ID A0A0W0TWL0_9GAMM Unreviewed; 568 AA.
AC A0A0W0TWL0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ATP-dependent RNA helicase DeaD {ECO:0000256|HAMAP-Rule:MF_00964};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00964};
DE AltName: Full=Cold-shock DEAD box protein A {ECO:0000256|HAMAP-Rule:MF_00964};
GN Name=deaD {ECO:0000256|HAMAP-Rule:MF_00964,
GN ECO:0000313|EMBL:KTD00168.1};
GN Synonyms=csdA {ECO:0000256|HAMAP-Rule:MF_00964};
GN ORFNames=E4T54_02970 {ECO:0000313|EMBL:QBS11788.1}, Lgee_1080
GN {ECO:0000313|EMBL:KTD00168.1};
OS Legionella geestiana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45065 {ECO:0000313|EMBL:KTD00168.1, ECO:0000313|Proteomes:UP000054785};
RN [1] {ECO:0000313|EMBL:KTD00168.1, ECO:0000313|Proteomes:UP000054785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49504 {ECO:0000313|EMBL:KTD00168.1,
RC ECO:0000313|Proteomes:UP000054785};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QBS11788.1, ECO:0000313|Proteomes:UP000294523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1308 {ECO:0000313|EMBL:QBS11788.1,
RC ECO:0000313|Proteomes:UP000294523};
RA Durieux I., Ginevra C., Attaiech L., Picq K., Juan P.A., Jarraud S.,
RA Charpentier X.;
RT "Diverse conjugative elements silence natural transformation in Legionella
RT species.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DEAD-box RNA helicase involved in various cellular processes
CC at low temperature, including ribosome biogenesis, mRNA degradation and
CC translation initiation. {ECO:0000256|HAMAP-Rule:MF_00964}.
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_00964};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00964}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DeaD/CsdA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00964}.
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DR EMBL; LNYC01000037; KTD00168.1; -; Genomic_DNA.
DR EMBL; CP038271; QBS11788.1; -; Genomic_DNA.
DR RefSeq; WP_028386952.1; NZ_UGNZ01000001.1.
DR AlphaFoldDB; A0A0W0TWL0; -.
DR STRING; 45065.Lgee_1080; -.
DR KEGG; lgt:E4T54_02970; -.
DR PATRIC; fig|45065.4.peg.1156; -.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000054785; Unassembled WGS sequence.
DR Proteomes; UP000294523; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070417; P:cellular response to cold; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd12499; RRM_EcCsdA_like; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00964; DEAD_helicase_DeaD; 1.
DR InterPro; IPR034415; CsdA_RRM.
DR InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR028618; DEAD_helicase_DeaD.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47963:SF8; ATP-DEPENDENT RNA HELICASE DEAD; 1.
DR PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR Pfam; PF03880; DbpA; 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_00964}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00964};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00964};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00964};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00964}; Reference proteome {ECO:0000313|Proteomes:UP000054785};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00964};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00964}.
FT DOMAIN 6..34
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 37..208
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 232..379
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 435..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..34
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 438..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 62989 MW; 4F4B04FFD2ADC3C1 CRC64;
MTDQAITFAS LALSEPLLQA LSDMQFVTPS AIQAQTIPPL LAGNDVVGQA QTGTGKTAAF
ALPILHRLTP KSRETQALVI APTRELAIQV AEQCMTLGAR MQGLTVAILC GGQDYRTQLK
QLRDGAQIVV GTPGRILDHL DRGTLQTAAL NTVVLDEADE MLRMGFIEDM ESILSRLPET
RQTALFSATM PPRIRQIANR YLKDPVSVEI RMETATVKSI EQRFLFASQA QKPDALIRVL
AVEDYQGVIV FVRTKSGTEE VAEALQEQGM RAMAIHGDLT QALRERIIDQ FRKGAIDILV
ATDVAARGLD VERVTHVINY DVPHDCETYV HRIGRTGRAG RSGVTILFVT PRESRMLNLI
ERHTRQRIEK ILVPDAYTIE NTRRERFVAN VRARLTHEHI NDYRELVNTL TQDGETSALD
IAAALALLAQ QDKPWSRELP KPAPKPARED DSWRREREPR FSREKPARFG REKPRFEGRE
SRAFADDSGP QELYRIDVGR IHGVKPGNIV GAIANEAGLQ GRQIAGIKIH DDHTTLRLPG
GMSKAVLSTL AKAWVCGRKL NLTSLGSA
//
