ID V9EA63_PHYPR Unreviewed; 1331 AA.
AC V9EA63;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=F443_18237 {ECO:0000313|EMBL:ETI35418.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI35418.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI35418.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI35418.1,
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 -!- 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 Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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:ETI35418.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ANIZ01003145; ETI35418.1; -; Genomic_DNA.
DR EnsemblProtists; ETI35418; ETI35418; F443_18237.
DR eggNOG; KOG0926; Eukaryota.
DR HOGENOM; CLU_001832_0_0_1; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17982; DEXHc_DHX37; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721}.
FT DOMAIN 387..586
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 682..864
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..726
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1331 AA; 150375 MW; F7EFE6C59DCFF06F CRC64;
MAAKKRKQSG HAKAKKKAKT TEAVVTQERA EKMLQEPQEN ETNMEHEQDE TTTSEASGLL
SAELLEEMGG EDAGGALVLP GRREKKQKTD KMPDELLEQA QHMSKSKRKK LEAIAARKVK
EARRADLYKS LEKQQLSQDQ MKLLYSTSQM GHKETLRERL KRSLNRQKAG IELSEDAKSE
LFKKQDVREQ DEDESMEETK PKEKNSDRVK STEAQVIKHD KPNNDAVQDK TGKKKRRKKK
AAVVSRSVPM LETQEEAPVA GSSDAASAMA IQHTEENPEE EAKRTSSQSA AMTKLEALRK
KNEEKRRLRA LSKPQTADIP KQEEPTVNPS DAYVPKPIVM KTAEEMRALS KKTKISYKNT
LVTLSRKPEI QMARMQLPVC SSEQEIMEAI TDNDVIILCG ETGSGKTTQV PQFLYEAGYG
HPDHPSNSGR IGVTQPRRVA AVSTAKRVAE ELNVPFGAPK GHVGYQIRYD AEHVSEHTRI
KFMTDGILLK EIQQDFLLRQ YSILLLDEAH ERNVNTDILI GLLSRIAPLR AQMSREEEEA
YNSLPDEERE AADKPIKPLK LVIMSATLRV EDFTQNQRLF PNPPPVLRVD ARQYPVTIHF
NKRTELDNYV DEAYKKVIKI HKKLPEGGVL VFLTGQREIL QLCRKLSRAY SVAARNKKAA
ALKSSRAFRA QRRQTETSSK EDFLREHDDI EEEADLEDAQ VYGTEDIEDP TYELEEEQNS
DDEDEEMEKL AVPYLHVLPL YSLLPNDEQM KVFDTPPENH RLVVVATNVA ETSLTIPGIK
YVVDAGRTKE RVFDLANGIS SFEVQWISKA SADQRAGRAG RTGPGHCYRL YSSAVYDTEF
QKFSSPEILC QPIDDLVLQM KAMGIHNVLQ FPFPTPPDRQ AVKNALATLV NLGAVSPGDD
EAITGLGRAL VKFPVAARFA KMLLLAQKLN VVEYTIAIVA GLSGHSPFIH ALDRREKEKN
EEENDEEKSE MEEMEKEWRE AEEMRKHAQW IDQESDVLSL LRAAGAYAYT GGSSQFCKDN
HLHEKTMQNM LKLRQQLTRI VNKLYAEEDA IELKPKMPPP DLETQVVLRQ IVAAGFLDQV
AKRVPAGTIT EGTKIERNCA YIAATGQVKE PVYIHPHSSV FTPNPSKLPQ FVVYQHIMRT
TRAYMKMVTA IEPEWLAGIG KNTPLCKYAP PLAEPAPFYH PELDEVQCYA KAQYGMHQWS
LPAMRISYPD QDASESKDGL GGKYRWFAKF LLDGQVITSL RPFSSALKEP SHTLIRKKFD
KKIQLLVAKL QQNRVASRRA LVDRWSKADG KLFLKAELQS WIKDSHQTVF SQAWGALVKT
AVQEKRTASS S
//