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Protein

Alanine--tRNA ligase, cytoplasmic

Gene

Aars

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi605 – 6051ZincUniRule annotation
Metal bindingi609 – 6091ZincUniRule annotation
Metal bindingi723 – 7231ZincUniRule annotation
Metal bindingi727 – 7271ZincUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi1304832. Aars.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: RGD
  • extracellular exosome Source: Ensembl
  • membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 968968Alanine--tRNA ligase, cytoplasmicPRO_0000075284Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineUniRule annotationBy similarity
Modified residuei19 – 191N6-acetyllysineBy similarity
Modified residuei399 – 3991PhosphoserineBy similarity
Modified residuei555 – 5551PhosphoserineBy similarity
Modified residuei876 – 8761N6-acetyllysineBy similarity

Post-translational modificationi

ISGylated.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP50475.
PRIDEiP50475.

PTM databases

iPTMnetiP50475.

Expressioni

Gene expression databases

GenevisibleiP50475. RN.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025051.

Structurei

3D structure databases

ProteinModelPortaliP50475.
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.
OMAiFDFNCPR.
OrthoDBiEOG7M3HZH.
PhylomeDBiP50475.
TreeFamiTF300737.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. 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.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti459 – 4591G → E AA sequence (PubMed:2040280).Curated
Sequence conflicti474 – 4763RAK → ARA AA sequence (PubMed:2040280).Curated

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_006255580.2.
XP_006255643.1. XM_006255581.2.
XP_006255644.1. XM_006255582.2.
XP_006255645.1. XM_006255583.2.
UniGeneiRn.8645.

Genome annotation databases

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

Cross-referencesi

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_006255580.2.
XP_006255643.1. XM_006255581.2.
XP_006255644.1. XM_006255582.2.
XP_006255645.1. XM_006255583.2.
UniGeneiRn.8645.

3D structure databases

ProteinModelPortaliP50475.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025051.

PTM databases

iPTMnetiP50475.

Proteomic databases

PaxDbiP50475.
PRIDEiP50475.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi16.
RGDi1304832. Aars.

Phylogenomic databases

eggNOGiKOG0188. Eukaryota.
COG0013. LUCA.
GeneTreeiENSGT00390000016019.
HOGENOMiHOG000156964.
HOVERGENiHBG017874.
InParanoidiP50475.
KOiK01872.
OMAiFDFNCPR.
OrthoDBiEOG7M3HZH.
PhylomeDBiP50475.
TreeFamiTF300737.

Miscellaneous databases

NextBioi633629.
PROiP50475.

Gene expression databases

GenevisibleiP50475. RN.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. 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.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Alanyl-tRNA synthetase from Escherichia coli, Bombyx mori and Ratus ratus. Existence of common structural features."
    Dignam J.D., Dignam S.S., Brumley L.L.
    Eur. J. Biochem. 198:201-210(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 456-476.
    Tissue: Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 600-968.
    Tissue: Thymus.
  4. Maurya D.K., Bhargava P.
    Submitted (JAN-2009) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSYAC_RAT
AccessioniPrimary (citable) accession number: P50475
Secondary accession number(s): A6IZ80, Q4G057
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 13, 2009
Last modified: May 11, 2016
This is version 100 of the entry and version 3 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.