Q8K9I1

PR
Gene name
valS
Protein name
Valine--tRNA ligase
Names
Valyl-tRNA synthetase, ValRS
Species
Buchnera aphidicola subsp Schizaphis graminum (strain Sg)
KEGG Pathway
bas:BUsg_354
EC number
6.1.1.9: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

63-133 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8K9I1

Entry ID Method Resolution Chain Position Source
AF-Q8K9I1-F1 Predicted AlphaFoldDB

No variants for Q8K9I1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8K9I1

No associated diseases with Q8K9I1

5 regional properties for Q8K9I1

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 53 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 14 - 630 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 673 - 819 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 887 - 948 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 629 - 763 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
MKKNYNPKDI EEHLYNFWEK NGFFKPNNNL NKPAFCIMMP PPNITGNLHM GHAFQQTIMD
70 80 90 100 110 120
ILIRYNRMQG KNTLWQVGTD HAGIATQILI ERQIFSEERK TKKDYSRNDF IKKIWKWKKK
130 140 150 160 170 180
SNFSVKKQMK RLGNSVDWDR EKFTLDPDIS NSVKEAFIIL YKNNLIYQKK RLVHWDSKLE
190 200 210 220 230 240
TVISDLEVEH RLIKSKKWFI RYPIIKNIKN INIEYLLVAT TRPETLLGDT ALAINPKDDK
250 260 270 280 290 300
YNHLIGQSVI CPIVNRIIPI IADHYADMNK DTGCVKITPG HDFNDYEVGQ RHKLPMINIF
310 320 330 340 350 360
TFNGKIKSNF SIYDYQGSKS NFYDSSIPTE FQNLDILSAR KKIIYEIEKL GLLEKIEECN
370 380 390 400 410 420
FFTPYSERSG VIIQPMLTNQ WYLKTSHLSQ SAIDVVREKK IKFIPNQYKS MYLSWMNNIE
430 440 450 460 470 480
DWCISRQLWW GHQIPVWYDD KKNIYVGHSE KKIREEYNIS DDMILNQDND VLDTWFSSGL
490 500 510 520 530 540
WTFSTLGWPE KTEFLKIFHS TDVLVSGFDI IFFWIARMIM LTMYLVKDSY GNPQIPFKDV
550 560 570 580 590 600
YITGLIRDEE GKKMSKSKGN VIDPIDMIDG ISLNELIEKR TSNLLQPHLS QKIRYHTIKQ
610 620 630 640 650 660
FPNGISATGT DALRFTFSAL ASNTRDIQWD MNRLKGYRNF CNKLWNASRF VLKNTKDHDY
670 680 690 700 710 720
FNFSVNDNML LINKWILIKF NNTVKSYRNS LDSYRFDIAA NILYDFIWNV FCDWYLEFVK
730 740 750 760 770 780
SVIKSGSYQD IYFTKNVLIH VLELLLRLSH PIMPFITEAI WQRVKIIKHI KDRTIMLQSF
790 800 810 820 830 840
PEYNDQLFDK STLSNINWIK KIIIFIRNTR SKMNISSTKL LSLFLKNINS EKKKVIQENK
850 860 870 880 890 900
FILKNIASLE KISILSKQDD EPCLSLKEII DGVDILVPVL KAIDKEIELK RLNKEIEKIK
910 920 930 940 950
SKMLISEKKM SNQDFLSYAP KNIIDKEIKK LKSLNEIYLT LSQQLESLHD AFCKKNKIFN