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 Q8EX08

Entry ID Method Resolution Chain Position Source
AF-Q8EX08-F1 Predicted AlphaFoldDB

No variants for Q8EX08

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8EX08

No associated diseases with Q8EX08

5 regional properties for Q8EX08

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 51 - 62 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 23 - 559 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 606 - 744 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 808 - 866 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 562 - 692 IPR033705

Functions

Description
EC Number 6.1.1.9 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
aminoacyl-tRNA editing activity The hydrolysis of an incorrectly aminoacylated tRNA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
valine-tRNA ligase activity Catalysis of the reaction: L-valine + ATP + tRNA(Val) = L-valyl-tRNA(Val) + AMP + diphosphate + 2 H(+).

1 GO annotations of biological process

Name Definition
valyl-tRNA aminoacylation The process of coupling valine to valyl-tRNA, catalyzed by valyl-tRNA synthetase. The valyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a valine-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
MSNIKNNNDL SKKYDHKICE QQFSLWTTQK ELNKKNLKAN KNSYSILLPP PNVTGNLHLG
70 80 90 100 110 120
HALNGTIQDC LIRFNNLKGL SAYWICGMDH AGIATQTKYE KYLRENKISN KDKSRDEKVA
130 140 150 160 170 180
DLFEWSQNVG NNIRNQWKNM GFFLDYENEH FTLEKKSNEM VNQVFVKMYN DGLIYRSKTL
190 200 210 220 230 240
VNWDIKLQSA ISNIEVIKKE VETNLYYIRY YLSNSKDYLL VATTRPETIF VDECLVVNPK
250 260 270 280 290 300
DKRYKNYINK FAINPLTNKE IKIIADEYVD IQFGTGVMKC TPAHDFNDYE LGKKYKLNII
310 320 330 340 350 360
SCFNEDGTTN NYAVGFENLK IADARVKCVE YLEKNNLLEK VEKTISNVGF SERTNAVVEP
370 380 390 400 410 420
MMSEQWFVKV SEYSKKVIEL QKSSKKIQFF PIKFEKNLIN WMTNLNDWCI SRQLWWGHQI
430 440 450 460 470 480
PVWYKKDSKE IYVGTKPPKN EELYVRDNDV LDTWFSSGLW PITTTDALKS KDALFPTNVL
490 500 510 520 530 540
VTGFDIIFFW VFRMMFFSLY LKKEVPFKHC YITGLIRDEH NNKMSKSLGN GVDPNDVIEK
550 560 570 580 590 600
YGADALRLFL LSSSSPGEDL CYVEEKVKSC WGFINKLWNS FRYVEMNSSD FNFDEDKTPK
610 620 630 640 650 660
NLEDFDKWIL NKFNKAYSEF LQQFNKYNFL VSIKKILDFT WDDFCNTYIE LSKNRTSNQE
670 680 690 700 710 720
SKLWVLNYLI KKILILFHPM CPFVTSNLYD NFKFKTKDSI LLERLDFKKI SNLKESSIED
730 740 750 760 770 780
VLQIINKIRI FNFENKIPNN KVIDIHLEVL NPKLFKISDE VINILNTAKI NIVKQDIKSL
790 800 810 820 830 840
KPDYVENNYL IFILNKEDLL GSNNEANNIE KIKKEIEFVK SEISRCNGML SNKSFIEKAP
850 860
KEKIELEKSK KEKHEMKLKE LEKLLSSHK