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IRC15_YEAST
ID   IRC15_YEAST             Reviewed;         499 AA.
AC   Q02733; D6W3Z5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=Increased recombination centers protein 15;
GN   Name=IRC15; OrderedLocusNames=YPL017C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 6400 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
CC   -!- CAUTION: Although strongly related to the LPD1 dihydrolipoyl
CC       dehydrogenase, it lacks the redox-active disulfide bond suggesting that
CC       it has no dehydrogenase activity. {ECO:0000305}.
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DR   EMBL; U36624; AAB68170.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11411.1; -; Genomic_DNA.
DR   PIR; S63465; S63465.
DR   RefSeq; NP_015308.1; NM_001183831.1.
DR   AlphaFoldDB; Q02733; -.
DR   SMR; Q02733; -.
DR   BioGRID; 36160; 137.
DR   IntAct; Q02733; 3.
DR   STRING; 4932.YPL017C; -.
DR   MaxQB; Q02733; -.
DR   PaxDb; Q02733; -.
DR   PRIDE; Q02733; -.
DR   EnsemblFungi; YPL017C_mRNA; YPL017C; YPL017C.
DR   GeneID; 856090; -.
DR   KEGG; sce:YPL017C; -.
DR   SGD; S000005938; IRC15.
DR   VEuPathDB; FungiDB:YPL017C; -.
DR   eggNOG; KOG1335; Eukaryota.
DR   GeneTree; ENSGT00550000074844; -.
DR   HOGENOM; CLU_016755_1_2_1; -.
DR   InParanoid; Q02733; -.
DR   OMA; PVDIQMR; -.
DR   BioCyc; YEAST:G3O-33936-MON; -.
DR   PRO; PR:Q02733; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q02733; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005874; C:microtubule; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IDA:SGD.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:SGD.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:SGD.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:SGD.
DR   GO; GO:0034453; P:microtubule anchoring; IMP:SGD.
DR   GO; GO:0007020; P:microtubule nucleation; IDA:SGD.
DR   GO; GO:0006312; P:mitotic recombination; IMP:SGD.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:SGD.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome.
FT   CHAIN           1..499
FT                   /note="Increased recombination centers protein 15"
FT                   /id="PRO_0000268179"
FT   BINDING         47..56
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   499 AA;  54156 MW;  1EF2A29D4327031B CRC64;
     MGGEDEILST MEDFAAVYDV LVIGCGPGGF TAAMQASQAG LLTACVDQRA SLGGAYLVDG
     AVPSKTLLYE SYLYRLLQQQ ELIEQRGTRL FPAKFDMQAA QSALKHNIEE LGNVYKRELS
     KNNVTVYKGT AAFKDPHHVE IAQRGMKPFI VEAKYIVVAT GSAVIQCPGV AIDNDKIISS
     DKALSLDYIP SRFTIMGGGT IGLEIACIFN NLGSRVTIVE SQSEICQNMD NELASATKTL
     LQCQGIAFLL DTRVQLAEAD AAGQLNITLL NKVSKKTYVH HCDVLMVSIG RRPLLKGLDI
     SSIGLDERDF VENVDVQTQS LLKYPHIKPI GDVTLGPMLA LKAEEQAIRA IQSIGCTGSD
     GTSNCGFPPN VLYCQPQIGW VGYTEEGLAK ARIPYQKGRV LFSQNVRYNT LLPREENTTV
     SPFIKVLIDS RDMKILGVHM INDDANELLS QASMAVSLGL TAHDVCKVPF PHPSLSESFK
     QAVQLAMANG TSPGVHVRE
 
 
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