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 A1BDY0

Entry ID Method Resolution Chain Position Source
AF-A1BDY0-F1 Predicted AlphaFoldDB

No variants for A1BDY0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1BDY0

No associated diseases with A1BDY0

4 regional properties for A1BDY0

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class Ia 416 - 602 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 661 - 773 IPR013155
domain Methionyl/Leucyl tRNA synthetase 38 - 172 IPR015413
domain Leucyl-tRNA synthetase, editing domain 217 - 402 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
MRYDFSTIEK KWQSFWLKNN SFSSGESTDK PKYYVLDMFP YPSGSGLHVG HLEGYTATDI
70 80 90 100 110 120
VARYKRSCGY NVLHPMGWDA FGLPAEQFAI KTGTHPKNTT EKNISSFRET LQAMGFSYDW
130 140 150 160 170 180
SREINTTSPD YFRWTQWIFI KLYELGLAYV SEVDINWCEE LKTVLANEEV EEKVKEGYTV
190 200 210 220 230 240
IRKPLRQWVL KITAYAERLL DDLDELDWPE NVKQMQRNWI GRSEGMEIDF ELRCHNRKLR
250 260 270 280 290 300
VYTTRPDTLF GATFLVISPE HPLALKLATA QQLVAVTQYI KEAKLKSELE RTGLQKDKTG
310 320 330 340 350 360
IFTGSFAINP ATGDPLPVWI SDFVLTSYGT GAIMSVPAHD SRDWEFAKKF GLPIIEVIKS
370 380 390 400 410 420
PDGVDDAAFE GKESVSINSS NPEISIDGLH FSEAFQIMAH WLETKGLGER KVTYKLRDWI
430 440 450 460 470 480
FSRQRYWGEP IPVKHYEDGS IRTESNLPLQ LPEVEAYQPS ETGESPLATM HDWLYGADEF
490 500 510 520 530 540
GSFRRETNTM PQWAGSCWYY LRFIDPENNA QLIDPAKEKY WMNVDLYIGG AEHAVLHLLY
550 560 570 580 590 600
ARFWHKVLYD LGVVSSREPF KKLFNQGMIL GEDNEKMSKS RGNVIPADQV LKDYGADAVR
610 620 630 640 650 660
LYEMFLGPLE QVKPWNTNGI EGISRFLGKV WRLVYPDSEN PDQRDQAAVL DENPLPEILQ
670 680 690 700 710 720
RRMHKTIKKV TEDTDHLKFN TAISEMMVFV NELQKNGCRQ KSAVENLLLM LAPYAPHITA
730 740 750 760 770 780
ELWQAIGHTS PISAEPFPVF DPAIAEDPVV TIAVQVNGKL RGRFTAPAKS PEESLVDMAK
790 800 810
HVDTVIKFLE GQTIVKEIVI QDKLVNFAVK QSIPNH