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 A8G7C4

Entry ID Method Resolution Chain Position Source
AF-A8G7C4-F1 Predicted AlphaFoldDB

No variants for A8G7C4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8G7C4

No associated diseases with A8G7C4

3 regional properties for A8G7C4

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
MSEIKEARLQ KARSLVSKGF ASYAQSFKVS NTTSFLLQEF DYLENGQEAD FSVSVAGRVL
70 80 90 100 110 120
AKRVMGKIAF FTISDQEGQI QLYLDKRIIN LNLEKQKLLS FEDIKEIVDI GDWIGVYGTI
130 140 150 160 170 180
KKTNKGELSI KVEKWEMLSK SLQPLPDKWH GLTDIEKRYR QRYLDLIVNP HSKNVFKTRA
190 200 210 220 230 240
KCISFIRKWL DNRNFLEIET PILQSEAGGA EARPFITHHN TLDIPLYLRI ATELHLKRMV
250 260 270 280 290 300
VGGFEKVYEM GRIFRNEGIS TRHNPEFTSV EIYEAYSDYF DMMNLTEELI KDVVADSCGS
310 320 330 340 350 360
LIINYQNKEI DFSKPWLRIS MKDIVKKYTG IDFDSFSGDF LAAKQAVKNI NVDLSNKVNT
370 380 390 400 410 420
MGRLLNEVFE QKVESKLIEP TFVIDYPVEI SPLARPHFDN KEIVQRFELF IVGRELANAF
430 440 450 460 470 480
SELIDPVDQR ERMQLQQSLR DEGDLEAHCI DEDFLNALEI GMPPTGGLGI GIDRLIMLIT
490 500 510
NSASIRDVIP FPLLKPEITS KKSEKLPLNE VK