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 Q31JY3

Entry ID Method Resolution Chain Position Source
AF-Q31JY3-F1 Predicted AlphaFoldDB

No variants for Q31JY3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q31JY3

No associated diseases with Q31JY3

6 regional properties for Q31JY3

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 286 - 494 IPR002314
domain Anticodon-binding 506 - 594 IPR004154
domain Aminoacyl-tRNA synthetase, class II 228 - 511 IPR006195
domain Threonyl/alanyl tRNA synthetase, SAD 121 - 173 IPR012947
domain Threonine-tRNA ligase catalytic core domain 197 - 504 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 504 - 593 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
MVQSAPSTEA IQLPKTSESA QLKRIRHTMS HVMAMAVQKL FPKAQVTIGP WTETGFYYDF
70 80 90 100 110 120
DTPEPFTEAD LKAIKKEMVK IIQQKLPVVR EEVSREEAQQ RIEALGEPYK LEILQGLTEP
130 140 150 160 170 180
ITLYHLGDRW WDLCAGPHVE TTAELNPKAF DLESVAGAYW RGDETKAQLQ RIYGTAWETP
190 200 210 220 230 240
EQLTEYKRRK EEALKRDHRK LGRELGLFLF ADPVGPGLPL WTPKGTILRS TLEDFLKQEQ
250 260 270 280 290 300
MKRGYQSVVT PHLARVDLFK VSGHWQNYRE DMFPMMAEDD EARGLEQGFV LKPMNCPFHI
310 320 330 340 350 360
QIYKNELRSY RELPIRLAEF GTVYRYEQSG ELGGLTRVRG FTVDDSHLFV RPDQLASEFL
370 380 390 400 410 420
SVVDLILSVF KALNLKKFKA RLSFRDPESD KYIGSDDVWE KAESAIQAAA ETLGMDYFIG
430 440 450 460 470 480
VGEAAFYGPK LDFIFQDALD REWQLGTVQV DYNLPERFDL EYVAEDGSRQ RPVMIHRAPF
490 500 510 520 530 540
GSLERLIGIL IEEYAGDFPL WLAPEQIRLL PVTETVLDYC QQVADQLRAI GVRVQVDCSG
550 560 570 580 590 600
DRLGKLIRNA EKAKIPVMAV IGAQEAESET LSIRTRATGD LGSLTVADLT KRLSSAIAEK
LPHL