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 Q87LG6

Entry ID Method Resolution Chain Position Source
AF-Q87LG6-F1 Predicted AlphaFoldDB

No variants for Q87LG6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q87LG6

No associated diseases with Q87LG6

1 regional properties for Q87LG6

Type Name Position InterPro Accession
domain Histone H2A/H2B/H3 1 - 132 IPR007125

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
MEKTYNPTSI EQALYQTWEE KGYFKPHGDT TKESYSIMIP PPNVTGSLHM GHAFQDTIMD
70 80 90 100 110 120
TLIRCERMKG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TKHDYGRDAF IDKIWEWKGE
130 140 150 160 170 180
SGGTITKQLR RLGASVDWDR ERFTMDDGLS NAVQEVFVRL YEDDLIYRGK RLVNWDPKLH
190 200 210 220 230 240
TAISDLEVEN KDTKGHMWHF RYPLADGVKT ADGKDYIVVA TTRPETMLGD TGVAVNPEDP
250 260 270 280 290 300
RYKDLIGKEI ILPIVDRRIP IVGDEHADME KGTGCVKITP AHDFNDYEVG KRHQLPMINI
310 320 330 340 350 360
LTFDANIRGA AEVFNTNGEP SDAYSTELPA KYHGMERFAA RKAIVAEFDE LGLLEEVKDH
370 380 390 400 410 420
DLQVPYGDRG GVVIEPMLTD QWYVRTAPLA KTAVEAVENG DIQFVPKQYE NMYFSWMRDV
430 440 450 460 470 480
QDWCISRQLW WGHRIPAWYD NQGNVYVGRT EEEVRKNNNL ESVIELHQDE DVLDTWFSSA
490 500 510 520 530 540
LWTFGTQGWP EQTDDLKVFH PSDVLVTGFD IIFFWVARMI MMTMHFVKDE NGKPQVPFKT
550 560 570 580 590 600
VYVTGLIRDE NGDKMSKSKG NVLDPIDMID GIDLESLVEK RTGNMMQPQL AKKIEKNTRK
610 620 630 640 650 660
TFENGIEAYG TDALRFTLAA MASTGRDINW DMKRLEGYRN FCNKLWNASR YVMMNTEEQD
670 680 690 700 710 720
CGFNGGEIEY SLADKWIESQ FELAAKAFNN HIDNFRLDMA SNTLYEFIWN QFCDWYLELT
730 740 750 760 770 780
KPVLWKGTEA QQRGTRRTLI TVLEKTLRLA HPVIPYITET IWQSIKPLVE GVEGETIMLQ
790 800 810 820 830 840
ALPQFDEANF NQEALDDIEW VKAFITSIRN LRAEYDINPG KPLDVMLKAA NAEDAARLEA
850 860 870 880 890 900
NKQVLMSLAK LESVRVLAAD EETPACATAL VAKSELMIPM AGLIDKDAEL ARLDGEIKKT
910 920 930 940 950
HGEIKRIEGK LGNEGFVAKA PEAVVAKERE KLEGYKETLA KLEEQKKTIA AL