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PUS9_YEAST
ID   PUS9_YEAST              Reviewed;         462 AA.
AC   Q12069; D6VRV8; Q6B2P8;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=tRNA pseudouridine(32) synthase, mitochondrial;
DE            EC=5.4.99.28;
DE   AltName: Full=tRNA pseudouridine synthase 9;
DE   AltName: Full=tRNA pseudouridylate synthase 9;
DE   AltName: Full=tRNA-uridine isomerase 9;
DE   Flags: Precursor;
GN   Name=PUS9; OrderedLocusNames=YDL036C; ORFNames=D2743;
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=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
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).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=15466869; DOI=10.1074/jbc.m409581200;
RA   Behm-Ansmant I., Grosjean H., Massenet S., Motorin Y., Branlant C.;
RT   "Pseudouridylation at position 32 of mitochondrial and cytoplasmic tRNAs
RT   requires two distinct enzymes in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 279:52998-53006(2004).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=25219674; DOI=10.1016/j.cell.2014.08.028;
RA   Schwartz S., Bernstein D.A., Mumbach M.R., Jovanovic M., Herbst R.H.,
RA   Leon-Ricardo B.X., Engreitz J.M., Guttman M., Satija R., Lander E.S.,
RA   Fink G., Regev A.;
RT   "Transcriptome-wide mapping reveals widespread dynamic-regulated
RT   pseudouridylation of ncRNA and mRNA.";
RL   Cell 159:148-162(2014).
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-32 in
CC       mitochondrial transfer RNAs. {ECO:0000269|PubMed:15466869,
CC       ECO:0000269|PubMed:25219674}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(32) in tRNA = pseudouridine(32) in tRNA;
CC         Xref=Rhea:RHEA:42544, Rhea:RHEA-COMP:10107, Rhea:RHEA-COMP:10108,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.28;
CC         Evidence={ECO:0000269|PubMed:15466869, ECO:0000269|PubMed:25219674};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:15466869}.
CC   -!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC       {ECO:0000305}.
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DR   EMBL; Z71781; CAA96453.1; -; Genomic_DNA.
DR   EMBL; Z74084; CAA98595.1; -; Genomic_DNA.
DR   EMBL; AY692682; AAT92701.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11818.1; -; Genomic_DNA.
DR   PIR; S67569; S67569.
DR   RefSeq; NP_010248.1; NM_001180095.1.
DR   AlphaFoldDB; Q12069; -.
DR   SMR; Q12069; -.
DR   BioGRID; 32022; 41.
DR   DIP; DIP-5399N; -.
DR   MINT; Q12069; -.
DR   STRING; 4932.YDL036C; -.
DR   iPTMnet; Q12069; -.
DR   MaxQB; Q12069; -.
DR   PaxDb; Q12069; -.
DR   PRIDE; Q12069; -.
DR   EnsemblFungi; YDL036C_mRNA; YDL036C; YDL036C.
DR   GeneID; 851525; -.
DR   KEGG; sce:YDL036C; -.
DR   SGD; S000002194; PUS9.
DR   VEuPathDB; FungiDB:YDL036C; -.
DR   eggNOG; KOG1919; Eukaryota.
DR   GeneTree; ENSGT00420000029802; -.
DR   HOGENOM; CLU_016902_12_4_1; -.
DR   InParanoid; Q12069; -.
DR   OMA; VAYHDEM; -.
DR   BioCyc; MetaCyc:G3O-29460-MON; -.
DR   BioCyc; YEAST:G3O-29460-MON; -.
DR   BRENDA; 5.4.99.28; 984.
DR   PRO; PR:Q12069; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q12069; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IDA:UniProtKB.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IDA:SGD.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR   InterPro; IPR006224; PsdUridine_synth_RluC/D_CS.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00005; rluA_subfam; 1.
DR   PROSITE; PS01129; PSI_RLU; 1.
DR   PROSITE; PS50889; S4; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Mitochondrion; Reference proteome; RNA-binding; Transit peptide;
KW   tRNA processing.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..462
FT                   /note="tRNA pseudouridine(32) synthase, mitochondrial"
FT                   /id="PRO_0000162756"
FT   DOMAIN          127..188
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT   ACT_SITE        238
FT                   /evidence="ECO:0000250|UniProtKB:P0AA37"
FT   CONFLICT        458
FT                   /note="W -> R (in Ref. 3; AAT92701)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  53399 MW;  300E676D8E3819F0 CRC64;
     MQRNNRLRNL FTVPVIMARQ LKRNALSAGL AFAGNATSNE FDEHLQNEVE REREIQKKKK
     IKRTQSKKSP DLINKSTFQS RTIGSKKEKH RQLDPEYEIV IDGPLRKIKP YHFTYRTFCK
     ERWRDKKLVD VFISEFRDRE SEYYKRTIEN GDVHINDETA DLSTVIRNGD LITHQVHRHE
     PPVTSRPIKV IFEDDNIMVI DKPSGIPVHP TGRYRFNTIT KMLQNNLGFV VNPCNRLDRL
     TSGLMFLAKT PKGADNIGDQ LKAREVTKEY VAKVVGEFPE TEVIVEKPLK LIEPRLALNA
     VCQMDEKGAK HAKTVFNRIS YDGKTSIVKC KPLTGRSHQI RVHLQYLGHP IANDPIYSND
     EVWGNNLGKG GQADFDIVIT KLDEIGKRKP AKSWFHSNGG YGEVLRQEKC SICESDLYTD
     PGPNDLDLWL HAYLYESTET EEGTEKKKWC YKTEYPEWAL RR
 
 
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