ID   Q5E0J2_VIBF1            Unreviewed;       634 AA.
AC   Q5E0J2;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   01-OCT-2014, entry version 71.
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.
CC       {ECO:0000256|RuleBase:RU000492}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DeaD
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00964}.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC       {ECO:0000256|HAMAP-Rule:MF_00964}.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC       {ECO:0000256|HAMAP-Rule:MF_00964}.
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DR   EMBL; CP000021; AAW87454.1; -; Genomic_DNA.
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; COG0513; -.
DR   HOGENOM; HOG000268810; -.
DR   KO; K05592; -.
DR   OMA; MEHAPES; -.
DR   OrthoDB; EOG6GBMBM; -.
DR   BioCyc; AFIS312309:GIWP-3126-MONOMER; -.
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.
DR   InterPro; IPR028618; DEAD_helicase_DeaD.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
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:RU000452};
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:RU000452, ECO:0000313|EMBL:AAW87454.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00964,
KW   ECO:0000256|RuleBase:RU000452};
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       37    208       Helicase ATP-binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00964}.
FT   DOMAIN      231    379       Helicase C-terminal. {ECO:0000256|HAMAP-
FT                                Rule:MF_00964}.
FT   NP_BIND      50     57       ATP. {ECO:0000256|HAMAP-Rule:MF_00964}.
FT   MOTIF         6     34       Q motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_00964}.
FT   MOTIF       156    159       DEAD box. {ECO:0000256|HAMAP-Rule:
FT                                MF_00964}.
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
//