A8MBZ5

PR
Gene name
thrS
Protein name
Threonine--tRNA ligase
Names
Threonyl-tRNA synthetase, ThrRS
Species
Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)
KEGG Pathway
cma:Cmaq_0493
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)

1-180 (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 A8MBZ5

Entry ID Method Resolution Chain Position Source
AF-A8MBZ5-F1 Predicted AlphaFoldDB

No variants for A8MBZ5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8MBZ5

No associated diseases with A8MBZ5

5 regional properties for A8MBZ5

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 280 - 480 IPR002314
domain Anticodon-binding 502 - 590 IPR004154
domain Aminoacyl-tRNA synthetase, class II 222 - 492 IPR006195
domain Threonyl-tRNA synthetase, editing domain, archaea 1 - 139 IPR015011
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 500 - 588 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
MRLLLIHARS FSFEVRDKAV ENPEPLTEEL KRGSADNTLV VFTTVEENDN DSPSFLERVA
70 80 90 100 110 120
DDVLDVAGKV KASSVFLYPY AHLSPNLAPP PKAITILNAL YETLKGKASI PVYRAPFGWY
130 140 150 160 170 180
KAFNISCLGH PLSELSRTIT PQESAPQRKP YTRDYYVIVS PDGSIHDPAS YSFSERDADL
190 200 210 220 230 240
KVLVDKEVFK RELEGKEQPR YIDYCLKFGF EWEPLSDVGH MRYGPYATVM LELLDDYSYQ
250 260 270 280 290 300
VAKSLGIPVF KVKGTNMFRL SDKAISEHAG LFGERMYITE SDEELVMRYA ACFQQFAMIK
310 320 330 340 350 360
DWVLSYRNLP LGMLEIADSY RYEQPGETVL CFRLRRFYMP DLHIFVKDLK EAMDVGLRLH
370 380 390 400 410 420
AKIFEEIRRI GRDYVSLYNV SKEFFDQNKD YLVELARREG KPILVRVLEG AKYYWVLNVE
430 440 450 460 470 480
YHIIDELKRP REIATFQFDI GNAQRFGIKY RDEGNNIKYP VIIHTAILGS IERFIFALLD
490 500 510 520 530 540
TAAINEANGK VPALPTWITP VQVRVIPVSS GYNEGAIELA RRIEEAGFRV EVDDRDETVG
550 560 570 580 590 600
RKIRDAETLW VPYIVVFGER EAKTGSLSVR VRGVGQVSMS IEELLNRLNE ETKGYPRKPL
610
TAPMLLSIRP PLP