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 B4SJ70

Entry ID Method Resolution Chain Position Source
AF-B4SJ70-F1 Predicted AlphaFoldDB

No variants for B4SJ70

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B4SJ70

No associated diseases with B4SJ70

5 regional properties for B4SJ70

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 54 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 17 - 628 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 669 - 818 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 880 - 942 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 627 - 760 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
MTQLASSYDP KSFETDLYEA WEKAGHFKPS GTGEPYTILL PPPNVTGTLH MGHAFQQTLM
70 80 90 100 110 120
DALVRYHRMR GYDTLWQVGT DHAGIATEMV VSRNLALEGK GETRDSLGRE GFIGKVWEWK
130 140 150 160 170 180
QQSGDIIERQ MRRLGTSADW SRSTFTMDPQ PSAAVNEAFV RWYEQGLIYR GQRLVNWDPV
190 200 210 220 230 240
LKTAISDLEV ESAEEDGFLW SIAYTLDDGL SYEHVERDAD GVETLRETRD YLVVATTRPE
250 260 270 280 290 300
TLLGDTAVMV HPEDARYAHL IGKSVVLPLT GRRVPVIADD YVDRAFGTGV VKVTPAHDFN
310 320 330 340 350 360
DYEVGVRHSL PMINLFTPVA ALNENAPERF QGLDRYAARK AVLAELEDLG ILVETKAHKL
370 380 390 400 410 420
QVPRGDRTGQ VIEPYLTDQW FVKMDDLAKR GLELVEDGSI SFVPPNWINT YRHWMNNIQD
430 440 450 460 470 480
WCISRQLWWG HRIPAWFDEA TGSCYVGRSE EEVRAKHSLG SDVVLNQESD VLETWFSSQL
490 500 510 520 530 540
WPFSTLGWPN EQAMAERGFD RYLPSSVLIT GFDIIFFWVA RMIMATDNLV GKIPFKDVYF
550 560 570 580 590 600
TGLIRDGQGQ KMSKSKGNVL DPLDIIDGIS IDDLVAKRTG GLMQPKMVEK IEKATRKEFP
610 620 630 640 650 660
DGIAAHGADA LRFTIAALAT HGRDIKFDMN RAEGYKNFCN KLWNASRFTL MNTEGAAFTG
670 680 690 700 710 720
MPTPRTDAER WILSRLAAVS SEAQGHYANY RFDLLAQCLY EFAWNEFCDW FLELSKPALN
730 740 750 760 770 780
GADAADAEST RHTLLYVLEA LLRLLHPLTP FITEQLWQQL APRLGLAETT LSLRPYPTAA
790 800 810 820 830 840
EFEGDFAQAE ADVEWLKAVI SAVRRVRSEL NVAPSKQVPL RLQAGLEQDR VRIERFSASL
850 860 870 880 890 900
SFLLKLDSIQ WLAEGESAPP AAAAIVGELK LLVPLEGLVD LDAERVRLDK EIARVEVEKE
910 920 930 940
KSETKLAKFT DKVPPAVVEQ ERVRLVDWNT QLAGLREQRA KL