GenomeNet

Database: UniProt
Entry: W6LG78_9TRYP
LinkDB: W6LG78_9TRYP
Original site: W6LG78_9TRYP 
ID   W6LG78_9TRYP            Unreviewed;       719 AA.
AC   W6LG78;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=GSHART1_T00007450001 {ECO:0000313|EMBL:CCW69981.1};
OS   Phytomonas sp. Hart1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW69981.1, ECO:0000313|Proteomes:UP000053358};
RN   [1] {ECO:0000313|EMBL:CCW69981.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW69981.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW69981.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW69981.1};
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).
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DR   EMBL; HF955205; CCW69981.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6LG78; -.
DR   EnsemblProtists; CCW69981; CCW69981; GSHART1_T00007450001.
DR   OrthoDB; 5488182at2759; -.
DR   Proteomes; UP000053358; 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:SF234; ATP-DEPENDENT RNA HELICASE DHX40-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:UP000053358}.
FT   DOMAIN          18..187
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          212..384
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          558..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..574
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..589
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  79744 MW;  63C9E761A98F931D CRC64;
     MSSHADALPV AEARPAIVRL LKRHQVVVIV GETGSGKTTQ IPQYVWDDVV STYPAEKRGL
     VGCTQPRRVA AVSIARHVAK QRQGTLGAEV GYAVRFDDVC TDATRIKYLT DGILLREIQT
     DPDLEKYSYI ILDEAHERTL HGDILFGLLK AIVRRRGKAL KIVVMSATLN AEQFRAFWWN
     APIGVVHGRT FPVSILHTLE PQADYVEASV SAILQIHLNE EPGDVLCFLT GQEEIEDAKR
     ILENRVKLLQ EDVQGFVVLT LYSAMPYELQ LRVFDVAPSG RRKIILATNI AETSITVEGI
     KYIVDSGVVK AKYYNSKTGI EALVEVDISR AQALQRSGRA GRMSVGKCFR LYTAEAFEAL
     QVDTTPEIRR SSLVSVVLHM KSLGIDDILN FEFMDPPRAS SVVKAEEMLL LLQALDKHGK
     ITRLGKRLTD FPIDPTSAKT LLAAKSIGVA RDAVAVVALT NTENLFLTSH EFRDRADRCK
     ASFAKAAGDH ATLLSIYQTF CRTLEKDRRV WCETNGINYK QMLKAEDIKT QLSAILLAQG
     EDDDELFQKN GVVSSNGVQN AKKPDLSSSS KSITLSKRLR EEDKGDDGAT ELNLSAPQDS
     LEMGDIDNGS SSVAPMSNSE AGHGRQKWRD YELLRRALCA GFFLNTAYFD AKIGMYKTVV
     GQQAVHLHPS SVLFSHRKKP ALVIFNSVVW TNKCYMKDVS VVYEEWLSET ASSFFIPAS
//
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