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 A4WE42

Entry ID Method Resolution Chain Position Source
AF-A4WE42-F1 Predicted AlphaFoldDB

No variants for A4WE42

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4WE42

No associated diseases with A4WE42

3 regional properties for A4WE42

Type Name Position InterPro Accession
domain Regulator of K+ conductance, N-terminal 402 - 524 IPR003148
domain K+/H+ exchanger 14 - 283 IPR004771
domain Cation/H+ exchanger 11 - 373 IPR006153

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

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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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.
nucleic acid binding Binding to a nucleic acid.

1 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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSEQQAQGTD AVVDLNNELK TRREKLAALR EQGIPFPNDF RRDHTSDQLH ADFDAKENEE
70 80 90 100 110 120
LEALNVEVSV AGRMMTRRIM GKASFVTLQD VGGRIQLYVS RDDLPEGIYN EQFKKWDLGD
130 140 150 160 170 180
ILGAKGKLFK TKTGELSIHC TELRLLTKAL RPLPDKFHGL QDQEARYRQR YLDLISNDES
190 200 210 220 230 240
RKTFKIRSQI MAGIRQFMVG RDFMEVETPM MQVIPGGASA RPFVTHHNAL DLDMYLRIAP
250 260 270 280 290 300
ELYLKRLVVG GFERVFEINR NFRNEGISVR HNPEFTMMEL YMAYADYKDL IELTESLFRT
310 320 330 340 350 360
LAQNILGTTE VPYGDEVFDF GKPFVKLTMR EAIKKYRPET EMADLDNYDS AKAIAESIGI
370 380 390 400 410 420
KVEKSWGQGR IVTEIFEEVA EAHLIQPTFI TEYPAEVSPL ARRNDENPEI TDRFEFFIGG
430 440 450 460 470 480
REIGNGFSEL NDAQDQAQRF QDQVDAKAAG DDEAMFFDED YVTALEHGLP PTAGLGIGID
490 500
RMVMLFTNSH TIRDVILFPA MRPVK