Q8Y722

PR
Gene name
alaS
Protein name
Alanine--tRNA ligase
Names
Alanyl-tRNA synthetase, AlaRS
Species
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
KEGG Pathway
lmo:lmo1504
EC number
6.1.1.7: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

33-105 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8Y722

Entry ID Method Resolution Chain Position Source
AF-Q8Y722-F1 Predicted AlphaFoldDB

No variants for Q8Y722

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8Y722

No associated diseases with Q8Y722

4 regional properties for Q8Y722

Type Name Position InterPro Accession
domain DHHA1 domain 735 - 874 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 655 - 698 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 8 - 556 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 4 - 711 IPR018165

Functions

Description
EC Number 6.1.1.7 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
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

6 GO annotations of molecular function

Name Definition
alanine-tRNA ligase activity Catalysis of the reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
amino acid binding Binding to an amino acid, organic acids containing one or more amino substituents.
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.
tRNA binding Binding to a transfer RNA.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
alanyl-tRNA aminoacylation The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine accetping tRNA.
tRNA modification The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKQLSSAEVR QLFLDFFKEK GHTIEPSAPL VPNNDPTILW INSGVATMKK YFDGSVIPDN
70 80 90 100 110 120
PRMANAQKSI RTNDIENVGK TARHHTFFEM LGNFSIGDYF KEGAIVFAWE FLTSPKWIGF
130 140 150 160 170 180
DPDKLYVTVY PEDEEAKTLW REKIGLSDDH IVEIEDNFWD IGIGPSGPDS EIFYDRGPAF
190 200 210 220 230 240
GDDASDPELY PGGENERYLE IWNLVFSQFN HNPDGTYTPL PKQNIDTGMG LERMVSIIQD
250 260 270 280 290 300
APTNFETDLF MPIIREVEQI AGVKYGHSQE NDVAFKVIAD HIRTVAFAIG DGALPSNEGR
310 320 330 340 350 360
GYILRRLLRR AVRYAKVLTI NEPFMYKLVP VVGKIMNSFY PEVENQTDFI QKVIRTEEER
370 380 390 400 410 420
FHETLNEGLA ILETILKTAK ETNEQVIKGA DIFKLYDTFG FPVELTEEYA EDHGLKVDHA
430 440 450 460 470 480
GFEAEMKEQR ARARAARADV KSMQVQGELL ANLTEKSAFV GYNSTEHVSE ILYLIQNDTL
490 500 510 520 530 540
VDEVAAGNEA QVIFKETPFY AESGGQVADK GTIESETGLA YVEDVQKAPN KQNLHRISVK
550 560 570 580 590 600
EGVLKTGDTV KLAVDKVKRR ETIKNHTATH LLHRALKDTL GEHVNQAGSL VSPDRLRFDF
610 620 630 640 650 660
SHFGQITEEE LTKMEEIVNE KIWEQINVVI EEMPIAEAKE LGAMALFGEK YGDIVRVVQV
670 680 690 700 710 720
GKYSIELCGG VHVRNTADIG LFKIVSETGI GAGTRRIEAV TGKEAYRFVT EQENTLKQAA
730 740 750 760 770 780
SLLKTTTKET PQKVELLQAD LREVKRENES LLSKLASAAS ADIFESPEEI GGVKVIAKQV
790 800 810 820 830 840
NAKDMNQLRQ FVDNWKDKKI GGILVLGAVQ GDKVNLISAV SEEAIKAGYH AGKLLKEVAT
850 860 870
RCGGNGGGRP DMAQAGGKNP AELGTALDYV STWVKEQQA