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 A5N399

Entry ID Method Resolution Chain Position Source
AF-A5N399-F1 Predicted AlphaFoldDB

No variants for A5N399

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5N399

No associated diseases with A5N399

4 regional properties for A5N399

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class Ia 409 - 598 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 659 - 771 IPR013155
domain Methionyl/Leucyl tRNA synthetase 39 - 184 IPR015413
domain Leucyl-tRNA synthetase, editing domain 217 - 395 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
MYSTKTDKKW QQKWDQTNIY TFDEKKSSKK LYTLEMFSYP SGSNLHAGHW FNYAPVDSWA
70 80 90 100 110 120
RMKRMQGYNV FQPMGFDAFG LPAENYAIKT GIHPKDSTEK NIDTMEKQLK SMGAMFNWEN
130 140 150 160 170 180
EVVTCRPDYY KWNQWLFLQL YKHDLAYRKN APVNWCPSCN TVLANEQVKE GECERCGTEV
190 200 210 220 230 240
TKKDLTQWFF KITDYTEELL KDLDNIDWPE KTKAMQRHWM GKSTGTDVTF KVADSDIKFN
250 260 270 280 290 300
VFTTRVDTLF GVTYVVISPE NDLVDSVTKE EYKEEIEKYR EAAKKQTDIE RQSITREKTG
310 320 330 340 350 360
VSTGSYAINP INGRKVPIWI GDYVLNTYGT GAVMAVPAHD ERDFEFATKY KLPIERVIEG
370 380 390 400 410 420
GSSLPYVEYG KMINSDKFNG LYTPEGKEAV TKELENIGLG SGKTNYRLRD WLVSRQRYWG
430 440 450 460 470 480
TPIPIIYCKK CGTVPVPESD LPVELPYNVQ FSPDGKSPLL KSEEFMNTTC PICGEPAKRE
490 500 510 520 530 540
ADTLDTFVCS SWYYLRYADN KNTEKAFDKD KINKLLPVDM YVGGPEHACM HLLYARFITK
550 560 570 580 590 600
ALRDMGFLNF DEPFLSLRHQ GLILGPDGQK MSKSKGNTIS PDDCIQKYGS DVFRMYLMFG
610 620 630 640 650 660
FDYAEGGAWN DDGIKSMSKF VDRIERIVGN IKELINSGKN FKNSMDAAEK ELNYSRNYSI
670 680 690 700 710 720
KSVSEDAGKF QFNTAIARIM EFTNSLYKYI QEDTKNISLL KDTILDFIKI IAPFAPHFAE
730 740 750 760 770 780
EQWEVLGQKY SIFNEKWPEF DPKALVKEEV EIAIQINGKI KAKINIPTNL SDEQIKELSI
790 800 810
SNDNIKPLLE GKNIKKVIVV KGRLVNIVVK P