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 A2QAF9

Entry ID Method Resolution Chain Position Source
AF-A2QAF9-F1 Predicted AlphaFoldDB

No variants for A2QAF9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A2QAF9

No associated diseases with A2QAF9

2 regional properties for A2QAF9

Type Name Position InterPro Accession
domain Peptidase M24 141 - 462 IPR000994
binding_site Peptidase M24A, methionine aminopeptidase, subfamily 2, binding site 227 - 243 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
MGSKSPEGHR QTPDASNSSE LKPANPNPKP ARNGSQSADL DGGNLDDDND DDGEANEEAG
70 80 90 100 110 120
VKTSADSTDK KKKRKRSKKK TKKGTLPLKQ SSPPRVLVSS LFPSGYPIGE CVPYQDDNTS
130 140 150 160 170 180
RTTDEELRYN SRLWDKDFLD EYRQAAEIHR QVRQYAQNEL IKPGASLTTI AEGIEDGVRA
190 200 210 220 230 240
LSGHQGLEPG DGFKAGMGFP TGLCLNNVAA HWTPNPGAKD VFLDKSDVLK VDFGVHVNGR
250 260 270 280 290 300
IVDSAFTVAF DHTYDNLLTA VKEATNTGIM HAGIDARVSE IGAAIQEVME SYEVEIAGKT
310 320 330 340 350 360
HPVKAIRNIT GHDILRYNIH GGKQVPFIKN DRPDKMEEGE VFAIETFGST GRGVLHDDVG
370 380 390 400 410 420
LCLSNVFSKA NAPQVGVYGY GRNTDVSGAN LRLSSAKNLL KTIDANFGSL VFCRRYLERL
430 440 450 460 470
GVEKYHLGMR HLIDNGIVEY YEPLVDVKGS YTAQFEHTIL LHNGGKEVIS RGDDY