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Protein

Alanine--tRNA ligase, cytoplasmic

Gene

Aars

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.UniRule annotation

Catalytic activityi

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei77ATPBy similarity1
Binding sitei95ATP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei176ATPBy similarity1
Binding sitei216L-alanineBy similarity1
Binding sitei239L-alanineBy similarity1
Binding sitei243ATP; via amide nitrogenBy similarity1
Metal bindingi605ZincUniRule annotation1
Metal bindingi609ZincUniRule annotation1
Metal bindingi723ZincUniRule annotation1
Metal bindingi727ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi214 – 216ATPBy similarity3

GO - Molecular functioni

  • alanine-tRNA ligase activity Source: RGD
  • amino acid binding Source: RGD
  • aminoacyl-tRNA editing activity Source: UniProtKB
  • ATP binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • tRNA binding Source: RGD

GO - Biological processi

Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase, RNA-binding, tRNA-binding
Biological processProtein biosynthesis
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligase, cytoplasmicUniRule annotation (EC:6.1.1.7UniRule annotation)
Alternative name(s):
Alanyl-tRNA synthetaseUniRule annotation
Short name:
AlaRSUniRule annotation
Gene namesi
Name:Aars
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi1304832 Aars

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000752841 – 968Alanine--tRNA ligase, cytoplasmicAdd BLAST968

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineUniRule annotationBy similarity1
Modified residuei3PhosphoserineBy similarity1
Modified residuei19N6-acetyllysineBy similarity1
Modified residuei399PhosphoserineBy similarity1
Modified residuei555PhosphoserineBy similarity1
Modified residuei876N6-acetyllysineBy similarity1

Post-translational modificationi

ISGylated.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP50475
PRIDEiP50475

PTM databases

iPTMnetiP50475
PhosphoSitePlusiP50475

Expressioni

Gene expression databases

BgeeiENSRNOG00000018404
GenevisibleiP50475 RN

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025051

Structurei

3D structure databases

ProteinModelPortaliP50475
SMRiP50475
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.UniRule annotation

Sequence similaritiesi

Belongs to the class-II aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0188 Eukaryota
COG0013 LUCA
GeneTreeiENSGT00390000016019
HOGENOMiHOG000156964
HOVERGENiHBG017874
InParanoidiP50475
KOiK01872
OMAiFEMMAHH
OrthoDBiEOG091G00Z9
PhylomeDBiP50475
TreeFamiTF300737

Family and domain databases

HAMAPiMF_00036_B Ala_tRNA_synth_B, 1 hit
InterProiView protein in InterPro
IPR002318 Ala-tRNA-lgiase_IIc
IPR018162 Ala-tRNA-ligase_IIc_anticod-bd
IPR018165 Ala-tRNA-synth_IIc_core
IPR018164 Ala-tRNA-synth_IIc_N
IPR023033 Ala_tRNA_ligase_euk/bac
IPR003156 DHHA1_dom
IPR018163 Thr/Ala-tRNA-synth_IIc_edit
IPR009000 Transl_B-barrel_sf
IPR012947 tRNA_SAD
PfamiView protein in Pfam
PF02272 DHHA1, 1 hit
PF01411 tRNA-synt_2c, 1 hit
PF07973 tRNA_SAD, 1 hit
PRINTSiPR00980 TRNASYNTHALA
SMARTiView protein in SMART
SM00863 tRNA_SAD, 1 hit
SUPFAMiSSF101353 SSF101353, 1 hit
SSF50447 SSF50447, 1 hit
SSF55186 SSF55186, 1 hit
TIGRFAMsiTIGR00344 alaS, 1 hit
PROSITEiView protein in PROSITE
PS50860 AA_TRNA_LIGASE_II_ALA, 1 hit

Sequencei

Sequence statusi: Complete.

P50475-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSTLTAREI RERFINYFKR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK
60 70 80 90 100
PIFLNTVDPS HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM
110 120 130 140 150
LGSWSFGDYF KELACKMALE LLTQEFGIPV ERLYVTYFGG DEAAGLEPDL
160 170 180 190 200
ECRQIWQNLG LDEAKILPGN MKDNFWEMGD TGPCGPCSEI HYDRIGGRDA
210 220 230 240 250
AHLVNQDDPN VLEIWNLVFI QYNRESDGVL KPLPKKSIDT GMGLERLVSV
260 270 280 290 300
LQNKMSNYDT DLFVPYFEAI QKGTGARPYT GKVGAEDTDG IDMAYRVLAD
310 320 330 340 350
HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYSHEKLN ASRGFFATLV
360 370 380 390 400
DVVVQSLGDA FPELKKDPDM VKDIINEEEV QFLKTLSRGR RILDRKIQSL
410 420 430 440 450
GDCQTIPGDT AWLLYDTYGF PVDLTGLIAE EKGLVVDMDG FEEERKLAQL
460 470 480 490 500
KSQGKGAGGE DLIMLDIYAI EELRAKGLEA TDDSPKYNYH SDSSGSYVFE
510 520 530 540 550
CTVATVLALR REKMFVDEVV TGQECGVVLD KTCFYAEQGG QIFDEGYLVK
560 570 580 590 600
VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GNLRVGDQVR LFIDEPRRRP
610 620 630 640 650
VMSNHTATHI LNFALRSVLG DADQKGSLVA PDRLRFDFTA KGAMSTEQIK
660 670 680 690 700
KTEEIVNGMI EAAKPVYTLD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG
710 720 730 740 750
VPVSELLDDP SGPAGSLTSV EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR
760 770 780 790 800
RIVAVTGAEA QKALRKSETL KKSLSAMEVK VKAQSAPNKD VQKEIADLGE
810 820 830 840 850
VLATAVIPQW QKDEQRETLK SLKKVMDDLD RASKADVQKR VLEKTKQLID
860 870 880 890 900
SNPNQPLVIL EMESGASAKA LNEALKLFKT HSPQTSAMLF TVDNEAGKIT
910 920 930 940 950
CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDMSAQA TGKNVGCLQE
960
ALQLATSFAQ LRLGDVKN
Length:968
Mass (Da):106,790
Last modified:October 13, 2009 - v3
Checksum:i10BF81F46F7AF546
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti459G → E AA sequence (PubMed:2040280).Curated1
Sequence conflicti474 – 476RAK → ARA AA sequence (PubMed:2040280).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473972 Genomic DNA Translation: EDL92558.1
BC098738 mRNA Translation: AAH98738.1
PIRiS16073
RefSeqiNP_001093987.1, NM_001100517.1
XP_006255642.1, XM_006255580.3
XP_006255643.1, XM_006255581.2
XP_006255644.1, XM_006255582.3
XP_006255645.1, XM_006255583.3
UniGeneiRn.8645

Genome annotation databases

EnsembliENSRNOT00000025052; ENSRNOP00000025051; ENSRNOG00000018404
ENSRNOT00000082151; ENSRNOP00000075266; ENSRNOG00000018404
GeneIDi292023
KEGGirno:292023
UCSCiRGD:1304832 rat

Similar proteinsi

Entry informationi

Entry nameiSYAC_RAT
AccessioniPrimary (citable) accession number: P50475
Secondary accession number(s): A6IZ80, Q4G057
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 13, 2009
Last modified: May 23, 2018
This is version 113 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

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