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 Q47N93

Entry ID Method Resolution Chain Position Source
AF-Q47N93-F1 Predicted AlphaFoldDB

No variants for Q47N93

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q47N93

No associated diseases with Q47N93

2 regional properties for Q47N93

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 40 - 50 IPR001412
domain RNA-binding S4 domain 366 - 427 IPR002942

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.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
RNA binding Binding to an RNA molecule or a portion thereof.
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
MTDIIDDLQW RGLIAQTTDL DDLRKALADG PVTLYCGFDP TAGSLHVGHL TQALTLARFQ
70 80 90 100 110 120
RAGHRPIALV GGATGMIGDP KPNAERTLNS PETIRQWVGN LKRQLSSFLE FTPEGAEPKP
130 140 150 160 170 180
TDALLLDNAE WLGKLTAIGL LRDIGKHFSI NQMLARETVK TRLEGAGMSY TEFSYVLLQS
190 200 210 220 230 240
YDYVELYRRH GCTLQIGGSD QWGNITAGLD LIRRMEGNEP HGPAHALTTT LLTKADGTKF
250 260 270 280 290 300
GKTESGAVWL DPELTSPYAF YQFWFNSDDR DIPRYLRIFS FRSREEIEEL EQKTIERPAE
310 320 330 340 350 360
RAAQRALAEE LTTLVHGEQE CRNVIEASKA LFGHGTLADL NPDTLGAALK EVPHVELSGT
370 380 390 400 410 420
VRELPPLVDL FASTGLVPSK SAARRTIQEG GAYLNNAKVT DIEARVSEAD LLHGRYLVLR
430
RGKRNVGGVI LR