ID   SYA_ANAPZ               Reviewed;         876 AA.
AC   Q2GJ36;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=APH_1059;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(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; CP000235; ABD44304.1; -; Genomic_DNA.
DR   RefSeq; YP_505615.1; -.
DR   GeneID; 3930808; -.
DR   GenomeReviews; CP000235_GR; APH_1059.
DR   KEGG; aph:APH_1059; -.
DR   NMPDR; fig|212042.5.peg.1003; -.
DR   TIGR; APH_1059; -.
DR   HOGENOM; Q2GJ36; -.
DR   OMA; Q2GJ36; GEFVIKL.
DR   BioCyc; APHA212042:APH_1059-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    876       Alanyl-tRNA synthetase.
FT                                /FTId=PRO_0000347490.
SQ   SEQUENCE   876 AA;  96764 MW;  93320B0A64AC0E1E CRC64;
     MSSSSVSGIR EAFLDFFEKQ GHTRYPSAPL IAEGDASLLF TNAGMVPFKQ RFITGVSDVK
     TATTSQKCLR AGGKHNDLEN VGYTNRHHTF FEMLGNFSFG DYFKETAIEL AWRFVTKELG
     LSKERLWITV YSEDQEAFDI WKKITGYTDH KIIRISTSDN FWSMGDTGPC GPCSEIFYDY
     GDGVPGGLPG TDESDGARYT EIWNLVFMQY NRDESGELHK LPRGCIDTGM GLERIAAVMQ
     GVCDNYETDM FQAIIDRSRS IFGSHDHPIA HRVIADHVRA ASFLIAEGLT PGNEGRNYVL
     RRIIRRAVRY IYQIVGDKFS LHEVVPVLTR EGSAGYMGNA YPEIVKAEQS IVSTLKIEED
     GFADTLRRGT GILEQEIRGL KSGEVLSGEI AFKLYDTYGF PLDITLDVAK ERGLKFDEDG
     FNRCMAKQKE QSRKHWKGSG EAQTASSHIL NKHKATSFVG YENHRVKSMV KEIFCSGEAV
     TSMGEGEEGI AVLDITPFYA ESGGQEGDTG LLKVVTTKCG SVAEVVDTTK SNNVHLHKIR
     VIRGTLKVGD VVEAVVDKQR REKLRANHSA THILQSVLRT LIGEGIQQKG SLVAADKLRF
     DFSHALPLTK EQLRTVEMEV NRQIMANQPV IIDHCSLEDA VQEGAIALFG EKYNDQNVRV
     VSMGSSKELC GGTHVRFTGD IGAFRIISET GIAQGVRRIE AITGHEVVSS MNRDSESLQQ
     VAECLSVPVD QVIEKLKKVF VEQREINKKM ATICYTHMNS CAKCIEVGSE IKLYVGEFSN
     IPVEVVASYV KEKMHTNEVL AISTTDGKRT TFIVGVGESA IKRIKATDIV KALQQIQGKG
     GGNASIARAS LPSEYSAKAA EIIRQTVIDA IQNSGA
//