PRP5_ASHGO
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 03-AUG-2022, entry version 108.
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 Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC 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 Saccharomyces
RT 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 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; AE016819; AAS53345.2; -; Genomic_DNA.
DR RefSeq; NP_985521.2; NM_210875.2.
DR AlphaFoldDB; Q754U8; -.
DR SMR; Q754U8; -.
DR STRING; 33169.AAS53345; -.
DR EnsemblFungi; AAS53345; AAS53345; AGOS_AFL027C.
DR GeneID; 4621754; -.
DR KEGG; ago:AGOS_AFL027C; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_2_1; -.
DR InParanoid; Q754U8; -.
DR OMA; ANCLDVI; -.
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: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:0000348; P:mRNA branch site recognition; IEA:EnsemblFungi.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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..855
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT /id="PRO_0000227963"
FT DOMAIN 307..487
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 498..668
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 113..119
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 275..304
FT /note="Q motif"
FT MOTIF 435..438
FT /note="DEAD box"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 320..327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
