ID   SYA_AYWBP               Reviewed;         864 AA.
AC   Q2NJ60;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=AYWB_416;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A.,
RA   Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W.,
RA   Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to
RT   diverse environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(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; CP000061; ABC65533.1; -; Genomic_DNA.
DR   RefSeq; YP_456612.1; -.
DR   GeneID; 3865575; -.
DR   GenomeReviews; CP000061_GR; AYWB_416.
DR   KEGG; ayw:AYWB_416; -.
DR   HOGENOM; Q2NJ60; -.
DR   OMA; Q2NJ60; GEFVIKL.
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    864       Alanyl-tRNA synthetase.
FT                                /FTId=PRO_0000347494.
SQ   SEQUENCE   864 AA;  100363 MW;  65658154C3A15DC3 CRC64;
     MTSFEIRQMW IKFFASKNHH IEKSFSLIPR NEDNLLWVNA GITPLKKYFD GTQTPSFRRI
     TNVQKCIRTK DIKNVGKTSR HHTFFEMLGN FSIGNYFKKE AIHYAFELLT SPKWFGFPLE
     KLYITYFFQD QDTYQYWLDL GVNKNHLIHL KDNFWQIGPG PSGPCTEIFF DRGKTFDPRN
     KELIIEDLEN DRFIEIWNIV FSQYNCDPKL PIEKYQELPS KNIDTGAGLE RLACILQNTK
     TNFETDLFFP LIKALEKMTQ ITYTGQESFK IIADHLKTLV FAINDGAVLT NEKRGYVLKK
     LLRRAANEGK KLGLEKPFLY KLVPPTVAMM KDFYKELCTN QEMIAKVLLQ QENIFEKTLK
     TAEKTFLQHL TQNTLSGKNF FKLYDTYGIP ENLILDYAKK KNITTDYQKF QELLHEQQNL
     SKKNQTSQTN MNKQEEAFLH FLTPSEFIGY TNFACKTKVI KVFDEGIVLE KTPFYANMGG
     QIEDEGWIDN NKVTKITKLP NGQILHEFKG NFCEGQEVYA CIDKTKRKQI SYHHTATHLL
     EVVLQKQLGN HIKKQGSSVG FSSLRYDFNH FEKITPQTLL QIEKEVNQLI QKRVPVKIEQ
     LSIQDAQKKY ATLLEQNQKA KYKDKVRIVN IDTFSVDLCG GTHATNTKDL EHFTILSYES
     ISSGIYRIEA VCNKNCQESL NAKLAPYQNE LHQLTQKAKS LQTQNLDFEI KKFPPITKSY
     QDIINYQKHI KTQQQALVLF EKKVLEHHQK KMIQAESNFL PPQINKKMML TIKEEKPLEV
     IKFFMNHIFY KYHLEVLFLS YVQPEKIVFL CQSKTLHAGN LIKEGVSLAC GSGGGNASLA
     QGGTKKTQNL EKMLNFVKNK LKIN
//