ID   SYA_BORAP               Reviewed;         594 AA.
AC   Q0SNU2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
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=BAPKO_0228;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(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; CP000395; ABH01486.1; -; Genomic_DNA.
DR   RefSeq; YP_709662.1; -.
DR   GeneID; 4227838; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0228.
DR   KEGG; baf:BAPKO_0228; -.
DR   NMPDR; fig|390236.5.peg.283; -.
DR   HOGENOM; Q0SNU2; -.
DR   OMA; Q0SNU2; DIDEVGD.
DR   BioCyc; BAFZ390236:BAPKO_0228-MON; -.
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; IPR018165; Ala-tRNA-synth_IIc_cons-reg.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR00980; TRNASYNTHALA.
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    594       Alanyl-tRNA synthetase.
FT                                /FTId=PRO_0000347510.
SQ   SEQUENCE   594 AA;  67983 MW;  B421D9E684186517 CRC64;
     MTLDKLRKKY IDFFKSKKHF EIMGKSLVPE NDPTVLFNTA GMQPLIPYLL GEVHPSGDML
     VNVQKCLRTG DIDEVGDLSH LTFFEMLGNW SLGAYFKEYS VKCSFEFLTS SEYLNIPKDR
     LYVSVFEGDQ EIPRDTETAK VWESLGIPKD RIYYLSKDHN FWGPVGSKGP CGPDTEIYVD
     TGKIKCSINC NVTCSCGKYF EIWNNVFMQY NKDENGNYME LDRKCVDTGM GLERTIAFLQ
     GKSSVYDTDA FMPIIKRIEF ISGKIYGQKE DDDRCIRIIS DHIKAACFIL ADSSGVFPSN
     LGQGYVLRRL IRRSIRYAKK LGIKSHFLAD LVDSVETIYR SFYNELTEKK DFIKKELSTE
     EEKFFKTLFQ GEQEFIKITR NLSSKTIPGD IAFKLYDTYG FPYELTEELA FEYGFDIDKS
     GFNEYFKKHQ KTSKKGGDKV FKGGLADYTY ETTKLHTATH LLHKALQLVL GDHVKQKGSN
     ITAERLRFDF VHSKKMTDDE IKKVEDIVNL QIKNSLSVKK SIMELSEARE KGAMALFGEK
     YDNLVSVYEI DGFSLEVCGG PHVENTNELG TFKIQKEQSS SSGIRRIKAI LIDE
//