CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023398
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alanine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Alanyl-tRNA synthetase; AlaRS 
Gene Name
 Aats-ala 
Gene Synonyms/Alias
 alaS; CG13391 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
7*MKLLTAKEVRNAYLacetylation[1]
487TNDTFKYKYEAVSDEacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702
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 604 604 Zinc (Potential).
 METAL 608 608 Zinc (Potential).
 METAL 723 723 Zinc (Potential).
 METAL 727 727 Zinc (Potential).  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 966 AA 
Protein Sequence
MKLLTAKEVR NAYLDFFKEQ KHIYVHSSST IPLDDPTLLF ANAGMNQFKP IFLGTADPNS 60
EMSKWVRVAN TQKCIRAGGK HNDLDDVGKD VYHHTFFEML GNWSFGDYFK KEICSWAWEF 120
LTQRLALPKD RLYVTYFGGD AASGLEPDLE CKQMWLDLGL KPEHILPGSM KDNFWEMGET 180
GPCGPCSELH FDRIGGRSVP ELVNMDDPDV LEIWNLVFIQ YNRESDGSLK QLPKKHIDCG 240
MGFERLVSVI QNKRSNYDTD LFVPLFDAIQ AGTGAPPYQG RVGADDVDGI DMAYRVLADH 300
ARTITIALAD GGTPDNTGRG YVLRRILRRA VRYATEKLNA KPGFFATLVN TVVDLLGDAF 360
PEVKKDPQHI IDIINEEELQ FLKTLTRGRN LLNRTIEKLG NQTTIPGDVA WRLYDTYGFP 420
VDLTQLMAEE KSLKIDMDGY EAAKHNSYVL SQGKGASKIE EINLDVHAIS QLQEQGVPPT 480
NDTFKYKYEA VSDERDSAYN YGVCNSKIVA LRFENQFVNE ITSGQKAGIV LDKTNFYAES 540
GGQIYDQGAL VKVNDEANEF LVDRVYNRGG YILHIGVVEG TLKVGDELEL HIDVERRWLT 600
MKNHSATHAL NHCLLQVLGK DTEQKGSLVV PEKLRFDFNS KAAMTIEQVS KTEQLTKEMV 660
YKNVPIYAKE SKLALAKKIR GLRSVFDEVY PDPVRVISFG VPVDELEQNP DSEAGEQTSV 720
EFCGGTHLRR SGHIMDFVIS SEEAIAKGIR RIVALTGPEA LKALKKSEAF EQEIVRLKAT 780
IDNDKSGKDS KSHVKEIVEL TEQISHATIP YVKKDEMRNL LKGLKKTLDD KERALRAAVS 840
VTVVERAKTL CEANPNATVL VEQLEAFNNT KALDAALKQV RSQLPDAAAM FLSVDADSKK 900
IFCLSSVPKS AVEKGLKANE WVQHVSATLG GKGGGKPESA QASGTNYEKV DEIVQLASKF 960
AQSKLS 966 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004813; F:alanine-tRNA ligase activity; IEA:EC.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro. 
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.