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 Q8DNK8

Entry ID Method Resolution Chain Position Source
AF-Q8DNK8-F1 Predicted AlphaFoldDB

No variants for Q8DNK8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8DNK8

No associated diseases with Q8DNK8

3 regional properties for Q8DNK8

Type Name Position InterPro Accession
domain Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic 6 - 287 IPR006075
conserved_site Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site 144 - 158 IPR017958
domain Asn/Gln amidotransferase 328 - 475 IPR018027

Functions

Description
EC Number 2.7.7.12 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.

1 GO annotations of molecular function

Name Definition
UDP-glucose:hexose-1-phosphate uridylyltransferase activity Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.

1 GO annotations of biological process

Name Definition
galactose metabolic process The chemical reactions and pathways involving galactose, the aldohexose galacto-hexose. D-galactose is widely distributed in combined form in plants, animals and microorganisms as a constituent of oligo- and polysaccharides; it also occurs in galactolipids and as its glucoside in lactose and melibiose.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTLVDKFVTH VISESSFEEM DRIYLTNRVL SRVGEGVLEV ETNLDKLIDL KDQLVEETVR
70 80 90 100 110 120
LETIEDSQTA REILGTELMD LVTPCPSQVN RDFWEAYAYS PEQAIEDFYQ LSQKNDYIKL
130 140 150 160 170 180
KAIAKNIAYR VPSDYGELEI TINLSKPEKD PKEIAVAKLV QASNYPQCQL CLENEGYHGR
190 200 210 220 230 240
VNHPARSNHR IIRFEMVGQE WGFQYSPYAY FNEHCIFLDG QHRPMAISRQ SFERLLAIVE
250 260 270 280 290 300
QFPGYFAGSN ADLPIVGGSI LTHDHYQGGR HVFPMELAPL QKTFRFAGFE QVKAGIIKWP
310 320 330 340 350 360
MSVLRLTSDS KEDLINLADK IFQEWRQYSD SSVQILAETD GTPHHTITPI ARKRDGQFEL
370 380 390 400 410 420
DLVLRDNQTS AEHPDGIYHP HKDVQHIKKE NIGLIEVMGL AILPPRLKEE VEQVASYLVG
430 440 450 460 470 480
EAVTVADYHQ EWADQLKSQH PDLTDKEKAL AIVKDSVGAI FVRVLEDAGV YKQTEQGQTA
490
FMRFVEQVGI LLD