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 Q2A307

Entry ID Method Resolution Chain Position Source
AF-Q2A307-F1 Predicted AlphaFoldDB

No variants for Q2A307

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2A307

No associated diseases with Q2A307

5 regional properties for Q2A307

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 41 - 52 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 14 - 169 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 416 - 614 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 655 - 774 IPR013155
domain Leucyl-tRNA synthetase, editing domain 221 - 403 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
MNEYNFSDIE KSTQEYWRKN DTFKTIEDNT KEKFYCLSML PYPSGTLHMG HVRNYTIGDV
70 80 90 100 110 120
IARYQKMQGK NVLHPMGWDA FGLPAENAAI KHKKSPYEWT KSNIAYMRSQ FDSLGFSFDW
130 140 150 160 170 180
SREIATCDED YYKWEQWFFI QLYKKGLAYR KNSVVNWDPV DQTVLANEQV VDGRGWRSGA
190 200 210 220 230 240
LVEKKEIPQW FLKITDYADE LLQDINKLDN WPEAVKTMQI NWIGKSKGLT VKFKVKDSNQ
250 260 270 280 290 300
EIEVFTTRPD TLMGVNYLGI APEHPLALKE AKSNSQLAAF IEECKKTSTM EADLATQEKK
310 320 330 340 350 360
GFKTSIKVIH PISAETIDVW VANFVLMGYG SGAVMSVPAH DQRDWEFAQK YNIPLKQVIE
370 380 390 400 410 420
SNDNKLKIDL EKQAFTEKGI LINSGEFDGL NFKNAYQAIK KYLTKQNKGY ETTNFRIHDW
430 440 450 460 470 480
GISRQRYWGC PIPMIHCDDC GAVPEKEENL PVRLPTDVAL TEAGSPLKDI PEFINVACPE
490 500 510 520 530 540
CGKPAKRETD TFDTFFESSW YYARYTCPTS NQMLDQEANY WLPVDKYIGG IEHAIMHLLY
550 560 570 580 590 600
ARFFHKLMRD QGLVKSDEPF KNLLTQGMVL KDGAKMSKSK GNIVDPQELI DKYGADTVRL
610 620 630 640 650 660
FSMFAASPEQ SLEWSETGVE GANKFLRKVF NYAELNKVIF AKNITLESQK LTKEDKKARF
670 680 690 700 710 720
EIHSNLKQAI FDFDKSQFNT VVSACMKILN TLNNYDNLSE SVKVEGFSIL LRILAPFTPH
730 740 750 760 770 780
LCHYLWQQLN LGEDILHTSF PTVDNNALEK DEFLLVVQIN GKLKAKLELD ASLSSNQVEE
790 800 810
VVLADEHVKS FIDNKQVVKV IYVPQKLINI VIK