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 P28350

Entry ID Method Resolution Chain Position Source
AF-P28350-F1 Predicted AlphaFoldDB

No variants for P28350

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P28350

No associated diseases with P28350

2 regional properties for P28350

Type Name Position InterPro Accession
conserved_site ArgE/DapE/ACY1/CPG2/YscS, conserved site 100 - 137 IPR001261
domain Peptidase M20, dimerisation domain 177 - 283 IPR011650

Functions

Description
EC Number 6.1.1.9 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Mitochondrion
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

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
MPLSLWRLAI GSSRRHSLLK ITSTRVLPVP RPYSTYSNNK KVIMPGEDQP AAAPAAAPAA
70 80 90 100 110 120
QDAPGAPAPK KNDKKEKAKA DKAAKFAAKQ AAAKAKQPAA QSAPKEKKEK TPALPPYEDS
130 140 150 160 170 180
TPAGEKKVIQ SFEHPHFSAY NPSAVEAAWY QWWEKAGYFK PESCRKPSAG KFVIPLPPPN
190 200 210 220 230 240
VTGALHCGHA LANSLQDTLI RWYRMKGYET LWVPGCDHAG ISTQSVVEKM LWKKEKKIRQ
250 260 270 280 290 300
ELGREKFTDL VWEWKGEYHQ RINNAQKLMG GSMDWSREAF TMDKNLTAAT METFCRLHDE
310 320 330 340 350 360
GLIYRSNRLV NWCTHLNTAL SGLEVETKEI TGRTLLDVPG YDKKVEFGVL THFKYQIDGS
370 380 390 400 410 420
EETIEVATTR PETMLGDTGI AVNPEDPRYT HLVGKFARHP FVDRLLPIVT DNYVDKEFGT
430 440 450 460 470 480
GAVKLTPAHD FNDYQLGQRH NLEFINILNE NGTLNDNAGP FKGQKRFDAR YTVVEELTKL
490 500 510 520 530 540
GLFVKKEPNP MKIPLCEKSK DVIEPMMTEQ WWVRMKEMGE AALQVVEEGK VKISPESATK
550 560 570 580 590 600
SYKRWLADIQ DWCISRQLWW GHRIPAYRVI FEGEEGQREN EKSEWVVGRT QEEAQAKAEA
610 620 630 640 650 660
KFAGRKFTLE QDPDCLDTWF SSGLWPMAIL GWPNTENLDF KKFFPTSMLE TGWDILFFWV
670 680 690 700 710 720
SRMIMLSLKM TGEVPFTEVY CHSLIRDSEG RKMSKSLGNV IDPLDIIRGI ELEDLHAKLL
730 740 750 760 770 780
VGNLKEEEVA RATKYQKTAF PGGIPECGAD AMRFTLLSYT TGGGDINFDI RVMHAYRRFC
790 800 810 820 830 840
NKIWQASKYV LGKLPQDFMP KGELDTANFS VPEKWILHRM NVAVKGMNEA LEAREFSRAT
850 860 870 880 890 900
KVAYQFFYDE LCDVFIENSK GILSDGTPEE QQSVQQTLYH ALDVALRLLH PIMPYITEEL
910 920 930 940 950 960
WQRLPRKQGD GETIMLAPYP AFESQLEFAT EAEDYELGLK CAGGIRSLAA DYNIKSDGRA
970 980 990 1000 1010 1020
FIKATTADSL ATVSAQLAAI RTLCGKGVKE VNVLGADEEL PRGCAVYVIN AEITVLLQVG
1030 1040 1050 1060 1070 1080
GSISDIDAEI KKITTKLQKT DLTIKKQQEL LSKDGFEKVS EAVQESEKQK LADAQAAKEN
1090
YQRTLEEFSK LKI