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Protein

Pre-mRNA-processing ATP-dependent RNA helicase PRP5

Gene

PRP5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. Catalyzes an ATP-dependent conformational change of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA.8 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi300 – 3078ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • helicase activity Source: UniProtKB-KW
  • nucleic acid binding Source: InterPro
  • RNA-dependent ATPase activity Source: SGD

GO - Biological processi

  • mRNA branch site recognition Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29168-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-processing ATP-dependent RNA helicase PRP5 (EC:3.6.4.13)
Gene namesi
Name:PRP5
Synonyms:RNA5
Ordered Locus Names:YBR237W
ORF Names:YBR1603
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR237W.
SGDiS000000441. PRP5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi293 – 2931G → D in PRP5-1; no growth at 37 degrees Celsius and impairs pre-spliceosome formation in vitro. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 849849Pre-mRNA-processing ATP-dependent RNA helicase PRP5PRO_0000055126Add
BLAST

Proteomic databases

MaxQBiP21372.

PTM databases

iPTMnetiP21372.

Interactioni

Subunit structurei

Interacts with the U2 snRNP and HSH155.2 Publications

Protein-protein interaction databases

BioGridi32932. 18 interactions.
DIPiDIP-88N.
IntActiP21372. 3 interactions.
MINTiMINT-403988.

Structurei

Secondary structure

1
849
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi223 – 2264Combined sources
Helixi230 – 23910Combined sources
Beta strandi243 – 2486Combined sources
Helixi257 – 2593Combined sources
Helixi264 – 2729Combined sources
Helixi281 – 29111Combined sources
Beta strandi296 – 2994Combined sources
Helixi306 – 31914Combined sources
Beta strandi332 – 3365Combined sources
Helixi340 – 35415Combined sources
Beta strandi362 – 3676Combined sources
Helixi372 – 3787Combined sources
Beta strandi383 – 3875Combined sources
Helixi389 – 3957Combined sources
Helixi398 – 4014Combined sources
Beta strandi411 – 4144Combined sources
Helixi417 – 4226Combined sources
Helixi426 – 43510Combined sources
Beta strandi441 – 4477Combined sources
Helixi451 – 46010Combined sources
Beta strandi461 – 4633Combined sources
Beta strandi465 – 4728Combined sources
Beta strandi479 – 48810Combined sources
Helixi489 – 51022Combined sources
Beta strandi528 – 5336Combined sources
Helixi535 – 54713Combined sources
Beta strandi553 – 5553Combined sources
Helixi561 – 57313Combined sources
Beta strandi578 – 5825Combined sources
Helixi583 – 5864Combined sources
Beta strandi595 – 6017Combined sources
Helixi606 – 6138Combined sources
Helixi614 – 6163Combined sources
Helixi619 – 6213Combined sources
Beta strandi624 – 6307Combined sources
Helixi634 – 64310Combined sources
Helixi646 – 6505Combined sources
Helixi654 – 67219Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LJYX-ray1.95A206-698[»]
4LK2X-ray2.12A/B206-698[»]
ProteinModelPortaliP21372.
SMRiP21372. Positions 211-673.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini287 – 467181Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini502 – 661160Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili13 – 8169Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi90 – 967Nuclear localization signalSequence analysis
Motifi255 – 28430Q motifAdd
BLAST
Motifi415 – 4184DEAD box

Domaini

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00840000129934.
HOGENOMiHOG000007229.
InParanoidiP21372.
KOiK12811.
OMAiQCVLFSA.
OrthoDBiEOG7TJ3T2.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21372-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METIDSKQNI NRESLLEERR KKLAKWKQKK AQFDAQKEHQ TSRNDIVTNS
60 70 80 90 100
LEGKQTTEKF TERQERVKEE LRKRKNEFRK SDEPVSVKPS KKKSKRSKVK
110 120 130 140 150
KKISFDFSDD DDSEIGVSFR SKEHIQKAPE HDNEKDPLDE FMTSLKEEKM
160 170 180 190 200
SNSKGMYDRG DILDVEDQLF ELGGTDDEDV EDNTDNSNIA KIAKLKAKKR
210 220 230 240 250
VKQIYYSPEE LEPFQKNFYI ESETVSSMSE MEVEELRLSL DNIKIKGTGC
260 270 280 290 300
PKPVTKWSQL GLSTDTMVLI TEKLHFGSLT PIQSQALPAI MSGRDVIGIS
310 320 330 340 350
KTGSGKTISY LLPLLRQVKA QRPLSKHETG PMGLILAPTR ELALQIHEEV
360 370 380 390 400
TKFTEADTSI RSVCCTGGSE MKKQITDLKR GTEIVVATPG RFIDILTLND
410 420 430 440 450
GKLLSTKRIT FVVMDEADRL FDLGFEPQIT QIMKTVRPDK QCVLFSATFP
460 470 480 490 500
NKLRSFAVRV LHSPISITIN SKGMVNENVK QKFRICHSED EKFDNLVQLI
510 520 530 540 550
HERSEFFDEV QSENDGQSSD VEEVDAKAII FVSSQNICDF ISKKLLNAGI
560 570 580 590 600
VTCAIHAGKP YQERLMNLEK FKREKNSILL CTEVLSRGLN VPEVSLVIIY
610 620 630 640 650
NAVKTFAQYV HTTGRTARGS RSGTAITLLL HDELSGAYIL SKAMRDEEIK
660 670 680 690 700
ALDPLQAKEL QEMSAKFESG MKKGKFRLSK GFGGKGLENI KSKREEAQNK
710 720 730 740 750
DLELKKNDKR SDDLEKKISN PREGHDSVSE SSALIPRLNY ELFKESTDGS
760 770 780 790 800
IIFYAKVYIN DLPQIVRWEA TKNTTLLFIK HETGCSITNK GKFYPEGKEP
810 820 830 840
KNENDEPKLY LLIEGQDEKD IQLSIELLEQ KVKEGVVKAA SLSLKSTKY
Length:849
Mass (Da):96,359
Last modified:May 1, 1991 - v1
Checksum:i326AAB3473ED7423
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33191 Genomic DNA. Translation: AAA34914.1.
Z36106 Genomic DNA. Translation: CAA85200.1.
AY692817 Genomic DNA. Translation: AAT92836.1.
BK006936 Genomic DNA. Translation: DAA07353.1.
PIRiA35791.
RefSeqiNP_009796.1. NM_001178585.1.

Genome annotation databases

EnsemblFungiiYBR237W; YBR237W; YBR237W.
GeneIDi852539.
KEGGisce:YBR237W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33191 Genomic DNA. Translation: AAA34914.1.
Z36106 Genomic DNA. Translation: CAA85200.1.
AY692817 Genomic DNA. Translation: AAT92836.1.
BK006936 Genomic DNA. Translation: DAA07353.1.
PIRiA35791.
RefSeqiNP_009796.1. NM_001178585.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LJYX-ray1.95A206-698[»]
4LK2X-ray2.12A/B206-698[»]
ProteinModelPortaliP21372.
SMRiP21372. Positions 211-673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32932. 18 interactions.
DIPiDIP-88N.
IntActiP21372. 3 interactions.
MINTiMINT-403988.

PTM databases

iPTMnetiP21372.

Proteomic databases

MaxQBiP21372.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR237W; YBR237W; YBR237W.
GeneIDi852539.
KEGGisce:YBR237W.

Organism-specific databases

EuPathDBiFungiDB:YBR237W.
SGDiS000000441. PRP5.

Phylogenomic databases

GeneTreeiENSGT00840000129934.
HOGENOMiHOG000007229.
InParanoidiP21372.
KOiK12811.
OMAiQCVLFSA.
OrthoDBiEOG7TJ3T2.

Enzyme and pathway databases

BioCyciYEAST:G3O-29168-MONOMER.

Miscellaneous databases

NextBioi971604.
PROiP21372.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PRP5: a helicase-like protein required for mRNA splicing in yeast."
    Dalbadie-Mcfarland G., Abelson J.
    Proc. Natl. Acad. Sci. U.S.A. 87:4236-4240(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact to promote U2 snRNP binding to pre-mRNA."
    Ruby S.W., Chang T.-H., Abelson J.
    Genes Dev. 7:1909-1925(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-293.
  6. "Interactions between highly conserved U2 small nuclear RNA structures and Prp5p, Prp9p, Prp11p, and Prp21p proteins are required to ensure integrity of the U2 small nuclear ribonucleoprotein in Saccharomyces cerevisiae."
    Wells S.E., Ares M. Jr.
    Mol. Cell. Biol. 14:6337-6349(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The Saccharomyces cerevisiae Prp5 protein has RNA-dependent ATPase activity with specificity for U2 small nuclear RNA."
    O'Day C.L., Dalbadie-McFarland G., Abelson J.
    J. Biol. Chem. 271:33261-33267(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "In vitro studies of the Prp9.Prp11.Prp21 complex indicate a pathway for U2 small nuclear ribonucleoprotein activation."
    Wiest D.K., O'Day C.L., Abelson J.
    J. Biol. Chem. 271:33268-33276(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Invariant U2 RNA sequences bordering the branchpoint recognition region are essential for interaction with yeast SF3a and SF3b subunits."
    Yan D., Ares M. Jr.
    Mol. Cell. Biol. 16:818-828(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Probing interactions between the U2 small nuclear ribonucleoprotein and the DEAD-box protein, Prp5."
    Abu Dayyeh B.K., Quan T.K., Castro M., Ruby S.W.
    J. Biol. Chem. 277:20221-20233(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-293, INTERACTION WITH THE U2 SNRNP.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "ATP requirement for Prp5p function is determined by Cus2p and the structure of U2 small nuclear RNA."
    Perriman R., Barta I., Voeltz G.K., Abelson J., Ares M. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 100:13857-13862(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Interactions of the yeast SF3b splicing factor."
    Wang Q., He J., Lynn B., Rymond B.C.
    Mol. Cell. Biol. 25:10745-10754(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSH155.

Entry informationi

Entry nameiPRP5_YEAST
AccessioniPrimary (citable) accession number: P21372
Secondary accession number(s): D6VQN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: May 11, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 358 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.