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Database: UniProt
Entry: E3QHE4_COLGM
LinkDB: E3QHE4_COLGM
Original site: E3QHE4_COLGM 
ID   E3QHE4_COLGM            Unreviewed;      1159 AA.
AC   E3QHE4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   22-FEB-2023, entry version 48.
DE   SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:EFQ30306.1};
GN   ORFNames=GLRG_05450 {ECO:0000313|EMBL:EFQ30306.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; GG697348; EFQ30306.1; -; Genomic_DNA.
DR   RefSeq; XP_008094326.1; XM_008096135.1.
DR   AlphaFoldDB; E3QHE4; -.
DR   STRING; 645133.E3QHE4; -.
DR   EnsemblFungi; EFQ30306; EFQ30306; GLRG_05450.
DR   GeneID; 24410815; -.
DR   VEuPathDB; FungiDB:GLRG_05450; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_003662_1_0_1; -.
DR   OrthoDB; 5488444at2759; -.
DR   Proteomes; UP000008782; Unassembled WGS sequence.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:EnsemblFungi.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:EnsemblFungi.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:EnsemblFungi.
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; IPR033412; PFOR_II.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
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   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 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:UP000008782}.
FT   DOMAIN          772..1003
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1159 AA;  126482 MW;  F755C36214B9C8DF CRC64;
     MQFKQQESNG SAAVLDAPKS HTSSASQNKV SSTLPFGQPV ALSSISGPTY VTAQLLVQQV
     AFLLSDKIFS YSAPTFDLDL AAKVWSEAKE QNIHGETTDL VQLQTRTGAG ALALGYIFSP
     DFDLAKRHLP QTLLTPSLSL KNLRGALDQL SLLYGVAPPF VAHVAALDYD VANGLVPDYD
     TALRTAEDLG LGLVASSSAY ETQHMALFAT LMAALMPTLH IYDGVRLARE TSRIVDALSR
     SGIADLYNSI TSESTGVSER AAISSKVAGL LDVFNKHLDP TEDHESQHTA LLATLMTALT
     PNLGVEDGVK LAKKTLEASD ALNKKGVAET YKKISSEVQS LNKRLDDAGK VVELLRLFNN
     ELGTAYNLFE YHGHSDADAV LVVFGSAEAQ LAKQVVGRLA ADGVKVGAVN VRVYRPFVEE
     AFLASIPESA RTIAVLGQVK DELSVNDASL QSALYTDVLA SVSFSGKWRQ DPAVSDVKYA
     ASETPTPQAI ADIFGKLLDA NAEPKPFPAL VQAHQYTFWD VDSSVVADAP VVVSNLLSRE
     STSNVYVHES FDNLLQGGVV RTDIRSSKKA IEAPYAVEEA DVVAVGDEKL FKDLDILKSV
     KAGGKLLLNL PGFKEEDLEK RLSAVILKQV RDKSVELYVL DTTQSTVSEK EAKAAKVLLE
     FAFLQVARPD ITAEEVAKIA LSEGFALSLT ETQEALGQSL RKVDSQAAWA ELPADVVASP
     LPATIKPNSF VGFDKEEPED TPQLADWQSV AKGLAFKEAY GTQTSLRPEL PVKTHTITVK
     ENRRLTPQTY DRNIFHIEFD LGDSGLTYNI GEALGIHAEN DEDEVREFIG WYGLDPEAVV
     QVPAREDPNA LETRTVYQSL KQNIDVLGKP PKRFYEALSE FASDEREKAV LASLGGAEGA
     ADFKKRAEVD YVTYVDILQE FPSARPAFHD LARIISPLKR REYSIASAQA VTPNSVALMI
     VVVDWVDPRG RNRFGHATRY LSALPVGATV VASVKPSVMK LPASPKAPLI MAGLGTGLAP
     FRAFVQYRAL QKSRGEEIGS ILLYLGSRHQ REEYLYGEEW EAYVDAGVIT HLGAAFSRDQ
     PRKIYIQDRM RESMRDVVQS YIRDEGSFYL CGPTWPVPDV TDVLMEAINT EAKMSGKKVN
     ARNEIEKLKE DGRYVLEVY
//
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