Q65GK8

PR
Gene name
valS
Protein name
Valine--tRNA ligase
Names
Valyl-tRNA synthetase, ValRS
Species
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46)
KEGG Pathway
bli:BL00631
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)

712-781 (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 Q65GK8

Entry ID Method Resolution Chain Position Source
AF-Q65GK8-F1 Predicted AlphaFoldDB

No variants for Q65GK8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q65GK8

No associated diseases with Q65GK8

5 regional properties for Q65GK8

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 49 - 60 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 21 - 565 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 608 - 756 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 814 - 879 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 564 - 699 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
MDNQELTMPT KYDPSAVEKD RYDYWVNGKF FEAKNDPEKE PYTVVIPPPN VTGKLHLGHA
70 80 90 100 110 120
WDSTLQDIVT RMKRMQGYDV LWLPGMDHAG IATQAKVEAK LREEGKTRYD LGREKFLEET
130 140 150 160 170 180
WNWKEEYADF IRSQWAKLGL GLDYSRERFT LDEGLSKAVR EVFVKLYEKG LIYRGEYIIN
190 200 210 220 230 240
WDPATKTALS DIEVIYKDVQ GAFYHMRYPL KDGSGSIEIA TTRPETMLGD TAVAVHPEDE
250 260 270 280 290 300
RYKHLIGKTV ILPITGREIP IVGDDYVDME FGSGAVKITP AHDPNDFEIG NRHNLERILV
310 320 330 340 350 360
MNEDGTMNDN ALQYKGMDRF ECRKQIVKDL QEEGVLFKIE EHTHSVGHSE RSGAVVEPYL
370 380 390 400 410 420
STQWFVQMQP LADAAIELQK SEGKVNFVPD RFEKTYLHWM ENIRDWCISR QLWWGHRIPA
430 440 450 460 470 480
WYHKETGEIY VGVEAPEDAE NWEQDKDVLD TWFSSALWPF STMGWPDIDE EDFKRYYPTN
490 500 510 520 530 540
VLVTGYDIIF FWVSRMIFQG IEFTGERPFK DVLIHGLIRD DQGRKMSKSL GNGVDPMDVI
550 560 570 580 590 600
DKYGADSLRY FLATGSSPGQ DLRFSFEKVE STWNFANKIW NASRFALMNM DGMTYEELDL
610 620 630 640 650 660
SGEKSVADKW ILTRLNETIE TVTQLADKYE FGEVGRHLYN FIWDDFCDWY IEMAKLPLYG
670 680 690 700 710 720
EDEAAKKTTR SILAYVLDQT MRLLHPFMPF LTEEIWQHLP HEGESITVAK WPEAVKEYTD
730 740 750 760 770 780
TEAAADMKLL VEVIRAVRNI RSEVNTPLSK QIELYIKTST PEIAERLEEN RSYVERFTNP
790 800 810 820 830 840
SLLQIGTDIQ AVDKAMTAVV SGAELILPLE GLINIDEEIS RLQKELDKLT KEVERVQKKL
850 860 870
SNEGFMKKAP AHVIEEERAK EADYTAKREA VEKRIAELKN