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 E3RD74

Entry ID Method Resolution Chain Position Source
AF-E3RD74-F1 Predicted AlphaFoldDB

No variants for E3RD74

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for E3RD74

No associated diseases with E3RD74

2 regional properties for E3RD74

Type Name Position InterPro Accession
domain Peptidase M24 141 - 446 IPR000994
binding_site Peptidase M24A, methionine aminopeptidase, subfamily 2, binding site 226 - 242 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
MGSKSPEDHR QGPDGGSADT AIAIVNPPKS AAASGLLQGM LEGQDEDGDD DDDEKTGIDL
70 80 90 100 110 120
KTNDGAKKKR KRNKKKSKKL SVVQQTSPPR VPLATLFDNQ PYPEGQIVDY NVKDDNLQRT
130 140 150 160 170 180
TAEELRHLAA VRDMDDDFLK DYRKAAEVHR QVRRYAQAIA KPGVSMTRLA EEIDDGVRAL
190 200 210 220 230 240
TGHEGLETGD ALKAGLAFPT GLCLNHVGAH WTPNAGAKDV ILKHDDVLKV DFGVHVNGRI
250 260 270 280 290 300
VDSAFTVAAN PVYDNLLAAV KAATNTGLEE AGIDARIDHI SEAIQEVMES YEVELNGKTI
310 320 330 340 350 360
PIKAVRNITG HNILRYRIHG DKQVPFVKTK TDQRMEEGDI FAIETFGSTG KAYLQDDVGV
370 380 390 400 410 420
YGYGRNENMN PAVLHQSSAK SLLKTIDANF GTLVFARRQL ERLPGVEKYH LGMRTLVNSG
430 440 450
LVESYAPLVD IPGSYIAQFE HTVLLRPNCK EIISRGEDY