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 Q8NKR7

Entry ID Method Resolution Chain Position Source
AF-Q8NKR7-F1 Predicted AlphaFoldDB

No variants for Q8NKR7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8NKR7

No associated diseases with Q8NKR7

3 regional properties for Q8NKR7

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 54 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 12 - 689 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 726 - 858 IPR013155

Functions

Description
EC Number 6.1.1.4 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.
leucine-tRNA ligase activity Catalysis of the reaction: L-leucine + ATP + tRNA(Leu) = AMP + diphosphate + 2 H(+) + Leu-tRNA(Leu).

1 GO annotations of biological process

Name Definition
leucyl-tRNA aminoacylation The process of coupling leucine to leucyl-tRNA, catalyzed by leucyl-tRNA synthetase. The leucyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a leucine-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
MAELNFKAIE EKWQKRWMEA RVFEPDRKAK PKEKKFYITV AFPYLSGHLH VGHARTYTIP
70 80 90 100 110 120
DVIARFKRMQ GYNVLFPMGW HITGAPIVGI AERIKNRDPK TIHIYRDVYK VPEEILWKFE
130 140 150 160 170 180
DPKEIVKYFM KAAKETFIRA GFSVDWTREF HTTSLFPPFS KFIEWQFWTL KDMGLVVKGA
190 200 210 220 230 240
HRVRWDPVVG TPLGDHDIME GEDVQILEYV IIKFILEENG ETIYLPAATL RPETVYGVTN
250 260 270 280 290 300
MWLNPEATYV KAKVRKGDRE ELWIVSKEAA YKLSFQDREI EVIEEFKGEK LIGKYVKNPV
310 320 330 340 350 360
TGDEVIILPA EFVDPDNATG VVMSVPAHAP FDHIALEDLK KETEILLKYD IDPRVVEEIS
370 380 390 400 410 420
YISLISLEGY GEFPAVEEAE RLGVKSQKDK EKLEQATKNI YKAEYHKGIF KIEPYAGKPV
430 440 450 460 470 480
QEVKELVAKE MMEKGIAEIM YEFADKPVIS RFGNQAVIKI IHDQWFIDYG NPEWKAKARE
490 500 510 520 530 540
ALANMTIYPE SRRAQFEAVI DWLDKKACAR KVGLGTPLPW DPDWVIESLS DSTIYMAYYT
550 560 570 580 590 600
ISRHINQLRK EGKLDAEKLD REFFDYIFRE PFSEEKERKL SEKTGIPAET IHEMKEEFEY
610 620 630 640 650 660
WYPLDWRCSA KDLIPNHLTF FIFNHVAIFD KKHWPKGIAV NGFGTLEGQK MSKSKGNVLN
670 680 690 700 710 720
FIDAIEENGA DVVRLYIMGL AEHDSDFDWR RKEVGKLRKQ VERFYELVSE FATYEAKEGV
730 740 750 760 770 780
ELKDIDRWML HRLNKAIEGA TKALEEFRTR TAVQWAFYTV LNDLRWYLRR TEGRDDDAKR
790 800 810 820 830 840
YVLRTLADVW VRLMAPFTPH ISEELWEKLG GEGFVSLAPW PEPVPEWWNE TVEAEEDFVK
850 860 870 880 890 900
SLIEDIKEII TVAKIENPKR AYIYTAPEWK WRVVEVVAEK RDFKAAMAEL MKDPEMRKHG
910 920 930 940 950 960
KEVSKLIQRL IKERAFEVKR IDEEKALREA KDFIEKELGI EIIINPEEDR GGKKKQAMPL
KPAVFVE