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 A9KBJ2

Entry ID Method Resolution Chain Position Source
AF-A9KBJ2-F1 Predicted AlphaFoldDB

No variants for A9KBJ2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9KBJ2

No associated diseases with A9KBJ2

2 regional properties for A9KBJ2

Type Name Position InterPro Accession
domain Cysteinyl-tRNA synthetase, class Ia, DALR 339 - 401 IPR015273
domain tRNA synthetases class I, catalytic domain 2 - 310 IPR032678

Functions

Description
EC Number 6.1.1.16 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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
cysteine-tRNA ligase activity Catalysis of the reaction: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys).
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
cysteinyl-tRNA aminoacylation The process of coupling cysteine to cysteinyl-tRNA, catalyzed by cysteinyl-tRNA synthetase. A cysteinyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a cysteine-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
MKIFNSLTKQ KEIFKPIESG KVKLYVCGMT VYDYMHIGHG RSWIIFDMVV RYLRMRGYEV
70 80 90 100 110 120
TFVRNITDID DKIIKRAGEN KESPAALAER FIQILHEDEK ALRVLSPDQE PRATQYVPEI
130 140 150 160 170 180
IKLIQKLLDN QYAYTGQNGD VFFDVRRFKD YGKLSHRHLD ELQAGARVEV SDSKRDPLDF
190 200 210 220 230 240
VLWKKAKPGE PKWDSPWGEG RPGWHIECSA MSSSILGQPF DIHGGGLDLK FPHHENEIAQ
250 260 270 280 290 300
SEAGEEKPFV KLWMHAGLLE INKEKMSKSL GNIISIREAL KESDVEVLRY FLLSGHYRNP
310 320 330 340 350 360
LSYSKENLEN GRLALERFYL ALRGLPVVNH EKTSSYTDRF YEAMDDDFNT PIAFALLFEM
370 380 390 400 410 420
VREINRFRDN NQIEKAAVLA AELKCLGNIF GLLQYSPEQF LQGAKKEADV QEIKKLIDQR
430 440 450
NEARAKKDWK TADQIRDQLT DLGVAIEDSS DGTSWRQE