ID A6VTY7_MARMS Unreviewed; 463 AA.
AC A6VTY7;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
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 OrderedLocusNames=Mmwyl1_0985 {ECO:0000313|EMBL:ABR69916.1};
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR69916.1};
RN [1] {ECO:0000313|EMBL:ABR69916.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR69916.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) 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; CP000749; ABR69916.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VTY7; -.
DR STRING; 400668.Mmwyl1_0985; -.
DR KEGG; mmw:Mmwyl1_0985; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_28_3_6; -.
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 5..33
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 36..210
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 237..387
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 380..463
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 406..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 50814 MW; 0192535962DBDCE1 CRC64;
MRTSMSFNKL GLSAPILKAI EDQGYTEPSA IQAQAIPAIL EGQDVMAAAQ TGTGKTAGFT
LPLLEILSKG ENAQSNQVRA LVLTPTRELA AQVAESVKNY GQHLSLKSTV VFGGVKINPQ
MMALRRGADI LIATPGRMMD LYNQKAVRFD KLEVLVLDEA DRMLDMGFIH DIKKILAILP
KKRQNLLFSA TFSPEIRQLA KGLVNNPIEI SVTPRNATAV SVEQWLHPVD KKRKTELLIQ
LIADGRWDQA LVFSRTKHGA NKITKQLEDA GIRASAIHGN KSQGARTRAL ADFKEGRIRI
LVATDIAARG LDIEQLPHVV NFDLPDVAED YVHRIGRTGR AGATGKAISL VAADELDQLR
AIERLTQKLI ERRYEDDFMP THMLPDTTLD TRPIKPNKPK RPREQTNGPR QGNGAKQGGN
PAKQGNAPKS GNRRPSAPKA EMTPGQGLRS KPLAPARRNR KPD
//
