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 B8DU64

Entry ID Method Resolution Chain Position Source
AF-B8DU64-F1 Predicted AlphaFoldDB

No variants for B8DU64

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B8DU64

No associated diseases with B8DU64

2 regional properties for B8DU64

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 51 - 61 IPR001412
domain RNA-binding S4 domain 373 - 435 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
MAHVIDFKEA GFDSVLDELE WRGLISQSTD RDRLAHTLNG EPVHYYCGFD PTAPSLHIGN
70 80 90 100 110 120
LVQLIIMRHL QEAGHHPIAL VGGATGLIGD PRQSGERILN PKDIVEQWCE RLRIQIGGIL
130 140 150 160 170 180
EQEGSNPVTF VSNYDWTATM NVLDFLRDIG KNFRVGTMIS KDIVARRLNS EEGISFTEFS
190 200 210 220 230 240
YQVLQGNDYL YLYDHYDCVL ELGGSDQWGN LTSGLDLIHK VRGVNVNVMA SPIITDANGK
250 260 270 280 290 300
KFGKSEGNAV WLDPNMLSVY KFYQFWLNRP DVEMASLLKA FTFLPKAEIE RLVEATDTNP
310 320 330 340 350 360
GAREAQRVLA WEVTSLVHGD EPTRKAIDAS ASLFGRGGDL ADIDLETLES VLDGLKVENE
370 380 390 400 410 420
AGEKVFAQAL PGDRIAQAGV SAGLFKSISE ARKTIKSGGV YVNNVRVEDE EQLLGDGDFL
430
KGRFVVLRRG KKALGVVARS