(data stored in ACNUC7421 zone)

SWISSPROT: C5BFC3_EDWI9

ID   C5BFC3_EDWI9            Unreviewed;       634 AA.
AC   C5BFC3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
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   OrderedLocusNames=NT01EI_0475 {ECO:0000313|EMBL:ACR67710.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67710.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001600; ACR67710.1; -; Genomic_DNA.
DR   RefSeq; WP_015869910.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0475; -.
DR   EnsemblBacteria; ACR67710; ACR67710; NT01EI_0475.
DR   GeneID; 7961296; -.
DR   KEGG; eic:NT01EI_0475; -.
DR   PATRIC; fig|634503.3.peg.430; -.
DR   eggNOG; ENOG4105C1J; Bacteria.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268810; -.
DR   KO; K05592; -.
DR   OMA; LPQGMPK; -.
DR   OrthoDB; POG091H01ST; -.
DR   Proteomes; UP000001485; Chromosome.
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   CDD; cd12499; RRM_EcCsdA_like; 1.
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; 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;
DR   PRODOM; C5BFC3.
DR   SWISS-2DPAGE; C5BFC3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00964,
KW   ECO:0000256|RuleBase:RU000492};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00964};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_00964,
KW   ECO:0000256|RuleBase:RU000492, ECO:0000313|EMBL:ACR67710.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00964,
KW   ECO:0000256|RuleBase:RU000492, ECO:0000313|EMBL:ACR67710.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00964,
KW   ECO:0000256|RuleBase:RU000492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
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      232    379       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   MOTIF         6     34       Q motif. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00552}.
SQ   SEQUENCE   634 AA;  71335 MW;  6E26A1CB17147CF8 CRC64;
     MAEFETTFAD LGLAAPIIEA LNDLGYEKPS PIQAACIPHL LNGRDVLGMA QTGSGKTAAF
     SLPLLNNIDP SLKAPQVLVL APTRELAVQV AEAMADFSKH MHGVNVVALY GGQRYDVQLR
     ALRQGPQIVV GTPGRLLDHL KRGTLSLTSL RGLVLDEADE MLRMGFIEDV ETIMAQIPAE
     HQTALFSATM PEAIRRITRR FMNEPQEVRI QSSVTTRPDI SQSYWTVYGM RKNEALVRFL
     EAEDFDAAII FVRTKNATLE VAEALERNGY SSAALNGDMN QALREQTLER LKDGRLDILI
     ATDVAARGLD VDRISLVVNY DIPMDAESYV HRIGRTGRAG RAGRALLFVD NRERRLLRNI
     ERTMKLTIPE VELPNAELLS ARRLAKFGAR VQQQLESSDL DQYRALLAKL QPEDEQDMET
     LAAALLKMAQ GERPLILPPD PIVERRPRRE FRERDERGGD RFARRERDER GGDRPRRERR
     EVGDMELYRI EVGRDDGVEV RHIVGAIANE GDISSRYIGN IRLFGSHSTI ELPKGMPGDL
     LTHFTRTRIL NKPMNMQLIG DAPAREPRRE RNGERGGERR SFGGRDGGRD GDRRSFGGQR
     RFSDDRRGDR GFNRDSRSAR SDDNGNSRRR FNDA
//

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