ID Q5E0J2_VIBF1 Unreviewed; 634 AA. AC Q5E0J2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 15-FEB-2017, entry version 86. 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:AAW87454.1}; GN OrderedLocusNames=VF_A0384 {ECO:0000313|EMBL:AAW87454.1}; OS Vibrio fischeri (strain ATCC 700601 / ES114). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW87454.1, ECO:0000313|Proteomes:UP000000537}; RN [1] {ECO:0000313|EMBL:AAW87454.1, ECO:0000313|Proteomes:UP000000537} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537}; RX PubMed=15703294; DOI=10.1073/pnas.0409900102; RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., RA Stevens A., Visick K., Whistler C., Greenberg E.P.; RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium RT with pathogenic congeners."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005). CC -!- FUNCTION: DEAD-box RNA helicase involved in various cellular CC processes at low temperature, including ribosome biogenesis, mRNA CC degradation and translation initiation. {ECO:0000256|HAMAP- CC Rule:MF_00964}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {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 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00964}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000021; AAW87454.1; -; Genomic_DNA. DR RefSeq; WP_011263263.1; NC_006841.2. DR RefSeq; YP_206342.1; NC_006841.2. DR ProteinModelPortal; Q5E0J2; -. DR STRING; 312309.VF_A0384; -. DR EnsemblBacteria; AAW87454; AAW87454; VF_A0384. DR GeneID; 3280295; -. DR KEGG; vfi:VF_A0384; -. DR PATRIC; 20116748; VBIVibFis127983_2987. DR eggNOG; ENOG4105C1J; Bacteria. DR eggNOG; COG0513; LUCA. DR HOGENOM; HOG000268810; -. DR KO; K05592; -. DR OMA; TEGNATY; -. DR OrthoDB; POG091H01ST; -. DR Proteomes; UP000000537; Chromosome II. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070417; P:cellular response to cold; IEA:InterPro. DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00964; DEAD_helicase_DeaD; 1. DR InterPro; IPR005580; DbpA_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; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. 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; SSF52540; 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|HAMAP-Rule:MF_00964, KW ECO:0000256|RuleBase:RU000492}; KW Complete proteome {ECO:0000313|Proteomes:UP000000537}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00964}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_00964, KW ECO:0000256|RuleBase:RU000492, ECO:0000313|EMBL:AAW87454.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00964, KW ECO:0000256|RuleBase:RU000492}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00964, KW ECO:0000256|RuleBase:RU000492}; KW Reference proteome {ECO:0000313|Proteomes:UP000000537}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00964}; KW Stress response {ECO:0000256|HAMAP-Rule:MF_00964}. FT DOMAIN 6 34 Q_MOTIF. {ECO:0000259|PROSITE:PS51195}. FT DOMAIN 37 208 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 231 379 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. SQ SEQUENCE 634 AA; 70373 MW; 1F8F4153261FC71D CRC64; MSESITEFRQ LALDESILSA LDDMGFVAPT PIQAASIPLL LEGRDALGKA QTGTGKTAAF SLPLLNKINL KQHNPQAIIM APTRELAIQV AAEVKNLGRN IKGLKVLEIY GGASIVDQMR ALSRGAHIIV GTPGRVKDLL NRDRLNLGEV HTFILDEADE MLKMGFVDDV TWILEKAPDT AQRILFSATM PPMVKTIVDR YLREPARVDV AGTNHTVDKV EQNFWVVKGV EKDEAMSRLL ETEETDASIV FVRTRQDTER LADWLSARGF KAAALHGDIP QSQRERTVDN IKNGVIDILV ATDVVARGLD VPRITHVFNY DIPFDVESYI HRIGRTGRAG RKGKAILLVR TNQMRMLRTI ERVTKSTMEE IQLPHRDQVA ECRLAALAAE LQADKEFVAL DAFTDLINKL QETLEIDATT IAAMLLKRQQ GKRPLFYKGP DPMIAAMERA KNRRSDRGER GERGGRGDRP ERGERRQYNN DDFDTYQLEV GREQGVQVKD IVGALANELG FTKGSIGAIK LAPGHTYVQL PKKMSADVAG KLKKLRIRQN ETKAVVVEGV DLTIERRPRT GGGRDDNRGG NGRGGYRGNR ENREGGRGGE RRFDRNKGGD HRGSHRGERA PGGRGRGRSE RSEG //