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 A4TSH1

Entry ID Method Resolution Chain Position Source
AF-A4TSH1-F1 Predicted AlphaFoldDB

No variants for A4TSH1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4TSH1

No associated diseases with A4TSH1

1 regional properties for A4TSH1

Type Name Position InterPro Accession
domain MobA-like NTP transferase 7 - 156 IPR025877

Functions

Description
EC Number 2.7.7.77 Nucleotidyltransferases
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.

3 GO annotations of molecular function

Name Definition
GTP binding Binding to GTP, guanosine triphosphate.
metal ion binding Binding to a metal ion.
molybdenum cofactor guanylyltransferase activity Catalysis of the reaction GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor.

1 GO annotations of biological process

Name Definition
Mo-molybdopterin cofactor biosynthetic process The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MQPNITGVIL AGGRSSRMGG NDKGLIPLNG KPLFQYVIDR FKPQVSDLVI NANRNQGLYK
70 80 90 100 110 120
ESGIPVIDDI ITGFVGPLAG MHAGLSYAST EWVVFAPCDV PALPSDLVSQ LWQGKKQALA
130 140 150 160 170 180
AYANDDERAH PTFALMHISL KTQLADYLIR GDRKLMLFLD SINAQRVKFS GKADLFSNLN
190
TPADCDLWEQ KRRGQ