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 27-MAR-2024, entry version 205.
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 EMDB; EMD-13028; -.
DR EMDB; EMD-13033; -.
DR SMR; P21372; -.
DR BioGRID; 32932; 189.
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; 4932-YBR237W; -.
DR PeptideAtlas; P21372; -.
DR EnsemblFungi; YBR237W_mRNA; YBR237W; YBR237W.
DR GeneID; 852539; -.
DR KEGG; sce:YBR237W; -.
DR AGR; SGD:S000000441; -.
DR SGD; S000000441; PRP5.
DR VEuPathDB; FungiDB:YBR237W; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_2_1; -.
DR InParanoid; P21372; -.
DR OMA; FAQYVHT; -.
DR OrthoDB; 5477821at2759; -.
DR BioCyc; YEAST:G3O-29168-MONOMER; -.
DR BRENDA; 3.6.4.13; 984.
DR BioGRID-ORCS; 852539; 6 hits in 10 CRISPR screens.
DR PRO; PR:P21372; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P21372; Protein.
DR GO; GO:0000243; C:commitment complex; NAS: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 CDD; cd17953; DEADc_DDX46; 1.
DR CDD; cd22474; KH-I_PRP5_like; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR24031:SF25; ATP-DEPENDENT RNA HELICASE DDX46-RELATED; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
