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 Q5JF63

Entry ID Method Resolution Chain Position Source
AF-Q5JF63-F1 Predicted AlphaFoldDB

No variants for Q5JF63

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5JF63

No associated diseases with Q5JF63

2 regional properties for Q5JF63

Type Name Position InterPro Accession
domain Proteasome component (PCI) domain 180 - 360 IPR000717
domain eIF3 subunit M, C-terminal helix domain 343 - 369 IPR040750

Functions

Description
EC Number 6.1.1.1 Ligases forming aminoacyl-tRNA and related compounds
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.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
tyrosine-tRNA ligase activity Catalysis of the reaction: L-tyrosine + ATP + tRNA(Tyr) = L-tyrosyl-tRNA(Tyr) + AMP + diphosphate + 2 H(+).

1 GO annotations of biological process

Name Definition
tyrosyl-tRNA aminoacylation The process of coupling tyrosine to tyrosyl-tRNA, catalyzed by tyrosyl-tRNA synthetase. The tyrosyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tyrosine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDIERKIELI KKKPTEELLT EENLRHLLEV GAPLQHYIGF EISGYIHLGT GLMAGAKIAD
70 80 90 100 110 120
LQKAGVKTRI FLADWHSWIN DKLGGDLEVI QKVALTYFKE GMKQSIKVMG GDPDKVEFVL
130 140 150 160 170 180
ASEILDKGDY WQTVIDISKN VTLARMLRSI TIMGRQMGEA IDFAKLIYPA MQVADIFYQG
190 200 210 220 230 240
VTIAHAGMDQ RKAHVIAIEV AQKLKYHPLE WKGEKLKPVA LHHHLLLGLQ EPPVWPIESE
250 260 270 280 290 300
EQFKELKTQM KMSKSKPYSA VFIHDSPEEI KQKLRKAFCP AREVKYNPVL DWAEYIIFRE
310 320 330 340 350 360
EPTEFTIHRP AKFGGDVTYT TFEELKKDFA EGKLHPLDLK NAVAEYLIEL LKPVREYFEK
370
HPEPLELMRE IKITR