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 A4ST57

Entry ID Method Resolution Chain Position Source
AF-A4ST57-F1 Predicted AlphaFoldDB

No variants for A4ST57

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4ST57

No associated diseases with A4ST57

No regional properties for A4ST57

Type Name Position InterPro Accession
No domain, repeats, and functional sites for A4ST57

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
MAILDVLRFP DERLRTVAAP VETFTPELQH IVDDMFETMY AEEGIGLAAT QVDIHQRIIV
70 80 90 100 110 120
IDVSENREDP LVLINPEILE QAGSTGIEEG CLSVPDHRAL VPRAEWVKVR ALDRNGQPFE
130 140 150 160
LEADDLLAIC IQHEMDHLIG KLFVDYLSPL KRQRIRQKLE KMAREDRKAL