ID W6KY79_9TRYP Unreviewed; 973 AA.
AC W6KY79;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=GSHART1_T00000152001 {ECO:0000313|EMBL:CCW66023.1};
OS Phytomonas sp. Hart1.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Phytomonas.
OX NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW66023.1, ECO:0000313|Proteomes:UP000053358};
RN [1] {ECO:0000313|EMBL:CCW66023.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hart1 {ECO:0000313|EMBL:CCW66023.1};
RA Genoscope - CEA;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW66023.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hart1 {ECO:0000313|EMBL:CCW66023.1};
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};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR EMBL; HF955199; CCW66023.1; -; Genomic_DNA.
DR AlphaFoldDB; W6KY79; -.
DR EnsemblProtists; CCW66023; CCW66023; GSHART1_T00000152001.
DR OrthoDB; 3682876at2759; -.
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; 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; 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:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 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 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:UP000053358}.
FT DOMAIN 261..425
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 450..628
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 97..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 108709 MW; 61A50E597874AB0C CRC64;
MLGPRPEEKV ELYVNALFAQ PRFFRLGKDF PAIDDRRAVV EDDETGSAVL ATSLWAVAHE
AEGDIILPVV SPQCALAQLA LKGSVALAEL KRALSREQQN REAMDTSRSN LTQLLRKDTL
GREDPSPRVD NDENAPAKDL SASLLRDSDR LQSGQEEMEA LRRKVRLEQE ALGFNSIHLL
SDSRGKGKSD LREAPNRVRL SNETSREELQ RALKREKVER IVAAQSQLES TADSEMAESR
QVAIHRKQEQ LPIFRCRREL LRYIGENTVT IVVGETGSGK TTQLVRYLYE EGYARHGKLI
GCTQPRRLAT IAVARRVSEE MRCALGTTVG YSIHLDDTTT SQTKVKFMTD GVLLREVVRD
PDMDSYSVIM IDEAHERSVD TDVLMGILKN AISDRGDLKL IISSATMDVE KFSRFFGNAP
FYEIPGQTYE VVIHYSPKVV SDYVAEAVFR VCQLHLQAPM EEGQDILVFM TGRDDVYGTC
ELIRRRLREV SPGHLETLLL LPCLSEASGL VEAGALLEKT PRGLRKCVVA TNVAETSLTI
DGVRYVVDCG LMKTKVFRPR LGMNTLQRYP VSRAQANQRK GRAGRTAEGV CFRLFTDEQF
AREMLSNSVP EVQRSSLDSV LLLLKGVGVG RIQEFDFLDP PPAANIRSSM WRLWILGMLD
DEGEITREGR LAIEFPIAPA LAKLLLESTK HGCSFEVSRI VALITADPKN FFELPKGKEV
VAQQHFGRFF NNESDHLTLL NAFTQFLENG KSRQWAQDHY LHFPTLLRTW DVLEQLLDRL
RQLRLPIVSC QQTHGGGLDV VRYCLAHAFS LQAAQRSGSN WNEYRALLNL GVVCALHPSS
AICTSAVMPS FVIYNDLVLV NKEYLVLVTA VEPEWLAEGG LFGMKKSGKT STGPLEPAFP
ILDNMHNTRA MDGSTDKKRG GRENFHEHKT PTLSDVAAKL KLPFTTTPHV GSKNAPNSSK
FAASFSSKRR GNI
//