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 P44604

Entry ID Method Resolution Chain Position Source
AF-P44604-F1 Predicted AlphaFoldDB

No variants for P44604

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P44604

No associated diseases with P44604

1 regional properties for P44604

Type Name Position InterPro Accession
conserved_site Mrp, conserved site 184 - 200 IPR000808

Functions

Description
EC Number 2.7.13.3 Protein-histidine kinases
Subcellular Localization
  • Cell inner membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
phosphorelay sensor kinase activity Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response.
protein dimerization activity The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.

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
MYTKGSVSTR IAKYLFIILI VAGVISSLSL AIMSSNKYDA EAINISGSLR MQSYRLLYEM
70 80 90 100 110 120
QEQPESVETN LRRYHISLHS SALLEVQNQF FTPNVLKHSY QNILQRWTNM EKYARQQDVK
130 140 150 160 170 180
NYSKQLTDYV ADVDYFVFEL QRFSEQKWIL GVSVLGFAML LILLMVSYVI WYTNREVVKP
190 200 210 220 230 240
LHLMTKASMQ VQMRQFNHIP LDTRKQNELG TLARVFTQMS TELGQLYSRL EEAVNEKTQK
250 260 270 280 290 300
LRQTNRTLST LYQSAQLLNT NTINDKILNQ VLNYIFISDH LNFVKVEVMG AEHWDITLGK
310 320 330 340 350 360
QDANNELQIE TLSVDNEELG VLSWQAGLPC PDPRIMQNLA QMLARALYFH KNLRQKEQLL
370 380 390 400 410 420
LMEERSIIAR ELHDSLAQVL SFLQIQLTLL KHNLKKEDEQ SKEKSLAIIA NFEQALSGGY
430 440 450 460 470 480
AQLRELLATF RLTIQEANLQ LALKQVIDSL RSQTTMQMNV NCQLPSQSLN PQQLVHVLQI
490 500 510 520 530 540
VREATTNAIK HSQGTVIEIS ARINAEGEYE ILVEDDGVGI PNLEEPEGHY GLNIMAERCR
550 560
QLNAQLHIHR REQGGTQVKI TLPHTLY