Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for O27504

Entry ID Method Resolution Chain Position Source
AF-O27504-F1 Predicted AlphaFoldDB

No variants for O27504

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O27504

No associated diseases with O27504

7 regional properties for O27504

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 312 - 522 IPR002314
domain TGS 1 - 58 IPR004095
domain Anticodon-binding 535 - 624 IPR004154
domain Aminoacyl-tRNA synthetase, class II 261 - 528 IPR006195
domain Threonyl/alanyl tRNA synthetase, SAD 164 - 213 IPR012947
domain Threonine-tRNA ligase catalytic core domain 237 - 533 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 533 - 623 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
MRILLIHSDY LKYETKNKTG IAEEIPEDKM QGDFRESLVV FTAVEAEDED NPESVIENAV
70 80 90 100 110 120
NEIIKVFNDV KAENVVIYPY AHLSSSLSSP KTAVEVLEGM ESALRSEGVD VSRVPFGWYK
130 140 150 160 170 180
AFKISCKGHP LSELSRSIRP QPPKVEEESE ESEWFILHRG ETVKPGDFEF KNRDLENLVK
190 200 210 220 230 240
YELGELESSG EEPPHVRLMR EKGLADYEPS ADVGHLRWYP RGRLIRDLLA DYVYMLVTSE
250 260 270 280 290 300
GAMPVETPIM YDLEDEAIRV HAEKFGERQY RMKNRKELML RYACCFGAFR ILSDSFLTWK
310 320 330 340 350 360
NLPASIYELS TYSFRLEKKG EVVGLKRLRG FTMPDLHTVC ADLDQSLEEF ARQVEMCMRT
370 380 390 400 410 420
GQDLQVNYEV IFRATADFYE EYREWVHEVA DKIGKPVLLE ILPSRKHYWI AKMDFAAIDY
430 440 450 460 470 480
LGRPIENPTV QIDVESGERF GITYVNSDEE EVNPIILHCS PTGSIERVIC SLLEKTAIEM
490 500 510 520 530 540
DEKPPMLPLW LSPTQVRVLP IAERHMEYAS DLVSELIAAD VRADLDDRSE TLGKKIRNAA
550 560 570 580 590 600
QDWVPYVVVI GDSEMEGKLT VNVRETGEKL QMGLDELIER IRAETEGMPF RRLPLPVKLS
ERINF