wanglab/bioreason-pro-rl
Reinforcement Learning • 4B • Updated • 55 • 4
protein_id stringlengths 6 10 | protein_names stringlengths 2 1.26k | protein_function stringlengths 9 5.75k ⌀ | organism stringclasses 589
values | length float64 11 16k | subcellular_location stringlengths 7 6.16k ⌀ | sequence stringlengths 11 16k | go_ids listlengths 2 494 | go_bp listlengths 0 437 ⌀ | go_mf listlengths 0 59 ⌀ | go_cc listlengths 0 67 ⌀ | structure_path stringlengths 25 29 ⌀ | string_id stringlengths 10 27 ⌀ | interaction_partners listlengths 1 668 ⌀ | interpro_ids listlengths 1 20 ⌀ | interpro_location stringlengths 3 529 | ppi_formatted stringlengths 0 811 | interpro_formatted stringlengths 0 1.79k | go_pred stringlengths 369 15k |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Q13542 | Eukaryotic translation initiation factor 4E-binding protein 2 | Repressor of translation initiation involved in synaptic plasticity, learning and memory formation. Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. EIF4EBP2 is enriched in brain and acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation (By similarity). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (By similarity) | Homo sapiens (Human) | 120 | Cytoplasm. Nucleus | MSSSAGSGHQPSQSRAIPTRTVAISDAAQLPHDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGTLIEDSKVEVNNLNNLNNHDRKHAVGDDAQFEMDI | [
"GO:0005575",
"GO:0005622",
"GO:0005737",
"GO:0032838",
"GO:0035770",
"GO:0036464",
"GO:0042995",
"GO:0043005",
"GO:0043226",
"GO:0043228",
"GO:0043229",
"GO:0043232",
"GO:0071598",
"GO:0099080",
"GO:0099568",
"GO:0110165",
"GO:0120025",
"GO:0120111"
] | [] | [] | [
"GO:0005575",
"GO:0005622",
"GO:0005737",
"GO:0032838",
"GO:0035770",
"GO:0036464",
"GO:0042995",
"GO:0043005",
"GO:0043226",
"GO:0043228",
"GO:0043229",
"GO:0043232",
"GO:0071598",
"GO:0099080",
"GO:0099568",
"GO:0110165",
"GO:0120025",
"GO:0120111"
] | AF-Q13542-F1-model_v6.pdb | 9606.ENSP00000362314 | [
"Q96E95",
"Q8N102",
"Q9P2P3",
"O60516",
"Q6IBN3",
"Q7Z721",
"Q9Y4I3"
] | [
"IPR008606"
] | {"IPR008606": [7, 120]} | - Eukaryotic translation initiation factor 4E
- Regulatory-associated protein of mTOR
- Serine/threonine-protein kinase mTOR
- Eukaryotic translation initiation factor 4E-binding protein 1
- Eukaryotic translation initiation factor 4E-binding protein 3
- Ribosomal protein S6 kinase beta-1
- Eukaryotic translation initiation factor 4 gamma 1 | - IPR008606: Eukaryotic translation initiation factor 4E binding (family) [7-120] | Molecular Function (MF): GO:0003674 (molecular function), GO:0045182 (translation regulator activity), GO:0005488 (binding), GO:0030371 (translation repressor activity), GO:0005515 (protein binding), GO:0031369 (translation initiation factor binding), GO:0008190 (eukaryotic initiation factor 4E binding)
Biological Process (BP): GO:0008150 (biological process), GO:0065007 (biological regulation), GO:0048518 (positive regulation of biological process), GO:0050896 (response to stimulus), GO:0050789 (regulation of biological process), GO:0009987 (cellular process), GO:0023052 (signaling), GO:0048519 (negative regulation of biological process), GO:0019222 (regulation of metabolic process), GO:0022402 (cell cycle process), GO:0050794 (regulation of cellular process), GO:0007049 (cell cycle), GO:0051716 (cellular response to stimulus), GO:0048523 (negative regulation of cellular process), GO:0007154 (cell communication), GO:0007165 (signal transduction), GO:0009892 (negative regulation of metabolic process), GO:0048522 (positive regulation of cellular process), GO:0051726 (regulation of cell cycle), GO:0051172 (negative regulation of nitrogen compound metabolic process), GO:1903047 (mitotic cell cycle process), GO:0035556 (intracellular signal transduction), GO:0010605 (negative regulation of macromolecule metabolic process), GO:0044770 (cell cycle phase transition), GO:0009889 (regulation of biosynthetic process), GO:0051171 (regulation of nitrogen compound metabolic process), GO:0060255 (regulation of macromolecule metabolic process), GO:0031323 (regulation of cellular metabolic process), GO:0009890 (negative regulation of biosynthetic process), GO:0080090 (regulation of primary metabolic process), GO:0031324 (negative regulation of cellular metabolic process), GO:0000278 (mitotic cell cycle), GO:0045787 (positive regulation of cell cycle), GO:0044772 (mitotic cell cycle phase transition), GO:0007346 (regulation of mitotic cell cycle), GO:0034248 (regulation of amide metabolic process), GO:0045947 (negative regulation of translational initiation), GO:0010556 (regulation of macromolecule biosynthetic process), GO:0044843 (cell cycle G1/S phase transition), GO:0051246 (regulation of protein metabolic process), GO:0006446 (regulation of translational initiation), GO:0051248 (negative regulation of protein metabolic process), GO:0031326 (regulation of cellular biosynthetic process), GO:0010558 (negative regulation of macromolecule biosynthetic process), GO:0031327 (negative regulation of cellular biosynthetic process), GO:0045931 (positive regulation of mitotic cell cycle), GO:0031929 (TOR signaling), GO:0010629 (negative regulation of gene expression), GO:0010468 (regulation of gene expression), GO:0034249 (negative regulation of amide metabolic process), GO:0017148 (negative regulation of translation), GO:0000082 (G1/S transition of mitotic cell cycle), GO:2000112 (regulation of cellular macromolecule biosynthetic process), GO:0006417 (regulation of translation), GO:2000113 (negative regulation of cellular macromolecule biosynthetic process), GO:0010608 (post-transcriptional regulation of gene expression)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005737 (cytoplasm), GO:0005829 (cytosol), GO:0005622 (intracellular anatomical structure) |
P97288 | 5-hydroxytryptamine receptor 4 | G-protein coupled receptor for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone and a mitogen (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide- binding proteins (G proteins) and modulates the activity of downstream effectors (By similarity). HTR4 is coupled to G(s) G alpha proteins and mediates activation of adenylate cyclase activity (By similarity) | Mus musculus (Mouse) | 388 | Cell membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. Note=Interaction with SNX27 mediates recruitment to early endosomes, while interaction with NHERF1 and EZR might target the protein to specialized subcellular regions, such as microvilli | MDKLDANVSSNEGFRSVEKVVLLTFLAVVILMAILGNLLVMVAVCRDRQLRKIKTNYFIVSLAFADLLVSVLVMPFGAIELVQDIWAYGEMFCLVRTSLDVLLTTASIFHLCCISLDRYYAICCQPLVYRNKMTPLRIALMLGGCWVLPMFISFLPIMQGWNNIGIVDVIEKRKFSHNSNSTWCVFMVNKPYAITCSVVAFYIPFLLMVLAYYRIYVTAKEHAQQIQMLQRAGATSESRPQPADQHSTHRMRTETKAAKTLCVIMGCFCFCWAPFFVTNIVDPFIDYTVPEQVWTAFLWLGYINSGLNPFLYAFLNKSFRRAFLIILCCDDERYKRPPILGQTVPCSTTTINGSTHVLRDTVECGGQWESRCHLTATSPLVAAQPSDT | [
"GO:0001894",
"GO:0003008",
"GO:0006810",
"GO:0007154",
"GO:0007165",
"GO:0007186",
"GO:0007586",
"GO:0007589",
"GO:0008150",
"GO:0009987",
"GO:0010669",
"GO:0022600",
"GO:0023052",
"GO:0030277",
"GO:0032501",
"GO:0032941",
"GO:0042592",
"GO:0044087",
"GO:0046903",
"GO:0048871"... | [
"GO:0001894",
"GO:0003008",
"GO:0006810",
"GO:0007154",
"GO:0007165",
"GO:0007186",
"GO:0007586",
"GO:0007589",
"GO:0008150",
"GO:0009987",
"GO:0010669",
"GO:0022600",
"GO:0023052",
"GO:0030277",
"GO:0032501",
"GO:0032941",
"GO:0042592",
"GO:0044087",
"GO:0046903",
"GO:0048871"... | [] | [
"GO:0005575",
"GO:0005886",
"GO:0016020",
"GO:0030054",
"GO:0045202",
"GO:0071944",
"GO:0098794",
"GO:0098978",
"GO:0110165"
] | AF-P97288-F1-model_v6.pdb | 10090.ENSMUSP00000027560 | [
"Q61226",
"O70176",
"Q9R1C8",
"Q3UFE9",
"Q544U4",
"Q9D887",
"Q9Z1N8",
"Q8CGK7",
"Q5FW59",
"Q9QUN1",
"Q14A50"
] | [
"IPR017452",
"IPR001520",
"IPR000276"
] | {"IPR001520": [2, 359], "IPR000276": [21, 327], "IPR017452": [36, 312]} | - Guanine nucleotide-binding protein G(olf) subunit alpha
- VIP peptides
- VIP peptides
- Pro-opiomelanocortin
- 5-hydroxytryptamine receptor 6
- 5-hydroxytryptamine receptor 7
- Gastric inhibitory polypeptide
- Pro-glucagon
- Pituitary adenylate cyclase-activating polypeptide
- Natriuretic peptides A | - IPR017452: GPCR, rhodopsin-like, 7TM (domain) [36-312]
- IPR001520: 5-Hydroxytryptamine 4 receptor (family) [2-359]
- IPR000276: G protein-coupled receptor, rhodopsin-like (family) [21-327] | Molecular Function (MF): GO:0003674 (molecular function), GO:0060089 (molecular transducer activity), GO:0038023 (signaling receptor activity), GO:0004888 (transmembrane signaling receptor activity), GO:0099589 (serotonin receptor activity), GO:0004930 (G protein-coupled receptor activity), GO:0008227 (G protein-coupled amine receptor activity), GO:0004993 (G protein-coupled serotonin receptor activity)
Biological Process (BP): GO:0008150 (biological process), GO:0009987 (cellular process), GO:0023052 (signaling), GO:0065007 (biological regulation), GO:0050896 (response to stimulus), GO:0050789 (regulation of biological process), GO:0032501 (multicellular organismal process), GO:0051716 (cellular response to stimulus), GO:0007267 (cell-cell signaling), GO:0003008 (system process), GO:0007154 (cell communication), GO:0007165 (signal transduction), GO:0050794 (regulation of cellular process), GO:0050877 (nervous system process), GO:0007214 (gamma-aminobutyric acid signaling pathway), GO:0007186 (G protein-coupled receptor signaling pathway), GO:0050890 (cognition), GO:0007188 (adenylate cyclase-modulating G protein-coupled receptor signaling pathway), GO:0007189 (adenylate cyclase-activating G protein-coupled receptor signaling pathway)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0005737 (cytoplasm), GO:0071944 (cell periphery), GO:0016020 (membrane), GO:0005886 (plasma membrane) |
Q7ZWC3 | Oxidized purine nucleoside triphosphate hydrolase | Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool. Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy- dATP) into 2-oxo-dAMP. Also has a significant hydrolase activity toward 2-oxo-ATP, 8-oxo-dGTP and 8-oxo-dATP. Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A. Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA. Through this antimutagenic activity protects cells from oxidative stress | Danio rerio (Zebrafish) (Brachydanio rerio) | 156 | Cytoplasm, cytosol. Mitochondrion matrix. Nucleus | MFTSKLLTLVLVVQPGRVLLGMKKRGFGAGKWNGFGGKVQTGETIEQAARRELLEESGLTVDTLHKIGNIKFEFIGETELMDVHIFRADNYEGEPAESDEMRPQWFDIDKIPFSQMWADDILWFPLMLQKKRFLGYFKFQGHDVIVEHKLDEVEDL | [
"GO:0006139",
"GO:0006163",
"GO:0006753",
"GO:0006793",
"GO:0006796",
"GO:0008150",
"GO:0008152",
"GO:0009117",
"GO:0009151",
"GO:0009262",
"GO:0009394",
"GO:0009987",
"GO:0019637",
"GO:0044238",
"GO:0044281",
"GO:0055086",
"GO:0072521",
"GO:1901135"
] | [
"GO:0006139",
"GO:0006163",
"GO:0006753",
"GO:0006793",
"GO:0006796",
"GO:0008150",
"GO:0008152",
"GO:0009117",
"GO:0009151",
"GO:0009262",
"GO:0009394",
"GO:0009987",
"GO:0019637",
"GO:0044238",
"GO:0044281",
"GO:0055086",
"GO:0072521",
"GO:1901135"
] | [] | [] | AF-Q7ZWC3-F1-model_v6.pdb | 7955.ENSDARP00000040752 | [
"Q6IQ66",
"E7F6K6",
"Q568Q0",
"Q1LXZ5",
"A0A2R8RL21",
"B0R135",
"Q6DG97",
"Q4V8V2",
"A0A0R4ISD4",
"F1QQK5"
] | [
"IPR020084",
"IPR003563",
"IPR000086",
"IPR020476",
"IPR015797"
] | {"IPR015797": [1, 147], "IPR003563": [4, 154], "IPR000086": [3, 129], "IPR020476": [32, 61], "IPR020084": [37, 58]} | - 8-oxo-dGDP phosphatase NUDT18
- Nucleotide triphosphate diphosphatase NUDT15
- ADP-sugar pyrophosphatase
- m7GpppN-mRNA hydrolase NUDT17
- Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
- Uridine diphosphate glucose pyrophosphatase NUDT14
- Nudix (nucleoside diphosphate-linked moiety X)-type motif 22
- N-glycosylase/DNA lyase | - IPR020084: NUDIX hydrolase, conserved site (conserved_site) [37-58]
- IPR003563: Oxidized purine nucleoside triphosphate (family) [4-154]
- IPR000086: NUDIX hydrolase domain (domain) [3-129]
- IPR020476: NUDIX hydrolase (domain) [32-61]
- IPR015797: NUDIX hydrolase-like domain superfamily (homologous_superfamily) [1-147] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016787 (hydrolase activity), GO:0016817 (hydrolase activity, acting on acid anhydrides), GO:0016818 (hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides)
Biological Process (BP): GO:0008150 (biological process), GO:0032502 (developmental process), GO:0050896 (response to stimulus), GO:0032501 (multicellular organismal process), GO:0009628 (response to abiotic stimulus), GO:0048856 (anatomical structure development), GO:0007275 (multicellular organism development), GO:0009653 (anatomical structure morphogenesis), GO:0006950 (response to stress), GO:0048646 (anatomical structure formation involved in morphogenesis), GO:0009408 (response to heat), GO:0009266 (response to temperature stimulus), GO:0001525 (angiogenesis), GO:0035295 (tube development), GO:0006979 (response to oxidative stress), GO:0001568 (blood vessel development), GO:0048731 (system development), GO:0035239 (tube morphogenesis), GO:0048514 (blood vessel morphogenesis), GO:0002040 (sprouting angiogenesis), GO:0001944 (vasculature development), GO:0072359 (circulatory system development)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005737 (cytoplasm), GO:0043229 (intracellular organelle), GO:0005739 (mitochondrion), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle) |
Q568L5 | Aldo-keto reductase family 1 member A1-B | Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids. Acts as an aldehyde-detoxification enzyme (By similarity). Also acts as an inhibitor of protein S-nitrosylation by mediating degradation of S- nitroso-coenzyme A (S-nitroso-CoA), a cofactor required to S- nitrosylate proteins (By similarity). Also acts as a S-nitroso- glutathione reductase by catalyzing the NADPH-dependent reduction of S- nitrosoglutathione (By similarity). Displays no reductase activity towards retinoids (By similarity) | Danio rerio (Zebrafish) (Brachydanio rerio) | 324 | Cytoplasm, cytosol. Apical cell membrane | MNDFAVLSTGRKMPLLGLGTWKSEPGLVKQAVIWALESGYRHIDCAPIYANEPEIGEAFQETMGPDKGIRREDVFVTSKLWNTKHHPDDVEPSLLKTLKDLKLEYLDLYLIHWPYAFQRGDTPFPRKEDGTLLYDDIDYKLTWAAMEKLVGKGLVRAIGLSNFNSRQIDDILSVASIKPTVLQVESHPYLAQVELLSHCRDRGLVMTAYSPLGSPDRAWKHPDEPVLLEEPAIAALAKKYNKTPAQIIIRWQTQRGVVTIPKSITQSRIKENIQVFDFTLESEEMSQVTALHRGWRYIVPTITVDGKSVPRDAGHPHYPFNDPY | [
"GO:0006109",
"GO:0006111",
"GO:0008150",
"GO:0009889",
"GO:0010906",
"GO:0019222",
"GO:0033500",
"GO:0042592",
"GO:0042593",
"GO:0043255",
"GO:0048878",
"GO:0050789",
"GO:0050794",
"GO:0062012",
"GO:0065007",
"GO:0080090",
"GO:0003674",
"GO:0003824",
"GO:0008106",
"GO:0016491"... | [
"GO:0006109",
"GO:0006111",
"GO:0008150",
"GO:0009889",
"GO:0010906",
"GO:0019222",
"GO:0033500",
"GO:0042592",
"GO:0042593",
"GO:0043255",
"GO:0048878",
"GO:0050789",
"GO:0050794",
"GO:0062012",
"GO:0065007",
"GO:0080090"
] | [
"GO:0003674",
"GO:0003824",
"GO:0008106",
"GO:0016491",
"GO:0016614",
"GO:0016616",
"GO:0018455"
] | [] | AF-Q568L5-F1-model_v6.pdb | 7955.ENSDARP00000119785 | [
"Q90ZZ8",
"B8A4B0",
"Q6P696",
"F6NZ60",
"A2BGR9",
"B0S7W5",
"Q7ZVB2",
"F8W5X0",
"B0UYA3",
"F8W5X3",
"Q6AZW2",
"Q90ZZ7",
"E9QH31",
"F1QGS9",
"F1QR17",
"Q4V8T0",
"F2Z4R7",
"F1QGP1",
"Q7ZWC2",
"X1WBM4",
"A0A2R8RIE8",
"Q802W2"
] | [
"IPR044481",
"IPR023210",
"IPR018170",
"IPR020471",
"IPR036812"
] | {"IPR036812": [2, 324], "IPR020471": [5, 307], "IPR044481": [7, 311], "IPR023210": [16, 291], "IPR018170": [39, 275]} | - Aldehyde dehydrogenase
- Beta-glucuronidase
- Glucuronokinase with putative uridyl pyrophosphorylase
- Klotho
- Monoglyceride lipase
- Aldo-keto reductase family 1 member A1-A
- Inositol oxygenase
- Aldehyde dehydrogenase
- Lactoylglutathione lyase
- Aldehyde dehydrogenase | - IPR044481: Aldo-keto reductase family 1 member A1 (family) [7-311]
- IPR023210: NADP-dependent oxidoreductase domain (domain) [16-291]
- IPR018170: Aldo/keto reductase, conserved site (conserved_site) [39-275]
- IPR020471: Aldo-keto reductase (family) [5-307]
- IPR036812: NAD(P)-dependent oxidoreductase domain superfamily (homologous_superfamily) [2-324] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016491 (oxidoreductase activity), GO:0016614 (oxidoreductase activity, acting on CH-OH group of donors), GO:0016616 (oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0098754 (detoxification), GO:0050896 (response to stimulus), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0042221 (response to chemical), GO:0044281 (small molecule metabolic process), GO:0051716 (cellular response to stimulus), GO:0071704 (organic substance metabolic process), GO:1990748 (cellular detoxification), GO:0009056 (catabolic process), GO:0044238 (primary metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0044282 (small molecule catabolic process), GO:0044283 (small molecule biosynthetic process), GO:0046483 (heterocycle metabolic process), GO:0070887 (cellular response to chemical stimulus), GO:0006082 (organic acid metabolic process), GO:0044248 (cellular catabolic process), GO:0019637 (organophosphate metabolic process), GO:0009636 (response to toxic substance), GO:0110095 (cellular detoxification of aldehyde), GO:0044249 (cellular biosynthetic process), GO:0005996 (monosaccharide metabolic process), GO:1901700 (response to oxygen-containing compound), GO:0005975 (carbohydrate metabolic process), GO:0006766 (vitamin metabolic process), GO:1901575 (organic substance catabolic process), GO:0010033 (response to organic substance), GO:1901135 (carbohydrate derivative metabolic process), GO:0006081 (cellular aldehyde metabolic process), GO:0006793 (phosphorus metabolic process), GO:1901334 (lactone metabolic process), GO:0016054 (organic acid catabolic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0097237 (cellular response to toxic substance), GO:0046185 (aldehyde catabolic process), GO:0006767 (water-soluble vitamin metabolic process), GO:0009110 (vitamin biosynthetic process), GO:0046364 (monosaccharide biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:0016053 (organic acid biosynthetic process), GO:0018130 (heterocycle biosynthetic process), GO:0110096 (cellular response to aldehyde), GO:0016051 (carbohydrate biosynthetic process), GO:0090407 (organophosphate biosynthetic process), GO:0006796 (phosphate-containing compound metabolic process), GO:0019852 (L-ascorbic acid metabolic process), GO:1901137 (carbohydrate derivative biosynthetic process), GO:1901701 (cellular response to oxygen-containing compound), GO:0019752 (carboxylic acid metabolic process), GO:0042364 (water-soluble vitamin biosynthetic process), GO:1901336 (lactone biosynthetic process), GO:0046395 (carboxylic acid catabolic process), GO:0046394 (carboxylic acid biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process), GO:0072329 (monocarboxylic acid catabolic process), GO:0006063 (uronic acid metabolic process), GO:0019585 (glucuronate metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005737 (cytoplasm), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle), GO:0005634 (nucleus) |
P31037 | Protein A49R | Plays a role in the inhibition of host NF-kappa-B activation. Interacts with host BTRC and thereby diminishes ubiquitination of NF- kappa-B inhibitor alpha/NFKBIA. This stabilizes NFKBIA and its interaction with NF-kappaB, so retaining p65/RELA in the cytoplasm and preventing NF-kappa-B-dependent gene expression | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain | 162 | Host cytoplasm. Host nucleus | MDEAYYSGNLESVLGYVSDMHTELASISQLVIAKIETIDNDILNKDIVNFIMCRSNLDNPFISFLDTVYTIIDQENYQTELINSLDDNEIIDCIVNKFMSFYKDNLENIVDAIITLKYIMNNPDFKTTYAEVLGSRIADIDIKQVIRENILQLSNDIRERYL | [
"GO:0007154",
"GO:0007165",
"GO:0008150",
"GO:0009987",
"GO:0023052",
"GO:0035556",
"GO:0035821",
"GO:0038061",
"GO:0044003",
"GO:0044068",
"GO:0044403",
"GO:0044419",
"GO:0050789",
"GO:0050794",
"GO:0050896",
"GO:0051701",
"GO:0051716",
"GO:0052027",
"GO:0052029",
"GO:0065007"... | [
"GO:0007154",
"GO:0007165",
"GO:0008150",
"GO:0009987",
"GO:0023052",
"GO:0035556",
"GO:0035821",
"GO:0038061",
"GO:0044003",
"GO:0044068",
"GO:0044403",
"GO:0044419",
"GO:0050789",
"GO:0050794",
"GO:0050896",
"GO:0051701",
"GO:0051716",
"GO:0052027",
"GO:0052029",
"GO:0065007"... | [
"GO:0003674",
"GO:0140311",
"GO:0140313"
] | [
"GO:0005575",
"GO:0018995",
"GO:0030430",
"GO:0033643",
"GO:0033646",
"GO:0043656",
"GO:0044217",
"GO:0110165"
] | null | null | null | [
"IPR009473"
] | {"IPR009473": [1, 162]} | - IPR009473: Orthopoxvirus A49 (family) [1-162] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0050896 (response to stimulus), GO:0016032 (viral process), GO:0044419 (biological process involved in interspecies interaction between organisms), GO:0009605 (response to external stimulus), GO:0035821 (modulation of process of another organism), GO:0044068 (modulation by symbiont of host cellular process), GO:0019048 (modulation by virus of host process), GO:0044403 (biological process involved in symbiotic interaction), GO:0009607 (response to biotic stimulus), GO:0051707 (response to other organism), GO:0051701 (biological process involved in interaction with host), GO:0075136 (response to host), GO:0043207 (response to external biotic stimulus), GO:0052173 (response to defenses of other organism), GO:0019054 (modulation by virus of host cellular process), GO:0044003 (modulation by symbiont of host process), GO:0052200 (response to host defenses), GO:0019049 (mitigation of host antiviral defense response), GO:0030682 (mitigation of host defenses by symbiont)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0018995 (host cellular component), GO:0033643 (host cell part), GO:0043657 (host cell), GO:0033646 (host intracellular part), GO:0043656 (host intracellular region), GO:0033647 (host intracellular organelle), GO:0030430 (host cell cytoplasm), GO:0033648 (host intracellular membrane-bounded organelle), GO:0042025 (host cell nucleus) | |
Q01220 | Protein A52 | Bcl-2-like protein which targets host toll-like receptor signaling complexes to suppress innate immune response. Interacts with host TRAF6 to activate p38 and subsequently induce the expression of several cytokines such as IL-10. Also associates with host IRAK2 to inhibit NF-kappa-B signaling | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain | 190 | null | MDIKIDISISGDKFTVTTRRENEERKKYLPLQKEKTTDVIKPDYLEYDDLLDRDEMFTILEEYFMYRGLLGLRIKYGRLFNEIKKFDNDAEEQFGTIEELKQKLRLNSEEGADNFIDYIKVQKQDIVKLTVYDCISMIGLCACVVDVWRNEKLFSRWKYCLRAIKLFINDHMLDKIKSILQNRLVYVEMS | [
"GO:0007154",
"GO:0007165",
"GO:0007249",
"GO:0008150",
"GO:0009987",
"GO:0023052",
"GO:0035556",
"GO:0035821",
"GO:0038061",
"GO:0044003",
"GO:0044068",
"GO:0044403",
"GO:0044419",
"GO:0050789",
"GO:0050794",
"GO:0050896",
"GO:0051701",
"GO:0051716",
"GO:0052027",
"GO:0052029"... | [
"GO:0007154",
"GO:0007165",
"GO:0007249",
"GO:0008150",
"GO:0009987",
"GO:0023052",
"GO:0035556",
"GO:0035821",
"GO:0038061",
"GO:0044003",
"GO:0044068",
"GO:0044403",
"GO:0044419",
"GO:0050789",
"GO:0050794",
"GO:0050896",
"GO:0051701",
"GO:0051716",
"GO:0052027",
"GO:0052029"... | [] | [
"GO:0005575",
"GO:0018995",
"GO:0030430",
"GO:0033643",
"GO:0033646",
"GO:0043656",
"GO:0044217",
"GO:0110165"
] | null | null | null | [
"IPR043018",
"IPR022819"
] | {"IPR043018": [36, 190], "IPR022819": [20, 174]} | - IPR043018: Poxvirus domain superfamily (homologous_superfamily) [36-190]
- IPR022819: Poxvirus Bcl-2-like (family) [20-174] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0006725 (cellular aromatic compound metabolic process), GO:0034641 (cellular nitrogen compound metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:0006139 (nucleobase-containing compound metabolic process), GO:0043170 (macromolecule metabolic process), GO:0046483 (heterocycle metabolic process), GO:0090304 (nucleic acid metabolic process), GO:0010467 (gene expression), GO:0016070 (RNA metabolic process), GO:0006396 (RNA processing), GO:0034470 (ncRNA processing), GO:0034660 (ncRNA metabolic process), GO:0006399 (tRNA metabolic process), GO:0008033 (tRNA processing)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0018995 (host cellular component), GO:0033643 (host cell part), GO:0043657 (host cell), GO:0033644 (host cell membrane), GO:0033646 (host intracellular part), GO:0043656 (host intracellular region), GO:0033655 (host cell cytoplasm part), GO:0033647 (host intracellular organelle), GO:0020002 (host cell plasma membrane), GO:0030430 (host cell cytoplasm), GO:0033648 (host intracellular membrane-bounded organelle), GO:0044164 (host cell cytosol), GO:0042025 (host cell nucleus) | |
Q59RR0 | Cell wall transcription factor ACE2 | Transcription factor involved in the RAM (regulation of ACE2 transcription factor and polarized morphogenesis) signaling network that regulates polarized morphogenesis. Regulates expression of genes involved in cell separation such as CHT3, DSE1, and SCW11; or other cell wall genes such as ASH1, DSE4, PIR1, PRY2, and RME1. Required for regulation of morphogenesis, cell separation, adherence, biofilm formation, invasion, as well as virulence in a mouse model of infection | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) | 783 | Nucleus. Note=Localized in the nuclei of daughter cells | MHWKFSNFRKYHLSFHLNLFDLSLFFISFYCFPILYICFFNQVHSFRSTQPSLIMNKFDLFDDYSTKGSTIPLPNENFDQLFLSSEANDMEFLFNETLMGLQDLDVPSGYGIPQNTINNDFQHTPNKSKSHSRQYSGTAIFGFADHNKDLSINGVNNDLCKQSNKAINTQSVSPGELLKRSRGSQTPTPTSALPDTAQDILDFNFEEKPILLLEEDELEEEKHKQQQRMMTQSSPLKRVTTPSQSPFVQQPQTMKQRKPHKKTNEYIVANENPNSYKFPPSPSPTAKRQQYPPSSPIPYNPKSDSVGGNSYSAKYLQSLNKTQQIEYVDDIEPLLQEDNNNMKYIPIPVQEPMSYQKQKPVTPPLQSQNDSQQLEPLKTPQPQPKQQQQQQQPNNEQDKEFTANFNFNTFLPPPTPPNLINGSPDWNSSPEPHSPSPGRLQPPQQISPIHQNLGAMGNNINFYTPMYYELPVQAEQPQPQPQPHQQQHQQQQHQPELQNTYQQIKHIQQQQQMLQHQFHNQNNQLRQQHPNQFQNQNQNQNQNQTKTPYSQQSQFSPTHSNFNLSPAKQLNSNVGSMHLSPLKKQLPNTPTKQPPVTIEWSPVISPNSKQPLHKQIKESSPRRRIKKTSLLPPGELDNYWTGPDEDKIYTCTYKNCGKKFTRRYNVRSHIQTHLSDRPFGCQFCPKRFVRQHDLNRHVKGHIEARYSKCPCGKEFARLDALRKHQDRNICVGGNKNVISKPTKKKGTNNTQQQLLKTDTVVERIEKQLLQEDKSVTEEFLMLQ | [
"GO:0006355",
"GO:0006357",
"GO:0007155",
"GO:0008150",
"GO:0009889",
"GO:0009891",
"GO:0009893",
"GO:0009987",
"GO:0010468",
"GO:0010556",
"GO:0010557",
"GO:0010564",
"GO:0010570",
"GO:0010604",
"GO:0010810",
"GO:0010811",
"GO:0016043",
"GO:0019219",
"GO:0019222",
"GO:0030155"... | [
"GO:0006355",
"GO:0006357",
"GO:0007155",
"GO:0008150",
"GO:0009889",
"GO:0009891",
"GO:0009893",
"GO:0009987",
"GO:0010468",
"GO:0010556",
"GO:0010557",
"GO:0010564",
"GO:0010570",
"GO:0010604",
"GO:0010810",
"GO:0010811",
"GO:0016043",
"GO:0019219",
"GO:0019222",
"GO:0030155"... | [] | [
"GO:0005575",
"GO:0005622",
"GO:0005634",
"GO:0043226",
"GO:0043227",
"GO:0043229",
"GO:0043231",
"GO:0110165"
] | AF-Q59RR0-F1-model_v6.pdb | 237561.Q59RR0 | [
"Q5ACY4",
"Q59U34",
"Q5AP53",
"Q5ABC6"
] | [
"IPR013087",
"IPR036236"
] | {"IPR036236": [647, 701], "IPR013087": [649, 706]} | - Serine/threonine-protein kinase CBK1
- Cdh1p
- CBK1 kinase activator protein MOB2
- Biofilm and cell wall regulator 1 | - IPR013087: Zinc finger C2H2-type (domain) [649-706]
- IPR036236: Zinc finger C2H2 superfamily (homologous_superfamily) [647-701] | Molecular Function (MF): GO:0003674 (molecular function), GO:0140110 (transcription regulator activity), GO:0003700 (DNA-binding transcription factor activity), GO:0000981 (DNA-binding transcription factor activity, RNA polymerase II-specific)
Biological Process (BP): GO:0008150 (biological process), GO:0065007 (biological regulation), GO:0048518 (positive regulation of biological process), GO:0050789 (regulation of biological process), GO:0040007 (growth), GO:0009987 (cellular process), GO:0051703 (biological process involved in intraspecies interaction between organisms), GO:0019222 (regulation of metabolic process), GO:0044010 (single-species biofilm formation), GO:0098743 (cell aggregation), GO:0050794 (regulation of cellular process), GO:0048522 (positive regulation of cellular process), GO:1900190 (regulation of single-species biofilm formation), GO:0030448 (hyphal growth), GO:0098630 (aggregation of unicellular organisms), GO:0009889 (regulation of biosynthetic process), GO:0051171 (regulation of nitrogen compound metabolic process), GO:0030155 (regulation of cell adhesion), GO:0060255 (regulation of macromolecule metabolic process), GO:0031323 (regulation of cellular metabolic process), GO:0045785 (positive regulation of cell adhesion), GO:0090609 (single-species submerged biofilm formation), GO:0080090 (regulation of primary metabolic process), GO:0010811 (positive regulation of cell-substrate adhesion), GO:1900231 (regulation of single-species biofilm formation on inanimate substrate), GO:0010556 (regulation of macromolecule biosynthetic process), GO:0010810 (regulation of cell-substrate adhesion), GO:0031326 (regulation of cellular biosynthetic process), GO:0019219 (regulation of nucleobase-containing compound metabolic process), GO:0042710 (biofilm formation), GO:0051252 (regulation of RNA metabolic process), GO:0044011 (single-species biofilm formation on inanimate substrate), GO:0010468 (regulation of gene expression), GO:1900187 (regulation of cell adhesion involved in single-species biofilm formation), GO:0090605 (submerged biofilm formation), GO:2001141 (regulation of RNA biosynthetic process), GO:1900189 (positive regulation of cell adhesion involved in single-species biofilm formation), GO:0006355 (regulation of DNA-templated transcription), GO:0006357 (regulation of transcription by RNA polymerase II), GO:1903506 (regulation of nucleic acid-templated transcription)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005737 (cytoplasm), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle), GO:0005634 (nucleus) |
P83773 | Acetyl-CoA hydrolase | Presumably involved in regulating the intracellular acetyl- CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) | 524 | Cytoplasm | MSAILKQRVRYAPYLKKLRTGEQCIDLFKHGQYLGWSGFTGVGAPKVIPTTLVDHVEKNNLQGKLGFHLFVGASAGPEESRWAENNMILTRAPHQVGKPIAAAINDGRTQFFDKHLSMFPQDLTYGFYTKDKPNGSNLDYTIIEATAITEDGSIVPGPAVGASPEMISVSDKIIIEVNTKTPSFEGIHDIDMPVNPPFRQPYPHTSADFKIGKTAIPVDPEKVVAIVESTSGDKVPPNTPSDEQSRGIANHLIEFLEHEVKQGRLPANLHPLQSGIGNIANAVVEGLASSNFKNLTVWTEVLQDSFLDFFESGSLDYATATSIRLTNDGFKKFYDNWDTYSKKLCLRSQVVSNSPEIIRRLGVIAMNTPVEVDIYGHANSTNVMGSRMLNGLGGSADFLRNAKLSIMHTPSARPSKVDPTGLSCIVPMASHVDQTEHDLDVVVTEQGLADLRGLAPKARAKVIIDKCSHPDYKPQLQEYYDRSVFYATKKKTLHEPHILRDVFKMHLNFQENGTMKLDSWDQKF | [
"GO:0006082",
"GO:0006083",
"GO:0008150",
"GO:0008152",
"GO:0009268",
"GO:0009628",
"GO:0009987",
"GO:0010446",
"GO:0019752",
"GO:0032787",
"GO:0043436",
"GO:0044281",
"GO:0050896",
"GO:0051716",
"GO:0071214",
"GO:0071467",
"GO:0071469",
"GO:0104004",
"GO:0003674",
"GO:0003824"... | [
"GO:0006082",
"GO:0006083",
"GO:0008150",
"GO:0008152",
"GO:0009268",
"GO:0009628",
"GO:0009987",
"GO:0010446",
"GO:0019752",
"GO:0032787",
"GO:0043436",
"GO:0044281",
"GO:0050896",
"GO:0051716",
"GO:0071214",
"GO:0071467",
"GO:0071469",
"GO:0104004"
] | [
"GO:0003674",
"GO:0003824",
"GO:0003986",
"GO:0016289",
"GO:0016787",
"GO:0016788",
"GO:0016790",
"GO:0160215"
] | [
"GO:0005575",
"GO:0005622",
"GO:0005737",
"GO:0005739",
"GO:0005829",
"GO:0043226",
"GO:0043227",
"GO:0043229",
"GO:0043231",
"GO:0110165"
] | AF-P83773-F1-model_v6.pdb | 237561.P83773 | [
"Q5AH20",
"Q8NJN3",
"Q59TC4",
"A0A1D8PH52",
"A0A1D8PSH3",
"Q5AB86",
"Q5AGX8",
"A0A1D8PRR7",
"Q9P8Q2",
"A0A1D8PTB5",
"A0A1D8PM94",
"A0A1D8PSW6",
"A0A1D8PIF8",
"Q59XW4",
"A0A1D8PH13",
"Q59VG1",
"A0A1D8PC76",
"A0A1D8PGT5",
"Q5A8X6",
"A0A1D8PNQ8"
] | [
"IPR003702",
"IPR038460",
"IPR026888",
"IPR037171",
"IPR046433"
] | {"IPR037171": [6, 516], "IPR038460": [350, 496], "IPR046433": [2, 520], "IPR003702": [10, 228], "IPR026888": [329, 479]} | - Acetyl-coenzyme A synthetase 2
- Malate synthase
- Acetyl-coenzyme A synthetase
- Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial
- Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial
- Acetyl-CoA acetyltransferase
- Aldehyde dehydrogenase (NAD(P)(+))
- Acetyltransferase component of pyruvate dehydrogenase complex
- Acetyl-CoA carboxylase
- Aldehyde dehydrogenase domain-containing protein | - IPR003702: Acetyl-CoA hydrolase/transferase, N-terminal (domain) [10-228]
- IPR038460: Acetyl-CoA hydrolase/transferase, C-terminal domain superfamily (homologous_superfamily) [350-496]
- IPR026888: Acetyl-CoA hydrolase/transferase, C-terminal domain (domain) [329-479]
- IPR037171: NagB/RpiA transferase-like (homologous_superfamily) [6-516]
- IPR046433: Acetyl-CoA hydrolase/transferase (family) [2-520] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016740 (transferase activity), GO:0016787 (hydrolase activity), GO:0016788 (hydrolase activity, acting on ester bonds), GO:0016782 (transferase activity, transferring sulphur-containing groups), GO:0008410 (CoA-transferase activity), GO:0016790 (thiolester hydrolase activity), GO:0016289 (CoA hydrolase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044238 (primary metabolic process), GO:0044255 (cellular lipid metabolic process), GO:0006629 (lipid metabolic process), GO:0019541 (propionate metabolic process), GO:0006082 (organic acid metabolic process), GO:0006631 (fatty acid metabolic process), GO:0019679 (propionate metabolic process, methylcitrate cycle), GO:0043436 (oxoacid metabolic process), GO:0019752 (carboxylic acid metabolic process), GO:0046459 (short-chain fatty acid metabolic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0009986 (cell surface), GO:0071944 (cell periphery), GO:0030312 (external encapsulating structure), GO:0005618 (cell wall), GO:0009277 (fungal-type cell wall), GO:0030445 (yeast-form cell wall) |
Q4V9P6 | N6-Methyl-AMP deaminase | Catalyzes the hydrolysis of the free cytosolic methylated adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol monophosphate (IMP) and methylamine. Is required for the catabolism of cytosolic N6-mAMP, which is derived from the degradation of mRNA containing N6-methylated adenine (m6A) | Danio rerio (Zebrafish) (Brachydanio rerio) | 348 | null | MDTEADLFYRQLPKVELHAHLNGSVSFETMEKLIKRKPHLNIEHSMTAIRRGQRRTLDECFQVFKVIHQLVDSEEDILMVAKSVIQEFAADGVKYLELRSTPREVTETGLSKQRYIETVLEAIRQCKQEGVDIDVRFLVAVDRRHGPEVAMQTVKLAEDFLLSSDGTVVGLDLSGDPTVGHGKDLLAALQKAKNCGLKLALHLSEVPSQIDETELLLNLPPDRIGHGTFLHPDVGGSDSLVDKVCKQNIPIEICLTSNVKGQTVPSYDKHHFKYWYNRGHPCVLCTDDKGVFCTDLSQEYQLAASTFGLTKEAVWILSQQAIGYTFAPEPIKQRLEKTWAELKQQILQ | [
"GO:0001654",
"GO:0007275",
"GO:0007423",
"GO:0008150",
"GO:0032501",
"GO:0032502",
"GO:0043010",
"GO:0048513",
"GO:0048731",
"GO:0048856",
"GO:0048880",
"GO:0150063"
] | [
"GO:0001654",
"GO:0007275",
"GO:0007423",
"GO:0008150",
"GO:0032501",
"GO:0032502",
"GO:0043010",
"GO:0048513",
"GO:0048731",
"GO:0048856",
"GO:0048880",
"GO:0150063"
] | [] | [] | AF-Q4V9P6-F1-model_v6.pdb | 7955.ENSDARP00000067287 | [
"A0A0G2KGL2",
"Q6ZM69",
"F8W4R3",
"A0A0R4ISR7",
"F1QG13"
] | [
"IPR006330",
"IPR032466",
"IPR001365"
] | {"IPR032466": [8, 342], "IPR006330": [9, 345], "IPR001365": [13, 336]} | - IPR006330: Adenosine/adenine deaminase (family) [9-345]
- IPR032466: Metal-dependent hydrolase (homologous_superfamily) [8-342]
- IPR001365: Adenosine deaminase domain (domain) [13-336] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016787 (hydrolase activity), GO:0016810 (hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds), GO:0016814 (hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines), GO:0019239 (deaminase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0032502 (developmental process), GO:0002376 (immune system process), GO:0009987 (cellular process), GO:0032501 (multicellular organismal process), GO:0048869 (cellular developmental process), GO:0048856 (anatomical structure development), GO:0001775 (cell activation), GO:0045321 (leukocyte activation), GO:0048468 (cell development), GO:0030154 (cell differentiation), GO:0046649 (lymphocyte activation), GO:0030097 (hemopoiesis), GO:0002521 (leukocyte differentiation), GO:0030098 (lymphocyte differentiation), GO:1903131 (mononuclear cell differentiation)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005737 (cytoplasm), GO:0005622 (intracellular anatomical structure) | |
P05552 | Transcription factor Adf-1 | May play an important role not only in the regulation of Adh expression but also in the transcription of other genes | Drosophila melanogaster (Fruit fly) | 262 | Nucleus | MHTLTAAIEMDKLDANLEQQFDLNLIEAVKLNPVIYDRSHYNYKHFVRKAQTWKQIAETLGVPEQKCTKRWKSLRDKFAREMKLCQESRWRYFKQMQFLVDSIRQYRESLLGKCANGSQSANQVADPSQQQQAQQQTVVDIFAQPFNGSATTSAQALTHPHEITVTSDAQLATAVGKDQKPYFYEPPLKRERSEEEHSDNMLNTIKIFQNNVSQAVSAEDQSFGMVVTDMLNTLGVRQKAEAKVHIIKYLTDMQLLAQHNKY | [
"GO:0006355",
"GO:0006357",
"GO:0008150",
"GO:0009889",
"GO:0010468",
"GO:0010556",
"GO:0019219",
"GO:0019222",
"GO:0050789",
"GO:0050794",
"GO:0051252",
"GO:0060255",
"GO:0065007",
"GO:0080090",
"GO:2001141",
"GO:0000976",
"GO:0000981",
"GO:0001067",
"GO:0003674",
"GO:0003676"... | [
"GO:0006355",
"GO:0006357",
"GO:0008150",
"GO:0009889",
"GO:0010468",
"GO:0010556",
"GO:0019219",
"GO:0019222",
"GO:0050789",
"GO:0050794",
"GO:0051252",
"GO:0060255",
"GO:0065007",
"GO:0080090",
"GO:2001141"
] | [
"GO:0000976",
"GO:0000981",
"GO:0001067",
"GO:0003674",
"GO:0003676",
"GO:0003677",
"GO:0003690",
"GO:0003700",
"GO:0005488",
"GO:0043565",
"GO:0140110",
"GO:1990837"
] | [] | AF-P05552-F1-model_v6.pdb | 7227.FBpp0303284 | [
"Q9VUH2"
] | [
"IPR039353",
"IPR006578",
"IPR004210"
] | {"IPR039353": [16, 260], "IPR006578": [24, 104], "IPR004210": [217, 256]} | - Transcription activator GAGA | - IPR039353: Transcription factor Adf-1 (family) [16-260]
- IPR006578: MADF domain (domain) [24-104]
- IPR004210: BESS motif (domain) [217-256] | Molecular Function (MF): GO:0003674 (molecular function), GO:0140110 (transcription regulator activity), GO:0003700 (DNA-binding transcription factor activity), GO:0001216 (DNA-binding transcription activator activity), GO:0000981 (DNA-binding transcription factor activity, RNA polymerase II-specific), GO:0001228 (DNA-binding transcription activator activity, RNA polymerase II-specific)
Biological Process (BP): GO:0008150 (biological process), GO:0048518 (positive regulation of biological process), GO:0050789 (regulation of biological process), GO:0032501 (multicellular organismal process), GO:0065007 (biological regulation), GO:0032502 (developmental process), GO:0009987 (cellular process), GO:0048856 (anatomical structure development), GO:0007275 (multicellular organism development), GO:0019222 (regulation of metabolic process), GO:0071840 (cellular component organization or biogenesis), GO:0003008 (system process), GO:0050793 (regulation of developmental process), GO:0048522 (positive regulation of cellular process), GO:0050794 (regulation of cellular process), GO:0009893 (positive regulation of metabolic process), GO:0007610 (behavior), GO:0050773 (regulation of dendrite development), GO:0044085 (cellular component biogenesis), GO:0010604 (positive regulation of macromolecule metabolic process), GO:0048731 (system development), GO:0060255 (regulation of macromolecule metabolic process), GO:0009891 (positive regulation of biosynthetic process), GO:0031325 (positive regulation of cellular metabolic process), GO:0007611 (learning or memory), GO:0009889 (regulation of biosynthetic process), GO:0051171 (regulation of nitrogen compound metabolic process), GO:0016043 (cellular component organization), GO:0031323 (regulation of cellular metabolic process), GO:0050877 (nervous system process), GO:0080090 (regulation of primary metabolic process), GO:0051128 (regulation of cellular component organization), GO:0051173 (positive regulation of nitrogen compound metabolic process), GO:0050890 (cognition), GO:0031344 (regulation of cell projection organization), GO:0010556 (regulation of macromolecule biosynthetic process), GO:0010468 (regulation of gene expression), GO:0022607 (cellular component assembly), GO:0007613 (memory), GO:0010557 (positive regulation of macromolecule biosynthetic process), GO:0045935 (positive regulation of nucleobase-containing compound metabolic process), GO:0051254 (positive regulation of RNA metabolic process), GO:0007399 (nervous system development), GO:0031326 (regulation of cellular biosynthetic process), GO:0019219 (regulation of nucleobase-containing compound metabolic process), GO:0051252 (regulation of RNA metabolic process), GO:0034330 (cell junction organization), GO:0031328 (positive regulation of cellular biosynthetic process), GO:0007416 (synapse assembly), GO:0120035 (regulation of plasma membrane bounded cell projection organization), GO:2001141 (regulation of RNA biosynthetic process), GO:0006355 (regulation of DNA-templated transcription), GO:0034329 (cell junction assembly), GO:1902680 (positive regulation of RNA biosynthetic process), GO:0007616 (long-term memory), GO:0050808 (synapse organization), GO:0006357 (regulation of transcription by RNA polymerase II), GO:0045893 (positive regulation of DNA-templated transcription), GO:1903508 (positive regulation of nucleic acid-templated transcription), GO:1903506 (regulation of nucleic acid-templated transcription), GO:0010975 (regulation of neuron projection development), GO:0045944 (positive regulation of transcription by RNA polymerase II)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0098687 (chromosomal region), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0005705 (polytene chromosome interband), GO:0043228 (non-membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle), GO:0043232 (intracellular non-membrane-bounded organelle), GO:0005694 (chromosome), GO:0005634 (nucleus), GO:0005700 (polytene chromosome) |
Q5AF56 | Transcriptional regulator ADR1 | Transcription factor involved in the regulation of hyphal growth | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) | 1,418 | Nucleus | MISPTHQSQYLNYFVNPVLMTESGDIIDSVTGTTTTTANMSNTTIDAPTPASTTKNYKHKKQNTNTGTSMSPSNSINSTNNNAAAAAATTTTSKKSKDIPLELTAFGTTPSGKPRLFVCQVCTRAFARLEHLRRHERSHTKEKPFSCGVCQRKFSRRDLLLRHAQKLHAGCTDAITRLRRKSIKKSQDGDDDDDDDDDDEEMANSEDENDHDESGNASTKNGKKDKKDPPPEFNLNLFNSKQKPTKANTTKSKVAKLSTTTSRKNSTNPTRKNSSSLHKQVLDQRQKAAVNTKIVSSTKIVSGTNSGVSITPTRSRRGASFSAQSGANYAINIPEFNDIYPQSDNVEFSTPQFLPSSLDNEMTWLNNIPNIPGLSDSVSAANLMRQNSITNSADHVTPPVNVSQHGSFSHQSTFSATDMGQTRSESVNSLNTPFDGSYMMPTVTISNQEIQNGVAAHHHHQQQQQHQQHNHQHQPNQSSLGLSRNDMLSEDHYGYSFYDIPENILNFPMDSISTTSNAMSSGPIQNFKPLSPITQEIEHEITPRIDGRIGDFQNNNNTNDNPIHQNINYDLNFLHTIDDIGQDVISKFMPGGYSFYGDNNVSATSSANDYNSPNNIVSPSQQNNQFALHNQSSHPSGASPHLNQAMMNKMRLHNYSSNKLFTNHIRHMINKALGKYPISGIMTPTIPSNEKLEFYLSVFIQSFLAHLPFIHPSKLNEYEIMAMTGNEDINNESARVCLPLLTATMGALLANNKNDAEHLYEASRRTIHIYLESRKTNSTNDKNYKNGKDKSSSGNPLWLLQSLMLSVLYGLFSDNENNVYIVIRQLNALNSLVKTSIKNKGPIFFSNNGEDEELYNKLNSHDNGTSLFSNNLNDEMRYKNNINMQSQTRIVFIIYRLTNFLLMMYNVPLTFSINDINQLAVTSKDEETLWNFKNYQEFQEFSHKNNKTLDDYLNHKNEPIIFRELLLTVIKFGISDSNISPEIEKKVTHQLQNLCKYGFNCLVHGIYEIKQYQEMKEVDTFKVLDYLTKFYPTNDGLGFNCFRLPANKDLEKIDYALLVDFTKISSIIDLKLLKEQSWLKNYQDLTQNYHRLLDAHSTGNPLNSINDYDYLKLADCCISVLKLILFKVEDSNSNSRNRSKNDPTNEINNKLNNNNNNNNDMNNNNSNGDQLISAFDTDFGYLNMDNNGYAKKEEFSRFTDDELRYDKENTMSYFDKHIKLDIFEEVEKSSNLIQAQMLFHAFSVLSIFSVYVMRKNDNNSSPFANTDLIFELNHRYSMVLRLLERLETFLKLRYQTSAGGGGGGVNNNNNNALSIKLEQEFTNLYLYNGNVLSSDHNTNTNTTNTITTTTTTDNGTKQNQHHSQDFGLEKTLYILKMGENVLNYIYDLNLKVCVFKKLGDSLSEIRKYLIDNESTLNG | [
"GO:0006066",
"GO:0006109",
"GO:0006629",
"GO:0006694",
"GO:0006696",
"GO:0006950",
"GO:0006996",
"GO:0007031",
"GO:0008150",
"GO:0008152",
"GO:0008202",
"GO:0008204",
"GO:0008610",
"GO:0009058",
"GO:0009267",
"GO:0009607",
"GO:0009987",
"GO:0016043",
"GO:0016125",
"GO:0016126"... | [
"GO:0006066",
"GO:0006109",
"GO:0006629",
"GO:0006694",
"GO:0006696",
"GO:0006950",
"GO:0006996",
"GO:0007031",
"GO:0008150",
"GO:0008152",
"GO:0008202",
"GO:0008204",
"GO:0008610",
"GO:0009058",
"GO:0009267",
"GO:0009607",
"GO:0009987",
"GO:0016043",
"GO:0016125",
"GO:0016126"... | [
"GO:0001216",
"GO:0003674",
"GO:0003700",
"GO:0140110"
] | [] | AF-Q5AF56-F1-model_v6.pdb | 237561.Q5AF56 | [
"A0A1D8PN61",
"Q5A766"
] | [
"IPR013087",
"IPR051059",
"IPR036236"
] | {"IPR036236": [114, 163], "IPR051059": [98, 1403], "IPR013087": [117, 173]} | - DNA-binding transcription factor
- Carbon catabolite-derepressing protein kinase | - IPR013087: Zinc finger C2H2-type (domain) [117-173]
- IPR051059: Transcription factor verF-like (family) [98-1403]
- IPR036236: Zinc finger C2H2 superfamily (homologous_superfamily) [114-163] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0097159 (organic cyclic compound binding), GO:1901363 (heterocyclic compound binding), GO:0003676 (nucleic acid binding), GO:0003677 (DNA binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044249 (cellular biosynthetic process), GO:0006520 (amino acid metabolic process), GO:1901576 (organic substance biosynthetic process), GO:1901564 (organonitrogen compound metabolic process), GO:0044283 (small molecule biosynthetic process), GO:0006082 (organic acid metabolic process), GO:1901566 (organonitrogen compound biosynthetic process), GO:0008652 (amino acid biosynthetic process), GO:0016053 (organic acid biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:1901605 (alpha-amino acid metabolic process), GO:0019752 (carboxylic acid metabolic process), GO:0046394 (carboxylic acid biosynthetic process), GO:1901607 (alpha-amino acid biosynthetic process), GO:0009066 (aspartate family amino acid metabolic process), GO:0009067 (aspartate family amino acid biosynthetic process), GO:0006553 (lysine metabolic process), GO:0009085 (lysine biosynthetic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle), GO:0005634 (nucleus) |
Q9D1K7 | Adipose-secreted signaling protein | Adipocyte-secreted protein (adipokine) that acts as a key regulator for white adipose tissue (WAT) thermogenesis and glucose homeostasis at least in part through activation of protein kinase A (PKA) | Mus musculus (Mouse) | 174 | Secreted | MAAANRGSKPRVRSIRFAAGHDAEGSQSHVHFDEKLHDSVVMVTQESDNSFLVKVGFLKILHRYEITFTLPPVRRLSKDIRETPVHSLHLKLLSVTPTSEGYSIKCEYSAHKEGVLKEEMLLACEGDIGTCVRVTVQARVMDRHHGTPMLLDGVKCVGAELEYDSEQSDWLGFD | [
"GO:0008150",
"GO:0008152",
"GO:0009987",
"GO:0033500",
"GO:0042592",
"GO:0042593",
"GO:0048878",
"GO:1990845",
"GO:0005575",
"GO:0005576",
"GO:0005615",
"GO:0110165"
] | [
"GO:0008150",
"GO:0008152",
"GO:0009987",
"GO:0033500",
"GO:0042592",
"GO:0042593",
"GO:0048878",
"GO:1990845"
] | [] | [
"GO:0005575",
"GO:0005576",
"GO:0005615",
"GO:0110165"
] | AF-Q9D1K7-F1-model_v6.pdb | 10090.ENSMUSP00000028800 | null | [
"IPR026794"
] | {"IPR026794": [1, 174]} | - IPR026794: Adipose-secreted signaling protein (family) [1-174] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding), GO:0019899 (enzyme binding), GO:0019902 (phosphatase binding), GO:0019903 (protein phosphatase binding), GO:0008157 (protein phosphatase 1 binding)
Biological Process (BP): GO:0008150 (biological process), GO:0065007 (biological regulation), GO:0048518 (positive regulation of biological process), GO:0050789 (regulation of biological process), GO:0023056 (positive regulation of signaling), GO:0048584 (positive regulation of response to stimulus), GO:0050794 (regulation of cellular process), GO:0048583 (regulation of response to stimulus), GO:0023051 (regulation of signaling), GO:0048522 (positive regulation of cellular process), GO:0090287 (regulation of cellular response to growth factor stimulus), GO:0009967 (positive regulation of signal transduction), GO:0010646 (regulation of cell communication), GO:1903846 (positive regulation of cellular response to transforming growth factor beta stimulus), GO:0009966 (regulation of signal transduction), GO:0010647 (positive regulation of cell communication), GO:0090100 (positive regulation of transmembrane receptor protein serine/threonine kinase signaling pathway), GO:0030511 (positive regulation of transforming growth factor beta receptor signaling pathway), GO:0090092 (regulation of transmembrane receptor protein serine/threonine kinase signaling pathway), GO:1902533 (positive regulation of intracellular signal transduction), GO:1903844 (regulation of cellular response to transforming growth factor beta stimulus), GO:1902531 (regulation of intracellular signal transduction), GO:1901224 (positive regulation of NIK/NF-kappaB signaling), GO:1901222 (regulation of NIK/NF-kappaB signaling), GO:0017015 (regulation of transforming growth factor beta receptor signaling pathway)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005829 (cytosol), GO:0005737 (cytoplasm), GO:0031974 (membrane-enclosed lumen), GO:0005654 (nucleoplasm), GO:0043233 (organelle lumen), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle), GO:0070013 (intracellular organelle lumen), GO:0031981 (nuclear lumen), GO:0005634 (nucleus) | |
P37127 | Putative oxidoreductase AegA | Involved in formate-dependent uric acid degradation under microaerobic and anaerobic conditions. May reduce the enzymes necessary for uric acid degradation | Escherichia coli (strain K12) | 659 | null | MNRFIMANSQQCLGCHACEIACVMAHNDEQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSIQVNQQKCIGCKSCVVACPFGTMQIVLTPVAAGKVKATAHKCDLCAGRENGPACVENCPADALQLVTDVALSGMAKSRRLRTARQEHQPWHASTAAQEMPVMSKVEQMQATPARGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEHSVCEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNTLPEITGRVCPQDRLCEGACTIRDEHGAVTIGNIERYISDQALAKGWRPDLSHVTKVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCEVGKDVSLDSLLEQYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFLIANTKQVMGLEELPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPVEGSEFVMPADAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADVESQYRYQTTNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLGVKSVKSH | [
"GO:0008150",
"GO:0008152",
"GO:0009056",
"GO:0009987",
"GO:0019628",
"GO:0044281",
"GO:0044282",
"GO:0046415",
"GO:0072521",
"GO:0072523"
] | [
"GO:0008150",
"GO:0008152",
"GO:0009056",
"GO:0009987",
"GO:0019628",
"GO:0044281",
"GO:0044282",
"GO:0046415",
"GO:0072521",
"GO:0072523"
] | [] | [] | AF-P37127-F1-model_v6.pdb | 511145.b2468 | [
"Q2MAT2",
"Q2M900",
"P78239",
"Q2M6M5"
] | [
"IPR006006",
"IPR017900",
"IPR009051",
"IPR023753",
"IPR017896",
"IPR036188",
"IPR028261"
] | {"IPR009051": [161, 326], "IPR036188": [327, 651], "IPR006006": [187, 653], "IPR017896": [54, 145], "IPR028261": [205, 315], "IPR023753": [329, 640], "IPR017900": [87, 98]} | - Glutamate synthase [NADPH] large chain
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreA
- Formate dehydrogenase H
- NADH-quinone oxidoreductase subunit F | - IPR006006: Glutamate synthase NADPH small chain-like (family) [187-653]
- IPR017900: 4Fe-4S ferredoxin, iron-sulphur binding, conserved site (conserved_site) [87-98]
- IPR009051: Alpha-helical ferredoxin (homologous_superfamily) [161-326]
- IPR023753: FAD/NAD(P)-binding domain (domain) [329-640]
- IPR017896: 4Fe-4S ferredoxin-type, iron-sulphur binding domain (domain) [54-145]
- IPR036188: FAD/NAD(P)-binding domain superfamily (homologous_superfamily) [327-651]
- IPR028261: Dihydroprymidine dehydrogenase domain II (domain) [205-315] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0003824 (catalytic activity), GO:0005515 (protein binding), GO:0016491 (oxidoreductase activity), GO:0009055 (electron transfer activity)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0044237 (cellular metabolic process), GO:0006091 (generation of precursor metabolites and energy), GO:0015980 (energy derivation by oxidation of organic compounds), GO:0045333 (cellular respiration), GO:0009061 (anaerobic respiration)
Cellular Component (CC): GO:0005575 (cellular component), GO:0032991 (protein-containing complex), GO:1902494 (catalytic complex), GO:1990204 (oxidoreductase complex) |
Q8TGA2 | Fatty acid synthase alpha subunit aflA | Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide- derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). Within the aflatoxin pathway, the fungal fatty acid synthase aflA/aflB provides the hexanoyl starter unit to the acyl-carrier protein (ACP) domain of the norsolorinic acid synthase to allow the first step of the pathway. The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'- hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'- oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) | 1,671 | null | MVIQGKRLAASSIQLLASSLDAKKLCYEYDERQAPGVTQITEEAPTEQPPLSTPPSLPQTPNISPISASKIVIDDVALSRVQIVQALVARKLKTAIAQLPTSKSIKELSGGRSSLQNELVGDIHNEFSSIPDAPEQILLRDFGDANPTVQLGKTSSAAVAKLISSKMPSDFNANAIRAHLANKWGLGPLRQTAVLLYAIASEPPSRLASSSAAEEYWDNVSSMYAESCGITLRPRQDTMNEDAMASSAIDPAVVAEFSKGHRRLGVQQFQALAEYLQIDLSGSQASQSDALVAELQQKVDLWTAEMTPEFLAGISPMLDVKKSRRYGSWWNMARQDVLAFYRRPSYSEFVDDALAFKVFLNRLCNRADEALLNMVRSLSCDAYFKQGSLPGYHAASRLLEQAITSTVADCPKARLILPAVGPHTTITKDGTIEYAEAPRQGVSGPTAYIQSLRQGASFIGLKSADVDTQSNLTDALLDAMCLALHNGISFVGKTFLVTGAGQGSIGAGVVRLLLEGGARVLVTTSREPATTSRYFQQMYDNHGAKFSELRVVPCNLASAQDCEGLIRHVYDPRGLNWDLDAILPFAAASDYSTEMHDIRGQSELGHRLMLVNVFRVLGHIVHCKRDAGVDCHPTQVLLPLSPNHGIFGGDGMYPESKLALESLFHRIRSESWSDQLSICGVRIGWTRSTGLMTAHDIIAETVEEHGIRTFSVAEMALNIAMLLTPDFVAHCEDGPLDADFTGSLGTLGSIPGFLAQLHQKVQLAAEVIRAVQAEDEHERFLSPGTKPTLQAPVAPMHPRSSLRVGYPRLPDYEQEIRPLSPRLERLQDPANAVVVVGYSELGPWGSARLRWEIESQGQWTSAGYVELAWLMNLIRHVNDESYVGWVDTQTGKPVRDGEIQALYGDHIDNHTGIRPIQSTSYNPERMEVLQEVAVEEDLPEFEVSQLTADAMRLRHGANVSIRPSGNPDACHVKLKRGAVILVPKTVPFVWGSCAGELPKGWTPAKYGIPENLIHQVDPVTLYTICCVAEAFYSAGITHPLEVFRHIHLSELGNFIGSSMGGPTKTRQLYRDVYFDHEIPSDVLQDTYLNTPAAWVNMLLLGCTGPIKTPVGACATGVESIDSGYESIMAGKTKMCLVGGYDDLQEEASYGFAQLKATVNVEEEIACGRQPSEMSRPMAESRAGFVEAHGCGVQLLCRGDIALQMGLPIYAVIASSAMAADKIGSSVPAPGQGILSFSRERARSSMISVTSRPSSRSSTSSEVSDKSSLTSITSISNPAPRAQRARSTTDMAPLRAALATWGLTIDDLDVASLHGTSTRGNDLNEPEVIETQMRHLGRTPGRPLWAICQKSVTGHPKAPAAAWMLNGCLQVLDSGLVPGNRNLDTLDEALRSASHLCFPTRTVQLREVKAFLLTSFGFGQKGGQVVGVAPKYFFATLPRPEVEGYYRKVRVRTEAGDRAYAAAVMSQAVVKIQTQNPYDEPDAPRIFLDPLARISQDPSTGQYRFRSDATPALDDDALPPPGEPTELVKGISSAWIEEKVRPHMSPGGTVGVDLVPLASFDAYKNAIFVERNYTVRERDWAEKSADVRAAYASRWCAKEAVFKCLQTHSQGAGAAMKEIEIEHGGNGAPKVKLRGAAQTAARQRGLEGVQLSISYGDDAVIAVALGLMSGAS | [
"GO:0005575",
"GO:0005835",
"GO:0032991",
"GO:0140535",
"GO:1902494",
"GO:1990234"
] | [] | [] | [
"GO:0005575",
"GO:0005835",
"GO:0032991",
"GO:0140535",
"GO:1902494",
"GO:1990234"
] | AF-Q8TGA2-F1-model_v6.pdb | 1403190.Q8TGA2 | [
"A0A0F0IGH1",
"A0A0F0HZD0",
"A0A0F0IN54",
"A0A0F0I3U8",
"A0A0F0ILF1",
"A0A0F0IHY3",
"A0A0F0I549",
"A0A0F0I494",
"A0A0F0IK72",
"A0A0F0HZA4",
"A0A0F0III1",
"Q8TGA1",
"A0A0F0ILA6"
] | [
"IPR036291",
"IPR040899",
"IPR008278",
"IPR020841",
"IPR018201",
"IPR016039",
"IPR009081",
"IPR047224",
"IPR037143",
"IPR026025",
"IPR050830",
"IPR041550",
"IPR014030",
"IPR004568",
"IPR014031",
"IPR013968"
] | {"IPR036291": [492, 729], "IPR016039": [794, 1515], "IPR037143": [1547, 1665], "IPR026025": [10, 1666], "IPR050830": [25, 1493], "IPR040899": [74, 232], "IPR009081": [75, 153], "IPR041550": [259, 456], "IPR013968": [494, 569], "IPR020841": [833, 1428], "IPR047224": [994, 1425], "IPR014030": [1002, 1198], "IPR014031": [1275, 1382], "IPR004568": [1548, 1663], "IPR008278": [1549, 1642], "IPR018201": [1104, 1120]} | - Fatty acid synthase beta subunit aflB
- Acyl transferase domain protein
- Malonyl-CoA:ACP transacylase (MAT) domain-containing protein
- Acyl transferase domain protein
- Acetyl-CoA carboxylase central region
- Fatty acid synthase subunit alpha
- Ketosynthase family 3 (KS3) domain-containing protein
- Beta-ketoacyl synthase C-terminal domain protein
- Eukaryotic long-chain fatty acid CoA synthetase LC-FACS
- Fatty acid synthase subunit alpha | - IPR036291: NAD(P)-binding domain superfamily (homologous_superfamily) [492-729]
- IPR040899: Fatty acid synthase subunit alpha, acyl carrier domain (domain) [74-232]
- IPR008278: 4'-phosphopantetheinyl transferase domain (domain) [1549-1642]
- IPR020841: Polyketide synthase, beta-ketoacyl synthase domain (domain) [833-1428]
- IPR018201: Beta-ketoacyl synthase, active site (active_site) [1104-1120]
- IPR016039: Thiolase-like (homologous_superfamily) [794-1515]
- IPR009081: Phosphopantetheine binding ACP domain (domain) [75-153]
- IPR047224: Fatty acid synthase subunit alpha-like, C-terminal (domain) [994-1425]
- IPR037143: 4'-phosphopantetheinyl transferase domain superfamily (homologous_superfamily) [1547-1665]
- IPR026025: Fatty acid synthase alpha subunit, yeast (family) [10-1666]
- IPR050830: Fungal fatty acid synthase (family) [25-1493]
- IPR041550: Fatty acid synthase type I, helical (domain) [259-456]
- IPR014030: Beta-ketoacyl synthase-like, N-terminal (domain) [1002-1198]
- IPR004568: Phosphopantetheine-protein transferase domain (domain) [1548-1663]
- IPR014031: Beta-ketoacyl synthase, C-terminal (domain) [1275-1382]
- IPR013968: Polyketide synthase-like, ketoreductase domain (domain) [494-569] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016740 (transferase activity), GO:0016746 (acyltransferase activity), GO:0016747 (acyltransferase activity, transferring groups other than amino-acyl groups), GO:0004312 (fatty acid synthase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0019748 (secondary metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044550 (secondary metabolite biosynthetic process), GO:0044249 (cellular biosynthetic process), GO:0009404 (toxin metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006083 (acetate metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006082 (organic acid metabolic process), GO:1901376 (organic heteropentacyclic compound metabolic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0043385 (mycotoxin metabolic process), GO:0009403 (toxin biosynthetic process), GO:0045122 (aflatoxin biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:0018130 (heterocycle biosynthetic process), GO:0019752 (carboxylic acid metabolic process), GO:0043386 (mycotoxin biosynthetic process), GO:0046222 (aflatoxin metabolic process), GO:1901378 (organic heteropentacyclic compound biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0032991 (protein-containing complex), GO:0005829 (cytosol), GO:1902494 (catalytic complex), GO:0005622 (intracellular anatomical structure), GO:0005737 (cytoplasm), GO:0140535 (intracellular protein-containing complex) |
Q8TGA1 | Fatty acid synthase beta subunit aflB | Fatty acid synthase beta subunit; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide- derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). Within the aflatoxin pathway, the fungal fatty acid synthase aflA/aflB provides the hexanoyl starter unit to the acyl-carrier protein (ACP) domain of the norsolorinic acid synthase to allow the first step of the pathway. The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'- oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring- opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) | 1,888 | null | MGSVSREHESIPIQAAQRGAARICAAFGGQGSNNLDVLKGLLELYKRYGPDLDELLDVASNTLSQLASSPAAIDVHEPWGFDLRQWLTTPEVAPSKEILALPPRSFPLNTLLSLALYCATCRELELDPGQFRSLLHSSTGHSQGILAAVAITQAESWPTFYDACRTVLQISFWIGLEAYLFTPSSAASDAMIQDCIEHGEGLLSSMLSVSGLSRSQVERVIEHVNKGLGECNRWVHLALVNSHEKFVLAGPPQSLWAVCLHVRRIRADNDLDQSRILFRNRKPIVDILFLPISAPFHTPYLDGVQDRVIEALSSASLALHSIKIPLYHTGTGSNLQELQPHQLIPTLIRAITVDQLDWPLVCRGLNATHVLDFGPGQTCSLIQELTQGTGVSVIQLTTQSGPKPVGGHLAAVNWEAEFGLRLHANVHGAAKLHNRMTTLLGKPPVMVAGMTPTTVRWDFVAAVAQAGYHVELAGGGYHAERQFEAEIRRLATAIPADHGITCNLLYAKPTTFSWQISVIKDLVRQGVPVEGITIGAGIPSPEVVQECVQSIGLKHISFKPGSFEAIHQVIQIARTHPNFLIGLQWTAGRGGGHHSWEDFHGPILATYAQIRSCPNILLVVGSGFGGGPDTFPYLTGQWAQAFGYPCMPFDGVLLGSRMMVAREAHTSAQAKRLIIDAQGVGDADWHKSFDEPTGGVVTVNSEFGQPIHVLATRGVMLWKELDNRVFSIKDTSKRLEYLRNHRQEIVSRLNADFARPWFAVDGHGQNVELEDMTYLEVLRRLCDLTYVSHQKRWVDPSYRILLLDFVHLLRERFQCAIDNPGEYPLDIIVRVEESLKDKAYRTLYPEDVSLLMHLFSRRDIKPVPFIPRLDERFETWFKKDSLWQSEDVEAVIGQDVQRIFIIQGPMAVQYSISDDESVKDILHNICNHYVEALQADSRETSIGDVHSITQKPLSAFPGLKVTTNRVQGLYKFEKVGAVPEMDVLFEHIVGLSKSWARTCLMSKSVFRDGSRLHNPIRAALQLQRGDTIEVLLTADSEIRKIRLISPTGDGGSTSKVVLEIVSNDGQRVFATLAPNIPLSPEPSVVFCFKVDQKPNEWTLEEDASGRAERIKALYMSLWNLGFPNKASVLGLNSQFTGEELMITTDKIRDFERVLRQTSPLQLQSWNPQGCVPIDYCVVIAWSALTKPLMVSSLKCDLLDLLHSAISFHYAPSVKPLRVGDIVKTSSRILAVSVRPRGTMLTVSADIQRQGQHVVTVKSDFFLGGPVLACETPFELTEEPEMVVHVDSEVRRAILHSRKWLMREDRALDLLGRQLLFRLKSEKLFRPDGQLALLQVTGSVFSYSPDGSTTAFGRVYFESESCTGNVVMDFLHRYGAPRAQLLELQHPGWTGTSTVAVRGPRRSQSYARVSLDHNPIHVCPAFARYAGLSGPIVHGMETSAMMRRIAEWAIGDADRSRFRSWHITLQAPVHPNDPLRVELQHKAMEDGEMVLKVQAFNERTEERVAEADAHVEQETTAYVFCGQGSQRQGMGMDLYVNCPEAKALWARADKHLWEKYGFSILHIVQNNPPALTVHFGSQRGRRIRANYLRMMGQPPIDGRHPPILKGLTRNSTSYTFSYSQGLLMSTQFAQPALALMEMAQFEWLKAQGVVQKGARFAGHSLGEYAALGACASFLSFEDLISLIFYRGLKMQNALPRDANGHTDYGMLAADPSRIGKGFEEASLKCLVHIIQQETGWFVEVVNYNINSQQYVCAGHFRALWMLGKICDDLSCHPQPETVEGQELRAMVWKHVPTVEQVPREDRMERGRATIPLPGIDIPYHSTMLRGEIEPYREYLSERIKVGDVKPCELVGRWIPNVVGQPFSVDKSYVQLVHGITGSPRLHSLLQQMA | [
"GO:0005575",
"GO:0005835",
"GO:0032991",
"GO:0140535",
"GO:1902494",
"GO:1990234"
] | [] | [] | [
"GO:0005575",
"GO:0005835",
"GO:0032991",
"GO:0140535",
"GO:1902494",
"GO:1990234"
] | AF-Q8TGA1-F1-model_v6.pdb | 1403190.Q8TGA1 | [
"A0A0F0IN54",
"Q8TGA2",
"A0A0F0I3U8",
"A0A0F0ILF1",
"A0A0F0IGH1",
"A0A0F0HZD0",
"A0A0F0I2A0",
"A0A0F0III1",
"A0A0F0ILA6",
"A0A0F0IHY3",
"A0A0F0IK72",
"A0A0F0I494",
"A0A0F0HZA4"
] | [
"IPR001227",
"IPR013565",
"IPR029069",
"IPR039569",
"IPR040883",
"IPR016452",
"IPR003965",
"IPR050830",
"IPR002539",
"IPR013785",
"IPR014043",
"IPR032088",
"IPR016035"
] | {"IPR001227": [10, 1706], "IPR016035": [23, 1862], "IPR013785": [412, 695], "IPR029069": [1166, 1510], "IPR016452": [4, 1887], "IPR050830": [16, 1887], "IPR032088": [27, 257], "IPR003965": [434, 1704], "IPR013565": [581, 922], "IPR040883": [977, 1118], "IPR039569": [1134, 1255], "IPR002539": [1399, 1500], "IPR014043": [1517, 1877]} | - Fatty acid synthase subunit alpha
- Fatty acid synthase alpha subunit aflA
- Fatty acid synthase subunit alpha
- Ketosynthase family 3 (KS3) domain-containing protein
- Beta-ketoacyl synthase C-terminal domain protein
- Acetyl-CoA carboxylase central region
- Acyl transferase domain protein
- Malonyl-CoA:ACP transacylase (MAT) domain-containing protein
- Eukaryotic long-chain fatty acid CoA synthetase LC-FACS
- Acyl transferase domain protein | - IPR001227: Acyl transferase domain superfamily (homologous_superfamily) [10-1706]
- IPR013565: Fatty acid synthase beta subunit AflB /Fas1-like, central domain (domain) [581-922]
- IPR029069: HotDog domain superfamily (homologous_superfamily) [1166-1510]
- IPR039569: FAS1-like, dehydratase domain region (domain) [1134-1255]
- IPR040883: Fatty acid synthase, meander beta sheet domain (domain) [977-1118]
- IPR016452: Fatty acid synthase beta subunit AflB /Fas1-like, fungi (family) [4-1887]
- IPR003965: Fatty acid synthase (domain) [434-1704]
- IPR050830: Fungal fatty acid synthase (family) [16-1887]
- IPR002539: MaoC-like dehydratase domain (domain) [1399-1500]
- IPR013785: Aldolase-type TIM barrel (homologous_superfamily) [412-695]
- IPR014043: Acyl transferase domain (domain) [1517-1877]
- IPR032088: Starter unit:ACP transacylase, SAT domain (domain) [27-257]
- IPR016035: Acyl transferase/acyl hydrolase/lysophospholipase (homologous_superfamily) [23-1862] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016740 (transferase activity), GO:0016491 (oxidoreductase activity), GO:0016746 (acyltransferase activity), GO:0016627 (oxidoreductase activity, acting on the CH-CH group of donors), GO:0016747 (acyltransferase activity, transferring groups other than amino-acyl groups), GO:0016628 (oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0019748 (secondary metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044550 (secondary metabolite biosynthetic process), GO:0044249 (cellular biosynthetic process), GO:0009404 (toxin metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006083 (acetate metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006082 (organic acid metabolic process), GO:1901376 (organic heteropentacyclic compound metabolic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0043385 (mycotoxin metabolic process), GO:0009403 (toxin biosynthetic process), GO:0045122 (aflatoxin biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:0018130 (heterocycle biosynthetic process), GO:0019752 (carboxylic acid metabolic process), GO:0043386 (mycotoxin biosynthetic process), GO:0046222 (aflatoxin metabolic process), GO:1901378 (organic heteropentacyclic compound biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0032991 (protein-containing complex), GO:1902494 (catalytic complex) |
Q00278 | Norsolorinic acid ketoreductase | Norsolorinic acid ketoreductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide- derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). Within the aflatoxin pathway, the norsolorinic acid ketoreductase aflD performs the second step by catalyzing the dehydration of norsolorinic acid (NOR) to form (1'S)- averantin (AVN). The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'- oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring- opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) | 271 | Cytoplasm, cytosol. Vacuole | MNGSLSQHDQERLSTPYRDGPPEETVYLVTGASRGIGRGLIEAFLQRPKSTVVAWLRNVRTATPALSALTVAEGSRMIIVQLNSDSETDAQAAVQTLREEHGVTHLDVVVANAAMATNFGPASTMPLEHLQAHMMVNMYAPVLLFQATRLMLQQSKQQAKFVLIGAPISTITNMHDYSRAPLTAYGVSKLAANYMVRKFHFENKWLTAFIIDPGHVQTDMGDQGARLMGRPQAPTTVADSVAGICARIDEATKETTSGHFVIHTDGSQLPW | [
"GO:0005575",
"GO:0005622",
"GO:0005737",
"GO:0005773",
"GO:0005775",
"GO:0031974",
"GO:0043226",
"GO:0043227",
"GO:0043229",
"GO:0043231",
"GO:0043233",
"GO:0070013",
"GO:0110165"
] | [] | [] | [
"GO:0005575",
"GO:0005622",
"GO:0005737",
"GO:0005773",
"GO:0005775",
"GO:0031974",
"GO:0043226",
"GO:0043227",
"GO:0043229",
"GO:0043231",
"GO:0043233",
"GO:0070013",
"GO:0110165"
] | AF-Q00278-F1-model_v6.pdb | 1403190.Q00278 | null | [
"IPR036291",
"IPR051468",
"IPR002347"
] | {"IPR036291": [26, 271], "IPR002347": [26, 247], "IPR051468": [27, 271]} | - IPR036291: NAD(P)-binding domain superfamily (homologous_superfamily) [26-271]
- IPR051468: Fungal Secondary Metabolite SDRs (family) [27-271]
- IPR002347: Short-chain dehydrogenase/reductase SDR (family) [26-247] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016491 (oxidoreductase activity), GO:0016614 (oxidoreductase activity, acting on CH-OH group of donors), GO:0016616 (oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0019748 (secondary metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044550 (secondary metabolite biosynthetic process), GO:0044249 (cellular biosynthetic process), GO:0009404 (toxin metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006083 (acetate metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006082 (organic acid metabolic process), GO:1901376 (organic heteropentacyclic compound metabolic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0043385 (mycotoxin metabolic process), GO:0009403 (toxin biosynthetic process), GO:0045122 (aflatoxin biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:0018130 (heterocycle biosynthetic process), GO:0019752 (carboxylic acid metabolic process), GO:0043386 (mycotoxin biosynthetic process), GO:0046222 (aflatoxin metabolic process), GO:1901378 (organic heteropentacyclic compound biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005737 (cytoplasm), GO:0005829 (cytosol), GO:0005622 (intracellular anatomical structure) | |
Q12732 | Averantin hydroxylase | Averantin hydroxylase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). Within the aflatoxin pathway, the cytochrome P450 monooxygenase aflG catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'- oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring- opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) | 495 | Membrane; Single-pass membrane protein | MGGDGWPSDGHILLLIVLTVLTPPSLALYRLWIHPLRSYPGPRWWAIWRGPYILSNIRGNLVRDLQRLHQQFGPVVRIAPNELSFIVPEAASPIYTSNPEFPKDPMHLPPFHNGTPGILAADHAHHRRYRRLLAFSFSDKGLRHERSLIERSIDLLITQLHENCGQGPLDLALWFNWATFDIIGDLAFGDSFGCLENVQTHPWIASIQGNVKLIPILNAFRRYRLDGLLRLLGSRKLLEQRRRNAQFTTDQVDRRLKNSSTPRGDIWDAVLAQKPDGEPPMTRDEMISNASAIVLAGSETSATLLSGCTWLLLKNPSHLHQLTSRIRSQFTHASEIDSQSVSRVEGLQAVLEESLRLYPPVPMQSNRIVPQAGAYIAGGWVPGGTSVGLQQFVACRSSSNFHRPDEFLPERWQGQGEFAHDRREVSQPFSIGPRNCIGRQLAYVEMRLILVKLLWHFDLRLDTTRMKDTDWLAEQGIWILWDKKPLWVTLEPRNE | [
"GO:0003674",
"GO:0003824",
"GO:0016491",
"GO:0016705",
"GO:0140395"
] | [] | [
"GO:0003674",
"GO:0003824",
"GO:0016491",
"GO:0016705",
"GO:0140395"
] | [] | AF-Q12732-F1-model_v6.pdb | 1403190.Q12732 | [
"A0A0F0IM89",
"P87017"
] | [
"IPR050121",
"IPR017972",
"IPR001128",
"IPR002401",
"IPR036396"
] | {"IPR036396": [29, 495], "IPR050121": [13, 466], "IPR001128": [40, 469], "IPR002401": [69, 459], "IPR017972": [429, 438]} | - Short chain dehydrogenase
- 5'-hydroxyaverantin dehydrogenase | - IPR050121: Cytochrome P450 monooxygenase (family) [13-466]
- IPR017972: Cytochrome P450, conserved site (conserved_site) [429-438]
- IPR001128: Cytochrome P450 (family) [40-469]
- IPR002401: Cytochrome P450, E-class, group I (family) [69-459]
- IPR036396: Cytochrome P450 superfamily (homologous_superfamily) [29-495] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016491 (oxidoreductase activity), GO:0004497 (monooxygenase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0019748 (secondary metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044550 (secondary metabolite biosynthetic process), GO:0044249 (cellular biosynthetic process), GO:0009404 (toxin metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006083 (acetate metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006082 (organic acid metabolic process), GO:1901376 (organic heteropentacyclic compound metabolic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0043385 (mycotoxin metabolic process), GO:0009403 (toxin biosynthetic process), GO:0045122 (aflatoxin biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:0018130 (heterocycle biosynthetic process), GO:0019752 (carboxylic acid metabolic process), GO:0043386 (mycotoxin biosynthetic process), GO:0046222 (aflatoxin metabolic process), GO:1901378 (organic heteropentacyclic compound biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0016020 (membrane), GO:0005737 (cytoplasm), GO:0012505 (endomembrane system), GO:0031984 (organelle subcompartment), GO:0042175 (nuclear outer membrane-endoplasmic reticulum membrane network), GO:0031090 (organelle membrane), GO:0005783 (endoplasmic reticulum), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0098827 (endoplasmic reticulum subcompartment), GO:0043231 (intracellular membrane-bounded organelle), GO:0005789 (endoplasmic reticulum membrane) |
P87017 | 5'-hydroxyaverantin dehydrogenase | 5'-hydroxyaverantin dehydrogenase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide- derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). Within the aflatoxin pathway, the 5'-hydroxyaverantin dehydrogenase aflH transforms 5'hydroxyaverantin (HAVN) to 5'-oxoaverantin (OAVN). The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'- oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring- opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) | 278 | Cytoplasm, cytosol | MEVLDTTVDLGTLQGKSALITGGASGIGLATARAWAAAGMYVTIADIQPLETGQNILADLAGGHVHYVCCDVTSWESQITAFKEAIQFTPSKALDIVAAFAGVSFAGGNQVDHVLAAGDPRLDVNPSPPDIRNIQVNLIGVYYTSWLGLYYLRLSPTNKAANPSPDKSLILMGSIGSYMDSPKASTYPASKFGVRGLFRSTRARTRELGVRCNLLAPWFIDTPLIAPMKKAMAARGIDMAQRLTFASVDACVEAATTCAANPQLHGTPPIRYAYCLKT | [
"GO:0005575",
"GO:0005622",
"GO:0005737",
"GO:0005829",
"GO:0110165"
] | [] | [] | [
"GO:0005575",
"GO:0005622",
"GO:0005737",
"GO:0005829",
"GO:0110165"
] | AF-P87017-F1-model_v6.pdb | 1403190.P87017 | [
"Q12062",
"Q12732"
] | [
"IPR036291",
"IPR020904",
"IPR002347"
] | {"IPR036291": [12, 265], "IPR002347": [16, 229], "IPR020904": [174, 202]} | - Versicolorin B synthase
- Averantin hydroxylase | - IPR036291: NAD(P)-binding domain superfamily (homologous_superfamily) [12-265]
- IPR020904: Short-chain dehydrogenase/reductase, conserved site (conserved_site) [174-202]
- IPR002347: Short-chain dehydrogenase/reductase SDR (family) [16-229] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0003824 (catalytic activity), GO:0005515 (protein binding), GO:0016491 (oxidoreductase activity), GO:0042802 (identical protein binding), GO:0016614 (oxidoreductase activity, acting on CH-OH group of donors), GO:0046983 (protein dimerization activity), GO:0042803 (protein homodimerization activity), GO:0016616 (oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0019748 (secondary metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044550 (secondary metabolite biosynthetic process), GO:0044249 (cellular biosynthetic process), GO:0009404 (toxin metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006083 (acetate metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006082 (organic acid metabolic process), GO:1901376 (organic heteropentacyclic compound metabolic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0043385 (mycotoxin metabolic process), GO:0009403 (toxin biosynthetic process), GO:0045122 (aflatoxin biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:0018130 (heterocycle biosynthetic process), GO:0019752 (carboxylic acid metabolic process), GO:0043386 (mycotoxin biosynthetic process), GO:0046222 (aflatoxin metabolic process), GO:1901378 (organic heteropentacyclic compound biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005737 (cytoplasm), GO:0005829 (cytosol), GO:0005622 (intracellular anatomical structure) |
Q12437 | Averufin oxidase A | Averufin oxidase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). Within the aflatoxin pathway, the averufin oxidase aflI catalyzes the conversion of averufin (AVF) to versiconal hemiacetal acetate (VHA). The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'- hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'- oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) | 285 | Membrane; Single-pass membrane protein | MVTYALLGATGATGSSILRHLLQKSPDSLHIQVLVRSKVKLLQAFPDLETTRRPQVHVIQGMSTDSDALSECLRNASIVFMCVAQNGSPIGTTLCQDSARPIISVLQQQQQSEGASYQPCTIVQLRSASLNPALAAQVPAFVHRIVSFCLFANYADIKQACQYYSEAQKQGTLEYILVDPPTLHDANGTHPTGYRLISTEPQATALSYADLGAAMCEIAHRESEFHGRAVGVTATGRVRQTWGVLLRHLLEGGSSRLRETIAKEAVVVRVLCIFLVILACLMSSL | [
"GO:0003674",
"GO:0003824",
"GO:0016491"
] | [] | [
"GO:0003674",
"GO:0003824",
"GO:0016491"
] | [] | AF-Q12437-F1-model_v6.pdb | 1403190.Q12437 | null | [
"IPR036291",
"IPR051606",
"IPR016040"
] | {"IPR036291": [3, 232], "IPR051606": [3, 234], "IPR016040": [8, 220]} | - IPR036291: NAD(P)-binding domain superfamily (homologous_superfamily) [3-232]
- IPR051606: Polyketide Oxidoreductase-like (family) [3-234]
- IPR016040: NAD(P)-binding domain (domain) [8-220] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016491 (oxidoreductase activity), GO:0004497 (monooxygenase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0019748 (secondary metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044550 (secondary metabolite biosynthetic process), GO:0044249 (cellular biosynthetic process), GO:0009404 (toxin metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006083 (acetate metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006082 (organic acid metabolic process), GO:1901376 (organic heteropentacyclic compound metabolic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0043385 (mycotoxin metabolic process), GO:0009403 (toxin biosynthetic process), GO:0045122 (aflatoxin biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:0018130 (heterocycle biosynthetic process), GO:0019752 (carboxylic acid metabolic process), GO:0043386 (mycotoxin biosynthetic process), GO:0046222 (aflatoxin metabolic process), GO:1901378 (organic heteropentacyclic compound biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0031975 (envelope), GO:0016020 (membrane), GO:0005737 (cytoplasm), GO:0012505 (endomembrane system), GO:0031090 (organelle membrane), GO:0031967 (organelle envelope), GO:0005739 (mitochondrion), GO:0005783 (endoplasmic reticulum), GO:0005635 (nuclear envelope), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0009536 (plastid), GO:0043228 (non-membrane-bounded organelle), GO:0009526 (plastid envelope), GO:0042170 (plastid membrane), GO:0010646 (regulation of cell communication), GO:0043231 (intracellular membrane-bounded organelle), GO:0031976 (plastid thylakoid), GO:0043232 (intracellular non-membrane-bounded organelle), GO:0009941 (chloroplast envelope), GO:0005811 (lipid droplet) | |
Q9UW95 | Versicolorin B desaturase | Versicolorin B desaturase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). Within the aflatoxin pathway, the versicolorin B desaturase aflL catalyzes the conversion of versicolorin B (VERB) to versicolorin A (VERA). The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'- hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'- oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) | 500 | Membrane; Single-pass membrane protein | MYFLSLPSLVIVIPVGYLLFHLGYNLFFHPLRGYPGPLLWRASSLPWKIALLRGTMHHDLMRFHQKYGDTVRIKPDEISYANAQAWRDIHAHVPGRPEFLKDPVRLPLAPNGVMSILVSDTKNHARFRSLFGHAFSDKGLRTQESTIVQYADLLVEVLREVADTGRSAEMVYYFNMAIFDSIGALSFGESFDSLKSRQLHPWVDAIHKNLKSVAISHVLRSMGIEFLTPYVLPKELRGKRQENYSYAVEKLNKRMKMEGDQGDFWDKVLVKSADDNQRGDGMSAGEMLNNAAVMVVAGSETTASALSGAMYLLCLSGKIEKATAEIRKSFASPEDIDLISVSHLPYLTAVIDETLRMYPAVPGQPPRVVPASGATVCGRFVPEETRVGVSHLATYFADYNFTHADKFIPERHLQKTEEPFKYDNYGAYQPWSVGLRNCIGRNLAYAEVRLTLAKLLWHFDFTLDVDKTGNFLDQKIWSIWAKRELYMFIKTRGTSSSSPQ | [
"GO:0003674",
"GO:0003824",
"GO:0016491",
"GO:0016705",
"GO:0016717",
"GO:0140398"
] | [] | [
"GO:0003674",
"GO:0003824",
"GO:0016491",
"GO:0016705",
"GO:0016717",
"GO:0140398"
] | [] | AF-Q9UW95-F1-model_v6.pdb | 1403190.Q9UW95 | null | [
"IPR050121",
"IPR017972",
"IPR001128",
"IPR002401",
"IPR036396"
] | {"IPR036396": [24, 497], "IPR050121": [7, 465], "IPR001128": [38, 468], "IPR002401": [177, 461], "IPR017972": [431, 440]} | - IPR050121: Cytochrome P450 monooxygenase (family) [7-465]
- IPR017972: Cytochrome P450, conserved site (conserved_site) [431-440]
- IPR001128: Cytochrome P450 (family) [38-468]
- IPR002401: Cytochrome P450, E-class, group I (family) [177-461]
- IPR036396: Cytochrome P450 superfamily (homologous_superfamily) [24-497] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0019748 (secondary metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044550 (secondary metabolite biosynthetic process), GO:0044249 (cellular biosynthetic process), GO:0009404 (toxin metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006083 (acetate metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006082 (organic acid metabolic process), GO:1901376 (organic heteropentacyclic compound metabolic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0043385 (mycotoxin metabolic process), GO:0009403 (toxin biosynthetic process), GO:0045122 (aflatoxin biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:0018130 (heterocycle biosynthetic process), GO:0019752 (carboxylic acid metabolic process), GO:0043386 (mycotoxin biosynthetic process), GO:0046222 (aflatoxin metabolic process), GO:1901378 (organic heteropentacyclic compound biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005737 (cytoplasm), GO:0005829 (cytosol), GO:0005622 (intracellular anatomical structure) | |
P50161 | Versicolorin reductase 1 | Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). Within the aflatoxin pathway, with the cytochrome P450 monooxygenase aflN, the versicolorin reductase aflM, is involved in conversion of VERA to demethylsterigmatocystin (DMST). The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'- hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'- oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) | 262 | Cytoplasm, cytosol | MSDNHRLDGKVALVTGAGRGIGAAIAVALGERGAKVVVNYAHSREAAEKVVEQIKANGTDAIAIQADVGDPEATAKLMAETVRHFGYLDIVSSNAGIVSFGHLKDVTPEEFDRVFRVNTRGQFFVAREAYRHMREGGRIILTSSNTACVKGVPKHAVYSGSKGAIDTFVRCMAIDCGDKKITVNAVAPGAIKTDMFLAVSREYIPNGETFTDEQVDECAAWLSPLNRVGLPVDVARVVSFLASDTAEWVSGKIIGVDGGAFR | [
"GO:0003674",
"GO:0003824",
"GO:0016491",
"GO:0016614",
"GO:0042469",
"GO:0005575",
"GO:0005622",
"GO:0005737",
"GO:0005829",
"GO:0110165"
] | [] | [
"GO:0003674",
"GO:0003824",
"GO:0016491",
"GO:0016614",
"GO:0042469"
] | [
"GO:0005575",
"GO:0005622",
"GO:0005737",
"GO:0005829",
"GO:0110165"
] | AF-P50161-F1-model_v6.pdb | 1403190.P50161 | [
"Q6UEF2"
] | [
"IPR036291",
"IPR020904",
"IPR002347",
"IPR057326"
] | {"IPR036291": [8, 260], "IPR002347": [11, 259], "IPR057326": [10, 194], "IPR020904": [145, 173]} | - Oxidoreductase aflX | - IPR036291: NAD(P)-binding domain superfamily (homologous_superfamily) [8-260]
- IPR020904: Short-chain dehydrogenase/reductase, conserved site (conserved_site) [145-173]
- IPR002347: Short-chain dehydrogenase/reductase SDR (family) [11-259]
- IPR057326: Ketoreductase domain (domain) [10-194] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016491 (oxidoreductase activity), GO:0016614 (oxidoreductase activity, acting on CH-OH group of donors), GO:0016616 (oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0019748 (secondary metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044550 (secondary metabolite biosynthetic process), GO:0044249 (cellular biosynthetic process), GO:0009404 (toxin metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006083 (acetate metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006082 (organic acid metabolic process), GO:1901376 (organic heteropentacyclic compound metabolic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0043385 (mycotoxin metabolic process), GO:0009403 (toxin biosynthetic process), GO:0045122 (aflatoxin biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:0018130 (heterocycle biosynthetic process), GO:0019752 (carboxylic acid metabolic process), GO:0043386 (mycotoxin biosynthetic process), GO:0046222 (aflatoxin metabolic process), GO:1901378 (organic heteropentacyclic compound biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0032991 (protein-containing complex), GO:1902494 (catalytic complex) |
Q12120 | Sterigmatocystin 8-O-methyltransferase | Sterigmatocystin 8-O-methyltransferase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). Within the aflatoxin pathway, the O-methyltransferase aflP uses both sterigmatocystin (ST) and dihydrosterigmatocystin (DHST) as substrates to yield O- methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively. The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'- oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA- binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) | 418 | Cytoplasm. Vacuole | MALPSKAALVGLANTLSEQVKRYLATAGETKSPEDHKLCIESERTPSSNEHAQAWEIVRTCDRIGSLVHGPVPWLLSNALSHLDSACLAAATHLNLQDIIVDGPSPTSLDTIVAATGVSEDLLRRILRGCAQRFIFEEVAPDQYAHTDASKMLRVTGIHALVGFSCDEVMRSGASFSDFLQQTKGKPPSWNVPSPFSLAFDPTKGLFDYYSTVDEVRGRRFDLGMGGTEATKPLVEEMFDFSSLPEGSTVVDVGGGRGHLSRRVSQKHPHLRFIVQDLPAVIHGVEDTDKVTMMEHDIRRPNPVRGADVYLLRSILHDYPDAACVEILSNIVTAMDPSKSRILLDEMIMPDLLAQDSQRFMNQIDMTVVLTLNGKERSTKEWNSLITTVDGRLETEKIWWRKGEEGSHWGVQQLRLRK | [
"GO:0003674",
"GO:0003824",
"GO:0008168",
"GO:0008171",
"GO:0016740",
"GO:0016741",
"GO:0047146",
"GO:0005575",
"GO:0005622",
"GO:0005737",
"GO:0005829",
"GO:0110165"
] | [] | [
"GO:0003674",
"GO:0003824",
"GO:0008168",
"GO:0008171",
"GO:0016740",
"GO:0016741",
"GO:0047146"
] | [
"GO:0005575",
"GO:0005622",
"GO:0005737",
"GO:0005829",
"GO:0110165"
] | AF-Q12120-F1-model_v6.pdb | 1403190.Q12120 | [
"Q6UEG8",
"Q9UQY0",
"A0A0F0IBA6",
"A0A0F0IG46",
"O13345"
] | [
"IPR016461",
"IPR036388",
"IPR012967",
"IPR036390",
"IPR001077",
"IPR029063"
] | {"IPR036390": [65, 154], "IPR036388": [71, 153], "IPR029063": [158, 404], "IPR016461": [76, 415], "IPR012967": [80, 153], "IPR001077": [206, 387]} | - O-methylsterigmatocystin oxidoreductase
- Demethylsterigmatocystin 6-O-methyltransferase
- O-methyltransferase
- O-methyltransferase
- Aflatoxin biosynthesis regulatory protein | - IPR016461: O-methyltransferase-like (family) [76-415]
- IPR036388: Winged helix-like DNA-binding domain superfamily (homologous_superfamily) [71-153]
- IPR012967: O-methyltransferase, dimerisation domain (domain) [80-153]
- IPR036390: Winged helix DNA-binding domain superfamily (homologous_superfamily) [65-154]
- IPR001077: O-methyltransferase, C-terminal domain (domain) [206-387]
- IPR029063: S-adenosyl-L-methionine-dependent methyltransferase superfamily (homologous_superfamily) [158-404] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016740 (transferase activity), GO:0016741 (transferase activity, transferring one-carbon groups), GO:0008168 (methyltransferase activity), GO:0008171 (O-methyltransferase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0019748 (secondary metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044550 (secondary metabolite biosynthetic process), GO:0044249 (cellular biosynthetic process), GO:0009404 (toxin metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006083 (acetate metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006082 (organic acid metabolic process), GO:1901376 (organic heteropentacyclic compound metabolic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0043385 (mycotoxin metabolic process), GO:0009403 (toxin biosynthetic process), GO:0045122 (aflatoxin biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:0018130 (heterocycle biosynthetic process), GO:0019752 (carboxylic acid metabolic process), GO:0043386 (mycotoxin biosynthetic process), GO:0046222 (aflatoxin metabolic process), GO:1901378 (organic heteropentacyclic compound biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005737 (cytoplasm), GO:0005622 (intracellular anatomical structure) |
O13345 | O-methylsterigmatocystin oxidoreductase | O-methylsterigmatocystin oxidoreductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). Within the aflatoxin pathway, the O-methylsterigmatocystin oxidoreductase aflQ is involved in the last steps in which OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2. The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'- oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring- opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) | 528 | null | MIYSIIICAGALLGFLILQKLLAPKDTRPPLPPGPWRKPIIGNLTDFPPKGTPEWLFWAKHHERYGPMSSLEVMGQTIIMINDAHLGIEIMHKKSALSQMIPDAPFAHMAGWGMSLATERNKQAWKTIRANMKQEIGTRRAIATFHPKMEIGIRRFLLRTLDNPDDLRFHIRKEANAFMMDVAYGYTIAPHGKDELYDLTQQSVRQFSHIFSPGEWSVNFFPILRYVPSWFPGASFQIKAAEYKRTIERMTMVPYLWIKDQVARGCTRPSILLRLLQKGHYESGSHQEQVLVWTNAEFVMGGSDTTVSAVSSFFVAMALYPEVQHQAREELDRVVGPTTLATFEHRSQLPFIDALVKEVFRWHPASPLGAPHITQEDQIWDGYLLPKGALLLPNIWTFTHDPSVYHDPMVFKPERFLERQSSPPETDPMKFVFGFGRRICPGRFVTDEKLFLIACHAISCFLISPKDPGAPEPDWLPGVISQPGPFDLNVVPRSPAHEELIRSIETDHPWKNADATDISQFMARNQMI | [
"GO:0003674",
"GO:0003824",
"GO:0004497",
"GO:0016491"
] | [] | [
"GO:0003674",
"GO:0003824",
"GO:0004497",
"GO:0016491"
] | [] | AF-O13345-F1-model_v6.pdb | 1403190.O13345 | [
"Q12120"
] | [
"IPR017972",
"IPR001128",
"IPR002401",
"IPR050364",
"IPR036396"
] | {"IPR036396": [23, 496], "IPR050364": [6, 507], "IPR001128": [32, 489], "IPR002401": [62, 463], "IPR017972": [433, 442]} | - Sterigmatocystin 8-O-methyltransferase | - IPR017972: Cytochrome P450, conserved site (conserved_site) [433-442]
- IPR001128: Cytochrome P450 (family) [32-489]
- IPR002401: Cytochrome P450, E-class, group I (family) [62-463]
- IPR050364: Cytochrome P450 monooxygenase, fungi (family) [6-507]
- IPR036396: Cytochrome P450 superfamily (homologous_superfamily) [23-496] | Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016491 (oxidoreductase activity), GO:0004497 (monooxygenase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0019748 (secondary metabolic process), GO:0071704 (organic substance metabolic process), GO:0044281 (small molecule metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044550 (secondary metabolite biosynthetic process), GO:0044249 (cellular biosynthetic process), GO:0009404 (toxin metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006083 (acetate metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006082 (organic acid metabolic process), GO:1901376 (organic heteropentacyclic compound metabolic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0043385 (mycotoxin metabolic process), GO:0009403 (toxin biosynthetic process), GO:0045122 (aflatoxin biosynthetic process), GO:0043436 (oxoacid metabolic process), GO:0018130 (heterocycle biosynthetic process), GO:0019752 (carboxylic acid metabolic process), GO:0043386 (mycotoxin biosynthetic process), GO:0046222 (aflatoxin metabolic process), GO:1901378 (organic heteropentacyclic compound biosynthetic process), GO:0032787 (monocarboxylic acid metabolic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005737 (cytoplasm), GO:0012505 (endomembrane system), GO:0043229 (intracellular organelle), GO:0005783 (endoplasmic reticulum), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle) |
Q59Z29 | Iron-regulated transcriptional activator AFT2 | Transcription factor involved in iron metabolism, oxidative stress, surface adhesion, hyphal development and virulence. Functions as a negative regulator of MRS4 expression through the CACCC AFT-type sequence in a gene dose-dependent fashion. Acts as a repressor in flocculation, plastic adhesion, and surface hydrophobicity | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) | 798 | Nucleus | MTDRVTHRVSLDDLNLEKQKFDSKDDIKPWLQDNLQSTKGINVVIERSDTSKIIFKCKNKEKKTKIVESKKTASKTMIRKHTSCPFKIRANYSVRNKVWTLSIVSDEHDHVVDLPRSFVGKNLISNTIPGSSLNVLDSVAPRSNKKGIKPTSEIANTPSVTSYSPSCAVKRNEDVDAPKISSKKARNLTKKPSTQSTRSSSSSDGSSIVSFGSLTSQSSSTSLPENYKGQVPTSMDSMVVEESLTGKSLKPAASHPVKRKNMKANTMKKSKKLKQNPIVVSPIEEDSNLNSFDDANIDLQRQQSLQSPLSHLVQNQDPISLEQNPQLHTVYPQPRHSKQSSSLLKKNQQQDRIPDNMPLQPQENNRTLQNFPLNQFNANEILQNVQQVVRETVKSEILDSPNIDNTYKTDMMDSFVSSVILDYKDYLSSQFLFSLKQNLYDRREATHTNVDLEQNGSNENLFDEQPQHKHNHQHNENQFSYQSQIQNQRQNQNQNQGQNQNQNQSQSQTPGQNSNQNDSQTQIPLQSQTPQDRKSAMQQNWLPGSTPGVGGLIRLSPLLNDNDNNEYAAVAAAAVVGSTPGNPNGNSLENFTHLPGINSSTLNYLMQLPHPSANPNSGGVSSSQPASLMSLQGHQGLLQQQQQQQPMFSMQNSGQQLPPLSSIPKLPSSNNANVNLNSSSTLPLPLNNTGPTLNPSSLLKSTSRNSTNSGNINVNNINNSNNNSNSAFNSVFLNSSITTNPAFIFNSQGNPTNSNQSMVNSIMTTNSNKDGTATSNNNSSGNTSNNLLNDMPNYGPGW | [
"GO:0002831",
"GO:0002833",
"GO:0006355",
"GO:0006357",
"GO:0006873",
"GO:0006879",
"GO:0006950",
"GO:0006979",
"GO:0007155",
"GO:0008150",
"GO:0009267",
"GO:0009607",
"GO:0009889",
"GO:0009891",
"GO:0009893",
"GO:0009987",
"GO:0010468",
"GO:0010556",
"GO:0010557",
"GO:0010570"... | [
"GO:0002831",
"GO:0002833",
"GO:0006355",
"GO:0006357",
"GO:0006873",
"GO:0006879",
"GO:0006950",
"GO:0006979",
"GO:0007155",
"GO:0008150",
"GO:0009267",
"GO:0009607",
"GO:0009889",
"GO:0009891",
"GO:0009893",
"GO:0009987",
"GO:0010468",
"GO:0010556",
"GO:0010557",
"GO:0010570"... | [] | [
"GO:0005575",
"GO:0005622",
"GO:0005634",
"GO:0043226",
"GO:0043227",
"GO:0043229",
"GO:0043231",
"GO:0110165"
] | AF-Q59Z29-F1-model_v6.pdb | 237561.Q59Z29 | [
"Q5AF81",
"Q59SS1"
] | [
"IPR014842"
] | {"IPR014842": [21, 111]} | - Monothiol glutaredoxin
- Ccc1p | - IPR014842: Iron-regulated transcriptional activator AFT (family) [21-111] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0097159 (organic cyclic compound binding), GO:1901363 (heterocyclic compound binding), GO:0003676 (nucleic acid binding), GO:0003677 (DNA binding)
Biological Process (BP): GO:0008150 (biological process), GO:0050789 (regulation of biological process), GO:0065007 (biological regulation), GO:0050896 (response to stimulus), GO:0009987 (cellular process), GO:0048519 (negative regulation of biological process), GO:0009605 (response to external stimulus), GO:0009628 (response to abiotic stimulus), GO:0042221 (response to chemical), GO:0019222 (regulation of metabolic process), GO:0009892 (negative regulation of metabolic process), GO:0050794 (regulation of cellular process), GO:0051716 (cellular response to stimulus), GO:0006950 (response to stress), GO:0048523 (negative regulation of cellular process), GO:0007154 (cell communication), GO:0051172 (negative regulation of nitrogen compound metabolic process), GO:0006979 (response to oxidative stress), GO:0060255 (regulation of macromolecule metabolic process), GO:1901700 (response to oxygen-containing compound), GO:0031324 (negative regulation of cellular metabolic process), GO:0010033 (response to organic substance), GO:0009408 (response to heat), GO:0009991 (response to extracellular stimulus), GO:0010035 (response to inorganic substance), GO:0104004 (cellular response to environmental stimulus), GO:0042594 (response to starvation), GO:0070887 (cellular response to chemical stimulus), GO:0033554 (cellular response to stress), GO:0010605 (negative regulation of macromolecule metabolic process), GO:0071214 (cellular response to abiotic stimulus), GO:0009889 (regulation of biosynthetic process), GO:0051171 (regulation of nitrogen compound metabolic process), GO:0031323 (regulation of cellular metabolic process), GO:0009890 (negative regulation of biosynthetic process), GO:0031668 (cellular response to extracellular stimulus), GO:0009268 (response to pH), GO:0080090 (regulation of primary metabolic process), GO:0071496 (cellular response to external stimulus), GO:0034599 (cellular response to oxidative stress), GO:0010556 (regulation of macromolecule biosynthetic process), GO:0071310 (cellular response to organic substance), GO:0009267 (cellular response to starvation), GO:0062197 (cellular response to chemical stress), GO:0010446 (response to alkaline pH), GO:0010468 (regulation of gene expression), GO:0071467 (cellular response to pH), GO:0031667 (response to nutrient levels), GO:0031326 (regulation of cellular biosynthetic process), GO:0019219 (regulation of nucleobase-containing compound metabolic process), GO:0010558 (negative regulation of macromolecule biosynthetic process), GO:0031327 (negative regulation of cellular biosynthetic process), GO:0051252 (regulation of RNA metabolic process), GO:0042542 (response to hydrogen peroxide), GO:0051253 (negative regulation of RNA metabolic process), GO:1901701 (cellular response to oxygen-containing compound), GO:0031669 (cellular response to nutrient levels), GO:0000302 (response to reactive oxygen species), GO:0045934 (negative regulation of nucleobase-containing compound metabolic process), GO:0071469 (cellular response to alkaline pH), GO:2001141 (regulation of RNA biosynthetic process), GO:0006355 (regulation of DNA-templated transcription), GO:0036244 (cellular response to neutral pH), GO:0043618 (regulation of transcription from RNA polymerase II promoter in response to stress), GO:1902679 (negative regulation of RNA biosynthetic process), GO:0006357 (regulation of transcription by RNA polymerase II), GO:0045892 (negative regulation of DNA-templated transcription), GO:1903507 (negative regulation of nucleic acid-templated transcription), GO:1903506 (regulation of nucleic acid-templated transcription), GO:0000122 (negative regulation of transcription by RNA polymerase II)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle), GO:0005634 (nucleus) |
O67434 | Protein argonaute | A DNA-guided RNA endonuclease. Uses short ssDNA sequences as guides (gDNA) to bind complementary target strands, resulting in cleavage of the target RNA. The cleavage site is 10 nucleotides downstream of the residue base paired with the 5'-end of the gDNA. Binds ssDNA better than ssRNA, binds dsDNA and DNA- RNA hybrids but does not bind dsRNA. A 2 nucleotide 3'-overhang (possibly on the guide strand) may help load nucleic acids into the complex (Probable) | Aquifex aeolicus (strain VF5) | 706 | null | MGKEALLNLYRIEYRPKDTTFTVFKPTHEIQKEKLNKVRWRVFLQTGLPTFRREDEFWCAGKVEKDTLYLTLSNGEIVELKRVGEEEFRGFQNERECQELFRDFLTKTKVKDKFISDFYKKFRDKITVQGKNRKIALIPEVNEKVLKSEEGYFLLHLDLKFRIQPFETLQTLLERNDFNPKRIRVKPIGIDFVGRVQDVFKAKEKGEEFFRLCMERSTHKSSKKAWEELLKNRELREKAFLVVLEKGYTYPATILKPVLTYENLEDEERNEVADIVRMEPGKRLNLIRYILRRYVKALRDYGWYISPEEERAKGKLNFKDTVLDAKGKNTKVITNLRKFLELCRPFVKKDVLSVEIISVSVYKKLEWRKEEFLKELINFLKNKGIKLKIKGKSLILAQTREEAKEKLIPVINKIKDVDLVIVFLEEYPKVDPYKSFLLYDFVKRELLKKMIPSQVILNRTLKNENLKFVLLNVAEQVLAKTGNIPYKLKEIEGKVDAFVGIDISRITRDGKTVNAVAFTKIFNSKGELVRYYLTSYPAFGEKLTEKAIGDVFSLLEKLGFKKGSKIVVHRDGRLYRDEVAAFKKYGELYGYSLELLEIIKRNNPRFFSNEKFIKGYFYKLSEDSVILATYNQVYEGTHQPIKVRKVYGELPVEVLCSQILSLTLMNYSSFQPIKLPATVHYSDKITKLMLRGIEPIKKEGDIMYWL | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004521",
"GO:0004540",
"GO:0140098",
"GO:0140640"
] | [] | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004521",
"GO:0004540",
"GO:0140098",
"GO:0140640"
] | [] | AF-O67434-F1-model_v6.pdb | 224324.aq_1447 | [
"O67435",
"O67433"
] | [
"IPR003165",
"IPR012337",
"IPR003100",
"IPR036397",
"IPR036085"
] | {"IPR036085": [4, 314], "IPR012337": [334, 706], "IPR036397": [492, 705], "IPR003100": [168, 259], "IPR003165": [419, 694]} | - 8-OXO-dGTPase domain (MutT domain)
- Uncharacterized protein aq_1446 | - IPR003165: Piwi domain (domain) [419-694]
- IPR012337: Ribonuclease H-like superfamily (homologous_superfamily) [334-706]
- IPR003100: PAZ domain (domain) [168-259]
- IPR036397: Ribonuclease H superfamily (homologous_superfamily) [492-705]
- IPR036085: PAZ domain superfamily (homologous_superfamily) [4-314] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0006725 (cellular aromatic compound metabolic process), GO:0034641 (cellular nitrogen compound metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:0006139 (nucleobase-containing compound metabolic process), GO:0043170 (macromolecule metabolic process), GO:0046483 (heterocycle metabolic process), GO:0090304 (nucleic acid metabolic process), GO:0010467 (gene expression), GO:0016070 (RNA metabolic process), GO:0006396 (RNA processing), GO:0008380 (RNA splicing), GO:0034470 (ncRNA processing), GO:0034660 (ncRNA metabolic process), GO:0006399 (tRNA metabolic process), GO:0000394 (RNA splicing, via endonucleolytic cleavage and ligation), GO:0008033 (tRNA processing), GO:0006388 (tRNA splicing, via endonucleolytic cleavage and ligation)
Cellular Component (CC): GO:0005575 (cellular component), GO:0032991 (protein-containing complex), GO:1902494 (catalytic complex), GO:0140535 (intracellular protein-containing complex), GO:1905348 (endonuclease complex), GO:1905347 (endodeoxyribonuclease complex) |
A4WYU7 | Protein argonaute | A catalytically inactive argonaute protein. Binds 5'- phosphorylated RNA as the guide (gRNA) and short DNA as target DNA (tDNA); does not bind other nucleic acid combinations, does not bind tDNA alone. Has highest affinity for gRNA that begins with 5'-phospho-U and poor affinity for gRNA with 5'-OH. Upon expression in E.coli, plasmid sequences are found in RsAgo, its induction leads to plasmid degradation and suppression of genes encoded on foreign plasmids, suggesting it may also interfere with transcription. Does not interact with preformed gRNA:tDNA duplexes. Mismatches and nt bulges are tolerated in the ternary complex, however, they significantly reduce the affinity of RsAgo:gRNA for tDNA. Mismatched tDNA can cause dissociation of gRNA from RsAgo. In situ binds 2 populations of RNA (15-19 and 45 nucleotides, nt) and a population of ssDNA 22-24 nt in length. The small sense RNA is probably derived from mRNA degradation and strongly enriched for U in the first and U/C in the second positions. The small DNA is enriched for sequences complementary to the RNA, with 3 nt overhangs on both ends; another nuclease may trim the ends. The sequences are largely derived from exogenous plasmids or genome-encoded foreign elements such as prophages and transposons. Forms a ternary complex with gRNA and double-stranded tDNA only when the tDNA is open | Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter | 777 | null | MAPVQAADEMYDSNPHPDRRQLVSNGFEVNLPDQVEVIVRDLPDPSKVKEERTRLMGYWFVHWFDGKLFHLRIKAGGPNVDGEHRAIRTAEHPWLLRARLDDALEEALPKYAAVKKRPFTFLAQKDELIDAAATAAGLSHRLLNSFKVIPRFALSPKIYEPVDGTTRVGVFVTIGMRYDIEASLRDLLEAGIDLRGMYVVRRKRQPGERGLLGRVRAISDDMVQLFEETDLASVNVNDAKLEGSKENFTRCLSALLGHNYKKLLNALDDQEAGYRTGPRFDDAVRRMGEFLAKKPIRLADNINAQVGDRIVFSNEGQARNVRLAPKVEYVFDRTGAKSAEYAWRGLSQFGPFDRPSFANRSPRILVVYPSSTQGKVENFLSAFRDGMGSNYSGFSKGFVDLMGLTKVEFVMCPVEVSSADRNGAHTKYNSAIEDKLAGAGEVHAGIVVLFEDHARLPDDRNPYIHTKSLLLTLGVPTQQVRMPTVLLEPKSLQYTLQNFSIATYAKLNGTPWTVNHDKAINDELVVGMGLAELSGSRTEKRQRFVGITTVFAGDGSYLLGNVSKECEYEGYSDAIRESMTGILRELKKRNNWRPGDTVRVVFHAHRPLKRVDVASIVFECTREIGSDQNIQMAFVTVSHDHPFVLIDRSERGLEAYKGSTARKGVFAPPRGAISRVGRLTRLLAVNSPQLIKRANTPLPTPLLVSLHPDSTFKDVDYLAEQALKFTSLSWRSTLPAATPVTIFYSERIAELLGRLKSIPNWSSANLNIKLKWSRWFL | [
"GO:0006950",
"GO:0006952",
"GO:0008150",
"GO:0009605",
"GO:0009607",
"GO:0043207",
"GO:0044355",
"GO:0044419",
"GO:0050896",
"GO:0051707",
"GO:0098542",
"GO:0099046",
"GO:0140546",
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0140097"... | [
"GO:0006950",
"GO:0006952",
"GO:0008150",
"GO:0009605",
"GO:0009607",
"GO:0043207",
"GO:0044355",
"GO:0044419",
"GO:0050896",
"GO:0051707",
"GO:0098542",
"GO:0099046",
"GO:0140546"
] | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0140097",
"GO:0140640"
] | [] | AF-A4WYU7-F1-model_v6.pdb | null | null | [
"IPR003165",
"IPR036397",
"IPR012337"
] | {"IPR012337": [321, 777], "IPR036397": [516, 777], "IPR003165": [445, 757]} | - IPR003165: Piwi domain (domain) [445-757]
- IPR036397: Ribonuclease H superfamily (homologous_superfamily) [516-777]
- IPR012337: Ribonuclease H-like superfamily (homologous_superfamily) [321-777] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0006725 (cellular aromatic compound metabolic process), GO:0034641 (cellular nitrogen compound metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:0006139 (nucleobase-containing compound metabolic process), GO:0043170 (macromolecule metabolic process), GO:0046483 (heterocycle metabolic process), GO:0090304 (nucleic acid metabolic process), GO:0090305 (nucleic acid phosphodiester bond hydrolysis), GO:0016070 (RNA metabolic process), GO:0090501 (RNA phosphodiester bond hydrolysis), GO:0090502 (RNA phosphodiester bond hydrolysis, endonucleolytic)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0018995 (host cellular component), GO:0043657 (host cell), GO:0033643 (host cell part), GO:0033646 (host intracellular part), GO:0043656 (host intracellular region), GO:0033647 (host intracellular organelle), GO:0033648 (host intracellular membrane-bounded organelle), GO:0042025 (host cell nucleus) | |
A0A1M5A5Z8 | Protein argonaute | A highly versatile argonaute that uses 5'-phospho- and 5'- OH- guide RNA (gRNA) or DNA (gDNA) to cleave target RNA or ssDNA (tDNA) in all possible combinations; has no detectable activity in the absence of guide. Uses short guide sequences (18-21 nucleotides (nt) on average) to bind complementary target nucleic acids resulting in target cleavage in a site-specific manner. Using 5'-phospho-gRNA or 5'-OH-gRNA the cleavage site is 10 nt downstream of the target residue base-paired with the 5'-end of the gRNA, using 5'-phospho-gDNA the cleavage site is 11 nucleotides (nt) downstream, while with 5'-OH-gDNA the cleavage site is 9 nt downstream | Marinitoga hydrogenitolerans (strain DSM 16785 / JCM 12826 / AT1271) | 640 | null | MYLNLYEIKIPYRVKRLYYFNKENDPKEFARNLSRVNNIRFNDSKDLVWLEIPDIDFKITPQQAEKYKIEKNEIIGEKEDSDLFVKTIYRYIKKKFIDNNFYYKRGNNYISINDKFPLDSNTNVNAHLTYKIKLYKINERYYISVLPKFTFLSDKPALESPIKSTYLFNIKSGKTFPYISGLNGVLKIDLGENGIKEVLFPENYYFNFTSKEAEKFGFSKEIHNIYKEKIFSGYKKIKQSLYFLEDIININNYNLTMDKKIYVNIEYEFKKGISRNIKDVFKYSFYKNDQKIKIAFFFSSKKQIYEIQRSLKMLFQNKNSIFYQTIYEMGFSKVIFLREPKTNSSAFMYNPETFEISNKDFFENLEGNIMAIIILDKFLGNIDSLIQKFPENLILQPILKEKLEKIQPYIIKSYVYKMGNFIPECQPYVIRNLKDKNKTLYIGIDLSHDNYLKKSNLAISAVNNFGDIIYLNKYKNLELNEKMNLDIVEKEYIQILNEYYERNKNYPENIIVLRDGRYLEDIEIIKNILNIENIKYSLIEVNKSVNINSCEDLKEWIIKLSDNNFIYYPKTYFNQKGVEIKIIENNTDYNNEKILEQVYSLTRVVHPTPYVNYRLPYPLQVVNKVALTELEWKLYIPYMK | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004521",
"GO:0004536",
"GO:0004540",
"GO:0140097",
"GO:0140098",
"GO:0140640"
] | [] | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004521",
"GO:0004536",
"GO:0004540",
"GO:0140097",
"GO:0140098",
"GO:0140640"
] | [] | AF-A0A1M5A5Z8-F1-model_v6.pdb | 1122195.SAMN02745164_02104 | [
"A0A1M5A5N0",
"A0A1M5A679",
"A0A1M5A5P1"
] | [
"IPR054434",
"IPR054387",
"IPR003165",
"IPR012337",
"IPR036397"
] | {"IPR012337": [410, 626], "IPR036397": [433, 604], "IPR054387": [13, 75], "IPR054434": [262, 430], "IPR003165": [369, 633]} | - CRISPR-associated endonuclease Cas1
- TOTE conflict system primase domain-containing protein
- CRISPR-associated endoribonuclease Cas2 | - IPR054434: Argonaute, middle domain, bacteria (domain) [262-430]
- IPR054387: Argonaute, N-terminal domain, bacteria (domain) [13-75]
- IPR003165: Piwi domain (domain) [369-633]
- IPR012337: Ribonuclease H-like superfamily (homologous_superfamily) [410-626]
- IPR036397: Ribonuclease H superfamily (homologous_superfamily) [433-604] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0006725 (cellular aromatic compound metabolic process), GO:0034641 (cellular nitrogen compound metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:0006139 (nucleobase-containing compound metabolic process), GO:0043170 (macromolecule metabolic process), GO:0046483 (heterocycle metabolic process), GO:0090304 (nucleic acid metabolic process), GO:0010467 (gene expression), GO:0016070 (RNA metabolic process), GO:0006396 (RNA processing), GO:0006397 (mRNA processing), GO:0016071 (mRNA metabolic process), GO:0036260 (RNA capping), GO:0006370 (7-methylguanosine mRNA capping), GO:0009452 (7-methylguanosine RNA capping)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0018995 (host cellular component), GO:0043657 (host cell), GO:0033643 (host cell part), GO:0033646 (host intracellular part), GO:0043656 (host intracellular region), GO:0033647 (host intracellular organelle), GO:0033648 (host intracellular membrane-bounded organelle), GO:0042025 (host cell nucleus) |
H2J4R4 | Protein argonaute | An RNA-guided ssDNA endonuclease that may play a role in defense against invading mobile genetic elements. Uses short 5'-OH- ssRNA sequences as guides (gRNA) to bind complementary target DNA (tDNA) or target RNA resulting in target cleavage. The cleavage site is 10 nucleotides (nt) downstream of the target residue base-paired with the 5'-end of the gRNA. Reaction rates are fastest on 5'-OH-gRNA:tDNA followed by 5'-OH-gRNA:target RNA. gRNA between 17-21 nt supports equivalent rates of cleavage, has no preferred 5'-nt. Has weak activity on tDNA with 5'-phospho-gRNA, yielding products 1-2 nt longer. Unlike other characterized prokaryotic Ago proteins symmetric mismatches centered around the cleavage site reduce cleavage efficiency | Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3) | 639 | Cytoplasm | MYLNLYKIDIPKKIKRLYFYNPDMEPKLFARNLSRVNNFKFQDSNDLVWIEIPDIDFQITPKNVFQYKVEKEEIIKEEEDKKLFVKTLYKYIKKLFLDNDFYFKKGNNFISNSEVFSLDSNENVNAHLTYKIKIHNISNEYYLSILPKFTFLSKEPALESAIKSGYLYNIKSGKSFPYISGLDGILKIDIGNNQIVEVAYPENYLFNFTTRDAEKYGFSKEVHEIYKNKVFEGFKKIPKTLGFLNKITNLNENYQLKDGYKIFINVIYKFKNGESRYAKDVFKYSFYKNEQPLKAIFFFSSKKQFFEVQKSLKELFHNKHSVFYRAAAELGFSKVEFLRDSKTKSSAFLYNPEEFTVKNTEFINQIEDNVMAIVLLDKYIGNIDPLVRNFPDNLILQPILKEKLEDIKPFIIKSYVYKMGNFIPECKPFILKKMEDKEKNLYIGIDLSHDTYARKTNLCIAAVDNTGDILYIGKHKNLELNEKMNLDILEKEYIKAFEKYIEKFNVSPENVFILRDGRFIEDIEIIKNFISYNDTKYTLVEVNKNTNINSYDDLKEWIIKLDENTYIYYPKTFLNQKGVEVKILENNTDYTIEEIIEQIYLLTRVAHSTPYTNYKLPYPLHIANKVALTDYEWKLYIPY | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0140097",
"GO:0140640"
] | [] | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0140097",
"GO:0140640"
] | [] | AF-H2J4R4-F1-model_v6.pdb | 443254.Marpi_0405 | [
"H2J4R1",
"H2J4R2",
"H2J4R3"
] | [
"IPR054434",
"IPR054387",
"IPR003165",
"IPR012337",
"IPR036397"
] | {"IPR012337": [415, 627], "IPR036397": [436, 634], "IPR054387": [12, 76], "IPR054434": [263, 432], "IPR003165": [394, 634]} | - CRISPR-associated endonuclease Cas1
- CRISPR-associated endoribonuclease Cas2
- TOTE conflict system primase domain-containing protein | - IPR054434: Argonaute, middle domain, bacteria (domain) [263-432]
- IPR054387: Argonaute, N-terminal domain, bacteria (domain) [12-76]
- IPR003165: Piwi domain (domain) [394-634]
- IPR012337: Ribonuclease H-like superfamily (homologous_superfamily) [415-627]
- IPR036397: Ribonuclease H superfamily (homologous_superfamily) [436-634] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0006725 (cellular aromatic compound metabolic process), GO:0034641 (cellular nitrogen compound metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:0006139 (nucleobase-containing compound metabolic process), GO:0043170 (macromolecule metabolic process), GO:0046483 (heterocycle metabolic process), GO:0090304 (nucleic acid metabolic process), GO:0010467 (gene expression), GO:0016070 (RNA metabolic process), GO:0006396 (RNA processing), GO:0006397 (mRNA processing), GO:0016071 (mRNA metabolic process), GO:0036260 (RNA capping), GO:0006370 (7-methylguanosine mRNA capping), GO:0009452 (7-methylguanosine RNA capping)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0018995 (host cellular component), GO:0043657 (host cell), GO:0033643 (host cell part), GO:0033646 (host intracellular part), GO:0043656 (host intracellular region), GO:0030430 (host cell cytoplasm), GO:0033655 (host cell cytoplasm part), GO:0033647 (host intracellular organelle), GO:0033648 (host intracellular membrane-bounded organelle) |
Q58717 | Protein argonaute | A DNA-guided ssDNA endonuclease that may play a role in defense against invading genetic elements. Uses short ssDNA sequences as guides (gDNA) to bind complementary target strands, resulting in slicing of the target DNA (tDNA). Endonucleolytically cleaves tDNA (the gDNA indicates where to cleave); two major and two minor products are seen which correspond to cleavage sites between nucleotides 9/10, 10/11, 13/14, and 14/15 downstream of the target residue base-paired with the 5'-end of the gDNA. Efficient guide-dependent tDNA cleavage requires a minimal length of 15 bp and is maximal at 19 bp. Prefers gDNA with 5'-phosphorylated purines and 3'- pyrimidines; changing these bases alters the cleavage activity and patterns. Also has guide-independent activity on tDNA called 'chopping'. Probably a first round of guide- independent activity on an invading plasmid or virus would generate guide DNAs for subsequent, more efficient, guide-dependent degradation of invading nucleic acids. Has no activity on substrate with a mismatch at positions 10 and 11, on ssDNA or RNA, nor on DNA:RNA hybrids. Digests longer (750 bp) dsDNA as well as circular plasmid and naked genomic DNA, but not chromatin, in a guide DNA-independent manner. Addition of endogenous histone A3 protects DNA from cleavage, while cleavage is insensitive to methylation. When plasmid encoding active or mutated protein (Ala-541) is transformed into Sulfolobus acidocaldarius about 25-fold fewer transformants are found with active protein; reduced levels of plasmid are found in wild-type transformed cells. While S.acidocaldarius grows at a similar temperature to M.jannaschii (70 to 80 degrees Celsius) it has very different histone-like proteins, which presumably do not protect against MjAgo. Binds ssDNA, dsDNA and DNA-RNA hybrids; binding is most efficient with dsDNA | Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM | 713 | null | MVLNKVTYKINAYKIKEEFIPKEVHFYRIKSFVNEAFNFYRFVNFYGGMIINKKDKSFVLPYKVDNKVLKYKDGNNEIPIDIEYIKSLKLEYVKPEIAEKLVRGYLKSVHKIEPELSRIIKNIRKHKVVENIKVESYCEYEVKKHDGDYYLILNFRHTASITKHLWDFVNRDKALLEEYVGKKIIFKPNPKVRYTISLVDAPNPQKIEEIMSHIIKYYKWSEDMVKSTFGEIDYNQPIMYCEEILEPFAPQFCNLVFYMDELDSYILKELQSYWRLSNENKGKIINEIAKKLRFIDNTPKELEFMKFNNTPLLVKDVNKNPTKIYSTNTLFTWIYNQNAKIYLPYDVPEIIRNKNLLTYILIDEEIKDELKAIKDKVNKMFRNYNKIANKTELPKFNYANRWKYFSTDDIRGIIKEIKSEFNDEICFALIIGKEKYKDNDYYEILKKQLFDLKIISQNILWENWRKDDKGYMTNNLLIQIMGKLGIKYFILDSKTPYDYIMGLDTGLGIFGNHRVGGCTVVYDSEGKIRRIQPIETPAPGERLHLPYVIEYLENKANIDMENKNILFLRDGFIQNSERNDLKEISKELNSNIEVISIRKNNKYKVFTSDYRIGSVFGNDGIFLPHKTPFGSNPVKLSTWLRFNCGNEEGLKINESIMQLLYDLTKMNYSALYGEGRYLRIPAPIHYADKFVKALGKNWKIDEELLKHGFLYFI | [
"GO:0006950",
"GO:0006952",
"GO:0008150",
"GO:0009605",
"GO:0009607",
"GO:0043207",
"GO:0044355",
"GO:0044419",
"GO:0050896",
"GO:0051707",
"GO:0098542",
"GO:0099046",
"GO:0140546",
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0140097"... | [
"GO:0006950",
"GO:0006952",
"GO:0008150",
"GO:0009605",
"GO:0009607",
"GO:0043207",
"GO:0044355",
"GO:0044419",
"GO:0050896",
"GO:0051707",
"GO:0098542",
"GO:0099046",
"GO:0140546"
] | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0140097",
"GO:0140640"
] | [] | AF-Q58717-F1-model_v6.pdb | 243232.MJ_1321 | [
"Q58907",
"Q58719",
"Q58716",
"Q57841",
"Q58718"
] | [
"IPR003100",
"IPR054390",
"IPR012337",
"IPR003165",
"IPR054436",
"IPR036085",
"IPR036397"
] | {"IPR036085": [5, 305], "IPR012337": [301, 713], "IPR036397": [494, 713], "IPR054390": [22, 90], "IPR054436": [163, 258], "IPR003100": [164, 257], "IPR003165": [426, 699]} | - Uncharacterized protein MJ0398
- Reverse gyrase
- DNA double-strand break repair protein Mre11
- DNA double-strand break repair Rad50 ATPase
- Ribonuclease VapC4 | - IPR003100: PAZ domain (domain) [164-257]
- IPR054390: Argonaute, N-terminal domain, archaea (domain) [22-90]
- IPR012337: Ribonuclease H-like superfamily (homologous_superfamily) [301-713]
- IPR003165: Piwi domain (domain) [426-699]
- IPR054436: Argonaute, PAZ domain, methanocaldococcus (domain) [163-258]
- IPR036085: PAZ domain superfamily (homologous_superfamily) [5-305]
- IPR036397: Ribonuclease H superfamily (homologous_superfamily) [494-713] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0006725 (cellular aromatic compound metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:0034641 (cellular nitrogen compound metabolic process), GO:0006139 (nucleobase-containing compound metabolic process), GO:0043170 (macromolecule metabolic process), GO:0046483 (heterocycle metabolic process), GO:0090304 (nucleic acid metabolic process), GO:0010467 (gene expression), GO:0016070 (RNA metabolic process), GO:0006396 (RNA processing), GO:0006397 (mRNA processing), GO:0016071 (mRNA metabolic process), GO:0036260 (RNA capping), GO:0006370 (7-methylguanosine mRNA capping), GO:0009452 (7-methylguanosine RNA capping)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0018995 (host cellular component), GO:0043657 (host cell), GO:0033643 (host cell part), GO:0033646 (host intracellular part), GO:0043656 (host intracellular region), GO:0030430 (host cell cytoplasm), GO:0033655 (host cell cytoplasm part), GO:0033647 (host intracellular organelle), GO:0033648 (host intracellular membrane-bounded organelle) |
Q8U3D2 | Protein argonaute | A DNA-guided ssDNA endonuclease that may play a role in defense against invading mobile genetic elements. Uses short 5'- phospho-ssDNA sequences as guides (gDNA) to bind complementary target strands, resulting in cleavage of the target DNA (tDNA). Endonucleolytically cleaves DNA in short dsDNA (the gDNA indicates where to cleave on the tDNA). Efficient guide-dependent target DNA cleavage requires a minimal gDNA length of 15 nucleotides (nt) and works up to at least 31 nt. Overexpression decreases plasmid transformation efficiency. Has no appreciable activity with gRNA or on target RNA. Also has guide-independent activity on plasmid DNA called 'chopping'. The cleavage site is 10 nucleotides (nt) downstream of the target residue base-paired with the 5'-end of the gDNA, cleavage is insensitive to adenine methylation. DNA cleavage produces 5'-phosphomonoesters (as it can be ligated by T4 DNA ligase) | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) | 770 | null | MKAKVVINLVKINKKIIPDKIYVYRLFNDPEEELQKEGYSIYRLAYENVGIVIDPENLIIATTKELEYEGEFIPEGEISFSELRNDYQSKLVLRLLKENGIGEYELSKLLRKFRKPKTFGDYKVIPSVEMSVIKHDEDFYLVIHIIHQIQSMKTLWELVNKDPKELEEFLMTHKENLMLKDIASPLKTVYKPCFEEYTKKPKLDHNQEIVKYWYNYHIERYWNTPEAKLEFYRKFGQVDLKQPAILAKFASKIKKNKNYKIYLLPQLVVPTYNAEQLESDVAKEILEYTKLMPEERKELLENILAEVDSDIIDKSLSEIEVEKIAQELENKIRVRDDKGNSVPISQLNVQKSQLLLWTNYSRKYPVILPYEVPEKFRKIREIPMFIILDSGLLADIQNFATNEFRELVKSMYYSLAKKYNSLAKKARSTNEIGLPFLDFRGKEKVITEDLNSDKGIIEVVEQVSSFMKGKELGLAFIAARNKLSSEKFEEIKRRLFNLNVISQVVNEDTLKNKRDKYDRNRLDLFVRHNLLFQVLSKLGVKYYVLDYRFNYDYIIGIDVAPMKRSEGYIGGSAVMFDSQGYIRKIVPIKIGEQRGESVDMNEFFKEMVDKFKEFNIKLDNKKILLLRDGRITNNEEEGLKYISEMFDIEVVTMDVIKNHPVRAFANMKMYFNLGGAIYLIPHKLKQAKGTPIPIKLAKKRIIKNGKVEKQSITRQDVLDIFILTRLNYGSISADMRLPAPVHYAHKFANAIRNEWKIKEEFLAEGFLYFV | [
"GO:0006950",
"GO:0006952",
"GO:0008150",
"GO:0009605",
"GO:0009607",
"GO:0043207",
"GO:0044355",
"GO:0044419",
"GO:0050896",
"GO:0051707",
"GO:0098542",
"GO:0099046",
"GO:0140546",
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0005488"... | [
"GO:0006950",
"GO:0006952",
"GO:0008150",
"GO:0009605",
"GO:0009607",
"GO:0043207",
"GO:0044355",
"GO:0044419",
"GO:0050896",
"GO:0051707",
"GO:0098542",
"GO:0099046",
"GO:0140546"
] | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0005488",
"GO:0030145",
"GO:0036094",
"GO:0043167",
"GO:0043169",
"GO:0046872",
"GO:0046914",
"GO:0140097",
"GO:0140640"
] | [] | AF-Q8U3D2-F1-model_v6.pdb | 186497.PF0537 | null | [
"IPR003100",
"IPR012337",
"IPR057272",
"IPR003165",
"IPR021103",
"IPR036085",
"IPR036397",
"IPR055253"
] | {"IPR036085": [4, 323], "IPR012337": [325, 770], "IPR036397": [547, 770], "IPR055253": [19, 78], "IPR021103": [146, 272], "IPR003100": [154, 272], "IPR057272": [333, 753], "IPR003165": [473, 756]} | - IPR003100: PAZ domain (domain) [154-272]
- IPR012337: Ribonuclease H-like superfamily (homologous_superfamily) [325-770]
- IPR057272: Piwi domain, nematodes (domain) [333-753]
- IPR003165: Piwi domain (domain) [473-756]
- IPR021103: Argonaute PAZ domain, archaea (domain) [146-272]
- IPR036085: PAZ domain superfamily (homologous_superfamily) [4-323]
- IPR036397: Ribonuclease H superfamily (homologous_superfamily) [547-770]
- IPR055253: Argonaute, N-terminal domain, thermococcales (domain) [19-78] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0006725 (cellular aromatic compound metabolic process), GO:0034641 (cellular nitrogen compound metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:0006139 (nucleobase-containing compound metabolic process), GO:0043170 (macromolecule metabolic process), GO:0046483 (heterocycle metabolic process), GO:0090304 (nucleic acid metabolic process), GO:0010467 (gene expression), GO:0016070 (RNA metabolic process), GO:0006396 (RNA processing), GO:0034470 (ncRNA processing), GO:0034660 (ncRNA metabolic process), GO:0006399 (tRNA metabolic process), GO:0008033 (tRNA processing)
Cellular Component (CC): GO:0005575 (cellular component), GO:0032991 (protein-containing complex), GO:1902494 (catalytic complex), GO:0140535 (intracellular protein-containing complex), GO:1905348 (endonuclease complex), GO:1905347 (endodeoxyribonuclease complex) | |
Q31N05 | Protein argonaute | A DNA-guided ssDNA endonuclease that might play a role in defense against invading mobile genetic elements. Uses short ssDNA sequences as guides (gDNA) to bind complementary target strands, resulting in cleavage of the target DNA (tDNA). The cleavage site is 10 nucleotides (nt) downstream of the target residue base-paired with the 5'-end of the gDNA. Both 5'-P and 5'-OH gDNAs confer activity; a 5'-OH guide cleaves between nt 10-11 and nt 11-12. Guide DNA mismatches in the seed (nt 2-9) can enhance activity, mismatches 1-5 nt after the cleavage site block activity. Has no appreciable activity with guide RNA or on target RNA. In situ binds to 5'-phosphorylated DNA 14-20 nt in length; small DNA maps over the chromosome and plasmid with some preference for the replication origin and the probable termination site. Also has weak guide-independent nuclease activity on DNA called 'chopping'. Overexpression of wild-type or catalytically inactive mutant has no visible effect during growth under continuous high light for up to a month | Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) | 735 | null | MDLLSNLRRSSIVLNRFYVKSLSQSDLTAYEYRCIFKKTPELGDEKRLLASICYKLGAIAVRIGSNIITKEAVRPEKLQGHDWQLVQMGTKQLDCRNDAHRCALETFERKFLERDLSASSQTEVRKAAEGGLIWWVVGAKGIEKSGNGWEVHRGRRIDVSLDAEGNLYLEIDIHHRFYTPWTVHQWLEQYPEIPLSYVRNNYLDERHGFINWQYGRFTQERPQDILLDCLGMSLAEYHLNKGATEEEVQQSYVVYVKPISWRKGKLTAHLSRRLSPSLTMEMLAKVAEDSTVCDREKREIRAVFKSIKQSINQRLQEAQKTASWILTKTYGISSPAIALSCDGYLLPAAKLLAANKQPVSKTADIRNKGCAKIGETSFGYLNLYNNQLQYPLEVHKCLLEIANKNNLQLSLDQRRVLSDYPQDDLDQQMFWQTWSSQGIKTVLVVMPWDSHHDKQKIRIQAIQAGIATQFMVPLPKADKYKALNVTLGLLCKAGWQPIQLESVDHPEVADLIIGFDTGTNRELYYGTSAFAVLADGQSLGWELPAVQRGETFSGQAIWQTVSKLIIKFYQICQRYPQKLLLMRDGLVQEGEFQQTIELLKERKIAVDVISVRKSGAGRMGQEIYENGQLVYRDAAIGSVILQPAERSFIMVTSQPVSKTIGSIRPLRIVHEYGSTDLELLALQTYHLTQLHPASGFRSCRLPWVLHLADRSSKEFQRIGQISVLQNISRDKLIAV | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0140097",
"GO:0140640"
] | [] | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0140097",
"GO:0140640"
] | [] | AF-Q31N05-F1-model_v6.pdb | 1140.Synpcc7942_1534 | null | [
"IPR040895",
"IPR003165",
"IPR036397",
"IPR012337"
] | {"IPR012337": [307, 732], "IPR036397": [507, 735], "IPR040895": [185, 276], "IPR003165": [441, 720]} | - IPR040895: Argonaute, PAZ domain (domain) [185-276]
- IPR003165: Piwi domain (domain) [441-720]
- IPR036397: Ribonuclease H superfamily (homologous_superfamily) [507-735]
- IPR012337: Ribonuclease H-like superfamily (homologous_superfamily) [307-732] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0006725 (cellular aromatic compound metabolic process), GO:0034641 (cellular nitrogen compound metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:0044260 (cellular macromolecule metabolic process), GO:0006139 (nucleobase-containing compound metabolic process), GO:0043170 (macromolecule metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006259 (DNA metabolic process), GO:0090304 (nucleic acid metabolic process), GO:0006260 (DNA replication), GO:0006261 (DNA-templated DNA replication)
Cellular Component (CC): GO:0005575 (cellular component), GO:0032991 (protein-containing complex), GO:1902494 (catalytic complex), GO:0140535 (intracellular protein-containing complex), GO:1905348 (endonuclease complex), GO:1902555 (endoribonuclease complex) | |
Q746M7 | Protein argonaute | A DNA-guided ssDNA endonuclease. Uses short ssDNA sequences as guides (gDNA, also called small interfering DNA, siDNA) to bind complementary DNA target strands, resulting in cleavage of the target DNA (tDNA). The cleavage site is 10 nucleotides (nt) downstream of the target residue base-paired with the 5'-end of the gDNA. Plays a role in completion of DNA replication, participates in decatenating replicated DNA and plasmid. In situ purifies with 5'-phosphorylated long DNA (about 1160 nt, maps to the whole chromosome and plasmid), 25-35 nt RNAs that map to the whole chromosome and 15-18 nt DNA that maps to the replication terminus region (ter) on the chromosome and plasmid. Most short DNA starts with dC. Has been shown to have guide sequence-independent dsDNase activity called 'chopping', which requires unstable DNA (high AT-content, multiple mismatches or low salt conditions), and could be used to generate gDNA. Preferentially binds tDNA with dC at its 3'- terminus. Has also been shown to have no detectable guide sequence-independent dsDNase activity. The latter study proposes TtAgo may acquire gDNA from nicked dsDNA, by binding to 5'-phosphorylated-dC nicks, then cleaving 10 nt away on the opposite strand; subsequently an exonuclease (maybe AddA-AddB helicase/nuclease) trims the ends to generate the gDNA (Probable) | Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) | 685 | null | MNHLGKTEVFLNRFALRPLNPEELRPWRLEVVLDPPPGREEVYPLLAQVARRAGGVTVRMGDGLASWSPPEVLVLEGTLARMGQTYAYRLYPKGRRPLDPKDPGERSVLSALARRLLQERLRRLEGVWVEGLAVYRREHARGPGWRVLGGAVLDLWVSDSGAFLLEVDPAYRILCEMSLEAWLAQGHPLPKRVRNAYDRRTWELLRLGEEDPKELPLPGGLSLLDYHASKGRLQGREGGRVAWVADPKDPRKPIPHLTGLLVPVLTLEDLHEEEGSLALSLPWEERRRRTREIASWIGRRLGLGTPEAVRAQAYRLSIPKLMGRRAVSKPADALRVGFYRAQETALALLRLDGAQGWPEFLRRALLRAFGASGASLRLHTLHAHPSQGLAFREALRKAKEEGVQAVLVLTPPMAWEDRNRLKALLLREGLPSQILNVPLREEERHRWENALLGLLAKAGLQVVALSGAYPAELAVGFDAGGRESFRFGGAACAVGGDGGHLLWTLPEAQAGERIPQEVVWDLLEETLWAFRRKAGRLPSRVLLLRDGRVPQDEFALALEALAREGIAYDLVSVRKSGGGRVYPVQGRLADGLYVPLEDKTFLLLTVHRDFRGTPRPLKLVHEAGDTPLEALAHQIFHLTRLYPASGFAFPRLPAPLHLADRLVKEVGRLGIRHLKEVDREKLFFV | [
"GO:0006950",
"GO:0006952",
"GO:0008150",
"GO:0009605",
"GO:0009607",
"GO:0043207",
"GO:0044355",
"GO:0044419",
"GO:0050896",
"GO:0051707",
"GO:0098542",
"GO:0099046",
"GO:0140546",
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0005488"... | [
"GO:0006950",
"GO:0006952",
"GO:0008150",
"GO:0009605",
"GO:0009607",
"GO:0043207",
"GO:0044355",
"GO:0044419",
"GO:0050896",
"GO:0051707",
"GO:0098542",
"GO:0099046",
"GO:0140546"
] | [
"GO:0003674",
"GO:0003824",
"GO:0004518",
"GO:0004519",
"GO:0004520",
"GO:0004536",
"GO:0005488",
"GO:0030145",
"GO:0036094",
"GO:0043167",
"GO:0043169",
"GO:0046872",
"GO:0046914",
"GO:0140097",
"GO:0140640"
] | [] | AF-Q746M7-F1-model_v6.pdb | null | null | [
"IPR040895",
"IPR012337",
"IPR003165",
"IPR054764",
"IPR054763",
"IPR003100",
"IPR036397"
] | {"IPR012337": [282, 685], "IPR036397": [467, 685], "IPR054764": [26, 96], "IPR003100": [169, 265], "IPR040895": [181, 263], "IPR054763": [327, 444], "IPR003165": [404, 671]} | - IPR040895: Argonaute, PAZ domain (domain) [181-263]
- IPR012337: Ribonuclease H-like superfamily (homologous_superfamily) [282-685]
- IPR003165: Piwi domain (domain) [404-671]
- IPR054764: Argonaute, N-terminal domain, thermus (domain) [26-96]
- IPR054763: Argonaute, middle domain (domain) [327-444]
- IPR003100: PAZ domain (domain) [169-265]
- IPR036397: Ribonuclease H superfamily (homologous_superfamily) [467-685] | Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0016032 (viral process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0019058 (viral life cycle), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0019079 (viral genome replication), GO:0044249 (cellular biosynthetic process), GO:0006725 (cellular aromatic compound metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:0034641 (cellular nitrogen compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:0006139 (nucleobase-containing compound metabolic process), GO:0043170 (macromolecule metabolic process), GO:0046483 (heterocycle metabolic process), GO:0009059 (macromolecule biosynthetic process), GO:1901362 (organic cyclic compound biosynthetic process), GO:0044271 (cellular nitrogen compound biosynthetic process), GO:0090304 (nucleic acid metabolic process), GO:0034654 (nucleobase-containing compound biosynthetic process), GO:0019438 (aromatic compound biosynthetic process), GO:0018130 (heterocycle biosynthetic process), GO:0016070 (RNA metabolic process), GO:0032774 (RNA biosynthetic process), GO:0097659 (nucleic acid-templated transcription), GO:0006351 (DNA-templated transcription), GO:0006366 (transcription by RNA polymerase II)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005737 (cytoplasm), GO:0031974 (membrane-enclosed lumen), GO:0043233 (organelle lumen), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043228 (non-membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle), GO:0070013 (intracellular organelle lumen), GO:0043232 (intracellular non-membrane-bounded organelle), GO:0031981 (nuclear lumen), GO:0005730 (nucleolus), GO:0005634 (nucleus) | |
Q8R4S7 | Aryl hydrocarbon receptor | Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer. Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation. Xenobiotics can act as ligands: upon xenobiotic-binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists. Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands. Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity. Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1. Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1. The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription | Mus caroli (Ryukyu mouse) (Ricefield mouse) | 854 | Cytoplasm. Nucleus. Note=Initially cytoplasmic; upon binding with ligand and interaction with a HSP90, it translocates to the nucleus | MSSGANITYASRKRRKPVQKTVKPIPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDVINKLDKLSVLRLSVSYLRAKSFFDVALKSTPADRNGGQDQCRAQIRDWQDLQEGEFLLQALNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNPSQCTDSAQGVDEAHGPPQTAVYYTPDQLPPENASFMERCFRCRLRCLLDNSSGFLAMNFQGRLKYLHGQNKKGKDGALLPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPSGCDAKGQLILGYTEVELCTRGSGYQFIHAADMLHCAESHIRMIKTGESGMTVFRLLAKHSRWRWVQSNARLIYRNGRPDYIIATQRPLTDEEGREHLQKRSMSLPFMFATGEAVLYEISSPFSPIMDPLPIRAKSNTSRKDWAPQSTPSKDSFHPSSLMSALIQQDESIYLCPPSSPAPLDSHFLMGSVSKCGSWQDSFAAAGSEAALKHEQIGHAQDVNLALSGGPSELFPDNKNNDLYSIMRNLGIDFEDIRSMQNEEFFRTDSTATGEVDFKDIDITDEILTYVQDSLNNSTLLNSACQQQPVTQHLSCMLQERLQLEQQQQQQLQQPPTQALEPQQQLCQMECPQQDLGQRHTQINGSFASWNPTPPVSFNCPQQELKHYHLFSSLQGTAQEFPYKPEVDGMPYTQNFAPCNQPLLPEHSKSVQLDFPGRDFEPSLHPTTSNLDFVSCLQVPENQSHGINSQSAMVSPQTYYAGAMSMYQCQPGPQHTPVDQTQYSSEIPGSQAFLSKVQSRGVFNETYPSDLSSIGHAAQTTGHLHHLAEARPLPDITPGGFL | [
"GO:0008150",
"GO:0009987",
"GO:0042221",
"GO:0050896",
"GO:0051716",
"GO:0070887",
"GO:1904612",
"GO:1904613",
"GO:0000981",
"GO:0003674",
"GO:0003700",
"GO:0004879",
"GO:0038023",
"GO:0060089",
"GO:0098531",
"GO:0140110",
"GO:0005575",
"GO:0005622",
"GO:0005634",
"GO:0043226"... | [
"GO:0008150",
"GO:0009987",
"GO:0042221",
"GO:0050896",
"GO:0051716",
"GO:0070887",
"GO:1904612",
"GO:1904613"
] | [
"GO:0000981",
"GO:0003674",
"GO:0003700",
"GO:0004879",
"GO:0038023",
"GO:0060089",
"GO:0098531",
"GO:0140110"
] | [
"GO:0005575",
"GO:0005622",
"GO:0005634",
"GO:0043226",
"GO:0043227",
"GO:0043229",
"GO:0043231",
"GO:0110165"
] | AF-Q8R4S7-F1-model_v6.pdb | null | null | [
"IPR036638",
"IPR035965",
"IPR033348",
"IPR013767",
"IPR011598",
"IPR000014",
"IPR013655",
"IPR001610",
"IPR039091"
] | {"IPR036638": [30, 80], "IPR035965": [120, 386], "IPR039091": [6, 811], "IPR011598": [26, 87], "IPR033348": [27, 87], "IPR000014": [111, 384], "IPR013767": [112, 185], "IPR013655": [298, 380], "IPR001610": [346, 387]} | - IPR036638: Helix-loop-helix DNA-binding domain superfamily (homologous_superfamily) [30-80]
- IPR035965: PAS domain superfamily (homologous_superfamily) [120-386]
- IPR033348: Aryl hydrocarbon receptor, basic helix-loop-helix domain (domain) [27-87]
- IPR013767: PAS fold (domain) [112-185]
- IPR011598: Myc-type, basic helix-loop-helix (bHLH) domain (domain) [26-87]
- IPR000014: PAS domain (domain) [111-384]
- IPR013655: PAS fold-3 (domain) [298-380]
- IPR001610: PAC motif (repeat) [346-387]
- IPR039091: Aryl hydrocarbon receptor/Aryl hydrocarbon receptor repressor (family) [6-811] | Molecular Function (MF): GO:0003674 (molecular function), GO:0060089 (molecular transducer activity), GO:0005488 (binding), GO:0140110 (transcription regulator activity), GO:0003700 (DNA-binding transcription factor activity), GO:0097159 (organic cyclic compound binding), GO:1901363 (heterocyclic compound binding), GO:0038023 (signaling receptor activity), GO:0005515 (protein binding), GO:0008134 (transcription factor binding), GO:0004879 (nuclear receptor activity), GO:0051087 (chaperone binding), GO:0042802 (identical protein binding), GO:0003676 (nucleic acid binding), GO:0031072 (heat shock protein binding), GO:0098531 (ligand-activated transcription factor activity), GO:0005102 (signaling receptor binding), GO:0046983 (protein dimerization activity), GO:0000981 (DNA-binding transcription factor activity, RNA polymerase II-specific), GO:0051879 (Hsp90 protein binding), GO:0001067 (transcription regulatory region nucleic acid binding), GO:0046982 (protein heterodimerization activity), GO:0140297 (DNA-binding transcription factor binding), GO:0042803 (protein homodimerization activity), GO:0003677 (DNA binding), GO:0043565 (sequence-specific DNA binding), GO:0000976 (transcription cis-regulatory region binding), GO:0061629 (RNA polymerase II-specific DNA-binding transcription factor binding), GO:0003690 (double-stranded DNA binding), GO:1990837 (sequence-specific double-stranded DNA binding), GO:0000987 (cis-regulatory region sequence-specific DNA binding)
Biological Process (BP): GO:0008150 (biological process), GO:0065007 (biological regulation), GO:0050896 (response to stimulus), GO:0050789 (regulation of biological process), GO:0009987 (cellular process), GO:0042221 (response to chemical), GO:0019222 (regulation of metabolic process), GO:0050794 (regulation of cellular process), GO:0051716 (cellular response to stimulus), GO:0009410 (response to xenobiotic stimulus), GO:0070887 (cellular response to chemical stimulus), GO:0009889 (regulation of biosynthetic process), GO:0051171 (regulation of nitrogen compound metabolic process), GO:0060255 (regulation of macromolecule metabolic process), GO:0031323 (regulation of cellular metabolic process), GO:0080090 (regulation of primary metabolic process), GO:0071466 (cellular response to xenobiotic stimulus), GO:0010556 (regulation of macromolecule biosynthetic process), GO:0031326 (regulation of cellular biosynthetic process), GO:0019219 (regulation of nucleobase-containing compound metabolic process), GO:0051252 (regulation of RNA metabolic process), GO:0010468 (regulation of gene expression), GO:2001141 (regulation of RNA biosynthetic process), GO:0006355 (regulation of DNA-templated transcription), GO:0006357 (regulation of transcription by RNA polymerase II), GO:1903506 (regulation of nucleic acid-templated transcription)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005829 (cytosol), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005737 (cytoplasm), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle), GO:0005634 (nucleus) |
End of preview. Expand in Data Studio
🧬 BioReason-Pro
Advancing Protein Function Prediction with
Multimodal Biological Reasoning
BioReason-Pro RL Reasoning Data
Training dataset for reinforcement learning (GRPO) optimization of BioReason-Pro. Contains proteins with GO term annotations, InterPro domains, STRING protein-protein interactions, and protein metadata.
Citation
If you find this work useful, please cite our papers:
@article {Fallahpour2026.03.19.712954,
author = {Fallahpour, Adibvafa and Seyed-Ahmadi, Arman and Idehpour, Parsa and Ibrahim, Omar and Gupta, Purav and Naimer, Jack and Zhu, Kevin and Shah, Arnav and Ma, Shihao and Adduri, Abhinav and G{\"u}loglu, Talu and Liu, Nuo and Cui, Haotian and Jain, Arihant and de Castro, Max and Fallahpour, Amirfaham and Cembellin-Prieto, Antonio and Stiles, John S. and Nem{\v c}ko, Filip and Nevue, Alexander A. and Moon, Hyungseok C. and Sosnick, Lucas and Markham, Olivia and Duan, Haonan and Lee, Michelle Y. Y. and Salvador, Andrea F. M. and Maddison, Chris J. and Thaiss, Christoph A. and Ricci-Tam, Chiara and Plosky, Brian S. and Burke, Dave P. and Hsu, Patrick D. and Goodarzi, Hani and Wang, Bo},
title = {BioReason-Pro: Advancing Protein Function Prediction with Multimodal Biological Reasoning},
elocation-id = {2026.03.19.712954},
year = {2026},
doi = {10.64898/2026.03.19.712954},
publisher = {Cold Spring Harbor Laboratory},
URL = {https://www.biorxiv.org/content/early/2026/03/20/2026.03.19.712954},
eprint = {https://www.biorxiv.org/content/early/2026/03/20/2026.03.19.712954.full.pdf},
journal = {bioRxiv}
}
@misc{fallahpour2025bioreasonincentivizingmultimodalbiological,
title={BioReason: Incentivizing Multimodal Biological Reasoning within a DNA-LLM Model},
author={Adibvafa Fallahpour and Andrew Magnuson and Purav Gupta and Shihao Ma and Jack Naimer and Arnav Shah and Haonan Duan and Omar Ibrahim and Hani Goodarzi and Chris J. Maddison and Bo Wang},
year={2025},
eprint={2505.23579},
archivePrefix={arXiv},
primaryClass={cs.LG},
url={https://arxiv.org/abs/2505.23579},
}
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