PRP5_PICST
ID PRP5_PICST Reviewed; 875 AA.
AC A3LQ55;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE EC=3.6.4.13;
GN Name=PRP5; ORFNames=PICST_87539;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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; CP000496; ABN64616.2; -; Genomic_DNA.
DR RefSeq; XP_001382645.2; XM_001382608.1.
DR AlphaFoldDB; A3LQ55; -.
DR SMR; A3LQ55; -.
DR STRING; 4924.XP_001382645.2; -.
DR EnsemblFungi; ABN64616; ABN64616; PICST_87539.
DR GeneID; 4837624; -.
DR KEGG; pic:PICST_87539; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_2_1; -.
DR InParanoid; A3LQ55; -.
DR OMA; ANCLDVI; -.
DR OrthoDB; 245118at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
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; Coiled coil; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..875
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT /id="PRO_0000285149"
FT DOMAIN 304..482
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 519..669
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 177..217
FT /evidence="ECO:0000255"
FT MOTIF 272..301
FT /note="Q motif"
FT MOTIF 430..433
FT /note="DEAD box"
FT COMPBIAS 1..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 317..324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 875 AA; 98404 MW; CB425CEDDEC94E9D CRC64;
MDNTVTNDSD ESKLSKEEKL KKRREQLALW RQKKEQDSKN GEKEMNSNAT TSSDDKQKLR
QQRMEEWKKK RAQETKIDSK ESVKESPKQE NSILKRLASS IKKQELPFTK KRILFDEEEE
DESKRKPKFK KPTLDGHTED LQHREDDPNG KIDELDDFIA SLSKQESSSN DIPSQIIEDE
QLEVENEGDS EDEEIDQDKK QQELLSSKFQ KLQNEKQLET IDHSTMNYSD FRKNFYQEPS
EIQNWTAEQV ESIRLELDGI KVAGSNVPRP VLKWSHLGLP ASYMNIIEDK LEYKAPTSIQ
SQALPAIMSG RDIIGVAKTG SGKTLSFVLP MLRHIQDQPD LKDGEGPIGL ILSPTRELAV
QIHKEITNFT KRLGMTACCC YGGSPIESQI AELKKGAQIL VGTPGRIIEL LAANSGRITN
LRRVTYVVLD EADRMFDLGF EPQVTKISSQ IRPESQTVLF SATFPRKIEL LAKRLLYNPL
EIIVGGISVV ASEITQKVEL FEKGESSQLE DEKFDRLLNI LNVFSIESKH SKVLIFVEKQ
SAADDLLVKL LGSNHPCLTI HGGKDQIDRK YAIKEFSSKD SGVDILIATS IAARGLDVKG
LDLVINYDPP NHMEDYVHRV GRTGRAGMKG TAITFVSSDQ ERSVTDLVRA MTMSKIPEDE
IPSRLIEIRN QFLEKVKAGK FKYSFGFGGK GLEKLQQIRD STRSLQKKEY GPNDDDDVNF
VADKTNGTAK KDGATSLPAS EVAVDLPDFQ VIEGRAPETS GPDKSKFHSR ITINDLPQRA
RWFVVNRDSL SKIIESTSTS ITNKGQYYAP NVKVPQTVTV NGKESPAPPR LYLLVEGLTE
QSVREANSLI RDKMIEGLEV ASKESNMAPT GKYKV
