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 Q2H1T8

Entry ID Method Resolution Chain Position Source
AF-Q2H1T8-F1 Predicted AlphaFoldDB

No variants for Q2H1T8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2H1T8

No associated diseases with Q2H1T8

No regional properties for Q2H1T8

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q2H1T8

Functions

Description
EC Number
Subcellular Localization
  • Secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

3 GO annotations of molecular function

Name Definition
aminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain.
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.

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
MKVTNASLLA LLLPAVSGRF VETGEPDRSI LYPDGLPQPT ETGEKYHIEL SPGDTRWVTE
70 80 90 100 110 120
DEKWELRRSG KRFFDITDHP DLGALRAMTA SRKKSVFPEK PKYQKELKPF LAELSKTEME
130 140 150 160 170 180
DHLTTFTSFH TRYYKSDYGR QSSEWLLKQV RDTIEKAGAD KHVRAEHFKH PWGQNSIIAT
190 200 210 220 230 240
IPGKTNATVV IGAHQDSINL WLPSVLAAPG ADDDGSGTVT ILEAFRVILQ SEDIVKGNHE
250 260 270 280 290 300
NTLEFHWYSA EEGGLLGSQA IFSSYEKEGR DVKAMLQQDM TGFITRTLDA GKPESVGVIV
310 320 330 340 350 360
DFVDPNLTQF IKVVIDEYCS IPYVETKCGY ACSDHASASK AGYPSAFVIE SAFEYSDNHI
370 380 390 400
HSTEDLIKYL SFDHMLQHAR MTLAFGYELA FTDFAALEKP DHSDSL