P0A8N3

PR
Gene name
lysS (asuD, herC, b2890, JW2858)
Protein name
Lysine--tRNA ligase
Names
Lysyl-tRNA synthetase, LysRS
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b2890
EC number
6.1.1.6: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-87 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

5 structures for P0A8N3

Entry ID Method Resolution Chain Position Source
1BBU X-ray 270 A A 2-505 PDB
1BBW X-ray 270 A A 2-505 PDB
1KRS NMR - A 31-149 PDB
1KRT NMR - A 31-149 PDB
AF-P0A8N3-F1 Predicted AlphaFoldDB

No variants for P0A8N3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0A8N3

No associated diseases with P0A8N3

5 regional properties for P0A8N3

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 162 - 501 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 68 - 146 IPR004365
domain Aminoacyl-tRNA synthetase, class II 184 - 503 IPR006195
domain Lysyl-tRNA synthetase, class II, C-terminal 177 - 503 IPR018149
domain Lysine-tRNA ligase, class II, N-terminal 67 - 174 IPR044136

Functions

Description
EC Number 6.1.1.6 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ligase activity Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.
lysine-tRNA ligase activity Catalysis of the reaction: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).
magnesium ion binding Binding to a magnesium (Mg) ion.
tRNA binding Binding to a transfer RNA.

2 GO annotations of biological process

Name Definition
lysyl-tRNA aminoacylation The process of coupling lysine to lysyl-tRNA, catalyzed by lysyl-tRNA synthetase. The lysyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a lysine-accetping tRNA.
tRNA aminoacylation for protein translation The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, to be used in ribosome-mediated polypeptide synthesis.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P32048 MSK1 Lysine--tRNA ligase, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P15180 KRS1 Lysine--tRNA ligase, cytoplasmic Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P0A8N5 lysU Lysine--tRNA ligase, heat inducible Escherichia coli (strain K12) PR
Q6F2U9 Os03g0586800 Lysine--tRNA ligase Oryza sativa subsp japonica (Rice) PR
Q22099 kars-1 Lysine--tRNA ligase Caenorhabditis elegans PR
Q9ZPI1 At3g11710 Lysine--tRNA ligase, cytoplasmic Arabidopsis thaliana (Mouse-ear cress) PR
Q43776 LYSRS Lysine--tRNA ligase Solanum lycopersicum (Tomato) (Lycopersicon esculentum) PR
10 20 30 40 50 60
MSEQHAQGAD AVVDLNNELK TRREKLANLR EQGIAFPNDF RRDHTSDQLH AEFDGKENEE
70 80 90 100 110 120
LEALNIEVAV AGRMMTRRIM GKASFVTLQD VGGRIQLYVA RDDLPEGVYN EQFKKWDLGD
130 140 150 160 170 180
ILGAKGKLFK TKTGELSIHC TELRLLTKAL RPLPDKFHGL QDQEARYRQR YLDLISNDES
190 200 210 220 230 240
RNTFKVRSQI LSGIRQFMVN RGFMEVETPM MQVIPGGAAA RPFITHHNAL DLDMYLRIAP
250 260 270 280 290 300
ELYLKRLVVG GFERVFEINR NFRNEGISVR HNPEFTMMEL YMAYADYKDL IELTESLFRT
310 320 330 340 350 360
LAQDILGKTE VTYGDVTLDF GKPFEKLTMR EAIKKYRPET DMADLDNFDS AKAIAESIGI
370 380 390 400 410 420
HVEKSWGLGR IVTEIFEEVA EAHLIQPTFI TEYPAEVSPL ARRNDVNPEI TDRFEFFIGG
430 440 450 460 470 480
REIGNGFSEL NDAEDQAQRF LDQVAAKDAG DDEAMFYDED YVTALEHGLP PTAGLGIGID
490 500
RMVMLFTNSH TIRDVILFPA MRPVK