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 Q4IN00

Entry ID Method Resolution Chain Position Source
AF-Q4IN00-F1 Predicted AlphaFoldDB

No variants for Q4IN00

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4IN00

No associated diseases with Q4IN00

3 regional properties for Q4IN00

Type Name Position InterPro Accession
domain Oxoglutarate/iron-dependent dioxygenase 188 - 292 IPR005123
domain Non-haem dioxygenase N-terminal domain 38 - 151 IPR026992
domain Isopenicillin N synthase-like, Fe(2+) 2OG dioxygenase domain 193 - 291 IPR044861

Functions

Description
EC Number 5.2.1.8 Cis-trans isomerases
Subcellular Localization
  • Endoplasmic reticulum
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).

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).

2 GO annotations of biological process

Name Definition
chaperone-mediated protein folding The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
protein peptidyl-prolyl isomerization The modification of a protein by cis-trans isomerization of a proline residue.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKAALFLSAL ASTAVGVVAE ELKIDVTLPV ICERKTQKGD GVHMHYRGTL KDSGKQFDAS
70 80 90 100 110 120
YDRGTPLSFK VGAGQVIKGW DEGLLDMCIG EKRVLTIPPE FGYGQRAIGP IPAGSTLVFE
130 140 150 160 170 180
TELVGIDGVP KPEKIETKVV EGAESAAEAI SEATEAAATA SQKVAGKVAE AIVDAAKAAK
190
TIIADTDDAP EHEEL