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 A6VIL3

Entry ID Method Resolution Chain Position Source
AF-A6VIL3-F1 Predicted AlphaFoldDB

No variants for A6VIL3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6VIL3

No associated diseases with A6VIL3

5 regional properties for A6VIL3

Type Name Position InterPro Accession
domain Transglutaminase, N-terminal 10 - 121 IPR001102
domain Transglutaminase-like 270 - 363 IPR002931
domain Transglutaminase, C-terminal 507 - 603 IPR008958-1
domain Transglutaminase, C-terminal 620 - 717 IPR008958-2
active_site Transglutaminase, active site 276 - 293 IPR013808

Functions

Description
EC Number 6.3.4.20 Other carbon--nitrogen ligases
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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ligase activity, forming carbon-nitrogen bonds Catalysis of the joining of two molecules, or two groups within a single molecule, via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate.
zinc ion binding Binding to a zinc ion (Zn).

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRAICVLSGG LDSAVTSLAA KFENYDITTV TFNYGQMALN QEIKSAKKIS EILNADHHVI
70 80 90 100 110 120
DINFVKEFSK SGLNTGEIPE PEKEDLDDFE KSEKTMKAVW VPARNMIMFS IASGFAEGIG
130 140 150 160 170 180
AEKIFSGLNK EEGVTFPDNT PEFIERFNKS LEYGTLNKVK MVAPLYELNK PEIAKLGKEL
190 200 210 220 230
EVKLDLEVLK YSYSCYRDNG EDYLHCGTCE SCMRRKRAFK EAGIVDPTKY LVE