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 Q8Y6X9

Entry ID Method Resolution Chain Position Source
AF-Q8Y6X9-F1 Predicted AlphaFoldDB

No variants for Q8Y6X9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8Y6X9

No associated diseases with Q8Y6X9

5 regional properties for Q8Y6X9

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 51 - 62 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 24 - 567 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 610 - 754 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 816 - 881 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 566 - 701 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
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

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
MTTEHNEINM PTKYEPSNVE AGKYKWWLEK EFFKAEGNTD KEPYSIVIPP PNVTGKLHLG
70 80 90 100 110 120
HAWDTTLQDI ITRMKRMQGF DTLYLPGMDH AGIATQAKVE AKLKESNISR YDLGRENFVD
130 140 150 160 170 180
KTWEWKEEYA EFIREQWEKL GLGLDYSRER FTLDDGLSDA VKKVFVTLYN KGLIYRGQYI
190 200 210 220 230 240
INWDPEAKTA LSDIEVIHKD IEGSFYHLKY PLTDGSGYLE VATTRPETIP GDTAVAVHPK
250 260 270 280 290 300
DERYQHLIGK TIMLPILNRE IPIVADEYVE REFGSGAVKI TPAHDPNDFE VGNRHNLPRI
310 320 330 340 350 360
IVMHEDGTMN ENAGKYDGLD RFVARKEIIQ DFKDLGLFIK QEPHLHSVGH SERTGAVVEP
370 380 390 400 410 420
YLSLQWFVKM EPLAAEALEL QKTENKVNFV PARFEKTYET WMDNIHDWCI SRQLWWGHRI
430 440 450 460 470 480
PAWYHKETGE IYVGEKEPEN LSEWEQDEDV LDTWFSSALW PFSTMGWPDT ESPDFQHFFP
490 500 510 520 530 540
TNTLVTGYDI IFFWVSRMIF QSVEFTGERP FKDTLIHGLV RDSEGRKMSK SLGNGVDPIE
550 560 570 580 590 600
VIDKYGADSL RYTLATGSSP GQDLKFSYEK VESTWNFINK IWNASRFVLM NLDGMKYNEI
610 620 630 640 650 660
DLSNVTEVSD KWILTRLNET IQAVTSLGEK YEFGEVGRTL YNFIWDDFCD WYIEIAKIPL
670 680 690 700 710 720
YGEDEVAKQT TRSVLAYTLN ATMRLLHPFM PFVTEEIWQN LPHEGESITI AEWPKVNEQQ
730 740 750 760 770 780
IDTKSSTAMA TLVEVIRAVR NIRSEVNTPL SKPIVLEIKP KDTTYKEILE QNISYIERFC
790 800 810 820 830 840
NPEQVTISFD VEASKTAMTA VVSGAEIFIP LEALIDLNVE IARLEKELEK WNKEVARVQG
850 860 870 880
KLNNERFISK APESVVAEER LKEKDYLDKK ASVLERIETL KEV