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 Q65T71

Entry ID Method Resolution Chain Position Source
AF-Q65T71-F1 Predicted AlphaFoldDB

No variants for Q65T71

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q65T71

No associated diseases with Q65T71

2 regional properties for Q65T71

Type Name Position InterPro Accession
domain Mannitol dehydrogenase, C-terminal 232 - 475 IPR013118
domain Mannitol dehydrogenase, N-terminal 36 - 201 IPR013131

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
MSDINVVLAE LKRGVDEVLS EADLIEKLKE NRPLKIKLGA DPTAPDIHLG HTVVLNKLRQ
70 80 90 100 110 120
FQNFGHEVIF LIGDFTGMVG DPSGKNKTRP PLSREDVLRN AETYKQQIYK ILDPQKTRIV
130 140 150 160 170 180
FNSDWLGKLG TEGMIRLASN YTVARMLERD DFKKRFTEKQ PIAIHEFIYP LLQGHDSVAL
190 200 210 220 230 240
EADVELGGTD QKFNLLVGRE LQKSAGQKPQ VAMTLPLLVG LDGEKKMSKS LGNYIGVTDA
250 260 270 280 290 300
PNDMFGKIMS ISDDLMWDWY DLLSFRPLTE IAQFKEEVKN GRNPRDVKIL LAKEIIARFH
310 320 330 340 350 360
SEADADTAEQ EFINRFQKGA MPDEMPEFTF EGEIGLANLL KEAGLVASTS EANRMVQQDG
370 380 390
VKIDGEKVED AKTTISASTH VYQVGKRKFA RVTVR