ID A0A087MGY2_9GAMM Unreviewed; 579 AA.
AC A0A087MGY2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=N788_13660 {ECO:0000313|EMBL:KFL36135.1};
OS Arenimonas donghaensis DSM 18148 = HO3-R19.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1121014 {ECO:0000313|EMBL:KFL36135.1, ECO:0000313|Proteomes:UP000029085};
RN [1] {ECO:0000313|Proteomes:UP000029085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO3-R19 {ECO:0000313|Proteomes:UP000029085};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas donghaensis.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFL36135.1, ECO:0000313|Proteomes:UP000029085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO3-R19 {ECO:0000313|EMBL:KFL36135.1,
RC ECO:0000313|Proteomes:UP000029085};
RX PubMed=26380644; DOI=10.1186/s40793-015-0055-4;
RA Chen F., Wang H., Cao Y., Li X., Wang G.;
RT "High quality draft genomic sequence of Arenimonas donghaensis DSM
RT 18148(T).";
RL Stand. Genomic Sci. 10:59-59(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:KFL36135.1}.
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DR EMBL; AVCJ01000024; KFL36135.1; -; Genomic_DNA.
DR RefSeq; WP_034224610.1; NZ_AVCJ01000024.1.
DR AlphaFoldDB; A0A087MGY2; -.
DR STRING; 1121014.N788_13660; -.
DR PATRIC; fig|1121014.3.peg.1974; -.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000029085; 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; IPR022077; RhlB.
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 Pfam; PF12300; RhlB; 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:UP000029085};
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..220
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 231..391
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 394..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..579
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 420..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 63421 MW; B026C36404A6D35A CRC64;
MSDKPLTDIA FSSFELHPDL QAGLESAGFS RCTPIQALTL PIALRGGDVA GQAQTGTGKT
LAFLVALMNR LLTRPALAER KPEDPRALIL APTRELAIQI HKDAVKFGSD LGLRFALVYG
GVDYDKQRDL LQQGVDVIIA TPGRLIDYVK QHKVVSLHAC EVCVLDEADR MFDLGFIKDI
RFLLRRMPIR TERQTLLFSA TLSHRVLELA YEHMNEPEKL VVETETITAA RVRQRVYLPA
DEEKIPLLIG LLTRSEGQRT MVFVNTKVWV ERVAKALERA GFRVGVLSGD VPQKKRETLL
GRFQKGQLDL LVATDVAARG LHIDGVSHVY NYDLPFDAED YVHRIGRTAR LGAEGDAISF
ACERYAMSLP DIEAYIEQKL PVEPVTAELL VPMPRTPRAS DGEEAGETES VSAIYREVRE
AKAAEDERRG GSRSGSRGGR EGGRSGGASR ERGPRSSGPR REPRSATGDD APAASKAPDA
AADAGVERPA RRPAPSSPMQ EDPNAPARKR RRRRRGRPVG EAADAGTPRS ESPRKDAPRK
DAARKKPEAK PTADAKPSLL GRIKAGLSSL VKRNPPAKH
//
