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PRP5_YEAST
ID   PRP5_YEAST              Reviewed;         849 AA.
AC   P21372; D6VQN3;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 198.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE            EC=3.6.4.13;
GN   Name=PRP5; Synonyms=RNA5; OrderedLocusNames=YBR237W; ORFNames=YBR1603;
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 [GENOMIC DNA].
RX   PubMed=2349233; DOI=10.1073/pnas.87.11.4236;
RA   Dalbadie-Mcfarland G., Abelson J.;
RT   "PRP5: a helicase-like protein required for mRNA splicing in yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:4236-4240(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
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   [4]
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   [5]
RP   FUNCTION, AND MUTAGENESIS OF GLY-293.
RX   PubMed=8405998; DOI=10.1101/gad.7.10.1909;
RA   Ruby S.W., Chang T.-H., Abelson J.;
RT   "Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact
RT   to promote U2 snRNP binding to pre-mRNA.";
RL   Genes Dev. 7:1909-1925(1993).
RN   [6]
RP   FUNCTION.
RX   PubMed=8065365; DOI=10.1128/mcb.14.9.6337-6349.1994;
RA   Wells S.E., Ares M. Jr.;
RT   "Interactions between highly conserved U2 small nuclear RNA structures and
RT   Prp5p, Prp9p, Prp11p, and Prp21p proteins are required to ensure integrity
RT   of the U2 small nuclear ribonucleoprotein in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 14:6337-6349(1994).
RN   [7]
RP   FUNCTION.
RX   PubMed=8969184; DOI=10.1074/jbc.271.52.33261;
RA   O'Day C.L., Dalbadie-McFarland G., Abelson J.;
RT   "The Saccharomyces cerevisiae Prp5 protein has RNA-dependent ATPase
RT   activity with specificity for U2 small nuclear RNA.";
RL   J. Biol. Chem. 271:33261-33267(1996).
RN   [8]
RP   FUNCTION.
RX   PubMed=8969185; DOI=10.1074/jbc.271.52.33268;
RA   Wiest D.K., O'Day C.L., Abelson J.;
RT   "In vitro studies of the Prp9.Prp11.Prp21 complex indicate a pathway for U2
RT   small nuclear ribonucleoprotein activation.";
RL   J. Biol. Chem. 271:33268-33276(1996).
RN   [9]
RP   FUNCTION.
RX   PubMed=8622683; DOI=10.1128/mcb.16.3.818;
RA   Yan D., Ares M. Jr.;
RT   "Invariant U2 RNA sequences bordering the branchpoint recognition region
RT   are essential for interaction with yeast SF3a and SF3b subunits.";
RL   Mol. Cell. Biol. 16:818-828(1996).
RN   [10]
RP   FUNCTION, MUTAGENESIS OF GLY-293, AND INTERACTION WITH THE U2 SNRNP.
RX   PubMed=11927574; DOI=10.1074/jbc.m109553200;
RA   Abu Dayyeh B.K., Quan T.K., Castro M., Ruby S.W.;
RT   "Probing interactions between the U2 small nuclear ribonucleoprotein and
RT   the DEAD-box protein, Prp5.";
RL   J. Biol. Chem. 277:20221-20233(2002).
RN   [11]
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   [12]
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   [13]
RP   FUNCTION.
RX   PubMed=14610285; DOI=10.1073/pnas.2036312100;
RA   Perriman R., Barta I., Voeltz G.K., Abelson J., Ares M. Jr.;
RT   "ATP requirement for Prp5p function is determined by Cus2p and the
RT   structure of U2 small nuclear RNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13857-13862(2003).
RN   [14]
RP   FUNCTION, AND INTERACTION WITH HSH155.
RX   PubMed=16314500; DOI=10.1128/mcb.25.24.10745-10754.2005;
RA   Wang Q., He J., Lynn B., Rymond B.C.;
RT   "Interactions of the yeast SF3b splicing factor.";
RL   Mol. Cell. Biol. 25:10745-10754(2005).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved spliceosome assembly and
CC       in nuclear splicing. Catalyzes an ATP-dependent conformational change
CC       of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP
CC       association with intron RNA. {ECO:0000269|PubMed:11927574,
CC       ECO:0000269|PubMed:14610285, ECO:0000269|PubMed:16314500,
CC       ECO:0000269|PubMed:8065365, ECO:0000269|PubMed:8405998,
CC       ECO:0000269|PubMed:8622683, ECO:0000269|PubMed:8969184,
CC       ECO:0000269|PubMed:8969185}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Interacts with the U2 snRNP and HSH155.
CC       {ECO:0000269|PubMed:11927574, ECO:0000269|PubMed:16314500}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M33191; AAA34914.1; -; Genomic_DNA.
DR   EMBL; Z36106; CAA85200.1; -; Genomic_DNA.
DR   EMBL; AY692817; AAT92836.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07353.1; -; Genomic_DNA.
DR   PIR; A35791; A35791.
DR   RefSeq; NP_009796.1; NM_001178585.1.
DR   PDB; 4LJY; X-ray; 1.95 A; A=206-698.
DR   PDB; 4LK2; X-ray; 2.12 A; A/B=206-698.
DR   PDB; 7OQB; EM; 9.00 A; p=1-849.
DR   PDB; 7OQE; EM; 5.90 A; p=1-849.
DR   PDBsum; 4LJY; -.
DR   PDBsum; 4LK2; -.
DR   PDBsum; 7OQB; -.
DR   PDBsum; 7OQE; -.
DR   AlphaFoldDB; P21372; -.
DR   SMR; P21372; -.
DR   BioGRID; 32932; 186.
DR   ComplexPortal; CPX-1418; Spliceosomal commitment complex.
DR   DIP; DIP-88N; -.
DR   IntAct; P21372; 3.
DR   MINT; P21372; -.
DR   STRING; 4932.YBR237W; -.
DR   iPTMnet; P21372; -.
DR   MaxQB; P21372; -.
DR   PaxDb; P21372; -.
DR   PRIDE; P21372; -.
DR   EnsemblFungi; YBR237W_mRNA; YBR237W; YBR237W.
DR   GeneID; 852539; -.
DR   KEGG; sce:YBR237W; -.
DR   SGD; S000000441; PRP5.
DR   VEuPathDB; FungiDB:YBR237W; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   HOGENOM; CLU_003041_0_2_1; -.
DR   InParanoid; P21372; -.
DR   OMA; ANCLDVI; -.
DR   BioCyc; YEAST:G3O-29168-MON; -.
DR   BRENDA; 3.6.4.13; 984.
DR   PRO; PR:P21372; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P21372; protein.
DR   GO; GO:0000243; C:commitment complex; IC:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:SGD.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000348; P:mRNA branch site recognition; IMP:SGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Coiled coil; Helicase; Hydrolase;
KW   mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..849
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT                   /id="PRO_0000055126"
FT   DOMAIN          287..467
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          502..661
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          28..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          13..81
FT                   /evidence="ECO:0000255"
FT   MOTIF           90..96
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           255..284
FT                   /note="Q motif"
FT   MOTIF           415..418
FT                   /note="DEAD box"
FT   COMPBIAS        56..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..724
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         300..307
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MUTAGEN         293
FT                   /note="G->D: In PRP5-1; no growth at 37 degrees Celsius and
FT                   impairs pre-spliceosome formation in vitro."
FT                   /evidence="ECO:0000269|PubMed:11927574,
FT                   ECO:0000269|PubMed:8405998"
FT   HELIX           223..226
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           230..239
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          243..248
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           264..272
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           281..291
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          296..299
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           306..319
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          332..336
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           340..354
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          362..367
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           372..378
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          383..387
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           389..395
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           398..401
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          411..414
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           417..422
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           426..435
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          441..447
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           451..460
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          461..463
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          465..472
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          479..488
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           489..510
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          528..533
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           535..547
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          553..555
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           561..573
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          578..582
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           583..586
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          595..601
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           606..613
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           614..616
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           619..621
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   STRAND          624..630
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           634..643
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           646..650
FT                   /evidence="ECO:0007829|PDB:4LJY"
FT   HELIX           654..672
FT                   /evidence="ECO:0007829|PDB:4LJY"
SQ   SEQUENCE   849 AA;  96359 MW;  326AAB3473ED7423 CRC64;
     METIDSKQNI NRESLLEERR KKLAKWKQKK AQFDAQKEHQ TSRNDIVTNS LEGKQTTEKF
     TERQERVKEE LRKRKNEFRK SDEPVSVKPS KKKSKRSKVK KKISFDFSDD DDSEIGVSFR
     SKEHIQKAPE HDNEKDPLDE FMTSLKEEKM SNSKGMYDRG DILDVEDQLF ELGGTDDEDV
     EDNTDNSNIA KIAKLKAKKR VKQIYYSPEE LEPFQKNFYI ESETVSSMSE MEVEELRLSL
     DNIKIKGTGC PKPVTKWSQL GLSTDTMVLI TEKLHFGSLT PIQSQALPAI MSGRDVIGIS
     KTGSGKTISY LLPLLRQVKA QRPLSKHETG PMGLILAPTR ELALQIHEEV TKFTEADTSI
     RSVCCTGGSE MKKQITDLKR GTEIVVATPG RFIDILTLND GKLLSTKRIT FVVMDEADRL
     FDLGFEPQIT QIMKTVRPDK QCVLFSATFP NKLRSFAVRV LHSPISITIN SKGMVNENVK
     QKFRICHSED EKFDNLVQLI HERSEFFDEV QSENDGQSSD VEEVDAKAII FVSSQNICDF
     ISKKLLNAGI VTCAIHAGKP YQERLMNLEK FKREKNSILL CTEVLSRGLN VPEVSLVIIY
     NAVKTFAQYV HTTGRTARGS RSGTAITLLL HDELSGAYIL SKAMRDEEIK ALDPLQAKEL
     QEMSAKFESG MKKGKFRLSK GFGGKGLENI KSKREEAQNK DLELKKNDKR SDDLEKKISN
     PREGHDSVSE SSALIPRLNY ELFKESTDGS IIFYAKVYIN DLPQIVRWEA TKNTTLLFIK
     HETGCSITNK GKFYPEGKEP KNENDEPKLY LLIEGQDEKD IQLSIELLEQ KVKEGVVKAA
     SLSLKSTKY
 
 
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