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 Q8KC74

Entry ID Method Resolution Chain Position Source
AF-Q8KC74-F1 Predicted AlphaFoldDB

No variants for Q8KC74

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8KC74

No associated diseases with Q8KC74

5 regional properties for Q8KC74

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 55 - 66 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 25 - 573 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 630 - 779 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 837 - 900 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 575 - 721 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
MSDHSAQNLE KTYNHHEVEE RWRSAHWEAI GTFHAEHSRV LKEGATPYTV LMPPPNVTGS
70 80 90 100 110 120
LTLGHVLNHT LQDIFIRYAR MMGKEALWLP GTDHAGIATQ TVVEKKLRKE GVTRHDLGRR
130 140 150 160 170 180
DFLDKVWEWR EEYGGLILRQ LRKLGISCDW RRNLFTMDER ASEAVINTFV ALYREGLIYR
190 200 210 220 230 240
GRRIINWCPV SQTALSDEEV IMKSRRDKLV YISYPLAKDP TRSITIATVR PETILADVAI
250 260 270 280 290 300
AVNPNDERYA DLIGELVIVP IAGRHVPVIA DDYVDIEFGT GALKITPAHD PNDYEVAKRH
310 320 330 340 350 360
NLPVFSVIGK DARMTDECGY AGMDRFDARD KIVADLAELG YLVKLEEYEH NVGYSERADV
370 380 390 400 410 420
VVEPYLSEQW FVKMQPLAEP ALKVVNDGEI RFHPEHWINT YRHWMENIQD WCISRQLWWG
430 440 450 460 470 480
HRIPAWYDDK GNVWVASSYE EACHLAGTDK LSQDEDVLDT WFSSWLWPLT TLGWTGPHSD
490 500 510 520 530 540
NDDLRAFYPT DTLVTGPDII FFWVARMIMA GLHFKGDVPF RDVYFTSIIR DMKGRKLSKS
550 560 570 580 590 600
LGNSPDPLKV IDTYGTDALR FTIVYIAPLG QDVLFGEEKC ELGRNFATKI WNASRFVFMQ
610 620 630 640 650 660
REKLFATREE FVEAFANFTP QRELMSSAGR WLMSRYNAML ERYHQAMANF KVNDMVKIVH
670 680 690 700 710 720
EFFWGDYCDW YVEALKSELT GDITEERGRH AVCLAVSVLE GVLKALHPVM PFITDEIWHA
730 740 750 760 770 780
IAPRSAEETI ATEAMPQPDA SWRGEDAAAF DLVRNMVSEI RSLRSAFNVP HDLRAQAVIR
790 800 810 820 830 840
ASSPAALVAL QTGRAIFPAM TKCEVELGES VERPAHSAAS VVDGNELFIK LEGLISFEKE
850 860 870 880 890 900
KQRLEKEITK VTAYIESLEK KLSNEKFVSN APADVVAKEK EKLEESRSMV LKLQGNLEVL
S