ID   SYA_ANAVT               Reviewed;         880 AA.
AC   Q3MGN4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=Ava_0226;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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; CP000117; ABA19852.1; -; Genomic_DNA.
DR   RefSeq; YP_320747.1; -.
DR   GeneID; 3683029; -.
DR   GenomeReviews; CP000117_GR; Ava_0226.
DR   KEGG; ava:Ava_0226; -.
DR   NMPDR; fig|240292.3.peg.546; -.
DR   HOGENOM; Q3MGN4; -.
DR   OMA; Q3MGN4; GEFVIKL.
DR   BioCyc; AVAR240292:AVA_0226-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    880       Alanyl-tRNA synthetase.
FT                                /FTId=PRO_0000347487.
SQ   SEQUENCE   880 AA;  96994 MW;  1BCFE443E9011EEA CRC64;
     MSSNPQHLSG NEIRTRFLDF YAQRGHQILA SASLVPEDPT VLLTIAGMLP FKPIFLGQRT
     PEFKRATTSQ KCIRTNDIEN VGRTKRHQTF FEMLGNFSFG DYFKEQAIAW GWEISTEVFG
     LPKERLVVSV FEEDDEAYVI WRDQIGVTEA RIKRMGADDN FWVSGPTGPC GPCSEIYYDF
     HPERGDENID LEDDTRFIEF YNLVFMQYNR DASGNLTPLQ NKNIDTGMGL ERITQILQQV
     PNNYETDLIF PIIETAAKIA GIDYHSSDET TKVSLKVIGD HVRSVVHMIA DEIRASNVGR
     GYVLRRLIRR VVRHGRLIGI SGEFINQVAE RAIALSESAY PNVRKRETVI KAELEREEAN
     FLKTLDRGEK LLEEIIQQVK KQGQTIISGE SAFTLYDTYG FPLELTQEIA EENNLTVDED
     DFNVEMQKQV ERAKAAHETI DLTVQGSLDK LAEHIHATEF IGYSQATATA KVEVLLVDGV
     VQEEAEAGTE VQIVLDKTPF YAESGGQIGD RGYISGDGIV VQVEDVKKES DFFVHFGRIE
     RGTLRVGDSV TAQIDRAGRR RAQANHTATH LLQAALKTIV DGGISQAGSL VSFDRLRFDF
     NSPRGLTAEE IQQVEEQINT WIAEAHSAKI EVLPLAEAKA RGAVAMFGEK YGDEVRVIDF
     PGVSMELCGG THVSNTAEIG VFKIISEAGV ASGVRRIEAV SGLAVLDYLN VRDKVVKDLS
     DRFKVKPEEL PERITTLQNE LRTTEKQLET LKGQLAIAKS DSLLQTADTL GDHKIIVAQL
     EGVDPESLKS AAERLLQKIG NGAVVLGSVP EADKVSLVAA FSPEVNKKGL QAGKFIGAIA
     KICGGGGGGR PNLAQAGGRD ASKLPTALEQ AQSELKSALG
//