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 C1D6J9

Entry ID Method Resolution Chain Position Source
AF-C1D6J9-F1 Predicted AlphaFoldDB

No variants for C1D6J9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C1D6J9

No associated diseases with C1D6J9

5 regional properties for C1D6J9

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 44 - 55 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 16 - 625 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 669 - 818 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 874 - 936 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 624 - 758 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
MELAKSFEPG NIENRWYDRW EAAGYFKPSM DTDRPSFCIQ LPPPNVTGTL HMGHAFNQTI
70 80 90 100 110 120
MDGLTRYYRM KGDNTLWVPG ADHAGIATQI VVERQLAEQG VSRHDLGRDT FIGKVWEWKE
130 140 150 160 170 180
KSGGTITSQM RRVGCSVDWD KEYFTMDDKM STAVTEVFVR LYEQGLIYRG KRLVNWDPKL
190 200 210 220 230 240
GTAVSDLEVI SEEEDGKMWH IRYPVVGSDD VVVVATTRPE TLLGDVAVAV NPDDERYRHL
250 260 270 280 290 300
VGKQLELPLT GRTIPVIADD YVDAAFGTGF VKITPAHDFN DYQVGKRHNT ALINVMSLDA
310 320 330 340 350 360
TMLAKAQVFG FDGSAQGSID LPAAYAGLST ADARKAMLAD LDAAGLLVDT KPHKLMVPRG
370 380 390 400 410 420
DRTGSVIEPL LTDQWFVAMT KVGEGDATGK SITQKAIDAV ESGEVRFVPE NWVNTYNQWM
430 440 450 460 470 480
NNIQDWCISR QLWWGHQIPA WYDEDGKAYV GRTLEEVQAK APGKTLRRDE DVLDTWFSSA
490 500 510 520 530 540
LVPFSSLGWP NETPELKAFV PSQVLVTGYE IIFFWVARMI MMTTHFLGKV PFKDVYIHGI
550 560 570 580 590 600
VRDHEGKKMS KSEGNVIDPV DLIDGIALPE LITKRTTGLR RPEKAPQIVK ATEKLFPEGI
610 620 630 640 650 660
PAYGTDALRF TMASYASLGR SVNFDFKRAE GYRNFCNKLW NATRFVMMNV EGKDCGQDES
670 680 690 700 710 720
LPLEYSFVDK WIISRLQELE AAVTEALDTY RFDMASQLIY EFVWNEYCDW YVELAKVQLA
730 740 750 760 770 780
NGNEAQQRAT RRTLVRVLEV ALRLTHPLMP FITEELWQTV APLANAKKTD SIMVAAWPVA
790 800 810 820 830 840
DMSKVDAEAC GRMTVFKELV NAIRNLRGEM NLGPSVKAPL FVEGPAAYAD FLPYARLLGR
850 860 870 880 890 900
LSDAAVVEKL PDADAPVAIA GEARLMLKVE IDKAAETARL TKEIGKAESD VEKLTAKLEK
910 920 930
PGYVDKAPAQ LVERDRAQLA DLTDKLAKLK AQLLKLA