ID V9EK66_PHYPR Unreviewed; 1118 AA.
AC V9EK66;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5 {ECO:0000256|ARBA:ARBA00041162};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5 {ECO:0000256|ARBA:ARBA00040918};
GN ORFNames=F443_15834 {ECO:0000313|EMBL:ETI38442.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI38442.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI38442.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI38442.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00037330}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC subfamily. {ECO:0000256|ARBA:ARBA00038511}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETI38442.1}.
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DR EMBL; ANIZ01002767; ETI38439.1; -; Genomic_DNA.
DR EMBL; ANIZ01002767; ETI38440.1; -; Genomic_DNA.
DR EMBL; ANIZ01002767; ETI38441.1; -; Genomic_DNA.
DR EMBL; ANIZ01002767; ETI38442.1; -; Genomic_DNA.
DR AlphaFoldDB; V9EK66; -.
DR EnsemblProtists; ETI38439; ETI38439; F443_15834.
DR EnsemblProtists; ETI38440; ETI38440; F443_15834.
DR EnsemblProtists; ETI38441; ETI38441; F443_15834.
DR EnsemblProtists; ETI38442; ETI38442; F443_15834.
DR eggNOG; KOG0334; Eukaryota.
DR OrthoDB; 49359at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd17953; DEADc_DDX46; 1.
DR CDD; cd22475; KH-I_AtRH42_like; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47958:SF35; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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 {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721}.
FT DOMAIN 519..547
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 550..728
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 739..900
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 519..547
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 8..39
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..79
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..120
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 125822 MW; 00345D0B325D2D96 CRC64;
MAQDAASPRR HRRRRSRSKS RSSRRHSSSS RRKRSRSRSL SSRSASSDAS RSRSRSRERR
RSSKSGDRHR RKRSKTERRE RRRSPSYSRS RSRSEGRRSS YKKKRDRSHR SGRKSSRRSR
SRSETRAEAS RRKRSESKEE IKKHNEVKNG HAEHAKPQEA AATKSSGSSS EKKRAAKDPP
AVTAPTASAT LKKFKFGGIS LKPGNQKNVV KKKPAAFFNS LSEDTKPPLN DEKEPTKKQK
FLLEEQKQEE KAKFLAEEDA VPKQLDLNTE EEEEKGETPE ERKKREEEEV KQRERVQKVV
EEVDPLDAYM AGLVDASARA NPAANVISQS EIEAKGKINI YGTFLPPDAA EQATTVTTTP
SADTQTSTSV VNETPEEREA REERELKEFM RAIKEKRKQE ENNTNSGTEA AVATGNGAGP
EDLAVKQDTG RIYQGFEEDI IGEDSELMDQ RSALEILQDQ QKKKEIKPVD HSKMNYLPFQ
KKFYVAPKEI KDLSEEDMEA QRKESEIKVR GKNCPRPLQK WTQCGFSVRM LQLIKKHGYE
EPFAIQKQAL PAIMSGRDVI GIAKTGSGKT LAFLLPMFRH ILAQPPLQEN EGPIGIIMAP
ARELAQQIYV EARKFSKGLG LRATAVYGGS SVSEQIANLK RGSDIVICTP GRMIDILCMS
AGKMVSLQRV TYVVLDEADR MFDMGFEPQI TKIMMNIRPD RQTLLFSATF PRSVESLARK
VLKKPVEITV GTRSTASGDI TQYVEVREED DKFMRLLQLL GLWYEKGNIL VFVNKQQACD
QIFQDLMKAG YPALSLHGGK DQVDRDYTID DFKRKVRTVM VATSVAGRGL DVKDLVLVIN
YHCPNHMEDY VHRVGRTGRA GRKGTAYTFI SPDEEEYSVD LVKALENAKQ IVPPELTALA
EGFTAKVKRG EARYHGSGFK GKGFTFDETE RNETQRTADL QRRQYELDQG ILVEDSGAAD
DDDDEEPSKE NTANTTDKPS VPAGQKAMPI DGEAMSAFIK AQKIIQNLDL KYKGNGSGEN
HFVEELEIND YPQQARWRVT QKEASDSVAE LTGAAVIARG SYIPAGRKPN PSERKLYLAI
EGPTQASVIE ARRELQRILD ETTMQVGLGG DKYGKYSL
//
