ID   SYA_BLOPB               Reviewed;         879 AA.
AC   Q493M6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=BPEN_174;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
CC   -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP +
CC       diphosphate + L-alanyl-tRNA(Ala).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000016; AAZ40814.1; -; Genomic_DNA.
DR   RefSeq; YP_277687.1; -.
DR   GeneID; 3562669; -.
DR   GenomeReviews; CP000016_GR; BPEN_174.
DR   KEGG; bpn:BPEN_174; -.
DR   HOGENOM; Q493M6; -.
DR   OMA; Q493M6; ASGKHND.
DR   BioCyc; CBLO291272:BPEN_174-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; 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    879       Alanyl-tRNA synthetase.
FT                                /FTId=PRO_0000075068.
SQ   SEQUENCE   879 AA;  99895 MW;  AB11E160B35B1A04 CRC64;
     MYKNIDDIRQ EFLNFFKKKG HKIISSSTLI PNSDQTLLFT NSGMNQFKNI FLGIDKPLFK
     RVATAQRCVR AGGKHNDLNN VGYTERHLTF FEMLGNFSFG DYFKNEAIQF AWELLTDVNW
     FNLSKNKLWV TVHNCDGESY DIWSNQIDIP NEHIVKIGSN TNDFCDSDNF WQMGNIGPCG
     PCSEIFYDRG DRFQGGPPGS LEEFGERYVE IWNLVFIQFD RQENGRLLSL PMLSVDTGMG
     LERITSILQG VNSNFSIDVF KKLISSISRI MKINDIYINR SVYVIADHIR ACSFLIQDGV
     LPANEGRGYV LRRIIRRAIL HGKKLGVNDI FFYKLVSPLI KYMQHIADIL HEKKDFIAEI
     LLSEEKLFQD TLKRGLELLE KQLIRLKGNC LNGEIAFNLY DTYGFPFELT QDVCLKRGIH
     VDQEGFDQAM LTQKKYTKEL NKFDISYEKL SLCNVSSIFV GYDKLICKSR VMALFQNNKS
     INKIYTKEEG IVILNNTPFY GESGGQIGDC GQLNTISGFF QVSNTKKYGQ TIGHLGIVNS
     GTISVGEEIV AQVDQHKRKC ISLNHSATHL LRAALSQVLG SHVTQKGSLV NDRYLRFDFY
     HHATMTTTQM NTVENIVNEQ IWKNAPITVD VMPIELARNS GAVILINKQY DKKVRVLKIG
     NFSTELCGGT HAEHTGEIGV FMITKECSIA AGIRRVEAVT NNVALSAIHQ YKMLLKNIFQ
     STQSDDKNIL SKIHEFKCRY QKLEKEIDTL RNQQIIQQSL SFIKDVYYIK DVRILVKQVV
     NMTSKTLFNM TDCIKHQLKS GVIVLINLNT NKKINLVVAV TKDLIERNRI NALSLVHYII
     KILGGKGGGR PDFAQAGINN MATTSKISIE VNSLLHNIL
//