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 B8ZUG9

Entry ID Method Resolution Chain Position Source
AF-B8ZUG9-F1 Predicted AlphaFoldDB

No variants for B8ZUG9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B8ZUG9

No associated diseases with B8ZUG9

7 regional properties for B8ZUG9

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 374 - 580 IPR002314
domain TGS 15 - 84 IPR004095
domain Anticodon-binding 592 - 680 IPR004154
domain Aminoacyl-tRNA synthetase, class II 310 - 585 IPR006195
domain Threonyl/alanyl tRNA synthetase, SAD 189 - 255 IPR012947
domain Threonine-tRNA ligase catalytic core domain 279 - 590 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 590 - 680 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
MSAPVHPVPG ADGGDPLRPA TPGLRSPQVP IQVPAGSTAA AAVSEAGLPT HGAPDAIVVV
70 80 90 100 110 120
RDADGKLRDL SWVPDVDVEV TPVPVNTDDG RSVIRHSTAH VLAQAVQDLF PQAKLGIGPP
130 140 150 160 170 180
ITDGFYYDFD VAEPFTPEDL KALEKRMRQI VKEGQLFSRR IYESKEQART EWAGEPYKLE
190 200 210 220 230 240
LVDDESGDAE IMEVGGDELT AYDNLNARNG ERIWGDLCRG PHIPTTKHIP AFKLTRSSAA
250 260 270 280 290 300
YWRGNQKNAS LQRIYGTAWE SQEALDRHLE MITEAQRRDH RKLGIELDLF SFPDEIGSGL
310 320 330 340 350 360
AIFHPKGSIV RREMEEYSRR KHIEAGYQFV NTPHITKAQL FHTSGHLDWY AEGIFPPMHL
370 380 390 400 410 420
DAEHNDDGTV RKPGQDYYLK PMNCPMHTLI FSSRGRSYRE LPLRLFEFGT IYRYEKSGVV
430 440 450 460 470 480
HGLTRARGFT MDDSHIFCTR EQLHCELASL LRFVLDLLGD YGLEDFYLEL STKDPEKFVG
490 500 510 520 530 540
SEEIWEEATA ALAEVAENST LPLVPDPGGA AFYGPKISVQ VRDALGRSWQ MSTIQVDFNF
550 560 570 580 590 600
PERFALEYTS ADGTRQRPVM IHRALFGSIE RFFGILTEHY AGAFPAWLAP IQVVGIPVTG
610 620 630 640 650 660
EHVSYLEEVA AQLKSCGVRT EVDVSDDRMA KKIVRHTNQK VPFMLLAGDR DVRTGSVSFR
670 680 690 700
FGDRTQINGV ARDSAVEAIV CWIVDRENDF PTAELVKVTG GE