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

6 structures for P07236

Entry ID Method Resolution Chain Position Source
3UGQ X-ray 210 A A 26-462 PDB
3UGT X-ray 360 A A/B/C/D 26-462 PDB
3UH0 X-ray 200 A A 26-462 PDB
4EO4 X-ray 287 A A/B/C/D 26-462 PDB
4YYE X-ray 230 A A/B 26-462 PDB
AF-P07236-F1 Predicted AlphaFoldDB

11 variants for P07236

Variant ID(s) Position Change Description Diseaes Association Provenance
s11-78644 3 I>T No SGRP
s11-78623 10 C>Y No SGRP
s11-78620 11 S>C No SGRP
s11-78609 15 L>F No SGRP
s11-78351 101 E>K No SGRP
s11-77883 257 G>C No SGRP
s11-77861 264 P>L No SGRP
s11-77601 351 V>I No SGRP
s11-77573 360 V>A No SGRP
s11-77522 377 L>R No SGRP
s11-77449 401 E>D No SGRP

No associated diseases with P07236

5 regional properties for P07236

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 114 - 337 IPR002314
domain Anticodon-binding 349 - 456 IPR004154
domain Aminoacyl-tRNA synthetase, class II 67 - 342 IPR006195
domain Threonine-tRNA ligase catalytic core domain 44 - 347 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 347 - 459 IPR047246

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

2 GO annotations of molecular function

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

2 GO annotations of biological process

Name Definition
mitochondrial threonyl-tRNA aminoacylation The process of coupling threonine to threonyl-tRNA in a mitochondrion, catalyzed by threonyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA.
threonyl-tRNA aminoacylation The process of coupling threonine to threonyl-tRNA, catalyzed by threonyl-tRNA synthetase. The threonyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a threonine-accetping tRNA.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A6QNM8 TARS3 Threonine--tRNA ligase 2, cytoplasmic Bos taurus (Bovine) PR
P26639 TARS1 Threonine--tRNA ligase 1, cytoplasmic Homo sapiens (Human) PR
Q3UQ84 Tars2 Threonine--tRNA ligase, mitochondrial Mus musculus (Mouse) PR
Q9D0R2 Tars1 Threonine--tRNA ligase 1, cytoplasmic Mus musculus (Mouse) PR
Q68FW7 Tars2 Threonine--tRNA ligase, mitochondrial Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MKIQLVRWHC SRNALWNRAF YSTRKATKNA SSATPATMTS MVSQRQDLFM TDPLSPGSMF
70 80 90 100 110 120
FLPNGAKIFN KLIEFMKLQQ KFKFGFNEVV TPLIYKKTLW EKSGHWENYA DDMFKVETTD
130 140 150 160 170 180
EEKEEYGLKP MNCPGHCLIF GKKDRSYNEL PLRFSDFSPL HRNEASGALS GLTRLRKFHQ
190 200 210 220 230 240
DDGHIFCTPS QVKSEIFNSL KLIDIVYNKI FPFVKGGSGA ESNYFINFST RPDHFIGDLK
250 260 270 280 290 300
VWNHAEQVLK EILEESGKPW KLNPGDGAFY GPKLDIMVTD HLRKTHQVAT IQLDFQLPER
310 320 330 340 350 360
FDLKFKDQDN SYKRPIMIHR ATFGSIERFM ALLIDSNEGR WPFWLNPYQA VIIPVNTKNV
370 380 390 400 410 420
QQLDMCTALQ KKLRNELEAD DMEPVPLNDW HFNVDLDIRN EPVGYRIKSA ILKNYSYLII
430 440 450 460
VGDEEVQLQK YNIRERDNRK SFEKLTMSQI WEKFIELEKN YK