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 A7MQN9

Entry ID Method Resolution Chain Position Source
AF-A7MQN9-F1 Predicted AlphaFoldDB

No variants for A7MQN9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A7MQN9

No associated diseases with A7MQN9

2 regional properties for A7MQN9

Type Name Position InterPro Accession
domain Peptidase M24 168 - 430 IPR000994
conserved_site Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site 335 - 347 IPR001131

Functions

Description
EC Number 3.4.13.9 Dipeptidases
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

4 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
metalloexopeptidase activity Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of 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.
phosphoric triester hydrolase activity Catalysis of the hydrolysis of a phosphoric triester.
proline dipeptidase activity Catalysis of the reaction: H2O + a dipeptide with proline at the C-terminal <=> L-proline + a standard alpha amino acid.

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
MDSLTTLYKN HLDTLQERTR NVLARFNLDA LLIHSGELFN VFLDDHPYPF KVNPQFKAWV
70 80 90 100 110 120
PVTQVPNCWL LVDGVNKPKL WFYLPVDYWH NVEPLPSAFW TEEIDIIALP KADDIGGQLP
130 140 150 160 170 180
AARGNIAYIG PVPERALKLD VPADKINPKG VIDYLHFYRA YKTDYELACM REAQKTAVNG
190 200 210 220 230 240
HRAAHEAFLS GMSEFDINLA YLTATGHRDT DVPYSNIVAL NEHAAVLHYT RLDHRAPSEM
250 260 270 280 290 300
RSFLLDAGAE YNGYAADLTR TWAADGDSDF AALIKDVNEE QLALIGTMKA GVSYIDYHIQ
310 320 330 340 350 360
FHQRIAKLLR RHQIVTDISE EAMVEADITG PFMPHGIGHP LGLQVHDVAG FMQDDTGTHL
370 380 390 400 410 420
AAPAKYPYLR CTRVLQPRMV LTIEPGIYFI ESLLVPWREG PFSKHFNWQK IEALKPFGGI
430 440
RIEDNVVIHE HGVENMTRDL KLA