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 Q8G777

Entry ID Method Resolution Chain Position Source
AF-Q8G777-F1 Predicted AlphaFoldDB

No variants for Q8G777

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8G777

No associated diseases with Q8G777

5 regional properties for Q8G777

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 57 - 68 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 28 - 111 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 137 - 634 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 689 - 844 IPR013155
domain Valyl tRNA synthetase, anticodon-binding domain 637 - 787 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
MTEGKSIINA NLTPLPDKVG VDGLEDKWRT VWDEDGTYKF RNTRDRKAVY SIDTPPPTVS
70 80 90 100 110 120
GSLHVGHVFS YTHTDVIARY KRMRGYDVFY PMGWDDNGLP TERRVQNYYG VRVDVSLPYD
130 140 150 160 170 180
PDFKPPFEGT DGKKIDAKDQ VPISRKNFIE LCERLTAQDE KLFEALWRKL GLSIDWSQTY
190 200 210 220 230 240
HTIGQHPQRV AQKAFLRNLA RGEAYQQDAP GLWDVTFQTA VAQAELESRE YPGFYHKVAF
250 260 270 280 290 300
RFEDGTPIYI ETTRPELLAA CTSLIANPND ERYKQYFGQY VYSPLFKVKV PILAHPAAEM
310 320 330 340 350 360
DKGAGIAMCC TFGDVTDVEW WRDLKLPTRP IIQRNGRIVM DTPDWIEDPA GREVFAETAG
370 380 390 400 410 420
KTTFSARKII VDKLRESGDL DGEPTPTKRM TNFYEKGDKP LEIVTSRQWY LKNGGTDAKL
430 440 450 460 470 480
NAELIERGKE LEFHPDFMRV RYENWVHGLN GDWLISRQRF FGVPFPLWYP VNASGEPDYD
490 500 510 520 530 540
HPITPSEDRL PIDPTIDVPE GYDESQRDVP GGFTAEKDIM DTWATSSLTP QIVTHWAEPD
550 560 570 580 590 600
EASKALFAST FPMDLRPQGQ DIIRTWLFST VDRAHLENKC LPWAHATLSG WILDPDHKKM
610 620 630 640 650 660
SKSKGNVVVP NEPIEKFGAD AVRYWAAAAR LGLDATYDIG QMKIGRRLAI KLLNATKFAL
670 680 690 700 710 720
AIGREDENHH VGAAAEAAWN PADVTEPLDR AAMAKLALVV RQATEALESY EHSKALEVIE
730 740 750 760 770 780
SYFWQFCDDY IELVKNRAYG TPDEHGNVPS EKAVKSARTA LGLGLDAFAR LLAPYLPYAT
790 800 810 820 830 840
EEVWSWMHAG SGSVHRAAWP VVDPYVEAAT GASPELLTWA GKAVEQLRKI KSEAKVSMKT
850 860 870 880 890 900
PILSVALSAA SEGVEAIHAA LGDIAQAGRV VGKFDLVAKH AEESAAEGTP ETEVAVEASE
910
LGEPPAKKPK H