Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q87KD5

Entry ID Method Resolution Chain Position Source
AF-Q87KD5-F1 Predicted AlphaFoldDB

No variants for Q87KD5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q87KD5

No associated diseases with Q87KD5

No regional properties for Q87KD5

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q87KD5

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
MSVLQVLTFP DDRLRTVAKP VDAVTPEIQK IVDDMIETMY DEEGIGLAAT QVDIHKRIVV
70 80 90 100 110 120
IDISETRDEP MVLINPEILE KRGEDGIEEG CLSVPGARAL VPRAAEVTVK ALDRDGKEFT
130 140 150 160 170
FEADDLLAIC VQHELDHLQG KLFVDYLSPL KRKRIQDKLA KIKRFNEKQQ NA