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 A1APS3

Entry ID Method Resolution Chain Position Source
AF-A1APS3-F1 Predicted AlphaFoldDB

No variants for A1APS3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1APS3

No associated diseases with A1APS3

5 regional properties for A1APS3

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 53 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 13 - 172 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 420 - 620 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 662 - 785 IPR013155
domain Leucyl-tRNA synthetase, editing domain 221 - 406 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
MEQKYNPAAV EQKWQQQWET GASFAVNEQS DRPKYYLLEM FPYPSGRIHM GHVRNYSIGD
70 80 90 100 110 120
VIGRFKRMRG FNVLHPMGWD AFGMPAENAA IQNKSHPAKW TYENIDYMRG QLKKMGLSYD
130 140 150 160 170 180
WGRELATCDL EYYRWEQKIF LEMFAKGLAY KKTSYVNWCP TCETVLANEQ VEDGACWRCD
190 200 210 220 230 240
SPVQQKELDQ WFFRITQYAE ELLSYTEKLP GWPERVLVMQ KNWIGKSHGC EVDFPLEGGT
250 260 270 280 290 300
GSVRVFTTRP DTLFGATFMS LAPEHPQARE LTTPDRRDEV ERFIEKVRNT DRSKRTADDY
310 320 330 340 350 360
EKEGVFTGSY CINPLTQVRM PIYLANFVLT DYGTGAVMAV PTHDQRDFEF AKKYGLDLKV
370 380 390 400 410 420
VIQPEGTTLD PATMEAAYTE PGIMVNSGTF DGMGSEEAKQ AIADHLQEMG GGTKTVTYRL
430 440 450 460 470 480
RDWGISRQRY WGNPIPVIYC DCCGVVPVPE KDLPVRLPMD VEFTGEGGSP LARLESFINV
490 500 510 520 530 540
PCPTCGKPAR RETDTMDTFV QSSWYFLRYC CPDFHDAPLD RTRVDYWMSV DQYIGGIEHA
550 560 570 580 590 600
VLHLLYARFF TKVLRDLGYV ECSEPFTNLL TQGMVIKDGA KMSKSKGNVV DPNALIERYG
610 620 630 640 650 660
ADTARLFSLF AAPPEKDLDW NDQGVDGSFR FLNRVWKLVN DRLELISGAA PLDVPGLTGE
670 680 690 700 710 720
ERTLRRAVHK TIRKVTEDIE GRFHFNTAIA AVMELLNVLQ SADLSTPQAG AVMKEALESL
730 740 750 760 770 780
VLLLAPFVPH MAEELWQRMG QPGALSTTPW PEYDREAAVD DEVLMVVQVN GKLRSKITVA
790 800 810 820
AGSDEESLKA LALADDKVQP FLQGVQVRKV ICVKGKLVNI VVG