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 A1CCP2

Entry ID Method Resolution Chain Position Source
AF-A1CCP2-F1 Predicted AlphaFoldDB

No variants for A1CCP2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1CCP2

No associated diseases with A1CCP2

2 regional properties for A1CCP2

Type Name Position InterPro Accession
domain Peptidase M24 160 - 465 IPR000994
binding_site Peptidase M24A, methionine aminopeptidase, subfamily 2, binding site 246 - 262 IPR018349

Functions

Description
EC Number 3.4.11.18 Aminopeptidases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
metalloaminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain 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.

2 GO annotations of biological process

Name Definition
protein initiator methionine removal The protein modification process in which the translation-initiating methionine or formylmethionine residue is removed from a protein.
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
MGSKSPEGHN QAPHGAPNAL DKPANPAVKA QNGSGSADLD RGTISNDDDD ADDDEKETQI
70 80 90 100 110 120
NGSSNAGRIY LFPSRPAKFQ HRPTDTPSTP EKKKKKRKRS KKKAKPTEAK QTSPPRVPLS
130 140 150 160 170 180
TLFPSGYPVG ELVADDRTSR VTDEETRYNS RLWDDGFLAD YRQAAEIHRQ VRQYAQRELI
190 200 210 220 230 240
KPGATLSSIA DGIEDGVRAL SGHQGLETGD GLNAGMGFPT GLCVNHVAAH WTPNPGAKEV
250 260 270 280 290 300
VLEKSDVLKV DFGVHVNGRI VDSAFTVAFD PVYDNLLEAV KEATNTGIAH AGIDARVSDI
310 320 330 340 350 360
GAAIQEVMES YELEIAGKSV PVKAIRNITG HNILRYHIHG GKQVPFIKNN RRDKMEEGEV
370 380 390 400 410 420
FAIETFGSTG KGYLDDDFGI YGYGRNEHVP ATGLRLASAR SLVKTIDANF GSLVFSRRYL
430 440 450 460 470
ERLGVKSYHL AMKNLIDNGI VESYAPLVDV KGSYTAQFEH TILLHSGGKE VISRGDDY