ID F9S2D6_9VIBR Unreviewed; 524 AA.
AC F9S2D6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=VII00023_12728 {ECO:0000313|EMBL:EGU39623.1};
OS Vibrio ichthyoenteri ATCC 700023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=870968 {ECO:0000313|EMBL:EGU39623.1, ECO:0000313|Proteomes:UP000004605};
RN [1] {ECO:0000313|EMBL:EGU39623.1, ECO:0000313|Proteomes:UP000004605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700023 {ECO:0000313|EMBL:EGU39623.1,
RC ECO:0000313|Proteomes:UP000004605};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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}.
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:EGU39623.1}.
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DR EMBL; AFWF01000145; EGU39623.1; -; Genomic_DNA.
DR RefSeq; WP_006712247.1; NZ_AFWF01000145.1.
DR AlphaFoldDB; F9S2D6; -.
DR OrthoDB; 9808889at2; -.
DR Proteomes; UP000004605; Unassembled WGS sequence.
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}; 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..206
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 233..377
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 371..524
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 437..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 56101 MW; 2BB368E7CA26CF30 CRC64;
MGFTSLALSA PILKAIQEQG YDTPSPIQAQ AIPAVLEGQD VMAAAQTGTG KTAGFTLPIL
ELLSKGQKAK SNHVRALILT PTRELAAQIQ ENVHNYSRYL DLNSTVVFGG VKINPQMMQL
RKGSDILVAT PGRLLDLFNQ RAVNFSQLEV LVLDEADRML DMGFFRDISK ILNLLPKKRQ
NLLFSATFSP EIRDLAKGLV NNPVEISVAP ANSTAEKVEQ CIYPADKGKK PAMLLKLITD
GNWRQVLVFS RTKHGANRLA HYLNEQGVTA APIHGNKSQG ARTRALADFK SGDVRVLVAT
DIAARGIDIP QLPQVVNFDL PNVPEDYVHR IGRTGRAGEA GKAVSLVCAD ETDELFGIER
LIQTLLPRMD LEGFKPSNPL PESRLDTRPF KAKKPKKAKS PRSGHADGQR SGDNARGNKP
AGKNKRHFGP KSADGQKAQN GKPNSGSKPV GNGQKPAAKS GGNTGSGNTG GGNNANRNGN
AGGNRGNNNS SNNGNRSRSG GNANTAGKPQ QNRRPRPAAN SNRG
//
