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 Q9K4B1

Entry ID Method Resolution Chain Position Source
AF-Q9K4B1-F1 Predicted AlphaFoldDB

No variants for Q9K4B1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9K4B1

No associated diseases with Q9K4B1

1 regional properties for Q9K4B1

Type Name Position InterPro Accession
binding_site Inositol monophosphatase, metal-binding site 81 - 94 IPR020583

Functions

Description
EC Number 3.1.3.15 Phosphoric monoester hydrolases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

4 GO annotations of molecular function

Name Definition
histidinol-phosphatase activity Catalysis of the reaction: L-histidinol phosphate + H(2)O = L-histidinol + phosphate.
metal ion binding Binding to a metal ion.
phosphatase activity Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
phosphoric ester hydrolase activity Catalysis of the reaction: RPO-R' + H2O = RPOOH + R'H. This reaction is the hydrolysis of any phosphoric ester bond, any ester formed from orthophosphoric acid, O=P(OH)3.

2 GO annotations of biological process

Name Definition
histidine biosynthetic process The chemical reactions and pathways resulting in the formation of histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
inositol phosphate dephosphorylation The process of removing a phosphate group from any mono- or polyphosphorylated inositol.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPDYLDDLRL AHVLADAADA ATMDRFKALD LKVETKPDMT PVSEADKAAE ELIRGHLSRA
70 80 90 100 110 120
RPRDSVHGEE FGVAGTGPRR WVIDPIDGTK NYVRGVPVWA TLIALMEAKE GGYQPVVGLV
130 140 150 160 170 180
SAPALGRRWW AVEDHGAFTG RSLTSAHRLH VSQVSTLSDA SFAYSSLSGW EEQGRLDGFL
190 200 210 220 230 240
DLTREVWRTR AYGDFWPYMM VAEGSVDLCA EPELSLWDMA ANAIIVTEAG GTFTGLDGRP
250 260
GPHSGNAAAS NGRLHDELLG YLNQRY