B0S169

PR
Gene name
thrS
Protein name
Threonine--tRNA ligase
Names
Threonyl-tRNA synthetase, ThrRS
Species
Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508) (Peptostreptococcus magnus)
KEGG Pathway
fma:FMG_0691
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)

202-278 (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 B0S169

Entry ID Method Resolution Chain Position Source
AF-B0S169-F1 Predicted AlphaFoldDB

No variants for B0S169

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0S169

No associated diseases with B0S169

7 regional properties for B0S169

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 321 - 527 IPR002314
domain TGS 1 - 61 IPR004095
domain Anticodon-binding 539 - 627 IPR004154
domain Aminoacyl-tRNA synthetase, class II 266 - 532 IPR006195
domain Threonyl/alanyl tRNA synthetase, SAD 169 - 218 IPR012947
domain Threonine-tRNA ligase catalytic core domain 242 - 537 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 537 - 627 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
MFEVKLKDGS AKEFDGEISL LDVCKSISEG LARDCVGAVV DGKIMGLMET IDSDCEVQFV
70 80 90 100 110 120
KFDDDEGKQV FWHTSSHLMA YAIQRLYPGT KFAIGPSIDS GFYYDLDTDH KFVPEDLEKI
130 140 150 160 170 180
EAEMKKIVKE NPKLVRVEIS RKEALERFKN EGQDYKVDLI ENFDEDATIT LYEMGDFVDL
190 200 210 220 230 240
CRGPHLLDVK NIKAFKLLSI AGAYWRGDEN NKMLQRIYGI SFPKKKLLDE YLDRMEEAKK
250 260 270 280 290 300
RDHRKIGKEM GLFSIQEEGP GFPFFHPNGM VVLNELEKFL KEQLLERGYG QIKTPLILNE
310 320 330 340 350 360
HLWHQSGHWD HYKENMYFTK IDGEDYAIKP MNCPGSILVY KDELHSYREL PIKVAELGQV
370 380 390 400 410 420
HRHELSGALH GLFRVRTFVQ DDAHVFCLPE QIEEEVSKTI DFCDYIYSKF GFKYEVELST
430 440 450 460 470 480
RPEDSMGSDE DWDLAISSLK NALEHKGLPY KINEGDGAFY GPKIDFHLED AIGRTWQCGT
490 500 510 520 530 540
IQLDFQMPER FDMTYIASDG SKKRPAMIHR AILGSEERFM GILIEHYAGK FPLWLSPVQV
550 560 570 580 590 600
EILPISDKFN DYAYELQQKM KARGLRVKVD DRSEKIGLKI RESQLKKVNY SLIIGQNEID
610 620 630
NNEVSVRKRD IGDVGSKNTD EFINELVDEY QNRK