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 Q8EPN2

Entry ID Method Resolution Chain Position Source
AF-Q8EPN2-F1 Predicted AlphaFoldDB

No variants for Q8EPN2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8EPN2

No associated diseases with Q8EPN2

5 regional properties for Q8EPN2

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 52 - 63 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 24 - 568 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 612 - 757 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 818 - 883 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 568 - 703 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
MEQDKENKQS LPSKYNPKEV EEGRYQFWLD GKFFEATGDP DKEPYSIVIP PPNVTGRLHL
70 80 90 100 110 120
GHAWDTSMQD TITRMKRMQG YDVLWLPGMD HAGIATQAKV EARLKESGTN RYELGREKFL
130 140 150 160 170 180
EKAWEWKEEY AAFIRSQWEK LGLGLDYSRE RFTLDEGLSD AVREVFVKLY EKGLIYRGEY
190 200 210 220 230 240
IINWDPSTKT ALSDIEVIYE EIQGKFYHMR YPIKGSDETI EIATTRPETM LGDTAVAVHP
250 260 270 280 290 300
KDERYQHLIG KTVILPIVGR EIEIVADDYV DMELGSGAVK ITPAHDPNDF EIGNRHQLER
310 320 330 340 350 360
ILVMNEDGSM NENAGKYQGL DRFECRKQIV KDLKEQGVMF NIEERTHQVG HSERSGAVVE
370 380 390 400 410 420
PYLSTQWFVK MDPLAKSALD MQADADEKVN FVPDRFERTY FNWMDNIRDW CISRQLWWGH
430 440 450 460 470 480
RIPAWYHKET KEIYVGKEAP ADIENWEQDE DVLDTWFSSA LWPFSTMGWP NEDSADLKRY
490 500 510 520 530 540
FPTNVLVTGY DIIFFWVSRM IFQSKEFMNE KPFEDTLLHG LIRDADGRKM SKSLGNGVDP
550 560 570 580 590 600
MDVIEKYGAD SLRYFLMTGS TPGQDLRFHW EKVESTWNFA NKVWNASRFS IMNMEGFTYE
610 620 630 640 650 660
DIDLTGELSL PDRWILARLN ETIEQVTRNS NKYEFGEAGR HLYNFIWDEF CDWYIEMAKL
670 680 690 700 710 720
SLYGEDENKK KTTRSVLAHV LDQTMRMLHP FMPFITEEIW QQLPHEGPSI TVSKWPEVNS
730 740 750 760 770 780
EFDNPQAVQE MQRLVSIIRS VRNSRAEVDT PMSKQIKMLI KTENEQLTAE LEKNRDYLER
790 800 810 820 830 840
FCNPSELSIS TVIEAPDKAM TSVVTGAEIF LPLEGLIDFD KEIKRLENEL AKWTKEVERV
850 860 870 880
QKKLSNQGFV SKAPESVVEE EKRKEKDYLD KQAKVKTRLS ELK