ID A0A1S9B1R3_9BACT Unreviewed; 637 AA.
AC A0A1S9B1R3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 18-JUN-2025, entry version 32.
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=B0919_08530 {ECO:0000313|EMBL:OON69326.1};
OS Hymenobacter sp. CRA2.
OC Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC Hymenobacteraceae; Hymenobacter.
OX NCBI_TaxID=1955620 {ECO:0000313|EMBL:OON69326.1, ECO:0000313|Proteomes:UP000189843};
RN [1] {ECO:0000313|EMBL:OON69326.1, ECO:0000313|Proteomes:UP000189843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRA2 {ECO:0000313|EMBL:OON69326.1,
RC ECO:0000313|Proteomes:UP000189843};
RA Kabwe M.H., Vikram S., Govender N., Bezuidt O., Makhalanyane T.P.;
RT "Draft genome sequence of Hymenobacter sp. CRA2 isolated from the shrubland
RT biome in South Africa.";
RL Submitted (FEB-2017) 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:OON69326.1}.
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DR EMBL; MVBC01000004; OON69326.1; -; Genomic_DNA.
DR RefSeq; WP_078011811.1; NZ_MVBC01000004.1.
DR AlphaFoldDB; A0A1S9B1R3; -.
DR STRING; 1955620.B0919_08530; -.
DR OrthoDB; 974172at2; -.
DR Proteomes; UP000189843; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005840; C:ribosome; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0033592; F:RNA strand annealing activity; IEA:TreeGrafter.
DR GO; GO:0009409; P:response to cold; IEA:TreeGrafter.
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; PF25399; DeaD_dimer; 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:UP000189843}.
FT DOMAIN 4..32
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 35..206
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 217..378
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 528..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..32
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 528..537
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..572
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..616
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 70718 MW; A225AB42CBA0555B CRC64;
MEKVKFEELN LSQEVQRAIT DMGYEEASPI QTAAIPVLLE GKDVIGQAQT GTGKTAAFSI
PAIEKVDADS REVQVLVLCP TRELAVQVSG EIQKLGKYKR GLATVPIYGG SSYDRQFKAL
ERGVQVVIGT PGRVMDHLER GTLKLDNCKM IILDEADEML DMGFRDDIET VLSQMPEERQ
TVFFSATMSK PIMELTKKYQ REPQIVKVNH QEMTVSNIEQ MYYEVRGPQK KDVLSRVIDM
YSLKSVIVFA NTKRMVDDIV ADLQAKGYFA DGLHGDMSQQ ARQNTLDKFR KGTLEILVAT
DVAARGIDVD NVEAVVNYDL PADEEYYVHR IGRTGRAGKS GKAFTFVSGR DIYKLRDIMR
FTKAQIKQER IPSFEDVSEV KTTVLLSQIK EIIEKGNLDK YIGRVQRLID QEEEVTSLDI
AAALLKMVMK ETKQAEKALE SDRQKGTPRE GYTRLFVTMG KKDRLHPRDL VDLIVSSSSI
APGRVGDIEL YDKFSFVEVP TENVEEVVEQ LGRTSLYGRP VSFSLATQRE AGQAAAEGGD
ERRPRRTGGF GGPREGGYGQ RREGGYGGGN REGGYQRREG GFGGGQRSGG YGGGNREGGY
RGGNSYGGGQ RSGGYGGRRD SEGGYKPRRD RNEGFED
//
