Q1QET1

PR
Gene name
def
Protein name
Peptide deformylase
Names
PDF, Polypeptide deformylase
Species
Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5)
KEGG Pathway
pcr:Pcryo_0038
EC number
3.5.1.88: In linear amides
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

128-184 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q1QET1

Entry ID Method Resolution Chain Position Source
AF-Q1QET1-F1 Predicted AlphaFoldDB

No variants for Q1QET1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1QET1

No associated diseases with Q1QET1

No regional properties for Q1QET1

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q1QET1

Functions

Description
EC Number 3.5.1.88 In linear amides
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
peptide deformylase activity Catalysis of the reaction: formyl-L-methionyl peptide + H2O = formate + methionyl peptide.

1 GO annotations of biological process

Name Definition
translation The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MALLPILSYP DPRLRTIATP VKEVTAEIKT LITDMIETMY DAQGIGLAAS QVDHHIQLIV
70 80 90 100 110 120
MDLSEDKDSP RVFINPKVTP LVEEKQPYEE GCLSVPDVYD KVERPNKVRI EALDENGNKI
130 140 150 160 170 180
DEEVEGLLAV CIQHEMDHLN GVIFVDYLSR LKQTRARDKV RKVLKIREKQ GEQVAEKEPQ
PANS