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Database: UniProt
Entry: W2K0K2_PHYPR
LinkDB: W2K0K2_PHYPR
Original site: W2K0K2_PHYPR 
ID   W2K0K2_PHYPR            Unreviewed;      1066 AA.
AC   W2K0K2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=ATP-dependent RNA helicase DOB1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L917_20539 {ECO:0000313|EMBL:ETL78696.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL78696.1};
RN   [1] {ECO:0000313|EMBL:ETL78696.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL78696.1};
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 CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KI683216; ETL78696.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2K0K2; -.
DR   EnsemblProtists; ETL78696; ETL78696; L917_20539.
DR   VEuPathDB; FungiDB:PPTG_06148; -.
DR   Proteomes; UP000054423; 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:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR   CDD; cd18024; DEXHc_Mtr4-like; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 1.
DR   Gene3D; 1.20.1500.20; -; 1.
DR   Gene3D; 2.40.30.300; -; 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; IPR048392; MTR4-like_stalk.
DR   InterPro; IPR025696; MTR4_beta-barrel.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016438; SKI2-like.
DR   InterPro; IPR012961; Ski2/MTR4_C.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21408; MTR4-like_stalk; 1.
DR   Pfam; PF13234; MTR4_beta-barrel; 1.
DR   PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   DOMAIN          137..293
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          374..607
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          599..626
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        16..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1066 AA;  120019 MW;  B7EACF20377A3216 CRC64;
     MDEDLDLFGA FDDSSATLTA EEQAAASSTS TKRKEAPAAS PNDDKVSSPP AKKQQNEGRL
     ASTNLKVVEG KRIDATPVDS NDKHSANVVS TGTQQKNLIS FSVYPPDYEA KPTAGAAAKN
     PAKTYPFTLD PFQQQAVDYI ESGESVLVSA HTSAGKTAVA EYAIAKSLRD KQRVIYTSPI
     KALSNQKYRD LEEEFGDVGL MTGDITINPS ATCLIMTTEI LRSMLYRGSE VMREVAWVIY
     DEIHYMRDKE RGVVWEESII LLPHKVRFVF LSATIPNSKE FAGWICHIHH QPCHVVYTDY
     RPTPLQHYIF PAGGNGLHLV VDEKGKFRED NFQKAIATLS ASADDAAQEL ASYGSNTKRR
     KAQKSNPKKK IGTDVFRIVK LIMERQYDPV IIFSFSKREC EAYALLMSKL DFNTEEEKQS
     VDQLFKNAMD SLSDDDRALP QVDSILPLLR RGIGIHHGGL LPILKEVIEI LFGEGLLKCL
     FATETFSMGL NMPAKTVVFT NCRKYDGKDF RWITAGEYIQ MSGRAGRRSL DARGIVIQML
     SEQMEPQVAK GILYGQADPL FSTFHLGYNM LLNLMRVEDA DPEYMIKQSF HQFQNEQAAP
     VLEEALERAK EEKDQIVIKN EEEVAQYYYL SRSLVRLKEE FLAIRNKPDY VVRFLNGGRL
     VKLYCPDSDD GTTRPKWDWG VIVNFTTKNA SDSTSATPDT VVHVLLNCMT NNGNTKANDA
     TNGSTVSELP TPAPENMMGL STSANYEMKI CPVPLEMLDL ISSLRVYIPK DLRTLESRQA
     VGKSVKEVLR RFPQGVPLLD PREDMDIQDE QFLRVIEKTV DAEKKLKSSA FHNAADKEAR
     FALYNLKMES EAKMRELERK IKESKSLVLR DDLRRRRRVL RRLEFVDKEG VIQRKGRTAC
     EVSTTDELLV TEMIFNGQFN DLSVNDTVAL LSCLINTEKK KETDKPPQAD SLEIPVRQLR
     ETAQRIAKVM QDAKITIDVD EYAGAFNTSL VDVVIAWCQG AKFSQICKMS DAFEGTIIRC
     LRRLEELLRQ LTLAAHSIGD VELEKKFDEG GKKLKRDIVF AASLYL
//
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