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 B1YT20

Entry ID Method Resolution Chain Position Source
AF-B1YT20-F1 Predicted AlphaFoldDB

No variants for B1YT20

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B1YT20

No associated diseases with B1YT20

4 regional properties for B1YT20

Type Name Position InterPro Accession
domain AAA+ ATPase domain 290 - 487 IPR003593
domain ATPase, AAA-type, core 294 - 366 IPR003959
domain LIS1 homology motif 25 - 57 IPR006594
domain AAA ATPase, AAA+ lid domain 417 - 458 IPR041569

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
MTEPTQTQPA VAADENQIIA ERREKLRALR EQGVAYPNDF RPTHHAADLQ ATFADSDKAA
70 80 90 100 110 120
LEANPVEVSV AGRMMLKRVM GKASFATVQD GSGQIQFFVT PNDVGAETYD AFKKWDLGDI
130 140 150 160 170 180
VAARGVLFRT NKGELSVQCK ELRLLSKALR PLPDKFHGLA DQEMRYRQRY VDLIVTPETR
190 200 210 220 230 240
DTFRARTRTI ASIRKFMDNA DFMEVETPML HPIPGGAAAK PFVTHHNALD MQMFLRIAPE
250 260 270 280 290 300
LYLKRLIVGG FERVFEINRN FRNEGVSPRH NPEFTMMEFY AAYTDYRWLM DFTEQLIRQA
310 320 330 340 350 360
AIDALGTATI QYQGRELDLA KPFHRLTITQ AIQKYAPQYT DGQLSDDAFL RTELKRFGVD
370 380 390 400 410 420
VSQPAFLNAG IGALQLALFE ETAESQLWEP TYIIDYPVEV SPLARASDTT PGITERFELF
430 440 450 460 470 480
MTGREIANGF SELNDPEDQA ARFKKQVEQK DAGDEEAMFF DADYIRALEH GMPPTGGCGI
490 500
GIDRLVMLLT DSPTIRDVLL FPHLRRED