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 Q6NFV0

Entry ID Method Resolution Chain Position Source
AF-Q6NFV0-F1 Predicted AlphaFoldDB

No variants for Q6NFV0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6NFV0

No associated diseases with Q6NFV0

5 regional properties for Q6NFV0

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 66 - 77 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 38 - 596 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 643 - 797 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 856 - 919 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 603 - 741 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
MVGSRSASHQ KTVKIVPMTN RADKLPKSWD PQAVEKDLYE GWVEKGYFTA DPSSSKPAFS
70 80 90 100 110 120
IVLPPPNVTG QLHMGHALDH TLMDGIARRK RMQGYEVLWL PGMDHAGIAT QTKVEAMLKE
130 140 150 160 170 180
TEGKSRWDYS REEFIEHVWE WKRKFGGTIG TQMRAIGDSV DWSRERFTLD EGLSRAVQTI
190 200 210 220 230 240
FKQMYDRGMI YQANRLVNWS PILETAVSDI EVVYKDVEGE LVSIRYGSLN DDEPHVIVAT
250 260 270 280 290 300
TRVETMLGDV AVAVHPDDER YADLVGTTLP HPFLPDRQMI VVADDYVDPE FGTGAVKITP
310 320 330 340 350 360
AHDPNDYALG LRHNLDMPNI MDATGHIAGT GTQFDGMDRF EARVKIREAL AEQGRIVKEV
370 380 390 400 410 420
RPYVHSVGHS ERSGEPIEPR LSLQWWVKVE KLATMAGDAI REGDTVIHPK SSEPRYFDWV
430 440 450 460 470 480
DDMHDWCISR QLWWGHRIPI WYGPEDAEGN RDIVCVGPDE QPPAGYEQDP DVLDTWFSSA
490 500 510 520 530 540
LWPFSTMGWP DKTPELDKFY PTSVLVTAYD ILFFWVARMM MFGTLAGETT PEILGQGTDG
550 560 570 580 590 600
RPQIPFNDLF LHGLVRDEQG RKMSKSLGNG IDPMDWVERF GADALRFTLA RGANPGVDLP
610 620 630 640 650 660
VGEDSAQSSR NFATKLFNAT KFALMNGAEV GTLPERSELT DADRWILDRL EEVRVSVDDY
670 680 690 700 710 720
FDRYQFAKGN EALYQFAWGE FCDWYLEIAK VQIPRDMEAA SAQEQARGRN TQIVLGQVLD
730 740 750 760 770 780
ALLRMLHPAM PFVTEVLWKA LTDGESLNVA EWPTAAMTNG GVATDEVAAR RMADVEKLVT
790 800 810 820 830 840
EIRRFRSDQG VKPSQKVPGA VDFAAADLAA QEDLVRSLAR LDQPAEDFAA SASIEVRLSQ
850 860 870 880 890 900
ATIEISVDTS GTVDKEAERK RLDKDLAAAT KELETTAKKL GNESFLAKAP EAVVAKIRER
910
QQIAQEEVAR ISARLEELK