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Database: UniProt
Entry: W2W3X6_PHYPR
LinkDB: W2W3X6_PHYPR
Original site: W2W3X6_PHYPR 
ID   W2W3X6_PHYPR            Unreviewed;      1331 AA.
AC   W2W3X6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=F441_18112 {ECO:0000313|EMBL:ETP05237.1};
OS   Phytophthora parasitica CJ01A1.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317063 {ECO:0000313|EMBL:ETP05237.1, ECO:0000313|Proteomes:UP000018958};
RN   [1] {ECO:0000313|EMBL:ETP05237.1, ECO:0000313|Proteomes:UP000018958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ01A1 {ECO:0000313|EMBL:ETP05237.1,
RC   ECO:0000313|Proteomes:UP000018958};
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., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CJ01A1.";
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:ETP05237.1}.
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DR   EMBL; ANIX01003587; ETP05237.1; -; Genomic_DNA.
DR   EnsemblProtists; ETP05237; ETP05237; F441_18112.
DR   Proteomes; UP000018958; 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}.
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
//
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