Q31F14

PR
Gene name
thrS
Protein name
Threonine--tRNA ligase
Names
Threonyl-tRNA synthetase, ThrRS
Species
Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira crunogena)
KEGG Pathway
tcx:Tcr_1667
EC number
6.1.1.3: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

109-183 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q31F14

Entry ID Method Resolution Chain Position Source
AF-Q31F14-F1 Predicted AlphaFoldDB

No variants for Q31F14

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q31F14

No associated diseases with Q31F14

7 regional properties for Q31F14

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 317 - 530 IPR002314
domain TGS 1 - 61 IPR004095
domain Anticodon-binding 542 - 631 IPR004154
domain Aminoacyl-tRNA synthetase, class II 230 - 535 IPR006195
domain Threonyl/alanyl tRNA synthetase, SAD 169 - 218 IPR012947
domain Threonine-tRNA ligase catalytic core domain 241 - 540 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 540 - 629 IPR047246

Functions

Description
EC Number 6.1.1.3 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.

4 GO annotations of molecular function

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

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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPIITLPDGS KRAFEDAVTV MQVASDIGAG LAKATIAGRV NGQLKEASDL ITEDAELQLI
70 80 90 100 110 120
TLKDEDGLHI MRHSCAHLLG HALKQLYPAA KMAIGPVVEN GFYYDIDMEE KITPEDLKQI
130 140 150 160 170 180
EKRMKELAKT KYEVIKEMTP RAEALATFKE RQEDYKVELI EDMPDETEFG LYHHQEYIDM
190 200 210 220 230 240
CRGPHVPNMG FIKAFKLTHV AGAYWRGNSD NKMLQRIYGV AFADKQELKD YLRMMEEAEK
250 260 270 280 290 300
RDHRKLGKSL DLFHVDELAP GMAFWHPKGS TLYRVVENYM RQQLVENDYQ EIRTPLIMDR
310 320 330 340 350 360
TLWEKSGHWD KFKDNMFTTE TENRDYAVKP MNCPGHIQVY NHNLSSYRDL PIRLAEFGLV
370 380 390 400 410 420
HRNEPSGTLH GLMRVRSFTQ DDAHIFCTPE QIKEEVQACI DLVFNTYADF GFDNIQVKFS
430 440 450 460 470 480
TRPEQRVGED DVWDLAEEAL EQTLKDANLE YALQPGEGAF YGPKIEFQLK DCIGRVWQCG
490 500 510 520 530 540
TIQLDFSMTQ EERLNAVYIG ADNEKHHPVM IHRAILGSLE RFVGILVEHY EGKFPTWLAP
550 560 570 580 590 600
TQLVIASIAD VHNEYVNDFA KKLKKHGFRV ESDLRNEKVG FKIREHTLQR VPYILVVGDQ
610 620 630 640
EMENGTVNVR ARGGENLGSF SFEELIDHLS EDVSRLGRIV ES