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 B1YGS9

Entry ID Method Resolution Chain Position Source
AF-B1YGS9-F1 Predicted AlphaFoldDB

No variants for B1YGS9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B1YGS9

No associated diseases with B1YGS9

2 regional properties for B1YGS9

Type Name Position InterPro Accession
domain Cysteinyl-tRNA synthetase, class Ia, DALR 352 - 416 IPR015273
domain tRNA synthetases class I, catalytic domain 3 - 312 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
MIQLYNSMTG KKEPFKPLEE GKVKMYVCGP TVYNYIHIGN ARPAIVFDTV RRYFTYRGYD
70 80 90 100 110 120
VKYVSNFTDV DDKIIRTANE LGEDYHALTK RFIEAYHADT GALNVQKADI HPLVTETMDD
130 140 150 160 170 180
IIAFIEVLVK KGNAYASSGD VYFRTRSFKD YGQLSQQSID ELRSGARIEV GEKKEDPLDF
190 200 210 220 230 240
VLWKAAKPGE PAWTSPWGEG RPGWHIECSA MAKKYLGDTI DIHAGGQDLK FPHHENEIAQ
250 260 270 280 290 300
SEACNSQKFA NYWMHNGFLN IENEKMSKSL GNFLTVHEAI QAVDPMVLRF FMLSVQYRHP
310 320 330 340 350 360
INYSRDLIDQ AANGLARIRE SVANVEHRLT MTADLGTATE KWLNRIEEIK QHFVTSMDDD
370 380 390 400 410 420
FNTANAVTDL FDLSKEANLY LGEDQVAKEV LERFLAVFQE LSTVLGVTLT IEKGLLDEEV
430 440 450 460
EQLIRDRDTA RKERDFARAD AIRDQLRDQG ILLEDTAQGM RWKRG