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 Q97VF1

Entry ID Method Resolution Chain Position Source
AF-Q97VF1-F1 Predicted AlphaFoldDB

No variants for Q97VF1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q97VF1

No associated diseases with Q97VF1

3 regional properties for Q97VF1

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 200 - 416 IPR014782
domain ERAP1-like C-terminal domain 485 - 774 IPR024571
domain Aminopeptidase N-like, N-terminal domain 7 - 166 IPR045357

Functions

Description
EC Number
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.

3 GO annotations of molecular function

Name Definition
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.
peptide binding Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
peptide catabolic process The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
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
MPNIEKYEIF LDFNGNEYEG VEKIYLNSEE EKLELDSVNL EIRSVKSDGK DTKFELKGEK
70 80 90 100 110 120
LVIYGKIERE LEIKFKGKAS RDSILGIYVA PYDGKGMITT QFEAVYARRF IPCFDHPAMK
130 140 150 160 170 180
ARFKLSVRVQ KGLKVISNMP VERIEEDVDG KVIYRFQETP KMSTYLLYLG IDEFEEISDN
190 200 210 220 230 240
SKQPTVILAT VPGKSKRGLF AINVARKVIE FYEKYFEIPY QLPKVHLIQV PEFAAGAMEN
250 260 270 280 290 300
WGAITFRETA LLADDSSSIS QKFRVAEVVA HELAHQWFGN LVTLKWWDDL WLNESFATFM
310 320 330 340 350 360
SYKSIKHLFP QWDSEGHLIY DESIGALEDD SLSTTHPIEA HVKDPHEIEQ MFDNISYGKG
370 380 390 400 410 420
ASILKMIEAY VGEENFRRGV VNYLNSFKFG NAEGKDLWNS ISNAAGQSIG EIMADWITKP
430 440 450 460 470 480
GYPVIFVNAY GNSIRFSQKR FTLLDSGLNE VYKVPITYEI NDKFGTLLLD KESAEIRLDE
490 500 510 520 530 540
GLKSIKVNIN RTGFYRVLYD SLNLAFSSKL NAYEELGLVN DYWNFLLADL IDAKTYFGVI
550 560 570 580 590 600
GRFVYTSNSF VSREITSQLL TLYYLFKKNY GKDFLVNQVK IFRKANDDLG KLAYSTVISA
610 620 630 640 650 660
LARMDEEFAL GLSTLFDQYE NIDSNIKEAV AIAYAVTNND FNTLLEKYKR YTIDEEKNRI
670 680 690 700 710 720
LSAISSLRDP SIVVKVFSLI FERNIKAQDT RFVISSLLHN PHIREEVCSY LMNNFEEVKK
730 740 750 760 770 780
FVNTVYGGPW GLGSIVRSMS FCGVDKPKDI IDFLEKVKFK EIERPIKESE ERIKVYSRLK
QNLP