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 E3Q897

Entry ID Method Resolution Chain Position Source
AF-E3Q897-F1 Predicted AlphaFoldDB

No variants for E3Q897

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for E3Q897

No associated diseases with E3Q897

3 regional properties for E3Q897

Type Name Position InterPro Accession
domain Peptidase M24 208 - 502 IPR000994
conserved_site Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site 375 - 387 IPR001131
domain Aminopeptidase P, N-terminal 42 - 171 IPR007865

Functions

Description
EC Number 3.4.11.9 Aminopeptidases
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
manganese ion binding Binding to a manganese ion (Mn).
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.

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
METVVDHHVI EVDEFDALFI EVKTEAAPVE SVVSVAPIPA RFPAKLHARK IAAELNASDG
70 80 90 100 110 120
LVFLPGEPSR SYEDSDMGPA FRQRRYFYYL SGANFADCAV TYELASDRLI LWVPYVEPRQ
130 140 150 160 170 180
VLWFGSTPGI SECLKQFDVD DVRYTTQLNK FLYRHLTPGS TLYVIHADQV PLHGDFLQSA
190 200 210 220 230 240
AEVRIDVTSL QPAMDQARVV KTDYEVAMIR KAAAVSALAH RRVAEKLLRL ENESEIEAVY
250 260 270 280 290 300
QAWCTTSGAR EQAYAIIAGS GKNASTLHYD ANNEPLEGRE VVVFDAGCEW HCYASDITRT
310 320 330 340 350 360
LPISGKFSAE AKAVYDVVAK MQDECISFIR PGTLFFDLHI HASRVAQQGL LKLGVLKGDP
370 380 390 400 410 420
AEVWDAGTVA AFFPHGLGHH VGLEVHDVSG RERLLLLNNV MGAQGGRVGK REVVTPEMLG
430 440 450 460 470 480
AMVQASAPGA AAAAAPPPYK GRQYLRKNMI VTVEPGIYFC REYIEGYFLS NPRHARFINK
490 500 510 520
TVLERYYRVG GVRIEDDILV TDDGYENLST GAPKGEELLR VINGKA