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 P0A9L4

Entry ID Method Resolution Chain Position Source
AF-P0A9L4-F1 Predicted AlphaFoldDB

No variants for P0A9L4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0A9L4

No associated diseases with P0A9L4

2 regional properties for P0A9L4

Type Name Position InterPro Accession
domain Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal 11 - 108 IPR000774
domain FKBP-type peptidyl-prolyl cis-trans isomerase domain 117 - 206 IPR001179

Functions

Description
EC Number 5.2.1.8 Cis-trans isomerases
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

1 GO annotations of molecular function

Name Definition
peptidyl-prolyl cis-trans isomerase activity Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).

1 GO annotations of biological process

Name Definition
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTTPTFDTIE AQASYGIGLQ VGQQLSESGL EGLLPEALVA GIADALEGKH PAVPVDVVHR
70 80 90 100 110 120
ALREIHERAD AVRRQRFQAM AAEGVKYLEE NAKKEGVNST ESGLQFRVIN QGEGAIPART
130 140 150 160 170 180
DRVRVHYTGK LIDGTVFDSS VARGEPAEFP VNGVIPGWIE ALTLMPVGSK WELTIPQELA
190 200
YGERGAGASI PPFSTLVFEV ELLEIL