CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008297
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alanine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Alanyl-tRNA synthetase; AlaRS 
Gene Name
 Aars 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
19ERFINYFKRNEHTYVacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 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 (By similarity). 
Sequence Annotation
 METAL 605 605 Zinc (Potential).
 METAL 609 609 Zinc (Potential).
 METAL 723 723 Zinc (Potential).
 METAL 727 727 Zinc (Potential).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 19 19 N6-acetyllysine (By similarity).
 MOD_RES 399 399 Phosphoserine (By similarity).
 MOD_RES 555 555 Phosphoserine (By similarity).
 MOD_RES 876 876 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Metal-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding; Ubl conjugation; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 968 AA 
Protein Sequence
MDSTLTAREI RERFINYFKR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK PIFLNTVDPS 60
HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KELACKMALE 120
LLTQEFGIPV ERLYVTYFGG DEAAGLEPDL ECRQIWQNLG LDEAKILPGN MKDNFWEMGD 180
TGPCGPCSEI HYDRIGGRDA AHLVNQDDPN VLEIWNLVFI QYNRESDGVL KPLPKKSIDT 240
GMGLERLVSV LQNKMSNYDT DLFVPYFEAI QKGTGARPYT GKVGAEDTDG IDMAYRVLAD 300
HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYSHEKLN ASRGFFATLV DVVVQSLGDA 360
FPELKKDPDM VKDIINEEEV QFLKTLSRGR RILDRKIQSL GDCQTIPGDT AWLLYDTYGF 420
PVDLTGLIAE EKGLVVDMDG FEEERKLAQL KSQGKGAGGE DLIMLDIYAI EELRAKGLEA 480
TDDSPKYNYH SDSSGSYVFE CTVATVLALR REKMFVDEVV TGQECGVVLD KTCFYAEQGG 540
QIFDEGYLVK VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GNLRVGDQVR LFIDEPRRRP 600
VMSNHTATHI LNFALRSVLG DADQKGSLVA PDRLRFDFTA KGAMSTEQIK KTEEIVNGMI 660
EAAKPVYTLD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG VPVSELLDDP SGPAGSLTSV 720
EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR RIVAVTGAEA QKALRKSETL KKSLSAMEVK 780
VKAQSAPNKD VQKEIADLGE VLATAVIPQW QKDEQRETLK SLKKVMDDLD RASKADVQKR 840
VLEKTKQLID SNPNQPLVIL EMESGASAKA LNEALKLFKT HSPQTSAMLF TVDNEAGKIT 900
CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDMSAQA TGKNVGCLQE ALQLATSFAQ 960
LRLGDVKN 968 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:RGD.
 GO:0004813; F:alanine-tRNA ligase activity; IDA:RGD.
 GO:0016597; F:amino acid binding; IPI:RGD.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:Compara.
 GO:0005524; F:ATP binding; IPI:RGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000049; F:tRNA binding; IPI:RGD.
 GO:0006419; P:alanyl-tRNA aminoacylation; IDA:RGD.
 GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Compara.
 GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Compara.
 GO:0001942; P:hair follicle development; IEA:Compara.
 GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0050885; P:neuromuscular process controlling balance; IEA:Compara.
 GO:0006457; P:protein folding; IEA:Compara.
 GO:0043200; P:response to amino acid stimulus; IEA:Compara.
 GO:0043588; P:skin development; IEA:Compara.
 GO:0006400; P:tRNA modification; IEA:Compara. 
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; Pesterase_DHHA1.
 IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
 IPR012947; tRNA_SAD. 
Pfam
 PF02272; DHHA1
 PF01411; tRNA-synt_2c
 PF07973; tRNA_SAD 
SMART
 SM00863; tRNA_SAD 
PROSITE
 PS50860; AA_TRNA_LIGASE_II_ALA 
PRINTS
 PR00980; TRNASYNTHALA.