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 P39298

Entry ID Method Resolution Chain Position Source
AF-P39298-F1 Predicted AlphaFoldDB

No variants for P39298

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P39298

No associated diseases with P39298

1 regional properties for P39298

Type Name Position InterPro Accession
domain Peptidase S9, prolyl oligopeptidase, catalytic domain 86 - 234 IPR001375

Functions

Description
EC Number
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

3 GO annotations of molecular function

Name Definition
hydrolase activity Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
serine-type peptidase activity Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
short-chain carboxylesterase activity Catalysis of the reaction: a carboxylic ester + H2O = an alcohol + a carboxylic anion, where the carboxylic chain has 8 or fewer carbon atoms.

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
MIEIESRELA DIPVLHAYPV GQKDTPLPCV IFYHGFTSSS LVYSYFAVAL AQAGLRVIMP
70 80 90 100 110 120
DAPDHGSRFS GDAARRLNQF WQILLQSMQE FTTLRAAIAE ENWLLDDRLA VGGASMGAMT
130 140 150 160 170 180
ALGITARHPT VRCTASMMGS GYFTSLARSL FPPLIPETAA QQNEFNNIVA PLAEWEATNH
190 200 210 220 230 240
LEQLSDRPLL LWHGLDDDVV PADESLRLQQ ALSETGRDKL LTCSWQPGVR HRITPEALDA
AVTFFRQHL