Q11JM1

PR
Gene name
thrS
Protein name
Threonine--tRNA ligase
Names
Threonyl-tRNA synthetase, ThrRS
Species
Chelativorans sp (strain BNC1)
KEGG Pathway
mes:Meso_1007
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)

298-369 (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 Q11JM1

Entry ID Method Resolution Chain Position Source
AF-Q11JM1-F1 Predicted AlphaFoldDB

No variants for Q11JM1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q11JM1

No associated diseases with Q11JM1

7 regional properties for Q11JM1

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 329 - 543 IPR002314
domain TGS 1 - 64 IPR004095
domain Anticodon-binding 555 - 643 IPR004154
domain Aminoacyl-tRNA synthetase, class II 275 - 548 IPR006195
domain Threonyl/alanyl tRNA synthetase, SAD 172 - 222 IPR012947
domain Threonine-tRNA ligase catalytic core domain 246 - 553 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 553 - 642 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
MAEAASLTFP DGSVRNVDAA MTGADIAESI SKSLAKKAVA YAMDGSLRDL SDPVERSGKI
70 80 90 100 110 120
EIITREDPRA LELIRHDAAH VLAEAVQELW PGTQVTIGPV IENGFYYDFA RNEPFTLDDL
130 140 150 160 170 180
PVIEKKMREI VDRNKRFSKE VWPRDKAKKV FADKGESYKV ELIDAIPEDQ DLKIYFQGDW
190 200 210 220 230 240
FDLCRGPHMA STGQIGKAFK LMKVAGAYWR GDSNRPMLTR IYGTAWADQQ QLDSYLQMLE
250 260 270 280 290 300
EAEKRDHRRL GREMDLFHFQ EEGPGVVFWH AKGWRMFQNL VSYMRRRLDG VYQEVNAPQV
310 320 330 340 350 360
LDHSLWQTSG HWGWYKENMF KVECADEEAE DKRTFALKPM NCPGHVQIFK HGLKSYRDLP
370 380 390 400 410 420
IRLAEFGAVH RYEPSGALHG LMRVRGFTQD DAHIFCTEDQ LAEECLKIND LILSTYADFG
430 440 450 460 470 480
FEEIQVFFST RPEKRVGSDA LWDHAEEIMG GVLEQIAERS GGRIKTAINP GDGAFYGPKF
490 500 510 520 530 540
DYVLKDAIGR QWQCGTTQVD FNLPERFGAF YIDKDSEKKQ PVMIHRAICG SMERFLGILI
550 560 570 580 590 600
ENYAGHFPLW FAPLQVVVAT ITSDADDYAR QVTQQLKAAG LTAEADLRNE KINYKVREHS
610 620 630 640 650
LAKVPVILVC GKREAEEGSV NIRRLGSRDQ ASLLLAEAIA QLIDEATPPD IRRAKA