ID A0A2S2E5S2_9ALTE Unreviewed; 430 AA.
AC A0A2S2E5S2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ATP-dependent RNA helicase RhlE {ECO:0000256|HAMAP-Rule:MF_00968};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00968};
GN Name=rhlE {ECO:0000256|HAMAP-Rule:MF_00968};
GN ORFNames=HMF8227_02552 {ECO:0000313|EMBL:AWL13004.1};
OS Saliniradius amylolyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Saliniradius.
OX NCBI_TaxID=2183582 {ECO:0000313|EMBL:AWL13004.1, ECO:0000313|Proteomes:UP000245728};
RN [1] {ECO:0000313|EMBL:AWL13004.1, ECO:0000313|Proteomes:UP000245728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF8227 {ECO:0000313|EMBL:AWL13004.1,
RC ECO:0000313|Proteomes:UP000245728};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Salinimonas sp. HMF8227 Genome sequencing and assembly.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DEAD-box RNA helicase involved in ribosome assembly. Has RNA-
CC dependent ATPase activity and unwinds double-stranded RNA.
CC {ECO:0000256|HAMAP-Rule:MF_00968}.
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|HAMAP-Rule:MF_00968};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00968}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlE subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00968}.
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DR EMBL; CP029347; AWL13004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2E5S2; -.
DR KEGG; salh:HMF8227_02552; -.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000245728; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042255; P:ribosome assembly; 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 HAMAP; MF_00968; DEAD_helicase_RhlE; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR028622; DEAD_helicase_RhlE.
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; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 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|HAMAP-
KW Rule:MF_00968}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00968};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00968};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00968};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00968}; Reference proteome {ECO:0000313|Proteomes:UP000245728};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00968}.
FT DOMAIN 1..29
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 32..207
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 233..380
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 373..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..29
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 373..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 47122 MW; BD934D3CFF45F452 CRC64;
MLFNQLGLSA ELQRAVAEQG YSEPTPIQAK AIPEVLKGAD VLAGAQTGTG KTAGFTLPLL
HRLSQNAPKG GKRPVRALVL TPTRELAAQV SDSVKTYGKN LPLKSAVIFG GVSINPQIAA
LKRGVDILVA TPGRLLDHVG QGNLDLSEVE TLVLDEADRM LDMGFIHDIR KVLRLLPDQR
QNLLFSATFS DEIKRLADGF MHNPVLVEVA RRNTASETVE QIIHPVDKGN KRKLLSYLIG
SQNWQQVLVF TRTKHGANRL AKQLDKDGLT SAAIHGNKSQ GARTKALADF KSGKVRVLVA
TDIAARGLDI DQLPHVVNFE LPNVPEDYVH RIGRTGRAGN EGRAVSLLSV DENKQIRDIE
RLIKRQLPRE IIEGFEPDPN AKPEVKEDKP RNNQRRRRPR RGNNAGNGNN GNANGGSGRH
RSRQERSVSA
//
