ID S3C878_OPHP1 Unreviewed; 685 AA.
AC S3C878;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 03-MAY-2023, entry version 29.
DE SubName: Full=Fad binding domain-containing protein {ECO:0000313|EMBL:EPE09699.1};
GN ORFNames=F503_07475 {ECO:0000313|EMBL:EPE09699.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE09699.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE09699.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE09699.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KE148147; EPE09699.1; -; Genomic_DNA.
DR AlphaFoldDB; S3C878; -.
DR STRING; 1262450.S3C878; -.
DR VEuPathDB; FungiDB:F503_07475; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_17_5_1; -.
DR OMA; LCCGGGC; -.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000016923; Unassembled WGS sequence.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 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; SSF63380; Riboflavin synthase 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:UP000016923}.
FT DOMAIN 268..540
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 205..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 75437 MW; 1B0B576AAB13A1FE CRC64;
MSANVAHSRL SEIFNEEAAA AVAAAAATAA AAENILPAQL RAPSIAPSLT YSESGDDRDE
YDVDEAHLSS DDEVASIATP RRRRASTRLI AQNAADIQRI TGESSTQLIN RCCGGGCCLK
LDSKADGVQY ERVSLPDNEA YRSLNLKIGD IPTTLTSVAD IPEQIAYLLP LSSLTAPPTT
SEAEGAVTPT LEAAKVEAPT KALAEIPAEE QKDEEQSDSK QKTPESQEAD AEVIEGLKSL
VIEPEVEEML DLDTTIQPPL FVQPHPPYHV FPARIHNARE LTRPGAEKRT YHFDLDVTDY
PSETGMDFKV GGAIGVSAPN DEKLVDNILD LLMIPRFLRD KKVVLRTTKG RWPTVWGDDK
PRELVATRRE LLTWCSDIQS YPPTKPLLRI LAEYASDENE KKALLFLCSA EGQGAFCDFR
TGPHVSLQQM LSAFPSSKPP LDVLLSILQP QMPRFYSLSN DPHVSVAKNG DTTRRVVEIA
VTVHETSDWL TGTRTGIGSG FFERQALRYI KARERGEEID VYVPMFKGLM ANPLAKQFVP
DGPMLLIGAG VGIAPFRGFV QRRLKTANCA NKVWVLQGIR DSLVDELYSG EWGVHEDEVK
RVVESRSGTG RYVQEEVRQQ ADLVWFVINS VDGRVFVCGS TRGMGEGVQE ALIDVAMEKG
NLGREEARKF WDLKAEVGQY IAETW
//