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 Q8TH84

Entry ID Method Resolution Chain Position Source
AF-Q8TH84-F1 Predicted AlphaFoldDB

No variants for Q8TH84

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8TH84

No associated diseases with Q8TH84

6 regional properties for Q8TH84

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 158 - 495 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 55 - 140 IPR004365
domain Aminoacyl-tRNA synthetase, class II 178 - 497 IPR006195
domain Lysyl-tRNA synthetase, class II, C-terminal 171 - 497 IPR018149
domain KTSC domain 500 - 555 IPR025309
domain Lysine-tRNA ligase, class II, N-terminal 54 - 168 IPR044136

Functions

Description
EC Number
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

2 GO annotations of molecular function

Name Definition
NAD+ ADP-ribosyltransferase activity Catalysis of the reaction: NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
tRNA 2'-phosphotransferase activity Catalysis of the reaction: 2'-phospho-

2 GO annotations of biological process

Name Definition
tRNA processing The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.
tRNA splicing, via endonucleolytic cleavage and ligation Splicing of tRNA substrates via recognition of the folded RNA structure that brings the 5' and 3' splice sites into proximity and cleavage of the RNA at both the 3' and 5' splice sites by an endonucleolytic mechanism, followed by ligation of the exons.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIRKCTEHGY FRGGSCQQCK RPGRYVLDDS REEKLGRFVS GTLRHFPASA GVKMDEYGWV
70 80 90 100 110 120
DLNAFCDVMK KRYNWMRKEY LYALVESDEK GRYQIRGFMI RARYGHSVNI ELDYEESDAP
130 140 150 160 170 180
YVYYGASPEE VDVLLENGIF PIKQRYVHLS TSYEKAAEVA LIHTESPVIL QVDAFRAQED
190 200
GISLKLATDY IVLAEKIPPE YLYVIEE