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 Q6LZD2

Entry ID Method Resolution Chain Position Source
AF-Q6LZD2-F1 Predicted AlphaFoldDB

No variants for Q6LZD2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6LZD2

No associated diseases with Q6LZD2

4 regional properties for Q6LZD2

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 51 - 62 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 23 - 525 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 722 - 848 IPR013155
domain Methionyl/Leucyl tRNA synthetase 607 - 691 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
MDQKEVIGET GHKSVDLIKI MDKWQKKWTE AKIFEAEHDS RDKFFITAAF PYLNGVLHAG
70 80 90 100 110 120
HLRTFTIPET IARYQRMKNK NVLWTFGFHV TGTPILGLAN QIKERKEDII WAYNNLHNIP
130 140 150 160 170 180
MDELLKLNTP EAIVECFSKK ATEAFKRMGF SLDWRRNFKT DDKVFSKFIE WQFYKLKEMG
190 200 210 220 230 240
HITKGSHPVR YCPKCENPVE DHDLLHGEES TTVEYSLIKF TSKFDGKEII MPMATLRPET
250 260 270 280 290 300
VFGVTNAWVN PNEIYVMAEV HDEIQKLDSE DVDLKYNGIW IIGKECADKL KEQDRKIEIL
310 320 330 340 350 360
KEIKGSELLG LKIKNPVTKK EVPLLPADFV EMGIGTGCVM SVPAHAPYDY VALRDLGKVE
370 380 390 400 410 420
EVGLIPLIEI EGYDKYPAKE IVEKLGIKDQ NDEELLEQAT SKIYKDEFHK GKLNENCGEY
430 440 450 460 470 480
TGISVKDIKE KLTKDYINSN IAEIMYEFSE QKVVCRCGEK CIIKTVKGQW FINYSDENWK
490 500 510 520 530 540
KLAHECIDNM NFAPEGIRQE FHNKVDWMKD KACARKRGLG TILPFDENWI IESLSDSTIY
550 560 570 580 590 600
MAYYTIARFI NEGLTPEQLI PELFDYVYLG NGNAEEIAKN SKIQAETIEE MRKEFLYYYP
610 620 630 640 650 660
LDWRCSAKDL IPNHLTFMIF NHVALFGREH WPRGIEINGY VTIEGKKLSK SKGPVLPVSE
670 680 690 700 710 720
VAENFGADVA RFYITTCAEL PQDADVKFKE MEKARDNLIK LYDLAVSVME EESAEKELSL
730 740 750 760 770 780
IDKWLLHKTY SSINSAETAY EEFQLRKIGL MFYELINDLR WYKRRGGENN SVLKEVVEIW
790 800 810 820 830 840
TKLLSPVTPH LCEEIWEKLG YAGFISQEMY PVSKPELINE DLELGEEFIK SAMEDIRNIK
850 860 870 880 890 900
GVAKINPEKM YLYTADDWKY DLLEFMNENA EKNVKALIPM VMKEDKFKRH GKEVMKLINE
910 920 930 940 950
IMKIGVKKAI AEVEILENAK TFIESEFDCK VIVNGEDVKG KKKFAIPYKP AIYME