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   03-AUG-2022, entry version 70.
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 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces 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 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
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}.
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DR   EMBL; DS480402; EDO17551.1; -; Genomic_DNA.
DR   RefSeq; XP_001645409.1; XM_001645359.1.
DR   AlphaFoldDB; A7TJK8; -.
DR   SMR; A7TJK8; -.
DR   STRING; 436907.A7TJK8; -.
DR   EnsemblFungi; EDO17551; EDO17551; Kpol_534p31.
DR   GeneID; 5545774; -.
DR   KEGG; vpo:Kpol_534p31; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   HOGENOM; CLU_003041_0_2_1; -.
DR   InParanoid; A7TJK8; -.
DR   OMA; ANCLDVI; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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   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   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          34..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           276..305
FT                   /note="Q motif"
FT   MOTIF           436..439
FT                   /note="DEAD box"
FT   COMPBIAS        34..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..202
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..734
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         321..328
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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