| Type | Description |
|---|---|
| Definition | peptide deformylase |
| Date | Results | Publications |
|---|---|---|
| 2013-09-14 10:42:00 | Peptide deformylase has very fast association & dissociation kinetics which allows it to frequently sample ribosomes & ensure the processing of nascent chains after emergence. It competes with methionine aminopeptidase for ribosomal tunnel-exit binding sites. | 23770820 |
| 2012-08-04 11:42:00 | Data show that peptide deformylase, threonine dehydrogenase, and cytosine deaminase are very sensitve to hydrogen peroxide. | 22411989 |
| 2007-11-05 21:38:00 | N-terminus verified by Edman degradation on mature peptide | 8244948 |
| Type | IDs |
|---|---|
| Synonymous | ECK3273, fms |
| Gene |
UniProtKB-ID:
DEF_ECOLI
UniprotKB:
P0A6K3
UniParc:
UPI000014A58D
EMBL:
X77800,
X77091,
U18997,
AP009048,
U00096,
X65946,
X63666
EnsemblGenome:
BAE78005,
b3287
KO:
eco:b3287,
ecj:JW3248
|
| Nucleutide sequences |
EMBL-CDS:
BAE78005.1,
CAA54367.1,
CAA54826.1,
AAA58084.1,
AAC76312.1,
CAA45206.1
EnsemblGenome_TRS:
AAC76312,
BAE78005
|
| Protein sequencees |
EnsemblGenome_PRO:
BAE78005,
AAC76312
RefSeq:
NP_417745.1
|
| Others |
UniRef100:
UniRef100_B7UK10
UniRef90:
UniRef90_Q8Z1W9
UniRef50:
UniRef50_P44786
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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