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 C4LLD6

Entry ID Method Resolution Chain Position Source
AF-C4LLD6-F1 Predicted AlphaFoldDB

No variants for C4LLD6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C4LLD6

No associated diseases with C4LLD6

2 regional properties for C4LLD6

Type Name Position InterPro Accession
domain Glycosyl transferase, family 1 239 - 412 IPR001296
domain Glycosyltransferase subfamily 4-like, N-terminal domain 49 - 228 IPR028098

Functions

Description
EC Number 2.4.1.250 Hexosyltransferases
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

3 GO annotations of molecular function

Name Definition
acetylglucosaminyltransferase activity Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar.
D-inositol-3-phosphate glycosyltransferase activity Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + 1D-myo-inositol 3-phosphate = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside 3-phosphate + UDP + H+.
magnesium ion binding Binding to a magnesium (Mg) ion.

1 GO annotations of biological process

Name Definition
mycothiol biosynthetic process The chemical reactions and pathways resulting in the formation of mycothiol, which consists of N-acetyl-L-cysteine linked to a pseudodisaccharide, D-glucosamine and myo-inositol. Mycothiol is produced in actinomycetes like mycobacteria and serves similar functions to glutathione.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MHQAGASTRR LHGVAILSTL KSMSTTPRGR IAVISMHTSP IEQPGVGDAG GMNVYIRSTS
70 80 90 100 110 120
LELGALGYEV DIFTRATRSS QGKIVQLAPN VRLINIIAGP YEGLSKEELP TQMVAFTSGI
130 140 150 160 170 180
IEFAQCEKVS YSLIHSHYWM SGQVGWLLRD LWRVPQVHTA HTLALVKNSA LATGDRPEPE
190 200 210 220 230 240
SRRICEQQIV DNADRLVVNT EAGKDNLVFH YDADPEHIDV VLPGADVTQF SPGSDRATER
250 260 270 280 290 300
SRRELGVPLH ATVIAFVGRM QRLKGPQVLL RAVANMMKKH PDQELRVLMC GGPSGNGLAR
310 320 330 340 350 360
PTEFEDLARD LGIDPIVRFL APRPPEDLAS VYRAADIVAI PSYNESFGLV AVEAQASGTP
370 380 390 400 410 420
VVAARAGGLP ITIDDGTSGI LVDGHDPADW ATALQSLCDD DDRRIAMGEN ATDHASRFSW
430 440 450
ASSARHLSDI YEDAIRKGPH VRCGSDRAGA S