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 Q7VJ09

Entry ID Method Resolution Chain Position Source
AF-Q7VJ09-F1 Predicted AlphaFoldDB

No variants for Q7VJ09

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7VJ09

No associated diseases with Q7VJ09

6 regional properties for Q7VJ09

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 289 - 494 IPR002314
domain Anticodon-binding 507 - 597 IPR004154
domain Aminoacyl-tRNA synthetase, class II 235 - 500 IPR006195
domain Threonyl/alanyl tRNA synthetase, SAD 136 - 185 IPR012947
domain Threonine-tRNA ligase catalytic core domain 209 - 505 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 505 - 596 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
MSEVIGIKHN QHIYDLCTAD ELGITGDSIS FDNSQESLAI IRHSCAHLMA QAIKILYPEA
70 80 90 100 110 120
QFFVGPVVDE GFYYDFKVNT KISEEDLLVI EAKMKEIAKN AYPITKITLS RKEAQARFAH
130 140 150 160 170 180
DELKVAVMSR IPDEKLSIYT QGDFEDLCRG PHLPNTKLLE HFKLTKIAGA YLGGDENAQM
190 200 210 220 230 240
LIRIYGIAFA DKQSLKDYLF TLEEAKKRDH RKLGQEMGLF TFDEEIGAGL PIWLPKGARL
250 260 270 280 290 300
RHNIEHLLTQ ALKERGYEPV RGPEILKSDV WKKSGHYSNY KENMYFTIID EQEYGIKPMN
310 320 330 340 350 360
CVGHIKVYQS SPRSYRELPL RFYEYGIVHR HERSGVLHGL LRVREFTQDD AHIFCMTSQI
370 380 390 400 410 420
KSEVNQILDF TKGIMNAFGF HYEMELSTRP QKSIGNDEVW ENATAALKSA LEENHISYQI
430 440 450 460 470 480
DEGGGAFYGP KIDIKITDAL KRKWQCGTIQ IDMNLPERFE LSYTDEHNVQ VQPVMIHRAI
490 500 510 520 530 540
LGSFERFVAI LTEHFGGEFP LFIAPTQVIL IPIGEAQLEY ARILRDKIIT QSGAYAELMD
550 560 570 580 590 600
KNESLSKKIR LAEKQRVPLI VVIGAKEVES KILAIRDRRE KSQYELPEEA FIATLKTKIG
EVSF