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 A4SG27

Entry ID Method Resolution Chain Position Source
AF-A4SG27-F1 Predicted AlphaFoldDB

No variants for A4SG27

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4SG27

No associated diseases with A4SG27

4 regional properties for A4SG27

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class Ia 416 - 602 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 654 - 768 IPR013155
domain Methionyl/Leucyl tRNA synthetase 38 - 171 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
MRYDFSKTEK KWQARWKQQE TFKTGEAPEK PKYYVLDMFP YPSGSGLHVG HLEGYTASDI
70 80 90 100 110 120
SARYRRSRGY NVLHPMGWDA FGLPAEQFAI KTGTHPSDTT QKNIANFKET LQAMGFSYDW
130 140 150 160 170 180
SREINTTDPG YFQWTQWIFL KLHEMGLAYM SEVDVNWCVE LRAVLANEEV EEKLADGLTV
190 200 210 220 230 240
VRRPLRQWVL KITAYADRLL EDLDGLDWPE NVKQMQRNWI GRSEGVEVDF ELRCHRTMLR
250 260 270 280 290 300
VYTTRPDTLF GATYLVISPE HAMAEKLATA QQLVAVKEYI AKAKLKTELE RTGLQKDKTG
310 320 330 340 350 360
VFTGSYAINP ATGEPLPVWI SDFVLTSYGT GAIMSVPAHD SRDWEFAKQY GLPIIEVVKS
370 380 390 400 410 420
PHDVQQEVFE GKDSTVVNSS NNDISLNGLA FPEAFELMAS WLEKKKAGKR KVNYRLRDWI
430 440 450 460 470 480
FSRQRYWGEP IPIKHYPDGT LKPETSLPLM LPEVEAYQPT ETGESPLANI PEWLNGTDEN
490 500 510 520 530 540
GPFRRETNTM PQWAGSCWYY LRFIDPHNSK LPVDPAKEAY WMNVDLYIGG AEHAVLHLLY
550 560 570 580 590 600
ARFWHKVLFD LKVVSTKEPF QRLFNQGMIL GEDNEKMSKS RGNVIPADHV LQTYGADAVR
610 620 630 640 650 660
LYEMFLGPLE QVKPWNTNGI EGISRFLSRV WRLVWPEPEG TRADLSTLAP SPDLLRRMHK
670 680 690 700 710 720
TIKKVAADTE NLKFNTAIAE MMVFTNELHR TGEGSRIAVE TLLLLLAPYA PHLSEELWEA
730 740 750 760 770 780
LGHQESISLA PFPEFDPELA QDKEVTIAVQ VNGKLRGSFT AAPGSPKEQL LNEAKALEGV
790 800
KKFLEGVTIM KEIVVPDKLI NFAVK