ID A0A1J4KHN0_9EUKA Unreviewed; 447 AA.
AC A0A1J4KHN0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 03-MAY-2023, entry version 17.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=TRFO_19661 {ECO:0000313|EMBL:OHT10873.1};
OS Tritrichomonas foetus.
OC Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC Tritrichomonas.
OX NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHT10873.1, ECO:0000313|Proteomes:UP000179807};
RN [1] {ECO:0000313|Proteomes:UP000179807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA Tasca T., Bogo M.R., de Souza W.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|RuleBase:RU000492}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHT10873.1}.
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DR EMBL; MLAK01000599; OHT10873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4KHN0; -.
DR VEuPathDB; TrichDB:TRFO_19661; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000179807; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd18787; SF2_C_DEAD; 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 InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR24031:SF301; ATP-DEPENDENT RNA HELICASE DDX18; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
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; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000179807};
KW RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 8..36
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 39..215
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 242..395
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 374..404
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 8..36
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 447 AA; 49798 MW; A81AB433158A1C21 CRC64;
MSISLNPKTF DELPISKGLK KALHNSKFTH LKPIQSQTIP HLLAGRNVLG ASPTGSGKTL
AFLVPVIELL TYSRTRPNYG TIAIVLSPSR ELALQTFSVA NTLMKELSPT VMAIVGGQKG
FKDEAYALRT KGVNLLIATP GRLRQHLEGG YVKLDHFQFL VIDEADRMLE VGFANDLYSI
FEYIKSPPQT ALFSATLTKD VEGLMKINIS KTPIFCCPSD SSNVETLQHC YSIVPLIDRV
SILARILTHL KSKRIVCFIS NRKEAEFLTR IMNAIDISCD CLHGELNQAE RNLAFVKFNR
NETHVLFATN VASRGLDFPD VDWSISVGPP DRVKDYVHRA GRTARNEKFG QSLILLAPNE
EIFVKHVRNN GIKIKKIELT LSGLEEINQR IENAMNSSRQ FTQLALEAAL GFESSYQARP
AEEGISFDEV DMNDVRISFG LEPEGHI
//
