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 Q68FW7

Entry ID Method Resolution Chain Position Source
AF-Q68FW7-F1 Predicted AlphaFoldDB

1 variants for Q68FW7

Variant ID(s) Position Change Description Diseaes Association Provenance
rs199281165 143 V>L No EVA

No associated diseases with Q68FW7

7 regional properties for Q68FW7

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 404 - 606 IPR002314
domain TGS 64 - 126 IPR004095
domain Anticodon-binding 620 - 710 IPR004154
domain Aminoacyl-tRNA synthetase, class II 333 - 613 IPR006195
domain Threonyl/alanyl tRNA synthetase, SAD 233 - 282 IPR012947
domain Threonine-tRNA ligase catalytic core domain 305 - 618 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 618 - 709 IPR047246

Functions

Description
EC Number 6.1.1.3 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 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.

4 GO annotations of molecular function

Name Definition
aminoacyl-tRNA editing activity The hydrolysis of an incorrectly aminoacylated tRNA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
protein homodimerization activity Binding to an identical protein to form a homodimer.
threonine-tRNA ligase activity Catalysis of the reaction: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).

1 GO annotations of biological process

Name Definition
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.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P07236 MST1 Threonine--tRNA ligase, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
A6QNM8 TARS3 Threonine--tRNA ligase 2, cytoplasmic Bos taurus (Bovine) PR
Q9NYK5 MRPL39 39S ribosomal protein L39, mitochondrial Homo sapiens (Human) PR
P26639 TARS1 Threonine--tRNA ligase 1, cytoplasmic Homo sapiens (Human) PR
Q9D0R2 Tars1 Threonine--tRNA ligase 1, cytoplasmic Mus musculus (Mouse) PR
Q9JKF7 Mrpl39 39S ribosomal protein L39, mitochondrial Mus musculus (Mouse) PR
Q3UQ84 Tars2 Threonine--tRNA ligase, mitochondrial Mus musculus (Mouse) PR
Q8GZ45 At1g17960 Probable threonine--tRNA ligase, cytoplasmic Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MGLCLRWRRL GFPLPGFRRC ELHTVREAPI PTPPHWLAER FGLFEELWTA QVKRLASMTQ
70 80 90 100 110 120
KKARTIKISL PEGQKVDAVA WNTTPYQLAQ QISSTLADTA VAAEVNGELY DLDRPLETDC
130 140 150 160 170 180
HLRFLTFDSP EGKAVFWRSS AHVLGAAAEQ HLGAVLCRGP STESGFYLDF FLGKERTVRS
190 200 210 220 230 240
TELPTLERIC QEIITAAQPF RRLEASRGQL RQLFKDNHFK LHVIEEKVTG TTATVYGCGM
250 260 270 280 290 300
SVDLCQGPHL RHTGQIGALK LLTNSSALWR SSEAPETLQR VSGISFPKAE LLRNWEARRE
310 320 330 340 350 360
EAELRDHRRI GKEQELFFFH ELSPGSCFFL PRGTRIYNAL VAFIRAEYAR RGFSEVKTPT
370 380 390 400 410 420
LFSTKLWEQS GHWEHYRAHM FSLKPPGTDG VDSSQSGHPA RCPKDTLALK PMNCPAHCLM
430 440 450 460 470 480
FAHRPRSWRE LPVRLADFGV LHRAEASGSL GGLTRLWRFQ QDDAHIFCAP SQLEAEIRGC
490 500 510 520 530 540
LDFLRSVYSV LGFSFHLALS TRPPGFLGEP HLWDQAEKVL QQALEEFGEP WNLNPGDGAF
550 560 570 580 590 600
YGPKIDVHLH DALGRPHQCG TIQLDFQLPL RFDLQYKGPA GAPECPVLIH RAVLGSVERL
610 620 630 640 650 660
LGVLAESCGG RWPLWLSPFQ VVVIPVRTEQ EDYARQVQQC LQAAGLVSDL DADCGLTLSR
670 680 690 700 710 720
RVRRAQLAHY NFQFVVGQRE QSQMSVNVRT RDNRQLGERG LAESVQRLLE LQDARVPNAE
ELF