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 Q9X2D7

Entry ID Method Resolution Chain Position Source
AF-Q9X2D7-F1 Predicted AlphaFoldDB

No variants for Q9X2D7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9X2D7

No associated diseases with Q9X2D7

5 regional properties for Q9X2D7

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 54 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 16 - 563 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 603 - 748 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 800 - 864 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 562 - 691 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
MAELSTRYNP AEIETKWYRY WEEKGYFTPK GVGEKFSIVI PPPNITGRIH MGHALNITLQ
70 80 90 100 110 120
DIVVRYKRMK GYDVLWVPGE DHAGIATQNA VEKFLLQTQG KTREEIGREK FLEITWEWAN
130 140 150 160 170 180
KYRREIREQI KALGASVDWT RERFTLDEGL SRAVRKVFVE LYRKGLIYRG KYIVNWCPRC
190 200 210 220 230 240
KTVLSDEEVE HKEHKSKLYY VKYPVKDSDE YIVVATTRPE TMLGDTAVAV HPEDERYKNF
250 260 270 280 290 300
VGKTLILPLV GREIPVVADK YVDPKFGTGA VKVTPAHDPN DYLIAQRHNL PMIEIFDDNA
310 320 330 340 350 360
RINENGGKYK GLDRYEAREK IVKDLEEQGF LVKIEDYTHS VGHCYRCDTV IEPKLSDQWF
370 380 390 400 410 420
VSTKPLAKRA IEAVENGEIR FFPERWTKVY LNWMYEIRDW CISRQLWWGH RIPVWYCQDC
430 440 450 460 470 480
GHLNVSEEDV EKCEKCGSTN LKQDEDVLDT WFSSALWPFS TLGWPEETED LKRYYPTDLL
490 500 510 520 530 540
VTGFDIIFFW VARMIMMGYE FMNDKPFSHV YIHQLVRDKY GRKMSKSLGN GIDPLEVIDE
550 560 570 580 590 600
YGADPMRFTL AILAAQGRDI KLDPRYFDAY KKFANKIWNA TRFVLMNLED YKEVPLENLK
610 620 630 640 650 660
TVDKWILTRL NKTVEEVTNA LENYDFNIAA RTIYNFFWDD FCDWYIEASK PRLKTEERNL
670 680 690 700 710 720
VQTVLVKVLD ASLRLLHPFM PFLTEELWQK LPVAGESITI AKWPEIEREL IDETAEKEFT
730 740 750 760 770 780
RLMNMVRGVR NVRAEMNLPQ SQRVKVYIKG YEVTEEEELL LKTLGNIEEV SFVNEKPPKT
790 800 810 820 830 840
ATAYVEEEIE AYVDLGGLID FEKEKERLKQ IMEKIQKEID RLEKKLANKD FVEKAPEEVV
850 860
EETKEKLNTN RERLARLESI LRDLE