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Database: UniProt
Entry: S9PSP5_SCHOY
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Original site: S9PSP5_SCHOY 
ID   S9PSP5_SCHOY            Unreviewed;       579 AA.
AC   S9PSP5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=FAD binding protein {ECO:0000313|EMBL:EPX70513.1};
GN   ORFNames=SOCG_04693 {ECO:0000313|EMBL:EPX70513.1};
OS   Schizosaccharomyces octosporus (strain yFS286) (Fission yeast)
OS   (Octosporomyces octosporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=483514 {ECO:0000313|EMBL:EPX70513.1};
RN   [1] {ECO:0000313|EMBL:EPX70513.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YFS286 {ECO:0000313|EMBL:EPX70513.1};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [2] {ECO:0000313|EMBL:EPX70513.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YFS286 {ECO:0000313|EMBL:EPX70513.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Nusbaum C., Russ C., Rhind N., Niki H., Allshire R., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Birren B.;
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; KE503208; EPX70513.1; -; Genomic_DNA.
DR   RefSeq; XP_013020739.1; XM_013165285.1.
DR   AlphaFoldDB; S9PSP5; -.
DR   EnsemblFungi; EPX70513; EPX70513; SOCG_04693.
DR   GeneID; 25033655; -.
DR   VEuPathDB; FungiDB:SOCG_04693; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_001570_17_5_1; -.
DR   OMA; LCCGGGC; -.
DR   OrthoDB; 9164at2759; -.
DR   Proteomes; UP000016088; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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}.
FT   DOMAIN          143..398
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   579 AA;  64771 MW;  12CC1C14C26F0861 CRC64;
     MAPSVISPKH QHLSPNPPSS SSSSTTTAIN LPHSSSSAAE LGCVNCRCSS NKDANESAHL
     DDPSQDLADS ISNLVLNPQF NSLNLDLHLL HDNITIDRIP KLPARNVSFA PLTPEAKAAD
     SFHSSPLISE KMPPSFVQPH PPFHVFPSPV INIRELTKPN AYKRVFHFEI DVSHYPLPEG
     EEWMVGGSFG LMAPNDDAVV NHLLHLLQIP DDVADAPILL KTNGGRWPTI WAEDVPRELP
     TTRRELLKWS SDFMSAPPKK QLIRLLAEYA QNPTEKKILL FLVSRLGQRA FCDLRVNNNV
     TLLTLLEAFP SIRLPLDHLL SVLPQLMPRW YSLSNDPAQH NGVLEFAVAL VEIEKVGGGV
     HYGIGSGFLY QLAKQWMDGK RDLVLPMFRG LHRNAFVTHF TSDGPMCLIG TGVGIAPFRG
     FVQRRLMNAS CAGKVWIFHG CRDSELDELY HGEWENPSDN SRSNSPRPQD KQNNTEVDTL
     EFHNDAREGP HHMVVESRSR RKVYVQDELR MKGDIVWNVL NHPNGKIYLC GGKQGLLRGV
     DEALKDICMK YGNLSQNEAA NQLAAWQNPL SLKYIKEIW
//
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