| Tag | Content |
|---|
| CPLM ID | CPLM-003193 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ATP-dependent RNA helicase DeaD |
Protein Synonyms/Alias | Cold-shock DEAD box protein A; Translation factor W2 |
Gene Name | deaD |
Gene Synonyms/Alias | csdA; mssB; rhlD; b3162; JW5531 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 99 | EAMTDFSKHMRGVNV | acetylation | [1] | | 365 | RNIERTMKLTIPEVE | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity at low temperature. Involved in 50S ribosomal subunit assembly, acting after SrmB, and could also play a role in the biogenesis of the 30S ribosomal subunit. In addition, is involved in mRNA decay, via formation of a cold-shock degradosome with RNase E. Also stimulates translation of some mRNAs, probably at the level of initiation. |
Sequence Annotation | DOMAIN 37 208 Helicase ATP-binding.
DOMAIN 232 379 Helicase C-terminal.
NP_BIND 50 57 ATP (By similarity).
MOTIF 6 34 Q motif.
MOTIF 156 159 DEAD box. |
Keyword | ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Helicase; Hydrolase; Nucleotide-binding; Reference proteome; RNA-binding; Stress response. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 629 AA |
Protein Sequence | MAEFETTFAD LGLKAPILEA LNDLGYEKPS PIQAECIPHL LNGRDVLGMA QTGSGKTAAF 60
SLPLLQNLDP ELKAPQILVL APTRELAVQV AEAMTDFSKH MRGVNVVALY GGQRYDVQLR 120
ALRQGPQIVV GTPGRLLDHL KRGTLDLSKL SGLVLDEADE MLRMGFIEDV ETIMAQIPEG 180
HQTALFSATM PEAIRRITRR FMKEPQEVRI QSSVTTRPDI SQSYWTVWGM RKNEALVRFL 240
EAEDFDAAII FVRTKNATLE VAEALERNGY NSAALNGDMN QALREQTLER LKDGRLDILI 300
ATDVAARGLD VERISLVVNY DIPMDSESYV HRIGRTGRAG RAGRALLFVE NRERRLLRNI 360
ERTMKLTIPE VELPNAELLG KRRLEKFAAK VQQQLESSDL DQYRALLSKI QPTAEGEELD 420
LETLAAALLK MAQGERTLIV PPDAPMRPKR EFRDRDDRGP RDRNDRGPRG DREDRPRRER 480
RDVGDMQLYR IEVGRDDGVE VRHIVGAIAN EGDISSRYIG NIKLFASHST IELPKGMPGE 540
VLQHFTRTRI LNKPMNMQLL GDAQPHTGGE RRGGGRGFGG ERREGGRNFS GERREGGRGD 600
GRRFSGERRE GRAPRRDDST GRRRFGGDA 629 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0030684; C:preribosome; IDA:EcoCyc. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004004; F:ATP-dependent RNA helicase activity; IDA:EcoCyc. GO:0003723; F:RNA binding; IEA:UniProtKB-KW. GO:0070417; P:cellular response to cold; IMP:EcoCyc. GO:0000027; P:ribosomal large subunit assembly; IMP:EcoCyc. GO:0006401; P:RNA catabolic process; IGI:EcoCyc. |
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