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 Q887M3

Entry ID Method Resolution Chain Position Source
AF-Q887M3-F1 Predicted AlphaFoldDB

No variants for Q887M3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q887M3

No associated diseases with Q887M3

5 regional properties for Q887M3

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 66 - 77 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 38 - 596 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 643 - 797 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 856 - 919 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 603 - 741 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
MDKTYQPHAI ETSWYQTWES ENYFAPQGAG DSYTIMIPPP NVTGSLHMGH GFNNAIMDAL
70 80 90 100 110 120
IRFRRMQGRN TLWQPGTDHA GIATQMLVER RLEAQGVSRH ELGREKFLDK IWEWKAESGG
130 140 150 160 170 180
NISRQIRRLG SSVDWSRERF TMDDGLSDAV KEAFVRLHED GLIYRGKRLV NWDTKLHTAI
190 200 210 220 230 240
SDLEVENHDE KGHLWNLRYP LADGAKTAEG LDYLIVATTR PETMLGDAAV AVNPQDERYK
250 260 270 280 290 300
ALIGKFVELP LVGRRIPIIA DDYCDPEFGT GCVKITPAHD FNDYEVGKRH NLPLLNIFDK
310 320 330 340 350 360
NANVLPAAQV FNLDGKLNES VDGTLPAAYA GLDRFEARKQ IVAAFDAAGL LVSIDDHALK
370 380 390 400 410 420
VPKGDRSGTI IEPWLTDQWY VSTKPLAEPA IAAVEDGRIA FVPKQYENMY FSWMRDIQDW
430 440 450 460 470 480
CISRQLWWGH RIPAWYDESG KVYVGRDEAE VRAKNNLGPE IALQQDNDVL DTWFSSGLWT
490 500 510 520 530 540
FSTLGWPEKT KALETFHSTD VLVTGFDIIF FWVARMIMLT LHLVKNEDGT PQVPFKTVYV
550 560 570 580 590 600
HGLVRDGQGQ KMSKSKGNVL DPLDIVDGID LETLVEKRTS GLMQPQLAKK IEKQTRQEFA
610 620 630 640 650 660
DGIASYGTDA LRFTFCSLAS TGRDIKFDMG RVEGYRNFCN KIWNAARYVL DKGEDCGQNG
670 680 690 700 710 720
EAVELSLADR WIISQLQRTE AEVTRQLDQF RFDLAAQALY EFIWNQYCDW YLELSKPVLW
730 740 750 760 770 780
DETASIERQR GTRRTLVRVL EVALRLAHPF MPFITEEIWQ RLAPLAGVEG KTIMLQPWPV
790 800 810 820 830 840
ANEARIDQAA EDDIEWLKGL MLAVRNIRGE MNIGPGKPLQ LFLKNVSADD QRRLSENDYL
850 860 870 880 890 900
LRKLAKLESM TVLTDGAEAP LSATALVGDM EVLVPMAGLI DKGAELARLD KEIQRLQGEV
910 920 930 940
QRVGGKLSNA AFVDKAPPDV IAKERAKLTE AEQALGKLAE QHARIASL