Q2NE13

PR
Gene name
thrS
Protein name
Threonine--tRNA ligase
Names
Threonyl-tRNA synthetase, ThrRS
Species
Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)
KEGG Pathway
mst:Msp_1573
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)

103-238 (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 Q2NE13

Entry ID Method Resolution Chain Position Source
AF-Q2NE13-F1 Predicted AlphaFoldDB

No variants for Q2NE13

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2NE13

No associated diseases with Q2NE13

5 regional properties for Q2NE13

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 276 - 483 IPR002314
domain Anticodon-binding 502 - 590 IPR004154
domain Aminoacyl-tRNA synthetase, class II 200 - 495 IPR006195
domain Threonyl-tRNA synthetase, editing domain, archaea 1 - 138 IPR015011
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 500 - 589 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.

5 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.
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.
zinc ion binding Binding to a zinc ion (Zn).

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
MRTLMIHSDY LRYKTRSKTK IAEDIDDEKR VSGVDEALVA FIAVEKEDEE NPELIINKAV
70 80 90 100 110 120
KEILNVQNKV NAENIVIYPY AHLSSSLSNP DIAQKILKGI EAELLDNNEA VLRVPFGWYK
130 140 150 160 170 180
SFELSCKGHP LSELSRTITT EPEEESEDSE EEPSEPSKMF ILEEDGNIFD VEEYNYKNKT
190 200 210 220 230 240
LRQLVDHEEG KTKDTGKQPP HVRLMREKEL ASNEPAADVG HIRWYPKGKL VKDLLSDYVY
250 260 270 280 290 300
QLVTQRGAMP VETPVMYDLA NPAIREHAEK FGERQYRLKT KHRELMLRFA CCFGAFRILA
310 320 330 340 350 360
DSFLTWKNMP VGIYELSTFS FRFERQGEVV GLKRLRAFTM PDFHSVCLND DHAREVFANQ
370 380 390 400 410 420
VDMCAQTETD LDVHYEVAFR VTQDFFDENE DWIKEVVKNN IKKPVLLEVI PKMKHYWNAK
430 440 450 460 470 480
VDFAAIDDLG RPIENPTVQM DIQSAKRFGI TYLDENEEQQ YPTILHCSPT GSIERVICSL
490 500 510 520 530 540
LEKTSTDKGN KPSLPLWLAP TQVRIIPVTD NHLDYAKEIY QQIRDSNIRV DIDDTAERVG
550 560 570 580 590 600
KKIRNAGKEW IPYTIVVGDN EVENNSISVN RRVDNTKEEI SIEDLAEEIH TLTKDMPFRQ
610
LPLPYMVSKR VKFD