ID A8NXY0_COPC7 Unreviewed; 1056 AA.
AC A8NXY0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Assimilatory sulfite reductase {ECO:0000313|EMBL:EAU84917.2};
GN ORFNames=CC1G_00436 {ECO:0000313|EMBL:EAU84917.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU84917.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU84917.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU84917.2}.
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DR EMBL; AACS02000005; EAU84917.2; -; Genomic_DNA.
DR RefSeq; XP_001837300.2; XM_001837248.2.
DR AlphaFoldDB; A8NXY0; -.
DR STRING; 240176.A8NXY0; -.
DR GeneID; 6013857; -.
DR KEGG; cci:CC1G_00436; -.
DR VEuPathDB; FungiDB:CC1G_00436; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_003662_0_0_1; -.
DR InParanoid; A8NXY0; -.
DR OMA; MIVAVNW; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06207; CyPoR_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861}.
FT DOMAIN 671..902
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 114596 MW; CB4B50756A185B9C CRC64;
MPLSNSGWTT PLSSSSTLSS PPSPRLDPKS GVTPFENPRV QASQVVEYIA SRNTSTSVVY
VYDVAEQVGF GTLTKEWSKN SEKDIAPVVD LQTRAGAGLS LVGRLSQGTS VEAGRGSVLT
AYTTPNGLAL MAPAFAHLPS ANSSSRLVVQ VPTVSAVGDT LSLSPTLSPL SSIWPLLPEG
VAVLLSSTPQ QSVDFASIVY RLQNTHAVHL FDHSTSSREL GVTLREPQLS GQSLEELLQS
VGHSFFKYTG DAAAETVLVF LNGPLALAAE AVVAKLSGVG VLTVNVLRPW SDAALRAALP
ETVRAVHVVD EVPNRLVQGS LFLDVFSALY GEKSKPTVQA HRVAPSETQE FLNDNGAFVH
FISGIVPGSG DVAIPLSGLR TVLLFGVPRS PLAVVPQVFE DFFATHKNIN SRLLTDYDVF
SKEGGIFASR LVLSPKKAGE NSLPIPFILP LDQGSAGHAD FLAVLDQGLL KTHDVLKHAK
RASVVLVSSS WSTEEFIASL PASASALVHE RNLRIFTINT KAIASDLTSS ESGSANEAVQ
NLILYLAFLR LYLGATATEQ VVLQVAQKTF GESLFGVSLL KINARTWAEA NLVPLAEDFA
IESPISPLKD FDFNAIAVDA QDGNVVVNGA RLASWHDAAK HLLFPSVYSH PTQPSDELYP
QDPALRPEVP DRTFLVTCTV NKRLTPLEYD RNVFHLEFDT SGTGLKYAIG EALGVHGWND
EQEVLDFCNW YGVDPNRLVT IPVPGDETKV HTRTVLQALQ QQIDLFGKPP KSFYTDLAEY
ATSTVDKYAL RFIGSPEGSS TFKKLSEKDT VTFADILRKY PSARPGIERL CELIGDIAPR
HYSIASSQAV VGDRVDLLVV TVDWTTPEGA TRYGQCTRYL AGLKIGQKVT VSIKPSVMKL
PPNPQQPLIM AGLGTGAAPF RAFLQHLAWL AAQGKEIGPV YYYFGSRYQA AEYLYGEEIE
AWILDNIITR AGLAFSRDGP KKVYIQHRML EDAEALADML YNKQGVFYLC GPTWPVPDVY
EALVNAIVKL KGITPAEAGE FLESLKEEER YVLEVY
//