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

6 structures for O59196

Entry ID Method Resolution Chain Position Source
1XFO X-ray 196 A A/B/C/D 1-353 PDB
1Y0R X-ray 175 A A 1-353 PDB
1Y0Y X-ray 160 A A 1-353 PDB
6F3K Other 410 A A 1-353 PDB
6R8N Other 410 A A/B/C/D/E/F/G/H/I/J/K/L 1-353 PDB
AF-O59196-F1 Predicted AlphaFoldDB

No variants for O59196

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O59196

No associated diseases with O59196

No regional properties for O59196

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O59196

Functions

Description
EC Number
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

3 GO annotations of molecular function

Name Definition
aminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain.
metal ion binding Binding to a metal ion.
metallopeptidase activity Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEVRNMVDYE LLKKVVEAPG VSGYEFLGIR DVVIEEIKDY VDEVKVDKLG NVIAHKKGEG
70 80 90 100 110 120
PKVMIAAHMD QIGLMVTHIE KNGFLRVAPI GGVDPKTLIA QRFKVWIDKG KFIYGVGASV
130 140 150 160 170 180
PPHIQKPEDR KKAPDWDQIF IDIGAESKEE AEDMGVKIGT VITWDGRLER LGKHRFVSIA
190 200 210 220 230 240
FDDRIAVYTI LEVAKQLKDA KADVYFVATV QEEVGLRGAR TSAFGIEPDY GFAIDVTIAA
250 260 270 280 290 300
DIPGTPEHKQ VTHLGKGTAI KIMDRSVICH PTIVRWLEEL AKKHEIPYQL EILLGGGTDA
310 320 330 340 350
GAIHLTKAGV PTGALSVPAR YIHSNTEVVD ERDVDATVEL MTKALENIHE LKI