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 A6GY22

Entry ID Method Resolution Chain Position Source
AF-A6GY22-F1 Predicted AlphaFoldDB

No variants for A6GY22

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6GY22

No associated diseases with A6GY22

1 regional properties for A6GY22

Type Name Position InterPro Accession
conserved_site Cytochrome P450, conserved site 453 - 462 IPR017972

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
MIKITLPDGS IKEFENGVTP MDVAKSISEG LARNVISAAF NNITVEISTE LTTDGSLVLY
70 80 90 100 110 120
TWNDKDGKKA FWHSTSHVMA QVLEEMYPGL KLTLGPAIDN GFYYDVDFGD TKIVEADFKK
130 140 150 160 170 180
IESRILEISK EKHEFKLRPV TKADALELYK DNEYKFELIS NLEDGTITFC DHATFTDLCR
190 200 210 220 230 240
GGHIPNTGII KAVKIMSIAG AYWRGDEKNK QLTRVYGTSF PKQKDLTDYL ELLEEAKRRD
250 260 270 280 290 300
HRKLGKELEL FAFSQKVGQG LPLWLPKGAA LRDRLEQFLK KAQKKGGYEQ VVTPHIGQKE
310 320 330 340 350 360
LYVTSGHYAK YGADSFQPIS TPTEGEEFLL KPMNCPHHCE IYNVRPWSYK DLPKRYAEFG
370 380 390 400 410 420
TVYRYEQSGE LHGLTRVRGF TQDDAHIFCT PDQLDEEFKK VIDLVLYVFG SLGFENFTAQ
430 440 450 460 470 480
ISLRDKENRD KYIGSDENWE KAENAIINAA RDKNLNTVVE YGEAAFYGPK LDFMVKDALG
490 500 510 520 530 540
RSWQLGTIQV DYNLPERFEL TYKGSDDQLH RPVMIHRAPF GSMERFIAIL LEHTAGNFPL
550 560 570 580 590 600
WLMPEQAIIL CLSDKYEIYA KKVLNLLENH EIRALIDNRN ESIGRKIRDA EMQKTPFMLI
610 620 630 640
VGEEEEKNNT ISIRRHGQEG KGNITVTIEE FARIVNDEIS KTLKTFEV