PRP5_YARLI
ID PRP5_YARLI Reviewed; 974 AA.
AC Q6CCZ1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE EC=3.6.4.13;
GN Name=PRP5; OrderedLocusNames=YALI0C05368g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382129; CAG81772.1; -; Genomic_DNA.
DR RefSeq; XP_501471.1; XM_501471.1.
DR AlphaFoldDB; Q6CCZ1; -.
DR SMR; Q6CCZ1; -.
DR STRING; 4952.CAG81772; -.
DR PRIDE; Q6CCZ1; -.
DR EnsemblFungi; CAG81772; CAG81772; YALI0_C05368g.
DR GeneID; 2909377; -.
DR KEGG; yli:YALI0C05368g; -.
DR VEuPathDB; FungiDB:YALI0_C05368g; -.
DR HOGENOM; CLU_003041_0_3_1; -.
DR InParanoid; Q6CCZ1; -.
DR OMA; NREHERD; -.
DR Proteomes; UP000001300; Chromosome C.
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: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..974
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT /id="PRO_0000232368"
FT DOMAIN 409..595
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 654..800
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 378..406
FT /note="Q motif"
FT MOTIF 543..546
FT /note="DEAD box"
FT COMPBIAS 20..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 422..429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 974 AA; 107223 MW; 6F8B777E97B71CCC CRC64;
MPRDREYDQW GYSGTRRDGG GRYGYRDRSR DERDRFRDVR DRDRDRDRDR ERDRGGYRQD
PRDRRYSRSR ERERRGSGSR DRSRDRSRDR SRDAHRPPPS GRPHQPSGHD STKSSNSMSE
TSSTSQVTGT TPNTTNATPS QAEIDAKKAA KLAKVAEWKR KKELERSKSA SASPAPSTAP
ASPKAGFSMS GLSGLRKATD QGQVKRKMFF GGDSDEEDAG RKPAKLLKKL GEKEGSGKSE
GKGRGGSQSE AKNASEKNGA ASEPAEVDPL DAYMSSLTLP TTTSVSIADS TPLENLNVWE
QVDTLEKSQD PTLDLSALSK RKEIAIVDHS KQVYEDFRRQ FYVESSELAD MTEAETNELR
LSLDGIKIRG KDCPKPISKW TQLGLPGPTM GVLNDLRYDK PTSIQAQAIP AVMSGRDVIS
VAKTGSGKTL AFLLPMLRHI KHRVGVETHT TTLSGASSHP LGVIITPTRE LCVQIYRDLR
PFLAALELTA VCAYGGSPIK DQIAALKKGT HIIVCTPGRM IDLLAANQGR VLSLSRVTFL
VIDEADRMFD MGFEPQVLKL TQSIRPDRQT VLFSATFPKK MEQLARRVLS KRSSDSLGPI
EIIVGARSVV ASEITQFVEV FQNEKSKFPR LLEVLGKYFA QGFFDEQSEG RVGTGESAAT
PIPNPKCLIF VERQESADSL LKELIQSGYP CLSIHGGKEQ ADRDQAISDF KSGLVSVLIA
TSVAARGLDV KGLGLVVNWD SPNHMEDYVH RVGRTGRAGQ KGTALTFLLS DQERLAAEIS
RAIKSSGNAP PAPVQLMTER FEFKVRSGTE KRHMYGFSGK GLERLQDERD ATREHERRAY
EGDEAGEAET ESSTPAASTA NTDIIPKPVI VVTPPDSKSP TTAYHTTLQI NDFPQQARYR
ASSNTSVSRV IANTGCSITA KGEYYPPGRI PGPKDEPKLF ILIEGTSERA VKLAHHELSE
LLVSGLVKGA RYQV
