ID A0A4R2EQ78_9BACT Unreviewed; 592 AA.
AC A0A4R2EQ78;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase RhpA {ECO:0000256|ARBA:ARBA00074363};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=CLV25_10352 {ECO:0000313|EMBL:TCN70537.1};
OS Acetobacteroides hydrogenigenes.
OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC Rikenellaceae; Acetobacteroides.
OX NCBI_TaxID=979970 {ECO:0000313|EMBL:TCN70537.1, ECO:0000313|Proteomes:UP000294830};
RN [1] {ECO:0000313|EMBL:TCN70537.1, ECO:0000313|Proteomes:UP000294830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL-C {ECO:0000313|EMBL:TCN70537.1,
RC ECO:0000313|Proteomes:UP000294830};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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:ARBA00047984};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|ARBA:ARBA00038437, 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:TCN70537.1}.
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DR EMBL; SLWB01000003; TCN70537.1; -; Genomic_DNA.
DR RefSeq; WP_131838404.1; NZ_SLWB01000003.1.
DR AlphaFoldDB; A0A4R2EQ78; -.
DR OrthoDB; 9785240at2; -.
DR Proteomes; UP000294830; 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:0003723; F:RNA binding; IEA:TreeGrafter.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd12252; RRM_DbpA; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR FunFam; 3.40.50.300:FF:000108; ATP-dependent RNA helicase RhlE; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR050547; DEAD_box_RNA_helicases.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47963:SF8; ATP-DEPENDENT RNA HELICASE DEAD; 1.
DR PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR Pfam; PF03880; DbpA; 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; 1.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000294830}.
FT DOMAIN 5..33
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 37..206
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 217..379
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 517..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 5..33
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 548..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 65833 MW; 86D61EF42C141DA8 CRC64;
MDKLDEFRVL GLSESTLKAL DEKGFETPTP IQALAIPALL NGERDVIGQA QTGTGKTAAF
GLPILERVQP GKGVQALVLV PTRELAIQVT EEMASFKGDK KLFIISIYGG QSISEQLRRL
KKGVEVVVGT PGRVLDHLGR GSLVLDNLQY VILDEADEML NMGFVDDIEE ILQHAPEERR
MLLFSATMPQ RIAKLAKHYM KEPELLKVES KQVTADLTDQ IYFELRDSDR FDALTRIIDV
EPEFYGLVFC RTKNGVDEVT SKLIERGYDA DGLHGDISQA LREKILRKFR NKHINILVAT
DVAARGIDIN DLTHVINYSL PQDPESYVHR IGRTGRAGKQ GTAITFITPS EYRQFVAMQR
NVNVKIRKEK LPTANDVISI KKNKIKTDLE EIVGNESYME YLGMAEDLIA VNGPDIALAS
LLKLAFKDEL DENSYSEIRT VSVDTKGKAR LFIALGKFDG YNSKMIVDLL KDKAHLPDAV
IDDVKVMDAF SFVTIPFKEA EHTLEVLNTM RRGGGRPLAE IAGDSKGGNG GGRGDRRGGG
GGFGGGYRGE RGDRGERRGD RRSGGDRDRG DRGFRDRGDR PRRDRDSRSR RS
//
