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

6 structures for P80401

Entry ID Method Resolution Chain Position Source
1ADW X-ray 250 A A/B 23-145 PDB
3ERX X-ray 125 A A/B 23-145 PDB
4BWT X-ray 176 A A/B 23-145 PDB
4BWU X-ray 176 A A/B 23-145 PDB
4BXV X-ray 176 A A/B 23-145 PDB
AF-P80401-F1 Predicted AlphaFoldDB

No variants for P80401

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P80401

No associated diseases with P80401

2 regional properties for P80401

Type Name Position InterPro Accession
domain Blue (type 1) copper domain 28 - 114 IPR000923
binding_site Blue (type 1) copper protein, binding site 94 - 108 IPR028871

Functions

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

1 GO annotations of cellular component

Name Definition
periplasmic space The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).

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
MFHHSLAAAA AALLALAAPG FAATHEVHML NKGESGAMVF EPAFVRAEPG DVINFVPTDK
70 80 90 100 110 120
SHNVEAIKEI LPEGVESFKS KINESYTLTV TEPGLYGVKC TPHFGMGMVG LVQVGDAPEN
130 140
LDAAKTAKMP KKARERMDAE LAQVN