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YB63_SCHPO
ID   YB63_SCHPO              Reviewed;         571 AA.
AC   Q09744;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Uncharacterized FAD-binding protein C12C2.03c;
GN   ORFNames=SPBC12C2.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC       reductase family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA90816.1; -; Genomic_DNA.
DR   PIR; T39378; T39378.
DR   RefSeq; NP_596020.1; NM_001021928.2.
DR   AlphaFoldDB; Q09744; -.
DR   SMR; Q09744; -.
DR   BioGRID; 276688; 25.
DR   STRING; 4896.SPBC12C2.03c.1; -.
DR   iPTMnet; Q09744; -.
DR   MaxQB; Q09744; -.
DR   PaxDb; Q09744; -.
DR   PRIDE; Q09744; -.
DR   EnsemblFungi; SPBC12C2.03c.1; SPBC12C2.03c.1:pep; SPBC12C2.03c.
DR   GeneID; 2540152; -.
DR   KEGG; spo:SPBC12C2.03c; -.
DR   PomBase; SPBC12C2.03c; -.
DR   VEuPathDB; FungiDB:SPBC12C2.03c; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_001570_17_5_1; -.
DR   InParanoid; Q09744; -.
DR   OMA; LCCGGGC; -.
DR   PhylomeDB; Q09744; -.
DR   Reactome; R-SPO-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-SPO-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR   Reactome; R-SPO-203615; eNOS activation.
DR   Reactome; R-SPO-392154; Nitric oxide stimulates guanylate cyclase.
DR   Reactome; R-SPO-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-SPO-5578775; Ion homeostasis.
DR   Reactome; R-SPO-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-SPO-9033241; Peroxisomal protein import.
DR   PRO; PR:Q09744; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0030586; F:[methionine synthase] reductase activity; ISS:PomBase.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; ISM:PomBase.
DR   GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0050667; P:homocysteine metabolic process; IBA:GO_Central.
DR   GO; GO:0009086; P:methionine biosynthetic process; ISS:PomBase.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.80; -; 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   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..571
FT                   /note="Uncharacterized FAD-binding protein C12C2.03c"
FT                   /id="PRO_0000167630"
FT   DOMAIN          135..389
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  63977 MW;  D2EE992789307249 CRC64;
     MAPSVATSLK AEILPSPRTS SPSSNFKTCV SNENGCINCR CSPSEPHESA NVDESVNKLS
     KTFSKLSLNP TFQALNMDLG LLHENITLDR IPKVPENHVS LIDIDEARAK EDPNFQIHST
     PSRMPPHYVQ PHPPFSVFPA PILDVRELTK PGAVKRVFHF ELDVSNYPLP EGEEWMVGGS
     FGVMAPNNEE DVDELLQLLH INPDQADAPV LLKTDGGRWP TIWAEDTPRE LVTTRRELLK
     WTVEFMSVAP KKQLIRLLAE YAKDDTERQV LLFLVSRLGQ RAFCDLRDHN VTLITLLKAF
     PSVQLPLDHL LTVLPQLMPR WYSLSNDPKV SNNVLEFAVT VVEINKVEGG TRSGIGSGFL
     KRLALRFLNG ERDLVLPMYR GLHKNAFATH FASDGPMCLI GAGVGVAPFR GFVQRRLTNA
     TCAGKVWVFH GCRDQELDEL YHGEWENPLQ KSSDDDASST VSQQTETEMD SFEVKKDGTS
     GPNHLVVESR SHQHAYVQDE IRHRGDIVWS VLSHPHGKVY LCGGKKGFLD GVENALIDVC
     VQYGKMSRLE ATQQLALWQS PLNLKYIKEI W
 
 
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