CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012435
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alanine--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
 Alanyl-tRNA synthetase; AlaRS 
Gene Name
 Aars2 
Gene Synonyms/Alias
 Aarsl; Gm89; Kiaa1270 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
275LVAVLQGKRSTYDTDubiquitination[1]
859TAIRKLEKGQATEKSacetylation[2]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 
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 627 627 Zinc (Potential).
 METAL 631 631 Zinc (Potential).
 METAL 744 744 Zinc (Potential).
 METAL 748 748 Zinc (Potential).  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Metal-binding; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding; Transit peptide; tRNA-binding; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 980 AA 
Protein Sequence
MAVALAAAAG KLRRAIGRSC PWQPFSTEPG PPHGAAVRDA FLSFFRDRHG HRLVPSATVR 60
PRGDPSLLFV NAGMNQFKPI FLGTVDPRSE MAGFRRVVNS QKCVRAGGRH NDLEDVGRDL 120
SHHTFFEMLG NWAFGGEYFK EEACSMAWEL LTQVYGIPED RLWVSYFSGD SQTGLDPDLE 180
TRDIWLSLGV PASRVLSFGP QENFWEMGDT GPCGPCTEIH YDLAGGVGSP QLVELWNLVF 240
MQHYREADGS LQLLPQRHVD TGMGLERLVA VLQGKRSTYD TDLFSPLLDA IHQSCGAPPY 300
SGRVGAADEG RIDTAYRVVA DHIRTLSVCI ADGVSPGMSG APLVLRRILR RAVRYSTEVL 360
QAPPGFLGSL VPVVVETLGS AYPELEKNSV KIASLVSEDE AAFLASLQRG RRIIDRTVKR 420
LGPSDLFPAE VAWSLSLSGN LGIPLDLVEL MLEEKGVKLD TAGLEQLAQK EAQHRAQQAE 480
ADQEDRLCLD VHALEELHRQ GIPTTDDSPK YNYTLHPNGD YEFGLCEARV LQLYSETGTA 540
VASVGAGQRC GLLLDRTNFY AEQGGQASDR GYLVRTGQQD MLFPVAGAQL CGGFILHEAM 600
APERLQVGDQ VQLYVDKAWR MGCMVKHTAT HLLSWALRQT LGPTTEQRGS HLNPERLRFD 660
VATQTLLTTE QLRTVESYVQ EVVGQDKPVF MEEVPLAHTA RIPGLRSLDE VYPDPVRVVS 720
VGVPVAHALG PASQAAMHTS VELCCGTHLL STGAVGDLVI IGERQLVKGI TRLLAITGEQ 780
AQQAREVGQS LSQEVEAASE RLSQGSRDLP EAHRLSKDIG RLTEVAESAV IPQWQRQELQ 840
TTLKMLQRRA NTAIRKLEKG QATEKSQELL KRHSEGPLIV DTVSAESLSV LVKVVRQLCK 900
QAPSISVLLL SPQPTGSVLC ACQVAQDATP TFTAEAWALA VCSHMGGKAW GSRVVAQGTG 960
HTADLEAALG TARAYALSQL 980 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 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:0070143; P:mitochondrial alanyl-tRNA aminoacylation; IEA:Compara.
 GO:0033108; P:mitochondrial respiratory chain complex assembly; 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.
 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.