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 Q8NN37

Entry ID Method Resolution Chain Position Source
AF-Q8NN37-F1 Predicted AlphaFoldDB

No variants for Q8NN37

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8NN37

No associated diseases with Q8NN37

5 regional properties for Q8NN37

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 61 - 72 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 33 - 586 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 633 - 782 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 838 - 902 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 593 - 725 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
MVCVTDQNNE TTSQNRADKL PKSWDPKAVE ADLYQGWVDA GYFTADPASD KPGFSIVLPP
70 80 90 100 110 120
PNVTGQLHMG HALDHTLMDA LARRKRMQGF EVLWLPGMDH AGIATQTKVE EMLKETEGKT
130 140 150 160 170 180
RYDYDREEFI AKVWEWKQEY GGKIGEQMRA IGDSVDWSRE RFTLDDGLSR AVQTIFKKLF
190 200 210 220 230 240
DAGLIYQANR LVNWSPVLET AVSDIEVIYK DVEGELVSIR YGSLNDDEPH VIVATTRVET
250 260 270 280 290 300
MLGDVAVAVH PDDERYKDLV GQTLPHPFRD DLSLKVVADD YVDPEFGSGA VKITPAHDPN
310 320 330 340 350 360
DYALGLRHNL DMPTIMDKTG RIADTGTQFD GLTREEARIK VREELAAQGR IVKEIRPYVH
370 380 390 400 410 420
SVGHSERSGE AIEPRLSLQW FVKVEELAKM SGDAVREGDT TIHPKSLEPR YFDWVDNMHD
430 440 450 460 470 480
WTISRQLWWG HRIPIWYGPN DEIICVGPDE QAPEGYVQDP DVLDTWFSSA LWPFSTMGWP
490 500 510 520 530 540
EKTPELEKFY PTSVLVTAYD ILFFWVARMM MFGTFAAKET PELLGEGKDG RPQVPFTDLF
550 560 570 580 590 600
LHGLVRDEHG RKMSKSLGNG IDPMDWVENY GADALRFTLA RGANPGVDLP VGEDSAQSSR
610 620 630 640 650 660
NFATKLFNAT KFALMNGAVS EGLPAREELT DADRWIVDLL EQVRLDVDAY LDNYQFAKAN
670 680 690 700 710 720
EELYHFAWNE FCDWYLEIAK VQIPREGTSA QGENTQKVLG HVLDALLRLL HPAMPFVTEV
730 740 750 760 770 780
LWQALTDRTS IVVASWPTAA DTNGGVAVDA DAARRIGDVE KLVTEVRRFR ADQGVKPSQK
790 800 810 820 830 840
VPARLDFVAC DLQDLEDSVR SLVRIEQPED DFAASASLEI RLSQATITVE LDTSGTVDVA
850 860 870 880 890 900
AERKRLEKDL ANAQKELETT AKKLGNEAFL SKAPDAVVDK IRGRAQIAQE EVERINKRLE
ELA