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 B3EH05

Entry ID Method Resolution Chain Position Source
AF-B3EH05-F1 Predicted AlphaFoldDB

No variants for B3EH05

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B3EH05

No associated diseases with B3EH05

4 regional properties for B3EH05

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class Ia 416 - 602 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 653 - 766 IPR013155
domain Methionyl/Leucyl tRNA synthetase 38 - 171 IPR015413
domain Leucyl-tRNA synthetase, editing domain 217 - 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
MRYEFSAIEK KWQAIWQENG TFKTGESTEK PKYYVLDMFP YPSGSGLHVG HLEGYTASDI
70 80 90 100 110 120
IARFKRSRGF NVLHPMGWDA FGLPAEQYAI KTGTHPKITT ENNIRSFRET LQAMGFSYDW
130 140 150 160 170 180
SKEINTTDPA YFKWTQWIFL RLYEMGLAYM SDVDVNWCEE LKTVLANEEV DEKIADGYTV
190 200 210 220 230 240
VRKPLRQWVL KITAYAERLL ADLDELEWPE NVKQMQRNWI GRSEGVEIDF ELRCHGKNLR
250 260 270 280 290 300
VYTTRPDTLF GATYLVVSPE HPLAEKLATA DNLKEVKAYI SRAKLKTELE RTGLQKDKTG
310 320 330 340 350 360
VFTGSYAINP ATGNPLPVWI SDFVLISYGT GAIMSVPAHD SRDWEFAKKF DLPIIEVIKS
370 380 390 400 410 420
PHDVNDAVFE GKESVPVNSS NSEITIDGLP FREAFDTMAS WLEKKGAGKR TINYKLRDWI
430 440 450 460 470 480
FSRQRYWGEP IPIKHYEDGT LRTETILPLT LPDVEAYQPS ETGESPLATI HDWLYGSDEF
490 500 510 520 530 540
GSFRRETNTM PQWAGSCWYY LRFIDPENSG RLIDPEREKY WMNVDLYIGG AEHAVLHLLY
550 560 570 580 590 600
ARFWHKVLFD LNVVSTVEPF RKLFNQGMIL GEDNEKMSKS RGNVIPADHV LKTYGADAVR
610 620 630 640 650 660
LYEMFLGPLE QVKPWNTNGI EGISRFLGKV WRLVYPEQEG NKAELTDETM PEELLRRLHK
670 680 690 700 710 720
TIRKVTEDTE ALKFNTAIAE MMVLVNELQR NGCRNRTAVE SMILLLAPYA PHIAEELWQA
730 740 750 760 770 780
TGHTGSISNE PFPNYVAGLA TDSVVQIAVQ VNGKLRGTFS TPAGTPQNSL IETARNVESV
790 800
MKFLEGKAIM REIVVPDKLV NFAVK