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 Q8Q054

Entry ID Method Resolution Chain Position Source
AF-Q8Q054-F1 Predicted AlphaFoldDB

No variants for Q8Q054

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8Q054

No associated diseases with Q8Q054

4 regional properties for Q8Q054

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 41 - 52 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 13 - 326 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 396 - 671 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 710 - 834 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
MEQDYKPHEI ENKWQKKWNE SRIFQAEPDK REKFFITIPY PYLNGNLHAG HTRTFTIGDV
70 80 90 100 110 120
VARHKRMLGY NVLYPMGFHV TGTPIVGLAE LIASRDPQTM DVYERLHGIP GDILPALDTP
130 140 150 160 170 180
EKIVDYFKVE AEKAMRMIGY SIDWRRKFTT TDPTYKKFIE WQYTRLEEKD LIVKGSHPVK
190 200 210 220 230 240
WCPNDNNPVE DHDILHGEEA TIVEYTLIKF RYRDLVLPCA TLRPETTYGV TNLWVNPNVD
250 260 270 280 290 300
YVKARVEKDG NVEFWVVSRD AFRKLTFTDR TVEYVEDMPA KSIIGIKLTN PVTGDEVISL
310 320 330 340 350 360
PASFVKPENG SGIVMSVPAH APFDYLALRD LYDADLSEYG ITEDLRKIEL ISLIQVPEFG
370 380 390 400 410 420
EFPAKEIVES MGISDQKDPK AEEATKIVYR REFHGGVLKE LTGKYKGYPV SKIKDILTRD
430 440 450 460 470 480
FLASNAGETF YEFSEPVVCR CGTPCVVNMV KGQWFLNYSN PDWKAKVYKC LGQMRVIPTE
490 500 510 520 530 540
YRVEFENKID WLKDKACARR KGLGTRLPFD KEWLIESLGD STIYMSYYII ARFIEKGELA
550 560 570 580 590 600
LEHLTLSFFD YVLLGKGDSA AVSAETGLKP ELIEEIRSHF NYWYPVDLRS SGKDLVPNHL
610 620 630 640 650 660
LFFLFHHVAL FEEEKWPKAL AVNGFVSLEG QKMSKSKGPI LTLESAVSSY GADITRMYIL
670 680 690 700 710 720
STAEQTQDAD WQKAGIDSAR RQVDRFYAFA KDVIESGKRG TLSAELKQID RWMLSRMQNY
730 740 750 760 770 780
IKETNAALDS IQTREAIQNS FFLLINDVRW YQRRGGEALL YYVLDNWVRL MAPFTPHLCE
790 800 810 820 830 840
EVWEAMGHED PVSLAQYPLY NEDLIDNGAE LSEEAVKSTL NDIEEIIRVT KMTPQKVYLY
850 860 870 880 890 900
TAPAWKAEAI RCACGLQVEA PLEVGTLIKT LMAKPELKRF GKEIPKFVQK IVPEFKSGGA
910 920 930 940 950 960
ERYETFAYLG LDEKDLLKES ASFLEKEIGC PVEIQSADSP EYDPQKKSRF AEPLRPAIYI
EEKKEE