PRP5_YEAS7
ID PRP5_YEAS7 Reviewed; 849 AA.
AC A6ZLH6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE EC=3.6.4.13;
GN Name=PRP5; Synonyms=RNA5; ORFNames=SCY_0446;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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 -!- SUBUNIT: Interacts with the U2 snRNP and HSH155. {ECO:0000250}.
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; AAFW02000011; EDN64845.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZLH6; -.
DR SMR; A6ZLH6; -.
DR PRIDE; A6ZLH6; -.
DR EnsemblFungi; EDN64845; EDN64845; SCY_0446.
DR HOGENOM; CLU_003041_0_2_1; -.
DR Proteomes; UP000007060; 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; Coiled coil; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus.
FT CHAIN 1..849
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT /id="PRO_0000310229"
FT DOMAIN 287..467
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 502..661
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 28..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..81
FT /evidence="ECO:0000255"
FT MOTIF 255..284
FT /note="Q motif"
FT MOTIF 415..418
FT /note="DEAD box"
FT COMPBIAS 37..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 300..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 849 AA; 96412 MW; 3614673BB6392478 CRC64;
METIDSKQNI NRESLLEERR KKLAKWKQKK AQFDAQKENQ TSRNDIVTNS LEGKQTTEKF
TERQERVKEE LRKRKNEFRK SDEPVSVKPS KKKSKRSKVK KKISFDFSDD DDSEIGVSFR
SKEHIQKVPE HDNEKDPLDE FMTSLKEEKM SNSKGMYDRG DILDVEDQLF ELGGTDDEDV
EDNTDNSNIA KIAKLKAKKR VKQIYYSPEE LEPFQKNFYI ESETVSSMSE MEVEELRLSL
DNIKIKGTGC PKPVTKWSQL GLSTDTMVLI TEKLHFGSLT PIQSQALPAI MSGRDVIGIS
KTGSGKTISY LLPLLRQVKA QRPLSKHETG PMGLILAPTR ELALQIHEEV TKFTEADTSI
RSVCCTGGSE MKKQITDLKR GTEIVVATPG RFIDILTLND GKLLSTKRIT FVVMDEADRL
FDLGFEPQIT QIMKTVRPDK QCVLFSATFP NKLRSFAVRV LHSPISITIN SKGMVNENVK
QKFRICHSED EKFDNLVQLI HERSEFFDEV QSENDGQSSD VEEVDAKAII FVSSQNICDF
ISKKLLNAGI VTCAIHAGKP YQERLMNLEK FKREKNSILL CTEVLSRGLN VPEVSLVIIY
NAVKTFAQYV HTTGRTARGS RSGTAITLLL HDELSGAYIL SKAMRDEEIK ALDPLQAKEL
QEMSAKFESG MKKGKFRLSK GFGGKGLENI KSKREEAQNK DLELKKNDKR SDDLEKKINN
PHEGHDSEPE SSALIPRLNY ELFKESTDGS IIFYAKVYIN DLPQIVRWEA TKNTTLLFIK
HETGCSITNK GKFYPEGKEP KNENDEPKLY LLIEGQDEKD IQLSIELLEQ KVKEGVVKAA
SLSLKSTKY
