ID   SYA_BORA1               Reviewed;         873 AA.
AC   Q2KY72;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-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=BAV2356;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(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; AM167904; CAJ49966.1; -; Genomic_DNA.
DR   RefSeq; YP_786870.1; -.
DR   GeneID; 6265931; -.
DR   GenomeReviews; AM167904_GR; BAV2356.
DR   KEGG; bav:BAV2356; -.
DR   NMPDR; fig|521.1.peg.2283; -.
DR   HOGENOM; Q2KY72; -.
DR   OMA; Q2KY72; TLMFTNS.
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    873       Alanyl-tRNA synthetase.
FT                                /FTId=PRO_0000347508.
SQ   SEQUENCE   873 AA;  94983 MW;  4A90B5F50954C261 CRC64;
     MKSSEIRQKF LQFFQSKGHS IVPSSSLVPG NDPTLLFTNS GMVQFKDVFT GKEKRPYTRA
     TSSQRSVRAG GKHNDLENVG YTARHHTFFE MLGNFSFGDY FKQDAIRFAW ELLTTVYKLP
     VEKLWVTVYQ EDDEAYDIWA KEVGVPTERI IRIGDNKGAR YASDNFWQMG DTGPCGPCTE
     IFYDHGPDIW GGPPGSPEED GDRYIEIWNL VFMQFERDAA GNMTPLPKPC VDTGMGLERI
     AAVLQGVHSN YEIDLFQKLI TAAARETGVQ DLHDNSLKVI ADHIRACSFL IVDGVIPSNE
     GRGYVLRRIV RRALRHGYKL GQTKPFFYRL VPDLVAQMGE AYPELANMAE RVGQVLKQEE
     ERFGETLEHG MKILDVALAQ VPKGGLLDGN TLFTLYDTYG FPVDLTADIC REREVEIDMA
     GFEAAMERQR DQARAAGKFK MAEGLNYEGA QTRFEGYEQL ELSGAKVTAL YVDGTQTDQV
     RAGQQAVVVL DATPFYAESG GQVGDTGLLV ADGLRFAVAD TLKVQAGVFG HHGLLEEGVL
     KVGDTLLARV DAVRRARTVR NHSATHLMHK ALREVLGAHV QQRGSLVDPD KTRFDFAHDA
     PMTAEQIARV EAIVNAEVLA NQAAQARVMA YDDAVKGGAM ALFGEKYGDT VRVLDIGFSR
     ELCGGTHVSR TGDIGLFKIV SEGGVAAGVR RVEAITGDNA LVWVQEQNAL LQRAAGVLRS
     PVAELPERIA QVQDQVKALE KDLEQARAKL AASAGNDLAD KSAVEIKGVK VLAAVINDVD
     PKALRGMVDN LKDKLKPAIV LLAASADGKI SLVGGVTADQ TAKVKAGDLV GFVAAQVGGK
     GGGRPDMAMG GGTDVAALPA AIASVQDWVN ERL
//