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 Q9UYV2

Entry ID Method Resolution Chain Position Source
AF-Q9UYV2-F1 Predicted AlphaFoldDB

No variants for Q9UYV2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9UYV2

No associated diseases with Q9UYV2

2 regional properties for Q9UYV2

Type Name Position InterPro Accession
domain Cysteinyl-tRNA synthetase, class Ia, DALR 356 - 417 IPR015273
domain tRNA synthetases class I, catalytic domain 4 - 314 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
MGIKVYNTLT RKKEELKPLR DGEVRMYVCG PTVYDYPHLG HARTYIAFDV IRRYLEHRGF
70 80 90 100 110 120
TVLMVMNFTD IDDKIIKRAQ ETGEDPGKLA ERFIKVFLED MNALKVKPAD IYPRVTEHID
130 140 150 160 170 180
DIIEFIKKLK EKGYAYEGSD GVYFEVQKFK DYGKLSGVKI EELRKGARVE PGEGKKNPED
190 200 210 220 230 240
FALWKKAKPG EPKWDSPWGE GRPGWHIECS VMSSKYLGES FDIHGGGNDL IFPHHENEIA
250 260 270 280 290 300
QSEACFGHEW VRYWLHTGFV MVKGEKMSKS LGNFVTVREL LQRYSPEVIR LFVLQKHYRS
310 320 330 340 350 360
PLDYTEEGLQ HAKNNLERLY NTLENIRIAM RNAELSYKWS EKDFEAYEAI REARKKFYDA
370 380 390 400 410 420
MDDDFNTAEA LKAVFEVSNA INKYILEVDK PKESILRKAL EFFKVVSEVF GIFEDYFKEE
430 440 450 460 470
KKGEEEKLIE LLVEVRKQLR KEKRFDLADK IREELRKLGI QLEDKGQETV WKRVKVS