ID   SYA_ALHEH               Reviewed;         869 AA.
AC   Q0A8K7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-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=Mlg_1481;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000453; ABI56830.1; -; Genomic_DNA.
DR   RefSeq; YP_742320.1; -.
DR   GeneID; 4269954; -.
DR   GenomeReviews; CP000453_GR; Mlg_1481.
DR   KEGG; aeh:Mlg_1481; -.
DR   NMPDR; fig|187272.6.peg.1421; -.
DR   HOGENOM; Q0A8K7; -.
DR   OMA; Q0A8K7; 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    869       Alanyl-tRNA synthetase.
FT                                /FTId=PRO_0000347484.
SQ   SEQUENCE   869 AA;  95318 MW;  033C4BAC7D8AA86B CRC64;
     MKSSAEIRNA FLEFFEHRGH TVVPSSPLVP ANDPTLLFTN AGMVPFKDVF LGKEQRGYTR
     ACSSQRCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKREAIEYA WEFLTRTIGL
     PAERLWVTVY EEDDEAADIW LNEIGVDPER FGRIGAADNF WSMGDTGPCG PCSEIFYDHG
     PEVPGGPPGS PEEDGDRYVE IWNLVFMQYD RDAEGRLAPL PMPCVDTGMG LERLAAVVQG
     VHSNFEIDLF RRLIGAAAAL AGLPEDSDNA SLKVIADHIR ACAFLITDGV VPANDGRGYV
     LRRIIRRAVR HGYKLGIDEP FFHRLVQPLA DEMGGAFPEL PERQALVERL LLQEEQRFRE
     TLEQGLKLLE EDLRQLTGAE IPGETVFKLA DTYGFPVDLT ADIARERDLT LDMAGFEACM
     AAQRERARAH SQFKVQHGEG EQFEGESHFI GYDQLEGHGE VLALFRDGRS VQTLSAGEEG
     MVILDQTPFY AESGGQVGDQ GVLETAGGEV FEVRDTLKQG EGHGHLGRLR EGRIHVGDRL
     RAQVDAETRW ATALNHSATH LLHAALRGVL GTHVQQKGSL VAPDRLRFDF AHYEAPSTEQ
     LEQIERIVND EIRANRAADI EHMAYDDAIE TGAMALFGEK YGDQVRVLRF GEFSIELCGG
     THVERTGDIG LCKLISEGGV AGGVRRIEAV TGDRAVMWVQ RTEQRLVQVA ETVKASPDNA
     AVRVAQLVDR LKGQEKELER LKQKLASQAG SDLAGQAVDI GGVKVVAARV DADNKALRDT
     VDQLRNKLGT AVIVLGAVAG DKVRLVAGVS KDCTDRIKAG DLVRQVAEQV GGKGGGRPDF
     AQAGGEQPEH LETALASVES LVRDALGLE
//