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 Q9JX22

Entry ID Method Resolution Chain Position Source
AF-Q9JX22-F1 Predicted AlphaFoldDB

No variants for Q9JX22

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9JX22

No associated diseases with Q9JX22

5 regional properties for Q9JX22

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 53 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 14 - 629 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 675 - 824 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 881 - 944 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 628 - 764 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
MLDKYSPAEI ESKHYQNWEE QGYFQPDMDL TKPSFSIQLP PPNVTGTLHM GHAFNQTIMD
70 80 90 100 110 120
GLTRYYRMKG CNTAWIPGTD HAGIATQIVV ERQLAAQNVS RHDLGREKFL EKVWEWKEVS
130 140 150 160 170 180
GGTITQQMRR VGCSADWTRE YFTMDDVRAE TVTEVFVRLY EQGLIYRGKR LVNWDPVLGT
190 200 210 220 230 240
AVSDLEVESV EEQGSMWHIR YPLADNPAEA VIVATTRPET LLGDVAVAVN PEDERYTHLI
250 260 270 280 290 300
GKELILPLTG RTIPVIADEY VEKDFGTGCV KITPAHDFND YEVGKRHDTR LVNVFDLEAK
310 320 330 340 350 360
VLANAEVFNF KGEAQPSFAL PEKYAGLDRF AARKQMVADL QEQGFLVEIK AHTLMTPKGD
370 380 390 400 410 420
RTGSVIEPML TSQWFVAMSA TPNGGEPDSE FKGLSLADKA KKAVDSGAVR FIPENWVNTY
430 440 450 460 470 480
NQWMNNIQDW CISRQLWWGH QIPAWYDNEG NVYVARNQEE AEKQAGKTGL TREEDVLDTW
490 500 510 520 530 540
FSSALVPFST LGWPSETDEL KAFLPSNVLV TGYEIIFFWV ARMIMMTTHF TGKVPFKDVY
550 560 570 580 590 600
IHGIVRDHEG KKMSKSEGNV IDPVDLIDGI DLEKLLVKRT TGLRKPETAP KVEEASRKLF
610 620 630 640 650 660
PEGIPSMGAD ALRFTMASYA SLGRSVNFDF KRAEGYRNFC NKIWNATNFV LMNTENQDCG
670 680 690 700 710 720
YGATATEPRG YSFPDMWIVD RLNQTIEQVT QAYETYRFDL AAETLYSFMW NDYCDWYLEL
730 740 750 760 770 780
AKVQLQTGCA SRQRATRHTL LRVLEAALRL LHPIIPFITE ELWQTVAPMC DAKTADSIML
790 800 810 820 830 840
ARFPEADSGE IVQTAFEQMT VLQDLIGAVR NLRGEMGIQP NVKAPLFVES TDDLADYLKY
850 860 870 880 890 900
LPMMTRLTEA QQVATLPESE DAPVAVCNGA RLMLKVEIDK ATETARLSKE AEKLQKALDK
910 920 930 940
LNAKLSKPGY TEKAPAHLVE KDKADLAELE DKMAKVQTQL SKLKD