Q3A253

PR
Gene name
valS
Protein name
Valine--tRNA ligase
Names
Valyl-tRNA synthetase, ValRS
Species
Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1) (Pelobacter carbinolicus)
KEGG Pathway
pca:Pcar_2315
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)

13-149 (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 Q3A253

Entry ID Method Resolution Chain Position Source
AF-Q3A253-F1 Predicted AlphaFoldDB

No variants for Q3A253

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3A253

No associated diseases with Q3A253

5 regional properties for Q3A253

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 60 - 71 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 31 - 579 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 623 - 769 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 831 - 895 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 578 - 714 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
MSQSCMFCPK DELPMEPKLP KGYEPHDVEA KWYEFWTENG LFHADENSPK NPFSIVIPPP
70 80 90 100 110 120
NVTGVLHMGH ALNNTLQDIL ARWKRMDGHE VLWQPGTDHA GIATQNVVEK QLAAEGSSRH
130 140 150 160 170 180
DLGREGFVDR VWQWRTESGG QIINQLKRLG ASCDWERERF TMDEGLSRAV REVFVTLYEE
190 200 210 220 230 240
GLIYRDNRLI NWCPRCHTAL SDLEVEHQDQ KGNLWHLRYP VVGTDRHLVV ATTRPETMLG
250 260 270 280 290 300
DTAVAVHPED ERYADLIGKF IMLPLMDRQI PIIADEYVDK EFGSGAVKIT PAHDFNDFEI
310 320 330 340 350 360
GKRHDLEFIN IFDESGVVNG NGGRYQGLER FEARTRVLAD LDAAGLLEQT EEHLNAVGEC
370 380 390 400 410 420
YRCKTVIEPY MSLQWYVNVQ PLAEKAIEAV QTGQTRIIPQ QWEKTYFEWM FNIRDWCISR
430 440 450 460 470 480
QIWWGHRIPA WFCAACNEVT VSREDPTACS HCGATELRQE TDVLDTWFSS ALWPFSTMGW
490 500 510 520 530 540
PDKTVALEKF YPTSCLVTGF DILFFWVARM MMMGLKFMGQ VPFKDVYIHA LVRDAQGQKM
550 560 570 580 590 600
SKSKGNVIDP LTVIDEYGTD AFRFTLAAFA AQGRDVKLSV DRIAGYRNFV NKLWNASRFA
610 620 630 640 650 660
LMNLEDFDPS GIDLDDCQLT LAERWILTRL IDVAAETGKA LEEYKFNEAA SVLYAFTWHE
670 680 690 700 710 720
FCDWYIELSK DDLYGEDAAR KATSQAVLYT VLEQLLRLLH PLMPFVTEEI WQALPGERPA
730 740 750 760 770 780
VSIMSAAFST VSELPEDRQG ASHMERIMDV IKGVRNIRGE MNVPPGKRIA AVLDCKTSKA
790 800 810 820 830 840
AEVMAAGEGY IKSLARIDDL AFGVAVERPA QAATQVAGDI EILLPLAGLI DLDEEQKRLN
850 860 870 880 890
KEIAKVEKDV LMFSKKLSNE SFLAKAPAAV LEKDRQKLAD AEEKLSILKQ GLEKLAALQ