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 Q7M8H7

Entry ID Method Resolution Chain Position Source
AF-Q7M8H7-F1 Predicted AlphaFoldDB

No variants for Q7M8H7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7M8H7

No associated diseases with Q7M8H7

5 regional properties for Q7M8H7

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 69 - 80 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 37 - 594 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 636 - 769 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 828 - 892 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 593 - 717 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
MKSIQTPSKS HTNTKETPVM SQEETKGYNP REIEESYYKI WETRGYFEVE GNAQIQKPNQ
70 80 90 100 110 120
NFAVMLPPPN VTGSLHIGHA LNHTLIDIMT RYKRMDGYKT LWQPGTDHAG IATQNVVEKR
130 140 150 160 170 180
LLSKGIKKEE LGREAFLEKV WEWREESGGT ILSQMRKLGT SPAWSRTRFT MDEGLKNSVA
190 200 210 220 230 240
RAFVKLYEEG YIIRGNYMVN WCTHDGALSD IEVEYDANKG KLYHLRYFFK DSSDYIVVAT
250 260 270 280 290 300
TRPETFFGDT AVMVHPEDER YAHLIGQTLV LPLIGREIQI IADSYVDREF GTGMVKVTPA
310 320 330 340 350 360
HDPNDYEVGK RHDLEFITVF DKEGYLNHHA GEFEGLERLE AREAIVAKLQ EKGYIEKIEE
370 380 390 400 410 420
HENQVGKCYR CGNVVEPYIS KQWFVKKEVA QKAIERINSG EAAFYPAQWK NNYNAWMKEL
430 440 450 460 470 480
RDWCISRQLW WGHQIPVYYC DCGHEWASET TPSHCPKCQG SQFHQDPDVL DTWFSSALWP
490 500 510 520 530 540
FSTLGWGNGE AGKGSWWREE DLQEFYPNSL LITGFDILFF WVARMLMMGE HFLDNLPFKD
550 560 570 580 590 600
IYLHALVRDE KGQKMSKSKG NVIDPLELIE KYGCDSTRFT LAILCAQGRD VRLSSQQLEI
610 620 630 640 650 660
SKNFTNKLYN AANFLLLNAS SFKTLDEITP QTPLGRYMAS RFSLCVEELR GALDGYRFND
670 680 690 700 710 720
GATVLYRFLW GEFCDWGIEL SKANKEAINE LGAIFREAMK LLHPYMPFIS EHLYQKLGGA
730 740 750 760 770 780
RLEESTSIMI LPYPKANWRE EKIEMTFEVI MDAIISTRRL KATLELANQK IPVVFIKAPQ
790 800 810 820 830 840
GMDESLINTF IPRLAKVDSI ELLSEKPAAC VVDVGEKCEI YLSTAQLDLS PIISRLEKQQ
850 860 870 880 890
EKLQKEVDKL LGMLNNEKFV ANAPQNVLEQ NRVALKEAQT KLDKVKVELQ GIKG