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 A8A8T2

Entry ID Method Resolution Chain Position Source
AF-A8A8T2-F1 Predicted AlphaFoldDB

No variants for A8A8T2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8A8T2

No associated diseases with A8A8T2

3 regional properties for A8A8T2

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class Ia 178 - 735 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 773 - 910 IPR013155
domain Methionyl/Leucyl tRNA synthetase 41 - 115 IPR015413

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
MGDFVEDFVR YLKEIAAKWR EEWERARLHE ADVDPNRPKF YVTAAFPYPN SPMHLGHSRT
70 80 90 100 110 120
YSVTDAYARF KRMRGFNVLF PMGFHYTGTP IIAMSEKVKQ GLQALRSLGE VKTILEEIWK
130 140 150 160 170 180
IKVERNLSIG EAIKEYLRGA GREDLMDKTD SIEYLVLFYK VFEIPVEDLE KLTEPLSMAN
190 200 210 220 230 240
YFASITEEGM KELGYMIDWR RKFTTVDPDF QKFITWQFLK LYDLGYVEKG THPVAWDPVY
250 260 270 280 290 300
DTPVSQHDTK GDVEPEIEEY DVILFKLKDE DLYLPAATLR AETVFGVTNV WLNPEAEYEV
310 320 330 340 350 360
VEVDGKRWVL SKKAAYKIKF QKDEVKSLGP IDPKKLLKKM VINPATEEEV PVLPARFVDP
370 380 390 400 410 420
NVATGVVMSV PAHAPFDYVA LKELEGDPEY SDIVKSIELV QVIRVPEEGL LVPQLVEKLG
430 440 450 460 470 480
IRDTSDKKKL EEATREVYSK EYRKGRMLES VLERVKGDER LRAALKAFLG NDPVPDAREK
490 500 510 520 530 540
TAKWLKLFGA GDVFYEIKNA PVYSRFGNEV VVKVLKDQWF LNYGDPQWKE LARKALARMR
550 560 570 580 590 600
IIPENFLKEF EDTIDWLQKR ACARTRGLGT PLPWDKRWII ESLSDSTIYM AFYTVVNILR
610 620 630 640 650 660
GASVEPEKLQ PEVWDYIMLG KGNPKELEEK YGISAAVLEE ARRSFDYWYP VDSRHSGKDL
670 680 690 700 710 720
IRNHLTFFIF NHAAIFPEDK WPRQIVVNGF VNLEGKKMSK SLGNIIPITV AIRSFAPDII
730 740 750 760 770 780
RLVLLHSAEL GSDADFRTEM VSRAISNLRE IKSIVEKVKD YNGPRPANLT MLDAWYLSSF
790 800 810 820 830 840
VKDVENVTNM MEDLKIREVT NVLYFILLNR TKEYLNALEA MGRGLDEVAK WVLRYTVERW
850 860 870 880 890 900
VKMMTPFTPF FAEEMWHELG FNTFVVTEPW PVKDEELVNP LAEAAKEYVE KVIEDIKEII
910 920 930 940 950 960
KVAKIEKPKK VRIEVASPEQ VKMLKMAVEF VNSGKSLREF MAEATKVFGK KEAKSLRQAF
970 980 990 1000 1010 1020
ERATSLSESM RSVIARGEFD EKAVLEEFKR LIEEEVGSEV EIRRYEGGKK RPEPLRPAIY
VE