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ECOLI:DEAD

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) deaD (ECO:0000255 with HAMAP-Rule:MF_00964) (synonyms: csdA, mssB, rhlD)
Protein Name(s) ATP-dependent RNA helicase DeaD (ECO:0000255 with HAMAP-Rule:MF_00964)

Cold-shock DEAD box protein A (ECO:0000255 with HAMAP-Rule:MF_00964) Translation factor W2

External Links
UniProt P0A9P6
EMBL M63288
U18997
U00096
AP009048
U03750
PIR F65106
RefSeq NP_417631.2
YP_491349.1
ProteinModelPortal P0A9P6
SMR P0A9P6
DIP DIP-35752N
IntAct P0A9P6
MINT MINT-1219396
STRING 511145.b3162
SWISS-2DPAGE P0A9P6
PaxDb P0A9P6
PRIDE P0A9P6
EnsemblBacteria AAC76196
BAE77208
GeneID 12933435
947674
KEGG ecj:Y75_p3084
eco:b3162
PATRIC 32121742
EchoBASE EB0211
EcoGene EG10215
eggNOG COG0513
HOGENOM HOG000268810
InParanoid P0A9P6
KO K05592
OMA TRRFMKD
OrthoDB EOG6GBMBM
PhylomeDB P0A9P6
BioCyc EcoCyc:EG10215-MONOMER
ECOL316407:JW5531-MONOMER
PRO PR:P0A9P6
Proteomes UP000000318
UP000000625
Genevestigator P0A9P6
GO GO:0005737
GO:0005524
GO:0004004
GO:0003724
GO:0033592
GO:0006200
GO:0070417
GO:0048255
GO:0045727
GO:0000027
GO:0006401
Gene3D 3.40.50.300
HAMAP MF_00964
InterPro IPR021046
IPR005580
IPR011545
IPR028618
IPR014001
IPR001650
IPR027417
IPR000629
IPR014014
Pfam PF03880
PF00270
PF12343
PF00271
SMART SM00487
SM00490
SUPFAM SSF52540
PROSITE PS00039
PS51192
PS51194
PS51195

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0048255

mRNA stabilization

PMID:7526223[1]

ECO:0000315

P

Fig. 4

complete
CACAO 2600

GO:0016887

ATPase activity

PMID:15196029[2]

ECO:0000314

F

Table 1

complete
CACAO 2604

involved_in

GO:0048255

mRNA stabilization

PMID:7526223[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0070417

cellular response to cold

PMID:8552679[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0070417

cellular response to cold

PMID:20484467[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0070417

cellular response to cold

PMID:8552679[3]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045727

positive regulation of translation

PMID:24708042[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0033592

RNA strand annealing activity

PMID:23291905[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009314

response to radiation

PMID:27718375[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006401

RNA catabolic process

PMID:15554978[8]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P21513

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004004

ATP-dependent RNA helicase activity

PMID:17259309[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004004

ATP-dependent RNA helicase activity

PMID:15196029[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003724

RNA helicase activity

PMID:8552679[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0000027

ribosomal large subunit assembly

PMID:15148362[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000027

ribosomal large subunit assembly

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR028618

P

Seeded From UniProt

complete

enables

GO:0003676

nucleic acid binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011545

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR034415

F

Seeded From UniProt

complete

enables

GO:0004004

ATP-dependent RNA helicase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR028618

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011545

F

Seeded From UniProt

complete

enables

GO:0016817

hydrolase activity, acting on acid anhydrides

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR021046

F

Seeded From UniProt

complete

involved_in

GO:0070417

cellular response to cold

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR028618

P

Seeded From UniProt

complete

involved_in

GO:0000027

ribosomal large subunit assembly

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000110955

P

Seeded From UniProt

complete

involved_in

GO:0006401

RNA catabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000110955

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000110955

C

Seeded From UniProt

complete

enables

GO:0004004

ATP-dependent RNA helicase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000110955

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000110955

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000110955

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0694

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0004386

helicase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0347

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 Iost, I & Dreyfus, M (1994) mRNAs can be stabilized by DEAD-box proteins. Nature 372 193-6 PubMed GONUTS page
  2. ↑ 2.0 2.1 Bizebard, T et al. (2004) Studies on three E. coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases. Biochemistry 43 7857-66 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 Jones, PG et al. (1996) Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 93 76-80 PubMed GONUTS page
  4. ↑ Jagessar, KL & Jain, C (2010) Functional and molecular analysis of Escherichia coli strains lacking multiple DEAD-box helicases. RNA 16 1386-92 PubMed GONUTS page
  5. ↑ Vakulskas, CA et al. (2014) Global effects of the DEAD-box RNA helicase DeaD (CsdA) on gene expression over a broad range of temperatures. Mol. Microbiol. 92 945-58 PubMed GONUTS page
  6. ↑ Stampfl, S et al. (2013) Characterization of the kinetics of RNA annealing and strand displacement activities of the E. coli DEAD-box helicase CsdA. RNA Biol 10 149-56 PubMed GONUTS page
  7. ↑ Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page
  8. ↑ Prud'homme-Généreux, A et al. (2004) Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome'. Mol. Microbiol. 54 1409-21 PubMed GONUTS page
  9. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  10. ↑ Turner, AM et al. (2007) Mutational analysis of the Escherichia coli DEAD box protein CsdA. J. Bacteriol. 189 2769-76 PubMed GONUTS page
  11. ↑ Charollais, J et al. (2004) CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in the biogenesis of 50S ribosomal subunit. Nucleic Acids Res. 32 2751-9 PubMed GONUTS page
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