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Database: UniProt
Entry: A7TJK8
LinkDB: A7TJK8
Original site: A7TJK8 
ID   PRP5_VANPO              Reviewed;         872 AA.
AC   A7TJK8;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   11-DEC-2019, entry version 62.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE            EC=3.6.4.13;
GN   Name=PRP5; ORFNames=Kpol_534p31;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces
OS   polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC       subfamily. {ECO:0000305}.
DR   EMBL; DS480402; EDO17551.1; -; Genomic_DNA.
DR   RefSeq; XP_001645409.1; XM_001645359.1.
DR   SMR; A7TJK8; -.
DR   STRING; 36033.XP_001645409.1; -.
DR   PRIDE; A7TJK8; -.
DR   EnsemblFungi; EDO17551; EDO17551; Kpol_534p31.
DR   GeneID; 5545774; -.
DR   KEGG; vpo:Kpol_534p31; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   eggNOG; ENOG410XSQV; LUCA.
DR   InParanoid; A7TJK8; -.
DR   KO; K12811; -.
DR   OMA; RGIDCPK; -.
DR   OrthoDB; 245118at2759; -.
DR   PhylomeDB; A7TJK8; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:EnsemblFungi.
DR   GO; GO:0000348; P:mRNA branch site recognition; IEA:EnsemblFungi.
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   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..872
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT                   /id="PRO_0000310228"
FT   DOMAIN          308..488
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          539..685
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         321..328
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           276..305
FT                   /note="Q motif"
FT   MOTIF           436..439
FT                   /note="DEAD box"
SQ   SEQUENCE   872 AA;  99451 MW;  29CB2E350D11DDD2 CRC64;
     MSADNVSSID PEKERISRER REKLAKWRAK KALMDSQNEL KKETVPLEVK NSKITNNEND
     STSRSKLLER QHKLQEWKRK KREREEEQLI KEQENTKETS SHSKKKNKKQ NRGSQKRQIT
     FDDSDDETTG ESKDSFDKSE IVVEKSDMSG SKNNNEDDPL EAYMKSLVNG GQPLNHKIGE
     NILDEDGDDN SIEEDDEFSN SESDEESSRY KRISKAKAKK KVKEIKFTIK DLEPFPKSFY
     SEPDEVKLMT DDEVEEMRLS LGGIKVKGKH CPKLITRWSQ LGLPTDIMNL ITKELKYDEP
     TAIQSQAIPA IMSGRDLIGI SKTGSGKTIS YILPMLRQIK AQRTLSKNET GPLGLILAPT
     RELALQINEE VEKFTKQDRS IRTICCTGGS EMKKQINDLK RGVEIVVATP GRLIDILTLN
     SGKLISTKRI TFVVMDEADR LFDMGFEPQI TQIMKTVRPD KQCVLFSATF PNKLRSFAAR
     ILTDPLTVTI NSNNLVNENV NQSFYIEDNE NDKFNRLVNI LDGFYKVNKN ITSNSEEREI
     DEEVSDKKII IFVSSQQFCD LLYSKLENFG YFPYTIHAGK PYQERVMNLE KFKTTTNSIL
     LCTEVLSRGL NVPEVSLVII YNAAKTFAQY VHTTGRTARG THKGDAITLL LPDELAAAYI
     LKRALREREL SSIDPQMVED MKQMSERFES GMKEGKYKLS KGFGGKGLDN LDTKREEKQQ
     EEKHKLDKIE NDESTPSTSY KTTDNASSSS EVDSVTIPKL EFTIDRDKNI DSTISFTAIV
     NVNDLPQLVR WEATKNTTLM FIKHETGCSI TNKGKYYPEG KGPTSNKDQP KLYLQIEGKE
     EKDVLLSIEL LEQKVREGIK KVEYQSIKST KY
//
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