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 P31135

Entry ID Method Resolution Chain Position Source
AF-P31135-F1 Predicted AlphaFoldDB

No variants for P31135

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P31135

No associated diseases with P31135

3 regional properties for P31135

Type Name Position InterPro Accession
domain Calcineurin-like phosphoesterase domain, ApaH type 113 - 313 IPR004843
domain Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase 85 - 376 IPR006186
domain PP2B, metallophosphatase domain 70 - 374 IPR041751

Functions

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

5 GO annotations of cellular component

Name Definition
ATP-binding cassette (ABC) transporter complex A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter.
ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing A complex for the transport of metabolites into the cell, consisting of 5 subunits: two ATP-binding subunits, two membrane spanning subunits, and one substrate-binding subunit. In organisms with two membranes, the substrate-binding protein moves freely in the periplasmic space and joins the other subunits only when bound with substrate. In organisms with only one membrane the substrate-binding protein is tethered to the cytoplasmic membrane and associated with the other subunits. Transport of the substrate across the membrane is driven by the hydrolysis of ATP.
integral component of plasma membrane The component of the plasma 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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

2 GO annotations of biological process

Name Definition
putrescine transport The directed movement of putrescine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Putrescine is 1,4-diaminobutane, the polyamine formed by decarboxylation of ornithine and the metabolic precursor of spermidine and spermine.
transmembrane transport The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSTLEPAAQS KPPGGFKLWL SQLQMKHGRK LVIALPYIWL ILLFLLPFLI VFKISLAEMA
70 80 90 100 110 120
RAIPPYTELM EWADGQLSIT LNLGNFLQLT DDPLYFDAYL QSLQVAAIST FCCLLIGYPL
130 140 150 160 170 180
AWAVAHSKPS TRNILLLLVI LPSWTSFLIR VYAWMGILKN NGVLNNFLLW LGVIDQPLTI
190 200 210 220 230 240
LHTNLAVYIG IVYAYVPFMV LPIYTALIRI DYSLVEAALD LGARPLKTFF TVIVPLTKGG
250 260 270 280 290 300
IIAGSMLVFI PAVGEFVIPE LLGGPDSIMI GRVLWQEFFN NRDWPVASAV AIIMLLLLIV
310
PIMWFHKHQQ KSVGEHG