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Database: UniProt
Entry: W6KG67_9TRYP
LinkDB: W6KG67_9TRYP
Original site: W6KG67_9TRYP 
ID   W6KG67_9TRYP            Unreviewed;       932 AA.
AC   W6KG67;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=GSEM1_T00000551001 {ECO:0000313|EMBL:CCW59972.1};
OS   Phytomonas sp. EM1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=479712 {ECO:0000313|EMBL:CCW59972.1, ECO:0000313|Proteomes:UP000027080};
RN   [1] {ECO:0000313|EMBL:CCW59972.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EM1 {ECO:0000313|EMBL:CCW59972.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW59972.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM1 {ECO:0000313|EMBL:CCW59972.1};
RX   PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA   Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA   Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA   Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA   Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA   Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA   Wincker P., Dollet M.;
RT   "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT   Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL   PLoS Genet. 10:e1004007-e1004007(2014).
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};
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DR   EMBL; HF955061; CCW59972.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6KG67; -.
DR   EnsemblProtists; CCW59972; CCW59972; GSEM1_T00000551001.
DR   OrthoDB; 167906at2759; -.
DR   Proteomes; UP000027080; 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   CDD; cd17917; DEXHc_RHA-like; 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; 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:SF136; ATP-DEPENDENT RNA HELICASE DHX35-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; 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   4: Predicted;
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:UP000027080}.
FT   DOMAIN          188..389
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          403..588
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          227..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..261
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   932 AA;  103782 MW;  DF89C54CFC84AB40 CRC64;
     MDRDAIKKAQ QASRTAFLKK QSKLQSKTSS AVLEERIKDI EQGVVPQSLV EADFLLKRAE
     QVRAAQGLLQ TATHRHEMAD NTAIQSTKDL PSLSGDTVFG DRLGISEDVL PPYTRDVKDG
     AGSDAVGSGF VAMDSETIER RVKAHEYVPE KSIDEIERDR VASLQQRHEL LQAQRRSLPI
     YGVRAELLQL IKDNQVVVLV GETGSGKSTQ LLQYLYEEGF HLLSRTERRS TEAVSRPDPE
     NSAKEDRGDE DEAEDDDEGD ELRLICTQPR RIAAMSVAER VAQEVGCSCG SVVGYRVRFD
     DRSSSLTRIL FVTDGMMLNE FTKDPNLESV AAIMIDEAHE RSLSTDILLG LLRDVVRRNP
     HIRVIVASAT INAEKFSNFF NKAPILNVKG RTFAVDVFYV DVPITDYVSE SAQTALSLHL
     TKPLPGDILI FLPGQDAIES CAEILRQNLA ESQGTMRPLL ILPIYSAMPP KEQARIYTPT
     PPGARKVVIA TNIAETSITI DGIVYVVDCG LCKQDYYNAR AMVEELRVVP TSQASAQQRA
     GRAGRTQRGE CFRLYTPYTF RNELLEETTP EILRASMSAV VLQLKAIGVD NLLQFDFVDP
     PSTESLERAL DQLYLLGAMK ADGRLTVTGR RMSEFPLEPP LSKALLRACG LRCGRHMAMA
     AAMLSIDSIF LTSRDPQERQ LVESAKGELF AFGNGDVAGY VRVMEEWLRA GPQAGEFCRV
     HGIHPRSLLR ARDVLDQILK IYDRIGLDLK EDDSNERHPT TLAAPEARGA TEGLYPSGRM
     INTEALTKAL LSGFFFNVAK MGLDKRTYTI VRPIHTGGSS YGASLDDDAC TTEIHPNSFL
     FRSGMKALPN KGLAAMMQSK ETSNGADVDL RIPQVLRERP SLVVFTQLRR TTKRYMMHLT
     AIESVDMILE MSPLNYFTRE ELETKMRKRL RE
//
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