CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010094
UniProt Accession
Genbank Protein ID
 U00089 
Genbank Nucleotide ID
Protein Name
 Alanine--tRNA ligase 
Protein Synonyms/Alias
 Alanyl-tRNA synthetase; AlaRS 
Gene Name
 alaS 
Gene Synonyms/Alias
 MPN_419; MP422 
Created Date
 July 27, 2013 
Organism
 Mycoplasma pneumoniae (strain ATCC 29342 / M129) 
NCBI Taxa ID
 272634 
Lysine Modification
Position
Peptide
Type
References
780KITVNELKTEDFKWKacetylation[1]
Reference
 [1] Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.
 van Noort V, Seebacher J, Bader S, Mohammed S, Vonkova I, Betts MJ, Kühner S, Kumar R, Maier T, O'Flaherty M, Rybin V, Schmeisky A, Yus E, Stülke J, Serrano L, Russell RB, Heck AJ, Bork P, Gavin AC.
 Mol Syst Biol. 2012 Feb 28;8:571. [PMID: 22373819] 
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 Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (By similarity). 
Sequence Annotation
 METAL 567 567 Zinc (Potential).
 METAL 571 571 Zinc (Potential).
 METAL 671 671 Zinc (Potential).
 METAL 675 675 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
 900 AA 
Protein Sequence
MKWTTDKVRQ TWLDYFTAKG HLALPSKSLI PVNDPSLLWI NSGVATLKDY FSAKKTPPSK 60
RLANAQICLR VNDIENVGFT SRHQTLFEML GNFSIGDYFK EEAIGFANDL LVNHYHLDPK 120
RFYITVYQDD ELTFNTWLKH GIPASRIIKC DRDRNFWDLG LGPCGPCTEI YYDRGERFDP 180
HKVGEKLFFE DIENDRYVEV WNIVFSQFNN DGNGNYSELA QKNIDTGAGI ERLVAILQDA 240
PTNFDTDIFL KLIGIIEQHC KHKYDTNLYF KFDQKLNEAQ SAFRIISDHF KAITFTIAEG 300
VLPGPNERSY IVRRLLRRAL LACKKLDLDL KFIDPMVDAI ISVYGSYYQQ LQGKNQVVQQ 360
AIWKEVTAFD KTINLGLMLF EKSIAHNALQ PQVAFQLYET YGFPIEMIKE LVDKRQLQVD 420
WKAVEQLMEQ HRLISKQNSN TLSFEKQNEH LVNFKTASEF LYEANEITAK VIGLFDEQYQ 480
PVQKLHNQSG YVVFDQTVLY ATSGGQRYDE GYCINHSQND QRVSFQGVFK GPNKQHFHFF 540
LTGSFQLGDK VILVHDGKWR QLVKNNHSLE HLLHAALQNE IDPLIKQDGA FKSAQKATID 600
FNFSRALTWA ELERVEHRIR QIIQQDIQRE EIFTDLEGSQ KLNAIAYFEE EYSNHELLRV 660
IRFGDFSVEL CGGTHVEHTG LIENCFITDY YARGTGRWRI EIISSNETIA AYLNEQNGKL 720
SETINSLHNT LNNIANPALN KQKTALTKQL NHFHLPQVIT DLRKCQALLN ELKITVNELK 780
TEDFKWKQKQ LAEKIKQELL ELAKQDKAYV LASFAAVDPK LLSQVAQAVL NQHKNKLFVL 840
LNQFNNSPSF MLLGQDVSKC IQLLKAHFEL KGGGSNNFFR GSFNESVDVS KLQAILDTLQ 900 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004813; F:alanine-tRNA ligase activity; IEA:HAMAP.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:HAMAP.
 GO:0006419; P:alanyl-tRNA aminoacylation; IEA:HAMAP. 
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.
 IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
 IPR012947; tRNA_SAD. 
Pfam
 PF01411; tRNA-synt_2c
 PF07973; tRNA_SAD 
SMART
 SM00863; tRNA_SAD 
PROSITE
 PS50860; AA_TRNA_LIGASE_II_ALA 
PRINTS
 PR00980; TRNASYNTHALA.