ID C9ZIA2_TRYB9 Unreviewed; 739 AA.
AC C9ZIA2;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=TbgDal_I830 {ECO:0000313|EMBL:CBH08894.1};
OS Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH08894.1, ECO:0000313|Proteomes:UP000002316};
RN [1] {ECO:0000313|Proteomes:UP000002316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA Barry J.D., Berriman M., Hertz-Fowler C.;
RT "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT chronic human african trypanosomiasis.";
RL PLoS Negl. Trop. Dis. 4:E658-E658(2010).
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6
CC subfamily. {ECO:0000256|ARBA:ARBA00038200}.
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DR EMBL; FN554964; CBH08894.1; -; Genomic_DNA.
DR RefSeq; XP_011771335.1; XM_011773033.1.
DR AlphaFoldDB; C9ZIA2; -.
DR GeneID; 23858489; -.
DR KEGG; tbg:TbgDal_I830; -.
DR VEuPathDB; TriTrypDB:Tbg972.1.830; -.
DR OrthoDB; 154856at2759; -.
DR Proteomes; UP000002316; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd17956; DEADc_DDX51; 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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24031:SF68; ATP-DEPENDENT RNA HELICASE DDX51; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|RuleBase:RU365068, ECO:0000313|EMBL:CBH08894.1};
KW Hydrolase {ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 43..314
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 494..651
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 169..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 81692 MW; A9009F796EFADFC6 CRC64;
MLSPWNDCVG DDHQWILKPL QNRLRYERPL PVQQAVVPTV RRALLSGLPM DVCLTAPTGS
GKTLCYLLPL LQMITEAKKG TNHTRLLALV LVPTKALGQQ VTHELQRLTR GTTITTVSLC
DEMSVKEEAA ALVRTARLVG SGTHQTQGHY RNVPYMNIYN GDSVSLPSNA AGVAHNEDES
EDGASGSDGG NGEEVGYDSM VDSSLHYYSR ADIVISTPQR LLRHLDGTPG FTLLHLRLLV
IDEADQVLSG NFANFVAKVV ERFEEEQASR VGSTGDRRRL TQLTYSLHKF LCSATLSSHI
TRISEVRLRN CRHFTLDSFG TEIQREDEGE PLPLPSTDDT GSKKKNKRDQ ERGNANTKNK
RGDDVGKGGE EDSCEDGNEE VKLPLSRQQL VRTSFALPPR LQEHVVFVED WYRHAVLLKL
VRAIVDKQKK AEALVEEHKR REEGLAAQDD ESEGTGLGSN DYGTFSRENV RECESTEFRA
LPHRRRGASK LVGASDPSYP SCDDDAGRRI VIFCRSADEA RVMGHFLLSA GVQATEFTTL
ATESERRRAL LKSRPDSCVV ASDALMRGVD VPNVGHVIMY NPPETLSQYV HRAGRTARAM
RAGHLHLLLQ KLGPSGTMKD GEVAMFKAIS AAVSRMQPVR YERHFFMFDV APTQLGKVAI
ESSPEGGNNG EGRGLVKDKA RLLIEEADGY LKETQLRLTG RWVSALESAR RGDAVGNKPS
SATFGGSRRF ISQTKRERG
//
