependent oxidoreductase family
F7ODM1
null
DIOX1
A0A0B6VIJ5
reviewed
F6CGT_GENTR
Isovitexin/isoorientin synthase UF6CGT1 (EC 2.4.1.-) (UDP-glycosyltransferase UF6CGT1) (Gt6CGT) (GtUF6CGT1)
UF6CGT1 6CGT
Gentiana triflora (Clustered gentian)
null
PATHWAY: Flavonoid metabolism. {ECO:0000269|PubMed:25479084, ECO:0000269|PubMed:31399929}.
FUNCTION: UDP-glucose-dependent glucosyltransferase involved in C-glycosylflavone biosynthesis (PubMed:25479084, PubMed:31399929). Has a strict stereo selectivity and shows a preference for apigenin and luteolin as substrates, but could not recognize flavonols, anthocyanins and xanthones as glucosyl acceptors (PubMed:25479084, PubMed:31399929). No activity with orientin (luteolin 8-C-glucoside) and luteolin 4'-glucoside (PubMed:25479084). Can use UDP-galactose instead of UDP-glucose as a sugar donor, but not UDP-glucuronic acid (PubMed:25479084). {ECO:0000269|PubMed:25479084, ECO:0000269|PubMed:31399929}.
null
UDP-glycosyltransferase family
UF6CGT1
null
6CGT
A0A0B7P3V8
reviewed
YP41B_YEAST
Transposon Ty4-P Gag-Pol polyprotein (TY4A-TY4B) (Transposon Ty4 TYA-TYB polyprotein) [Includes: Capsid protein (CA); Ty4 protease (PR) (EC 3.4.23.-); Integrase (IN); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4)]
TY4B-P YPLCTy4-1 POL YPL060C-A
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
null
null
FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. {ECO:0000250}.; FUNCTION: The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP. {ECO:0000250}.; FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends. {ECO:0000250}.; FUNCTION: Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome. {ECO:0000250}.
DOMAIN: Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein. {ECO:0000250}.
null
TY4B-P
null
YPLCTy4-1 POL
A0A0B7P9G0
reviewed
UEX_DROME
Unextended protein (Putative metal transporter uex)
uex 41Ad GroupIII l(2)41Ad CG42595
Drosophila melanogaster (Fruit fly)
O61722
null
FUNCTION: Probable metal transporter (By similarity). Acts downstream of PRL-1 and protects the nervous system against olfactory carbon dioxide stimulation (PubMed:31404830). {ECO:0000250|UniProtKB:Q3TWN3, ECO:0000269|PubMed:31404830}.
null
ACDP family
uex
CG42595
41Ad GroupIII l(2)41Ad
A0A0C3RR82
reviewed
PGMA1_PHLG1
Methyltransferase/ribosomally synthesized type II borosin cyclic peptide precursor pgiMA1 (Type II borosin cyclic peptide biosynthesis cluster protein MA1) [Cleaved into: N-methyltranferase pgiM1 (EC 2.1.1.-); Ribosomally synthesized type II borosin core peptide pgiA1-I; Ribosomally synthesized type II borosin core peptide pgiA1-II; Ribosomally synthesized type II borosin core peptide pgiA1-III; Ribosomally synthesized type II borosin core peptide pgiA1-IV; Ribosomally synthesized type II borosin core peptide pgiA1-V; Ribosomally synthesized type II borosin core peptide pgiA1-VI; Ribosomally synthesized type II borosin core peptide pgiA1-VII; Ribosomally synthesized type II borosin core peptide pgiA1-VIII; Ribosomally synthesized type II borosin core peptide pgiA1-IX; Ribosomally synthesized type II borosin core peptide pgiA1-X; Ribosomally synthesized type II borosin core peptide pgiA1-XI; Ribosomally synthesized type II borosin core peptide pgiA1-XII]
pgiMA1 PHLGIDRAFT_54959
Phlebiopsis gigantea (strain 11061_1 CR5-6) (White-rot fungus) (Peniophora gigantea)
null
PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:31117659}.
FUNCTION: Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities (PubMed:31117659). Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM) (PubMed:31117659). The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product (By similarity). {ECO:0000250|UniProtKB:A0A2R2JFI5, ECO:0000269|PubMed:31117659}.
DOMAIN: Within the homodimer, the clasp domain wraps around the adjacent subunit to position the core peptide into the other subunit's active site for iterative intermolecular methylation. {ECO:0000305|PubMed:31117659}.
Precorrin methyltransferase family
pgiMA1
PHLGIDRAFT_54959
null
A0A0C3VJP4
reviewed
SCP1_MEDTR
Serine carboxypeptidase 1 (EC 3.4.16.-)
SCP1 MTR_3g079630 MtrunA17_Chr3g0118891
Medicago truncatula (Barrel medic) (Medicago tribuloides)
null
null
FUNCTION: Carboxypeptidase that, together with KPI106, controls mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis). {ECO:0000269|PubMed:23662629}.
null
Peptidase S10 family
SCP1
MtrunA17_Chr3g0118891
null
A0A0C5B5G6
reviewed
MOTSC_HUMAN
Mitochondrial-derived peptide MOTS-c (Mitochondrial open reading frame of the 12S rRNA-c)
MT-RNR1
Homo sapiens (Human)
null
null
FUNCTION: Regulates insulin sensitivity and metabolic homeostasis (PubMed:25738459, PubMed:33468709). Inhibits the folate cycle, thereby reducing de novo purine biosynthesis which leads to the accumulation of the de novo purine synthesis intermediate 5-aminoimidazole-4-carboxamide (AICAR) and the activation of the metabolic regulator 5'-AMP-activated protein kinase (AMPK) (PubMed:25738459). Protects against age-dependent and diet-induced insulin resistance as well as diet-induced obesity (PubMed:25738459). In response to metabolic stress, translocates to the nucleus where it binds to antioxidant response elements (ARE) present in the promoter regions of a number of genes and plays a role in regulating nuclear gene expression in an NFE2L2-dependent manner and increasing cellular resistance to metabolic stress (PubMed:29983246). Increases mitochondrial respiration and levels of CPT1A and cytokines IL1B, IL6, IL8, IL10 and TNF in senescent cells (PubMed:29886458). Increases activity of the serine/threonine protein kinase complex mTORC2 and reduces activity of the PTEN phosphatase, thus promoting phosphorylation of AKT (PubMed:33554779). This promotes AKT-mediated phosphorylation of transcription factor FOXO1 which reduces FOXO1 activity, leading to reduced levels of MSTN and promotion of skeletal muscle growth (PubMed:33554779). Promotes osteogenic differentiation of bone marrow mesenchymal stem cells via the TGFB/SMAD pathway (PubMed:30468456). Promotes osteoblast proliferation and osteoblast synthesis of type I collagens COL1A1 and COL1A2 via the TGFB/SMAD pathway (PubMed:31081069). {ECO:0000269|PubMed:25738459, ECO:0000269|PubMed:29886458, ECO:0000269|PubMed:29983246, ECO:0000269|PubMed:30468456, ECO:0000269|PubMed:31081069, ECO:0000269|PubMed:33468709, ECO:0000269|PubMed:33554779}.
null
null
MT-RNR1
null
null
A0A0C5CJR8
reviewed
APRA_PSEMA
Metallopeptidase AprA (EC 3.4.24.-) (Heat-resistant peptidase)
aprA
Pseudomonas marginalis (Pseudomonas panacis)
null
null
FUNCTION: Peptidase able to cleave azocasein and the milk substrates beta-casein and Na-caseinate. Can withstand UHT processing of milk, and is able to spoil UHT milk over the storage period. {ECO:0000269|Ref.1}.
null
Peptidase M10B family
aprA
null
null
A0A0C5PHQ7
reviewed
ELOV5_TACFU
Very long chain fatty acid elongase 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Elongation of very long chain fatty acids protein 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5)
ELOVL5 ELO
Tachysurus fulvidraco (Yellow catfish) (Pimelodus fulvidraco)
null
PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03205}.
FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate in the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators (By similarity). In conditions where the essential linoleic and alpha linoleic fatty acids are lacking it is also involved in the synthesis of Mead acid from oleic acid (By similarity). {ECO:0000250|UniProtKB:Q8BHI7, ECO:0000255|HAMAP-Rule:MF_03205}.
null
ELO family, ELOVL5 subfamily
ELOVL5
null
ELO
A0A0C5Q4Y6
reviewed
C76H2_ROSOF
Ferruginol synthase 1 (RoFS1) (EC 1.14.14.175) (11-oxomiltiradiene synthase) (EC 1.14.14.-) (Cytochrome P450 76AH22) (Ferruginol monooxygenase) (11-hydroxyferruginol synthase) (EC 1.14.14.60) (Miltiradiene oxidase)
CYP76AH22 FS1 HFS
Rosmarinus officinalis (Rosemary) (Salvia rosmarinus)
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30468448}.
FUNCTION: Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of abietatriene to produce ferruginol (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol (PubMed:27703160). Ferruginol and 11-hydroxyferruginol are intermediates in the biosynthesis of carnosate, a potent antioxidant (PubMed:26020634, PubMed:27703160). May also convert miltiradiene into 11-oxomiltiradiene (By similarity). {ECO:0000250|UniProtKB:A0A0S1TP26, ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}.
null
Cytochrome P450 family
CYP76AH22
null
FS1 HFS
A0A0C5QRZ2
reviewed
C76H2_SALFT
Ferruginol synthase (SfFS) (EC 1.14.14.175) (11-oxomiltiradiene synthase) (EC 1.14.14.-) (Cytochrome P450 76AH24) (Ferruginol monooxygenase) (11-hydroxyferruginol synthase) (EC 1.14.14.60) (Miltiradiene oxidase)
CYP76AH24 FS HFS
Salvia fruticosa (Greek sage)
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30468448}.
FUNCTION: Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of abietatriene to produce ferruginol (PubMed:26020634, PubMed:27703160). Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol (PubMed:27703160). Ferruginol and 11-hydroxyferruginol are intermediates in the biosynthesis of carnosate, a potent antioxidant (PubMed:26020634, PubMed:27703160). May also convert miltiradiene into 11-oxomiltiradiene (By similarity). {ECO:0000250|UniProtKB:A0A0S1TP26, ECO:0000269|PubMed:26020634, ECO:0000269|PubMed:27703160}.
null
Cytochrome P450 family
CYP76AH24
null
FS HFS
A0A0C5XL88
reviewed
PART_SPHYB
Prs ADP-ribosylating toxin (EC 2.4.2.-) (Mono-ADP-ribosyltransferase) (mART)
parT yblI TZ53_17660
Sphingobium sp. (strain YBL2)
null
null
FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Expression in E.coli inhibits cell growth; bacteriostasis is neutralized by expression of cognate antitoxin ParS. ADP-ribosylates E.coli ribose-phosphate pyrophosphokinase (RPPK, prs) using NAD(+) in vitro; ADP-ribosylates RPPK on 'Lys-182' and 'Ser-202'. Cannot use NADP(+). Also auto-ADP-ribosylates in vitro; in the presence of RPPK auto-ADP-ribosylation decreases. {ECO:0000269|PubMed:30598453}.
DOMAIN: Forms salt bridges between the 2 toxin molecules mediated by Glu-127 Glu-128 on one subunit and Arg-46 Arg-149 on the other. {ECO:0000269|PubMed:30598453}.
MbcT/ParT/Res family
parT
TZ53_17660
yblI
A0A0C6DRW4
reviewed
DSZC1_RHOER
Dibenzothiophene monooxygenase (DBT monooxygenase) (DBT-MO) (EC 1.14.14.21)
dszC
Rhodococcus erythropolis (Arthrobacter picolinophilus)
null
PATHWAY: Sulfur metabolism; dibenzothiophene degradation. {ECO:0000305|PubMed:25627402}.
FUNCTION: Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner (PubMed:11229908, Ref.2). Also acts on thioxanthen-9-one and 4,6-dimethyl DBT and 2,8-dimethyl DBT (Ref.2). {ECO:0000269|PubMed:11229908, ECO:0000269|Ref.2}.
DOMAIN: Has 3 domains, the helical N-terminus (residues 18-124), a beta-barrel central domain (125-233) and a helical C-terminus (234-417). The lid loop (residues 131-142) change conformation when FMN is bound and close the FMN-binding site. Other regions that probably contribute to FMN binding are residues 178-184 and 281-291. {ECO:0000269|PubMed:25627402}.
DszC flavin monooxygenase family
dszC
null
null

Dataset Card for UniProt Gene Lookup

Dataset Details

Dataset Description

This dataset is a lookup table of gene information curated from the reviewed entries of UniProtKB/Swiss-Prot. The dataset contains the protein-coding gene data, curated by expert biocurators to ensure high-quality and experimentally validated information. It is designed to assist researchers in mapping genes to corresponding protein sequences, functional annotations, and associated metadata.

  • Curated by: The UniProt Consortium (European Bioinformatics Institute (EBI), Georgetown University, University of Delaware, Swiss Institute of Bioinformatics (SIB)).
  • Language(s) (NLP): Not applicable (This dataset focuses on biological data).
  • License: Creative Commons Attribution 4.0 International (CC BY 4.0)【7†source】.

Dataset Sources

  • Repository: UniProtKB (Query: reviewed:true).
  • Paper: "UniProt: the Universal Protein Knowledgebase in 2023," Nucleic Acids Research, Vol. 51, D523–D531【7†source】.
  • Demo: Not available.

Uses

Direct Use

This dataset is suitable for biological research, particularly in bioinformatics, genomics, and proteomics. It can be used for gene annotation, protein function prediction, and understanding gene-protein relationships.

Out-of-Scope Use

This dataset may not be suitable for natural language processing tasks or non-biological fields. Misuse could include applications that do not consider the scientific validity or limitations of the curated gene annotations.

Dataset Structure

The dataset is structured as a tab-separated values (TSV) file containing gene identifiers, protein sequences, functional annotations, and associated metadata.

Dataset Creation

Curation Rationale

This dataset was created to provide researchers with a high-quality resource for gene-to-protein mapping, emphasizing experimentally verified annotations. It helps streamline bioinformatics workflows by providing reliable data that reduces the need for extensive literature searches.

Source Data

Data Collection and Processing

The data was collected from UniProtKB/Swiss-Prot, the reviewed section of UniProt. The dataset is curated by expert biocurators who continuously update it based on new scientific literature and computational predictions.

Who are the source data producers?

The source data producers include the UniProt Consortium, which integrates biological knowledge from multiple external resources and community contributions.

Bias, Risks, and Limitations

This dataset may have limitations in terms of coverage for less-studied organisms or gene variants that have not been experimentally validated. Researchers should consider potential biases in gene annotations, especially for organisms with fewer studies.

Recommendations

Researchers are advised to cross-check the dataset with the latest scientific literature and use it as a supplementary tool rather than a definitive source for gene annotations.

Citation

Please cite the dataset using the following BibTeX:

@article{UniProt2023,
  author = {The UniProt Consortium},
  title = {UniProt: the Universal Protein Knowledgebase in 2023},
  journal = {Nucleic Acids Research},
  year = {2023},
  volume = {51},
  number = {D1},
  pages = {D523--D531},
  doi = {10.1093/nar/gkac1052},
  url = {https://www.uniprot.org/uniprotkb?query=reviewed:true}
}

Dataset Card Authors

  • Don Branson

Dataset Card Contact

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