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 Q9K8G8

Entry ID Method Resolution Chain Position Source
AF-Q9K8G8-F1 Predicted AlphaFoldDB

No variants for Q9K8G8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9K8G8

No associated diseases with Q9K8G8

5 regional properties for Q9K8G8

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 49 - 60 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 20 - 564 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 608 - 755 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 814 - 879 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 564 - 699 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
MTKQDQEMPT KYHPQDIESK WYEYWIEGKF FEATSDETKK PYTIVIPPPN VTGKLHLGHA
70 80 90 100 110 120
WDTALQDILS RLKRMQGYDT LWLPGMDHAG IATQAKVEAK LREEGKSRYD LGREAFVEKT
130 140 150 160 170 180
WEWKEEYADF IRQQWAKLGL SLDYSRERFT LDEGLSKAVR EVFVKLYEKG LIYRGEYIIN
190 200 210 220 230 240
WDPVTKTALS DIEVIYKDVQ GYFYHMKYPL ADGDGAIEVA TTRPETMLGD TAVAVHPEDE
250 260 270 280 290 300
RYQHLIGKMV KLPITGREIP IVADDYVDME FGSGAVKITP AHDPNDFEIG NRHNLPRILV
310 320 330 340 350 360
MNEDGTMNEK AGQYEGMDRF ECRKQIVKDL QEQGVLFKIE EHVHSVGHSE RSGAVVEPYL
370 380 390 400 410 420
STQWFVKMKP LAEQAIELQT TENKVNFVPD RFEKTYLRWM ENIRDWCISR QLWWGHRIPA
430 440 450 460 470 480
WYHKETGEVY VGHEAPQDID NWKQDEDVLD TWFSSALWPF STMGWPDEEA PDYKRYYSTD
490 500 510 520 530 540
ALVTGYDIIF FWVSRMIFQG LEFTGQPPFK DVLIHGLVRD AEGQKMSKSL GNGVDPMEVI
550 560 570 580 590 600
DKYGADALRF FLATGSSPGN DLRFYWEKVE STWNFGNKIW NASRFALMNM DGMSYDEIDL
610 620 630 640 650 660
TGEKSIADQW ILTRLQETIE TVTRLIDAYE FGEVGRHLYN FIWDDLCDWY IEMAKLPLYG
670 680 690 700 710 720
EDEVAKKTTR SVLAYVLDQT MRLLHPLMPF ITEEIWQHLP HEGESITVAS WPVKSEEFTF
730 740 750 760 770 780
EQAMGDMELL KDIIRSVRNT RAELNVPMSK EIELHIQAKN EDVLTQLERG KHYIEKFCNP
790 800 810 820 830 840
STLVMGTAIE KPEKSMSNVL SGVELYLPLA GLLDLEEEIA RLEKEENKLE KEVERVQKKL
850 860 870
SNQGFLAKAP EKVIEEERKK EADYLEKRAA VRARIKELKG