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 P44573

Entry ID Method Resolution Chain Position Source
AF-P44573-F1 Predicted AlphaFoldDB

No variants for P44573

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P44573

No associated diseases with P44573

2 regional properties for P44573

Type Name Position InterPro Accession
domain Peptidase M3A/M3B catalytic domain 223 - 678 IPR001567
domain Oligopeptidase A, N-terminal domain 28 - 150 IPR045666

Functions

Description
EC Number 3.4.24.70 Metalloendopeptidases
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
metal ion binding Binding to a metal ion.
metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in 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
peptide metabolic process The chemical reactions and pathways involving peptides, compounds of two or more 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
MSMSNPLLNI QGLPPFSQIK PEHIRPAVEK LIQDCRNTIE QVLKQPHFTW ENFILPLTET
70 80 90 100 110 120
NDRLNRAWSP VSHLNSVKNS TELREAYQTC LPLLSEYSTW VGQHKGLYNA YLALKNSAEF
130 140 150 160 170 180
ADYSIAQKKA IENSLRDFEL SGIGLSEEKQ QRYGEIVARL SELNSQFSNN VLDATMGWEK
190 200 210 220 230 240
LIENEAELAG LPESALQAAQ QSAESKGLKG YRFTLEIPSY LPVMTYCENR ALREEMYRAY
250 260 270 280 290 300
ATRASEQGPN AGKWDNSKVM EEILTLRVEL AKLLGFNTYT ELSLATKMAE NPQQVLDFLD
310 320 330 340 350 360
HLAERAKPQG EKELQELKGY CEKEFGVTEL APWDIGFYSE KQKQHLYAIN DEELRPYFPE
370 380 390 400 410 420
NRVISGLFEL IKRIFNIRAV ERKGVDTWHK DVRFFDLIDE NDQLRGSFYL DLYAREHKRG
430 440 450 460 470 480
GAWMDDCIGR KRKLDGSIET PVAYLTCNFN APIGNKPALF THNEVTTLFH EFGHGIHHML
490 500 510 520 530 540
TQIDVSDVAG INGVPWDAVE LPSQFMENWC WEEEALAFIS GHYETGEPLP KEKLTQLLKA
550 560 570 580 590 600
KNFQAAMFIL RQLEFGIFDF RLHHTFDAEK TNQILDTLKS VKSQVAVIKG VDWARAPHSF
610 620 630 640 650 660
SHIFAGGYAA GYYSYLWAEV LSADAYSRFE EEGIFNPITG KSFLDEILTR GGSEEPMELF
670 680
KRFRGREPQL DALLRHKGIM N