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 A5V592

Entry ID Method Resolution Chain Position Source
AF-A5V592-F1 Predicted AlphaFoldDB

No variants for A5V592

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5V592

No associated diseases with A5V592

5 regional properties for A5V592

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 54 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 16 - 585 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 627 - 773 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 831 - 896 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 584 - 719 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
MTIDKTFDPA AIEARWYAHW EDNGLFRPER PEAEPYTIVI PPPNVTGSLH IGHALDDTLQ
70 80 90 100 110 120
DVLIRHARLK GKDALWVVGT DHAGIATQMV VERQLDAKGQ KRTDFTREQF IAKVWEWKEE
130 140 150 160 170 180
SGGTITRQLR RLGASCDWAN ERFTMDEGFS KAVLKVFVDL YNQGLLYRDK RLVNWDPGLK
190 200 210 220 230 240
TAISDLEVET KEVQGSFWHF SYPLADGSGA ISVATTRPET MLADMAVAVN PEDGRYRALI
250 260 270 280 290 300
GKSVKLPITG RLIPIVADEH ADPELGSGAV KITPGHDFND FEVGKRAGFK PADMLNMLDA
310 320 330 340 350 360
EAKVVQTADG LIPADYLGLD RFEARRKVVA AIEAEGRLEK VEDRVIQTPY GDRSNAVIEP
370 380 390 400 410 420
WLTDQWYVDA ETLAKPAIEA VRSGAIRVVP ESWTKTYYNW LDNIQPWCVS RQLWWGHQIP
430 440 450 460 470 480
AWYDADGQVY VAEDEAAASA LAGGKALTRD SDVLDTWFSS ALWPFGTIGW PDQAGQQPPE
490 500 510 520 530 540
AYQAGAAGKA SKLQRHYPND VLISGFDILF FWDARMIMQG LHFMGEVPFR TLYLHGLVRA
550 560 570 580 590 600
ADGSKMSKSK GNTVDPLGLI DKYGADALRF TLTAMESQGR DIKLDEKRVE GYRNFATKLW
610 620 630 640 650 660
NAARFAQGNG IGASTTIEPP AAELAVNRWI IAETVRTVQA LDLAIADLRY DESANTIYQF
670 680 690 700 710 720
VWASFCDWYL ELIKPVLAEG ADQGQAAETR AVAGWVLDQI LVMLHPFMPF ITEELWHALG
730 740 750 760 770 780
RRDYDIIVAK WPMADARAID PAAQQEIDWL IRMVGEVRAA RTGLNVPPGA RLPAYARGAS
790 800 810 820 830 840
EETRRRLAAN AVAIARMARI DLAEGEAPAG GAAQVVVDEA TYVLPLEGVI DLDAERARLA
850 860 870 880 890
KGIAAAEKER DGLAARLGNP AFVEKAKPEA VEKARADHAE KSLEAEQLGA ALARLG