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 Q9CMK5

Entry ID Method Resolution Chain Position Source
AF-Q9CMK5-F1 Predicted AlphaFoldDB

No variants for Q9CMK5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9CMK5

No associated diseases with Q9CMK5

5 regional properties for Q9CMK5

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 48 - 59 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 20 - 637 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 677 - 826 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 889 - 947 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 636 - 767 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
MTQNFEMADR FTPSAVEQAL YKHWEESGYF KPSEDTSKPS YSIAIPPPNV TGSLHMGHAF
70 80 90 100 110 120
QQTLMDILIR FNRMEGHNTL WQTGTDHAGI ATQMVVERKI AAEEGKTRHD YGREAFIDKI
130 140 150 160 170 180
WDWKAYSGGT ISQQMRRLGN SIDWERERFT MDEGLSDAVK EVFVRLHEEG LIYRGKRLVN
190 200 210 220 230 240
WDPKLHTAIS DLEVENKESK GSLWHFRYPL ANGAKTADGK DYLVVATTRP ETMLGDTAVA
250 260 270 280 290 300
VHPEDERYQS LIGKTVVLPL ANREIPIIAD DYVDREFGTG VVKITPAHDF NDYEVGKRHQ
310 320 330 340 350 360
LPMVNVMTLN ADIRAEAEII GSDGKILESY TALIPTKYQG MERFAARKQI VADFEELGLL
370 380 390 400 410 420
DEIKPHDLKV PYGDRGGVPI EPMLTDQWYV SVKPLAEVAV KAVEDGEIQF VPKQYENLYF
430 440 450 460 470 480
SWMRDIQDWC ISRQLWWGHR IPAWYDEQGN VYVARDEAEV RAKHNLPADL ALKQDEDVLD
490 500 510 520 530 540
TWFSSGLWTF STLGWPKQTP DLKMFHSTDV LITGFDIIFF WVARMIMFTM HFVKDENGKP
550 560 570 580 590 600
QVPFKTVYVT GLIRDEQGQK MSKSKGNVID PLDMIDGIDL ESLLEKRTGN MMQPQLAEKI
610 620 630 640 650 660
AKATIKAFPE GIAEHGTDAL RFTLTALATN GRDINWDMKR LEGYRNFCNK LWNASRFVLT
670 680 690 700 710 720
NDKLDLSEGS VEYSVADRWI QSEFNRTVEA FRNALAQFRF DLCATALYEF TWNQFCDWYL
730 740 750 760 770 780
ELTKPVLVNG SVAQKRGASQ TLINVLEKLL RLTHPVMPFI TEEIWHKVKA FAGVSGDTIM
790 800 810 820 830 840
LQAFPQFEQS ALDYQAEAEI NWMKEVIVAV RNIRAESNIP PSKGLDLLLR NLSEADQNAL
850 860 870 880 890 900
ENNRTLIQAM AKLDAIRVLE AGEDAPLSVA KLVNNAELLV PMAGFINKEA ELARLNKEIE
910 920 930 940 950
KYQGEIQRIE NKLANEAFVA KAPPAVIEKE RAKMAEYAEG LNKLKQQYLA IEAL