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 B7NBU7

Entry ID Method Resolution Chain Position Source
AF-B7NBU7-F1 Predicted AlphaFoldDB

No variants for B7NBU7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B7NBU7

No associated diseases with B7NBU7

4 regional properties for B7NBU7

Type Name Position InterPro Accession
domain Signal recognition particle, SRP54 subunit, GTPase domain 98 - 295 IPR000897
domain AAA+ ATPase domain 97 - 300 IPR003593
domain Signal recognition particle, SRP54 subunit, M-domain 327 - 428 IPR004125
domain Signal recognition particle SRP54, helical bundle 1 - 84 IPR013822

Functions

Description
EC Number 3.1.3.70 Phosphoric monoester hydrolases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
magnesium ion binding Binding to a magnesium (Mg) ion.
mannosyl-3-phosphoglycerate phosphatase activity Catalysis of the reaction: 2-(alpha-D-mannosyl)-3-phosphoglycerate + H(2)O = 2-(alpha-D-mannosyl)-D-glycerate + phosphate.

1 GO annotations of biological process

Name Definition
mannosylglycerate biosynthetic process The chemical reactions and pathways resulting in the formation of mannosylglycerate, a very common compatible solute in thermophilic and hyperthermophilic organisms.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLSIQQPLLV FSDLDGTLLD SHSYDWQPAA PWLSRLREAN VPVILCSSKT SAEMLYLQKM
70 80 90 100 110 120
LGLQGLPLIA ENGAVIQLAE QWQDIDGFPR IISGISHGEI SQVLNTLREK EHFKFTTFDD
130 140 150 160 170 180
VDDATIAEWT GLSRSQAALT QLHEASVTLI WRDSDERMAQ FTTRLHELGL QFMQGARFWH
190 200 210 220 230 240
VLDASAGKDQ AANWIIATYQ QLSGKRPTTL GLGDGPNDAP LLEVMDYAVI VKGLNREGVH
250 260 270
LHDEDPARVW RTQREGPEGW REGLDHFFSA H