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 A6LGA2

Entry ID Method Resolution Chain Position Source
AF-A6LGA2-F1 Predicted AlphaFoldDB

No variants for A6LGA2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6LGA2

No associated diseases with A6LGA2

4 regional properties for A6LGA2

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 52 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 12 - 144 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 796 - 905 IPR013155
domain Leucyl-tRNA synthetase, editing domain 276 - 437 IPR025709

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
MEYNFREIEK KWHDYWIAEK VYKVEKDTNK PKYYVLDMFP YPSGAGLHVG HPLGYIASDI
70 80 90 100 110 120
YSRFKRLQGF NVLHPMGYDA YGLPAEQYAI QTGQHPEITT KNNIARYREQ LEKIGFCYDW
130 140 150 160 170 180
SREIRTCDPE YYKWTQWAFI RMFNSYYCND EKQARPISEL IQAFETSGTE GLNVACGEEL
190 200 210 220 230 240
SFTAEEWKAK SDKEKQEILL NYRIAYRGET MVNWCAALGT VLANDEVVNG VSERGGYPVE
250 260 270 280 290 300
QKIMRQWCLR VSAYAQRLLD GLDTIDWTDS LKETQKNWIG RSEGAEVRFK VKDSDKEFTI
310 320 330 340 350 360
FTTRADTMFG VTFMVLAPES ELVQQLTTAD QKAEVDAYLD RTKKRTERER IADRQVTGVF
370 380 390 400 410 420
SGSYAINPFT GEAVPIWISD YVLAGYGTGA IMAVPAHDSR DYAFAKHFGL EIRPLVEGCD
430 440 450 460 470 480
VSKESFDAKE GIVCNSPRTG VTPYCDLSLN GLTIKEAIAA TKKYVKDHDL GRVKINYRLR
490 500 510 520 530 540
DAIFSRQRYW GEPFPVYYDA DSMPQMLPEE CLPLLLPEVD KFLPTETGEP PLGHAVKWAW
550 560 570 580 590 600
DTVNQKVTEV SKIDNQTIFP LELCTMPGFA GSSAYYLRYM DPHNDKALVA KDVDEYWRNV
610 620 630 640 650 660
DLYIGGTEHA TGHLIYSRFW NKFLFDLGIV CEEEPFKKLI NQGMIQGRSN FVYRINGTNK
670 680 690 700 710 720
FVSLNLKDQY EVTPIHVDVN IVSNDLLDIE AFKNWRPEYN DAEFVLEDGK YICGWAVEKM
730 740 750 760 770 780
SKSMFNVVNP DMIVEKYGAD TLRLYEMFLG PLEQSKPWDT NGIDGVHRFL KKLWGLFFGN
790 800 810 820 830 840
TDTLQVTDAE PTADELKSLH KLIKKVTFDI EHFSYNTSIS AFMICVNELT SLKCSKRAIL
850 860 870 880 890 900
EPLITLLAPF APHIAEELWH QLGHDTTICD ARWPKHNEEY LKEKSVVYAI SFNGKARYNL
910 920 930 940
ELPADISKED AEKAALNHEN SAKWMEGKTV KKVIVVPGKI VNIVVG