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Database: UniProt
Entry: Q754U8
LinkDB: Q754U8
Original site: Q754U8 
ID   PRP5_ASHGO              Reviewed;         855 AA.
AC   Q754U8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   16-OCT-2019, entry version 98.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE            EC=3.6.4.13;
GN   Name=PRP5; OrderedLocusNames=AFL027C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient
RT   Saccharomyces cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO N-TERMINUS.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved spliceosome assembly
CC       and in nuclear splicing. Catalyzes an ATP-dependent conformational
CC       change of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2
CC       snRNP 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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC       subfamily. {ECO:0000305}.
DR   EMBL; AE016819; AAS53345.2; -; Genomic_DNA.
DR   RefSeq; NP_985521.2; NM_210875.2.
DR   SMR; Q754U8; -.
DR   STRING; 33169.AAS53345; -.
DR   EnsemblFungi; AAS53345; AAS53345; AGOS_AFL027C.
DR   GeneID; 4621754; -.
DR   KEGG; ago:AGOS_AFL027C; -.
DR   HOGENOM; HOG000007229; -.
DR   InParanoid; Q754U8; -.
DR   KO; K12811; -.
DR   OMA; SICCTGG; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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; Complete proteome; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1    855       Pre-mRNA-processing ATP-dependent RNA
FT                                helicase PRP5.
FT                                /FTId=PRO_0000227963.
FT   DOMAIN      307    487       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      498    668       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     320    327       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       113    119       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       275    304       Q motif.
FT   MOTIF       435    438       DEAD box.
SQ   SEQUENCE   855 AA;  95774 MW;  76721BA8093A454D CRC64;
     MEPNTPAIDP KKERLARWKQ KKQQQDMLRQ KSGASSKSSH DQAEDGDAAR STQPFEGLDK
     MAERRKRLEL WKKKKKEQDE QKWKGDDAGQ ESATDIPVKG KAAPAEDAKA VPRGRKSRKG
     ADPEKRQIWD DSDDELEAPK LKLFKPGSTI QTETPPDEDP EDTLDTYMNT IQEKNEVQLL
     APREVFDQED DETTAFDYNR TDNGTGSEFM RLAKLKAKKQ LKPVIYSADE LKPFIKNFYQ
     EPEEISKLSE EEVADLRLSL DNVQVRGRDC PRPILKWSQL GLNSGIMNLL TRELEFTVPT
     PIQAQAIPAI MSGRDVIGIS KTGSGKTVSF ILPLLRQIKA QRPLGGDETG PLGLILSPTR
     ELALQIHEEV TKFTSGDPSI RSLCCTGGSE LKRQINDIKR GVEIVIATPG RFIDLLSLNS
     GNLINPKRIV FVVMDEADRL FDLGFEPQVN QIMKCIRPDK QCVLFSATFP NKLKSFASKI
     LHDPVYITVN SKSLINENIE QKVEIFSNEE DKFKSLIHWL ALTQQNLNDE KTIVFVSSQQ
     ICDILYNRLE ANGFTTFAIH AGKIYTERAW NLKCFKETAN GILICTEVLS RGLNVPEVSL
     VIIYNAAKTF AQYVHTTGRT ARGSNKGTAL TLLMNTELAA SYILMKSMRD EELNKHHDAT
     VSTLKQMSEK FNKGLKTGEY RLVKGFGGKG LDHLGKVYEE KHTEERNQLA LEAGLAATEV
     SVSAPDGGLG DESTSVSIPK LDYTVKKRSN PDGTSTYFAH VQVNDLPQIV RWEATKYTTL
     SSIKHETGCS ITNKGRYYPS GQGPQGPSDE PRLYLLVESA TDQDISLAID LLESKVRDGV
     RKSNMQEIRS NKYTI
//
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