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Database: UniProt
Entry: A0A1Y2IDU7_PYCCO
LinkDB: A0A1Y2IDU7_PYCCO
Original site: A0A1Y2IDU7_PYCCO 
ID   A0A1Y2IDU7_PYCCO        Unreviewed;      1066 AA.
AC   A0A1Y2IDU7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   SubName: Full=Assimilatory sulfite reductase {ECO:0000313|EMBL:OSC98662.1};
GN   ORFNames=PYCCODRAFT_1480395 {ECO:0000313|EMBL:OSC98662.1};
OS   Trametes coccinea BRFM310.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=1353009 {ECO:0000313|EMBL:OSC98662.1, ECO:0000313|Proteomes:UP000193067};
RN   [1] {ECO:0000313|EMBL:OSC98662.1, ECO:0000313|Proteomes:UP000193067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM310 {ECO:0000313|EMBL:OSC98662.1,
RC   ECO:0000313|Proteomes:UP000193067};
RX   PubMed=26692083; DOI=10.1186/s13068-015-0407-8;
RA   Couturier M., Navarro D., Chevret D., Henrissat B., Piumi F.,
RA   Ruiz-Duenas F.J., Martinez A.T., Grigoriev I.V., Riley R., Lipzen A.,
RA   Berrin J.G., Master E.R., Rosso M.N.;
RT   "Enhanced degradation of softwood versus hardwood by the white-rot fungus
RT   Pycnoporus coccineus.";
RL   Biotechnol. Biofuels 8:216-216(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; KZ084135; OSC98662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2IDU7; -.
DR   STRING; 1353009.A0A1Y2IDU7; -.
DR   OrthoDB; 5488444at2759; -.
DR   Proteomes; UP000193067; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd06207; CyPoR_like; 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:UP000193067}.
FT   DOMAIN          680..912
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1066 AA;  114705 MW;  40CF9E9C9CC7ADFC CRC64;
     MASATQSGTS TPFSSTTTLS APPTPKLKAA ANDLQRIAES GAITASTLIE YIASRTASSS
     SVFVYDLAEQ AGFGSLTKSW AEAGNGTAPV VSLQTRAGAG LSLVGRLSQG SSKDVAKGAI
     LTAYTTPSGL AAMVQSLTYL PPATPTSRLV IQVPTVTPVG EHFALSPTLA PLTPALPLLP
     EGFTVLISAT PQEAVELAAL SYQLTNTHVI HLFDHHGATR ETGHVAVPPV ILPEPGLTLQ
     EGLKKAGYSA FEYAGDQNAE TVVVLLNGPL ALTAKALARR VSGLGVVIVR VLRPWDEEAL
     RSVLPASVKK VHVFDDVPTE TTQGALYLDV FATLLNPLER GPVVKAHRVV PARTQQFLAD
     PVAFLTFVTD LLPFPQPIPS LAAPNLKKLL FFSTPQSVSA LPRMVETVFL PHKALTSRLL
     TDYDVFSKPG GVEADRIVLS PKQDDSPFIP LSAILPISPR SSGVADFVAI LDQQLLKSHD
     VLSHAASGSP VLVVTDATAA ELVASLPSEV QDLIRARNLR LCILDAKDLA ADLSKGNAHV
     QKALENVIAL LAFLRLYLGQ AATEELVAKV ARADLGDSVQ GVQLTQLVSK SWEGLVEVEL
     PAAEATPDAE KPAAAQLKPF EFNAIAVETG EGDTVVNGAR LATWHDAAKH ILFPSAFTPA
     GVAHTAPEEQ NPALRPELPE RTFLITCTVN RRLTPLEYDR NVFHLEFDTR GTGLKYEIGE
     ALGVHGWNDA SEVLEFCQWY GVDPDRLITL PVPGSDGARV HTRTVFQALQ QQVDLFGKPT
     KTFYTELAEH ASNIADKYAL RFIGSPEGSA TFKKLSEKDT VTFADILRRY ESARPGIEVL
     CELIGDIKPR HYSIASSQAV VGDRVDLLVV SVEWVTPSGS PRYGQCTRYL AGLKPGQKVT
     VSIKPSVMKL PPDHKQPIIM AGLGTGAAPF RAFLQHRALL AAQGVPVGPT YYYFGSRHQS
     QEYLYGEEIE AFLLDGTITR AGLAFSRDGP RKVYIQHKMR EHGADLARML WDERGVFYLC
     GPTWPVPDVY EALVDALVGH AGVSREEAGA FLEGLKEEER YVLEVY
//
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