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 Q8PRY4

Entry ID Method Resolution Chain Position Source
AF-Q8PRY4-F1 Predicted AlphaFoldDB

No variants for Q8PRY4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8PRY4

No associated diseases with Q8PRY4

7 regional properties for Q8PRY4

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 325 - 530 IPR002314
domain TGS 1 - 64 IPR004095
domain Anticodon-binding 542 - 631 IPR004154
domain Aminoacyl-tRNA synthetase, class II 275 - 535 IPR006195
domain Threonyl/alanyl tRNA synthetase, SAD 172 - 221 IPR012947
domain Threonine-tRNA ligase catalytic core domain 245 - 540 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 540 - 634 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
MQLLLIHSDY IEYETKKQTP VAEKIEESLK SGRLEEALTA FTAVESVDEA NPEEAIKKAV
70 80 90 100 110 120
SEIEKVAAQV KTNRIMLYPY AHLSSDLSSP KVAVQVLKGM EAALSSRYEV KRAPFGWYKA
130 140 150 160 170 180
FTVSCKGHPL SELSRSIRPE GAAKAEVKTE TCEKEEVVSE ALKAEGTARS YWRILTPDGE
190 200 210 220 230 240
LHEVEGFDLT PYPKLQQFVN YEISKSRAVE RAPPHVELMR RLELADYEPG SDSGNMRYYP
250 260 270 280 290 300
KGRLVKSLLE NYVLDVATEF GAMEVETPLM YDMNHPTLKK YLDRFPARQY SIESDKRHMF
310 320 330 340 350 360
LRFAACFGQF LMNHDMTISY KNLPLRMIEM TRYSFRKEQR GELVGLRRLR AFTMPDMHTL
370 380 390 400 410 420
CEDMDQAVNQ FKEQYDLCIS VLENVGIHIN DYEVAIRFTR DFYEANKDLV VNMAKTVNKP
430 440 450 460 470 480
VLVEMWDTRF FYFVLKFEFN FVDALAKASA LSTVQIDVEN AERYDISYVN ADGKLERPTV
490 500 510 520 530 540
LHCSPSGAIE RCIYALLEKA AMETEEGKVP MLPVWLSPTQ VRIVPISEKH IAFAEEVAKK
550 560 570 580 590 600
LDFRVDVDDR DLSIGKKVRE AGREWVPYVV VIGDKEMEES TINVTIREES GQDKPKKVQM
610 620 630
TPEELNARIK EETSGKPYRK LPLAKYLSAR PKFL