※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alanine--tRNA ligase
Protein Synonyms/Alias
 AlaRS
Gene Name
 alaS
Gene Synonyms/Alias
 CA_C1678
Created Date
 3-June-2014
Organism
 Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
NCBI Taxa ID
 272562
Phosphorylation
Position
Peptide
Code
Type
References
375 GMEILKNYIDELSLE Y HTP [1]
388 LENKKVMSGEKAFRL S HTP [1]
Reference
 [1]Phosphoproteomic investigation of a solvent producing bacterium Clostridium acetobutylicum.
 Bai X,Ji Z
 Appl. Microbiol. Biotechnol. 2012, Jul;95(1):201-11. [PMID:22627760]
Functional Description From UniProt
 FUNCTION: 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 From UniProt
 
Key Word From UniProt
 Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Proteinbiosynthesis; Referenceproteome; RNA-binding; tRNA-binding; Zinc
Protein Sequence
 MKYMGLNDIR ESYLSFFEKK EHLRLPSFSL IPKNDKSLLL INAGMAPLKP YFTGLQTPPK 60
 TRVTTCQKCI RTGDIENIGK TSRHGTFFEM LGNFSFGDYF KEEVISWAWE YITEVLKFPK 120
 DRIYITIYLD DDEAFKIWTE KAGVDPSRIF RFGKEDNFWE HGSGPCGPCS EMHFDRREKP 180
 DLIKTREKFI ELQDKDEVIE FWNLVFTQFD KDEDGNYNKL KNPNIDTGMG LERIATIMQN 240
 TDSIFEIDTI REVLDAVCKI CNVKYGENHK NDVSLRIITD HIRSVTFMIS DGILPSNEGR 300
 GYVLRRLLRR AARHGKTLGI EKTFLCGLCD VVIKNSKGAY KELEEKQDYI KNVIEIEEKR 360
 FDETLDSGME ILKNYIDELS LENKKVMSGE KAFRLYDTYG FPVELTQEIL EEKGIEIDMN 420
 DFHSEMEKQK NRARDAREES NYMGKEIKLI DKLPESVTTK FVGYNSTSTD SKVEVLIKDD 480
 EFVSTINEGE SGIVVTEETP FYAEMGGQIG DKGIIFGKNG EAKVVDCKNN ISGKIIHIVQ 540
 VVKGSIEKNE NVTLEVNYKK RKDICKNHTA THMLQAALKK VVGSHINQSG SYVDNERLRF 600
 DFTHFTALTD EEILKVEAMV NDEIMAAYDV KTDIMSVDEA KKTGAMALFD EKYGNRVRVV 660
 SVGDFSRELC GGTHVNNSGE IGLFKIISES GVAAGIRRIE AITGKEAVRY TEENDNLIRN 720
 IEQELKCSKK DILNKINQYH SELKEKEKEI NILKGKLASG FEENILSSVK EVSGVKYVAS 780
 EVKGISGDTL RELCDKVRNK IDDGMVLLAS KDGEKVQFVA MASKNAVKKG VHCGKVIKEV 840
 ASMCGGNGGG RPDMAQAGGK DGEKLETALK EVGNIMEKLV K 881
  GO:0005737   C:cytoplasm IEA:UniProtKB-SubCell
  GO:0004813   F:alanine-tRNA ligase activity IEA:UniProtKB-HAMAP
  GO:0005524   F:ATP binding IEA:UniProtKB-HAMAP
  GO:0000049   F:tRNA binding IEA:UniProtKB-KW
  GO:0008270   F:zinc ion binding IEA:UniProtKB-HAMAP
  GO:0006419   P:alanyl-tRNA aminoacylation IEA:UniProtKB-HAMAP
  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.
  IPR009000   Transl_B-barrel.
  IPR012947   tRNA_SAD.
  PF02272   DHHA1.
  PF01411   tRNA-synt_2c.
  PF07973   tRNA_SAD.
  SM00863   tRNA_SAD.
  PS50860   AA_TRNA_LIGASE_II_ALA.
  PR00980   TRNASYNTHALA.