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 Q7TV01

Entry ID Method Resolution Chain Position Source
AF-Q7TV01-F1 Predicted AlphaFoldDB

No variants for Q7TV01

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7TV01

No associated diseases with Q7TV01

6 regional properties for Q7TV01

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 56 - 67 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 27 - 185 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 435 - 591 IPR002300-2
domain Aminoacyl-tRNA synthetase, class Ia 630 - 670 IPR002300-3
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 724 - 842 IPR013155
domain Leucyl-tRNA synthetase, editing domain 237 - 420 IPR025709

Functions

Description
EC Number 6.1.1.4 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.

3 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.
leucine-tRNA ligase activity Catalysis of the reaction: L-leucine + ATP + tRNA(Leu) = AMP + diphosphate + 2 H(+) + Leu-tRNA(Leu).

1 GO annotations of biological process

Name Definition
leucyl-tRNA aminoacylation The process of coupling leucine to leucyl-tRNA, catalyzed by leucyl-tRNA synthetase. The leucyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a leucine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTESFPSTSA SSQSSARYDP IELETRWQKE WLRQGLDRTP VAETNQKRFY ALSMFPYPSG
70 80 90 100 110 120
KLHMGHVRNY VITDVIARVQ RMRGDAVLHP MGWDAFGLPA ENAAIARNVD PGDWTDQNIA
130 140 150 160 170 180
QMRAQLDRLG LSIDWDRQQA TCHQDYYRWT QWLFLELFAG GLAYQKEATV NWDPVDKTVL
190 200 210 220 230 240
ANEQVDGEGR SWRSGALVEQ RQLKQWFLRI TDYADALIDD LDELTGWPER VRTMQANWIG
250 260 270 280 290 300
RSHGAEIKFR VAGVANSIIT VFTTRPDTLH GASYVVLAPE HPLVESLTSP EQRLAVTAFC
310 320 330 340 350 360
DLISQLSVKD RTAEDQPKRG VPIGAQVINP VNGESLPVWI ADYVLADYGS GAVMGVPAHD
370 380 390 400 410 420
ERDFIFARSH ELPIRIVVQL PDTDEHHNDG QAWTGAGVLV NSGAFDGLST EEAKVAITTH
430 440 450 460 470 480
GASEGWAQSK VQYRLRDWLI SRQRYWGCPI PIIHCASCGI VPVPQEDLPV TLPRDIDLSG
490 500 510 520 530 540
KGGSPIAQEQ AWVEVKCPIC GEKAHRETDT MDTFMCSSWY YLRFADPLNS QRPFDKDIVD
550 560 570 580 590 600
EWLPVDQYVG GIEHAILHLL YARFFTKALH DRNLIGFKEP FNRLLTQGMV QGLTYRNAKN
610 620 630 640 650 660
GSYISPELVS DDSDPRDPES GDRLEVLFEK MSKSKYNGVD PAVVIDRYGA DTARMFILFK
670 680 690 700 710 720
APPEKDLEWD DADVEGQFRF LQRLIRLIDS FAWPKTDGEN ASISSANLII DSADLSEEEI
730 740 750 760 770 780
NMRRATHKAI EAITEDLSGD IQLNTAISEL MKLSNSLSGK LDKVRNEVAA EALSVLVRLM
790 800 810 820 830 840
APFAPHLAEE FWLKLHGHGS IHQQSWPVID PSALVLETIE LVIQVKGKVR GKIQVPANAD
850 860 870
KKTLEELALN SDIAVKWLEG QSPRRIIIVP GKLVNLVP