ID A0A0F4QJH8_9GAMM Unreviewed; 428 AA.
AC A0A0F4QJH8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=ATP-dependent RNA helicase RhlB {ECO:0000256|HAMAP-Rule:MF_00661};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00661};
GN Name=rhlB {ECO:0000256|HAMAP-Rule:MF_00661};
GN ORFNames=TW77_15285 {ECO:0000313|EMBL:KJZ07454.1};
OS Pseudoalteromonas rubra.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ07454.1, ECO:0000313|Proteomes:UP000033452};
RN [1] {ECO:0000313|EMBL:KJZ07454.1, ECO:0000313|Proteomes:UP000033452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2471 {ECO:0000313|EMBL:KJZ07454.1,
RC ECO:0000313|Proteomes:UP000033452};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
CC -!- FUNCTION: DEAD-box RNA helicase involved in RNA degradation. Has RNA-
CC dependent ATPase activity and unwinds double-stranded RNA.
CC {ECO:0000256|HAMAP-Rule:MF_00661}.
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_00661};
CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation.
CC {ECO:0000256|HAMAP-Rule:MF_00661}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00661}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00661}.
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:KJZ07454.1}.
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DR EMBL; JXYA01000037; KJZ07454.1; -; Genomic_DNA.
DR RefSeq; WP_046005853.1; NZ_JXYA01000037.1.
DR AlphaFoldDB; A0A0F4QJH8; -.
DR PATRIC; fig|43658.5.peg.3233; -.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000033452; 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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
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_00661; DEAD_helicase_RhlB; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; IPR023554; RNA_helicase_ATP-dep_RhlB.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959:SF10; ATP-DEPENDENT RNA HELICASE RHLB; 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_00661}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00661};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00661};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00661};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00661}; Reference proteome {ECO:0000313|Proteomes:UP000033452};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00661}.
FT DOMAIN 9..37
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 40..218
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 242..389
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 393..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..37
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 400..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 48225 MW; 003A3F5C8A6470BC CRC64;
MTKTHLTNKK FIDFALAPEV VAGLTASGFE YCTPIQAKCM PYISEGRDIA GQAQTGTGKT
LAFLTATCHR LLQSQSDAQV AGQPRALIMA PTRELAIQIH KDAQILAPAC GLKLGLVYGG
EEYEKQRSQL EKGVDILIGT TGRLIDFYKQ GAYNLNNIEV VVLDEADRMF DLGFIKDIRY
MFNRMPDTQQ RLNLLFSATL SYRVQELAFE HMHNPIHVQI EPDVKTGKRI KEELFHPSQE
DKIPLLLTLI EEEWPDKAIV FANTKHSCEN VYEWLKNDGH RVGLLTGDVN QKKRLSILSR
FTKGELDLLV ATDVAARGLH IPEVSHVLNF DLPDDCEDYV HRIGRTGRAG ASGHAISFAC
EQYAYNLHEI EEYIDHAIPV SHYDKSALLD DIKAPARQQR RRNPSGQRGN RSGNNRRQGS
YQKSRPRS
//
