ID   SYA_BAUCH               Reviewed;         884 AA.
AC   Q1LTQ4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Alanyl-tRNA synthetase;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanine--tRNA ligase;
DE            Short=AlaRS;
GN   Name=alaS; OrderedLocusNames=BCI_0205;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP +
CC       diphosphate + L-alanyl-tRNA(Ala).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000238; ABF13997.1; -; Genomic_DNA.
DR   RefSeq; YP_588660.1; -.
DR   GeneID; 4056745; -.
DR   GenomeReviews; CP000238_GR; BCI_0205.
DR   KEGG; bci:BCI_0205; -.
DR   HOGENOM; Q1LTQ4; -.
DR   OMA; Q1LTQ4; ASGKHND.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00036; -; 1.
DR   InterPro; IPR002318; Ala-tRNA-synth_IIc.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_cons-reg.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR003156; Pesterase_DHHA1.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Pfam; PF02272; DHHA1; 1.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR00980; TRNASYNTHALA.
DR   TIGRFAMs; TIGR00344; alaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    884       Alanyl-tRNA synthetase.
FT                                /FTId=PRO_0000347505.
SQ   SEQUENCE   884 AA;  99561 MW;  180A39380BE73293 CRC64;
     MSNNSTAELR QEFLNFFHQK GHKIVASSSL VSHNDPTLLF TNAGMNQFKD VFLGLDKRLY
     QSATTAQRCI RAGGKHNDLE KVGYTARHHT FFEMLGNFSF GAYFKCEAIQ LAWELLTGGQ
     WFNLPKDKLW VTVYATDDET YNIWAKQINI PRERIVRIGD NKGKAYASDN FWQMGDIGPC
     GPCSEIFFDH GNHLFGAPPG SQGEYGDRYI EIWNLVFIQF NRQMDGTLIP LQKPSVDTGM
     GLERIAAVLQ HVNSNYDIDI FSQLIKAVAD VTKATNTSSL QVIADHIRSC AFLVSDGVVP
     SQDGRGYVLR HIIRRAIRHG YMLGARDAFF YKLVAPLIEV MGSTADQLKQ QQNMVEQVLR
     TEEEQFSQTL ERGLFMLEQV LTKLTGDTLD GETAFSLYDT YGLPIYLTTD ICRERNIKVD
     ENGFKSAMEV QRNRAREASR FSYKYNSMLS INQYTRFLGY KHLKSQGKVT ALYLNDQSVE
     VIYHSEKAIV ILDYTPFYGE SGGQIGDSGK ITAANGIFEV IDTKKYGNAL GHLGMLNYGE
     LRIGDQVTAK VNQLRRDRIS VNHSATHLLQ SALRQLLGKH VVQRGSLVHD QYLRFDFSHH
     QAMQVEQIHE VEKIINQQIR RNLIIKTDMM TLEAAQNQGA ISVLDHQYES SQVRVLSIGD
     FSTELCCGTH ASRTGDIGLF WISSESGIAL GIRRIEAITG EFALKNLHQQ SNLVQQISQL
     FKNDGSNLVE KVRGLQNHIK QLESKYQQLK SKQVAQEIAV LSRKISKMHG TQVLVSKLEN
     IEPKIMRHIV DEIKHQLGSV VIILANINLV DGKVNLIAGV TDDLTNRIQA SDIIRTLIQK
     FGGRGGGSKK IAYAGSITTN ELSTVLYYIE KIVAVKFTES QEMN
//