ID X6MK96_RETFI Unreviewed; 796 AA.
AC X6MK96;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
DE Flags: Fragment;
GN ORFNames=RFI_22954 {ECO:0000313|EMBL:ETO14413.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO14413.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO14413.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
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. DDX10/DBP4
CC subfamily. {ECO:0000256|ARBA:ARBA00038084}.
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:ETO14413.1}.
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DR EMBL; ASPP01020048; ETO14413.1; -; Genomic_DNA.
DR AlphaFoldDB; X6MK96; -.
DR EnsemblProtists; ETO14413; ETO14413; RFI_22954.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000023152; 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; 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; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR24031:SF54; ATP-DEPENDENT RNA HELICASE DDX10-RELATED; 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; SM01178; DUF4217; 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.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000023152};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 174..202
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 205..382
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 404..567
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 729..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 174..202
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETO14413.1"
SQ SEQUENCE 796 AA; 91858 MW; 89B1B497EB09F985 CRC64;
FECLKVRNVL GTKRKKRDYP FCSVIKFIFL KTIKSAMSER KKNWRGNKEK KWLEEDIEEE
EEEGFAEDLA EGDKYLAIRP EGPITGAVWE NGKWIHVGQK RKRFKSKHED ENNDEYLDPH
TNVVTNPRKK QKFLMKVEQA EIEKLSREVK RKKPPRDVNP LLQLKGEGEY KLAEKFEELN
ISEYTKYMLK ENKWTYMTDI QKLCIPHGLV GRDILGAAKT GSGKTLSFVI PLIENLYRKA
WHVELGLGAL VLAPTRELAL QIFETIRMVG KRMRHLSIGL IIGGQHSKME EEKNLIGRMT
ILVATPGRLL SHLEQSFELN ANHLQILILD EADVMFDVGL FNQVQTILEY LPKKRQTMLF
SATLTMDILH LANLSLRRPI LIPLDAPNSQ ALPTQLMQTY IQIPLEQKLN LLWSFMQTHI
NDKILVFFAT LRQVKFARRV FNKLRPFSSL LALHSEMKQF KRMAMYQKFK IAKHRTVLFA
TEIAARGLDF PNVDWVINFD VPSHIHSYIH RVGRAARLTQ KGNCITFLIP QEMPFIQELQ
KFNISVRKLG IHTQQLKSIT PQIRTLLATD DKMLQLAKKS FFSFLKSYYR LASSNPLYIR
PDLLDKDLLA QMFGLMHTPN FSHIVSKYTK SSEFDQPKKI NSLKDNSIPQ DLKMLLLDTK
KKQRQSQKLK SLTLASSSIN PNNPQLLTPL DQRLSDAAKN TALNMPSHSL PLQRDTRIAK
SQLAMLVPDV EDHPKSNVNP PPSSSSKPDI SEWLEQDLND FLDDIDDNAD DDYTNTNTKN
NEDILEQSAL QAILNR
//
