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 P07211

Entry ID Method Resolution Chain Position Source
AF-P07211-F1 Predicted AlphaFoldDB

No variants for P07211

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P07211

No associated diseases with P07211

2 regional properties for P07211

Type Name Position InterPro Accession
domain Blue (type 1) copper domain 58 - 181 IPR000923
binding_site Blue (type 1) copper protein, binding site 160 - 175 IPR028871

Functions

Description
EC Number
Subcellular Localization
  • Cell outer membrane; Lipid-anchor
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cell outer membrane A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures.

2 GO annotations of molecular function

Name Definition
copper ion binding Binding to a copper (Cu) ion.
electron transfer activity Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKAYLALISA AVIGLAACSQ EPAAPAAEAT PAGEAPASEA PAAEAAPADA AEAPAAGNCA
70 80 90 100 110 120
ATVESNDNMQ FNTKDIQVSK ACKEFTITLK HTGTQPKASM GHNLVIAKAE DMDGVFKDGV
130 140 150 160 170 180
GAADTDYVKP DDARVVAHTK LIGGGEESSL TLDPAKLADG DYKFACTFPG HGALMNGKVT
LVD