ID   SYA_ACICJ               Reviewed;         878 AA.
AC   A5FXC2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
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=Acry_1038;
OS   Acidiphilium cryptum (strain JF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163;
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., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) 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; CP000697; ABQ30254.1; -; Genomic_DNA.
DR   RefSeq; YP_001234173.1; -.
DR   GeneID; 5160168; -.
DR   GenomeReviews; CP000697_GR; Acry_1038.
DR   KEGG; acr:Acry_1038; -.
DR   OMA; A5FXC2; 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    878       Alanyl-tRNA synthetase.
FT                                /FTId=PRO_0000347468.
SQ   SEQUENCE   878 AA;  94424 MW;  1FC00F031C6DB515 CRC64;
     MTSSNDIRAT FLDFFARNGH EVVPSAPLVP RNDPTLMFVN AGMVPFKNVF TGHEHRPYVR
     AASSQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKDVAIENA WTLLTRDFGL
     PKEKLLVTVY HEDDEAASLW KRIAGLPDEK IIRIATDDNF WRMGDTGPCG PCSEIFYDHG
     PSIPGGPPGS PDEDGDRFIE IWNLVFMQFL EEPAGVRNPL PRPSIDTGMG LERFAAILQG
     KHDNYDTDTL RALILASAEV SHTDPDGAHK VSHRVIADHL RATSFLIADG VLPSNEGRGY
     VLRRIMRRAM RHAHRLGMRE PFIYRLVPAL TRQMGVAFPE LPRAEALIVE TLKLEEQKFA
     VMLERGLSLL EDEVQKLGSG EKLPGAVAFK LYDTYGFPLD LTEDALREQH RGLDHEGFTA
     SMAEQKARAR AAWAGSGDAA TETVWLDLRD RLGGTEFLGY STEESDASIL AVVVNGAPAG
     RAEAGQEVAL ILNQTPFYAE SGGQVGDTGT LTAPGVTIRV TDTQKKAGDL FVHYGTIEEG
     EIAPGNSVHA EVDHARRGAI RAHHSATHLL HEALRRALGP HVTQKGSLNA PDRLRFDISQ
     PRPVTGAELR AVEREVNARI RENAAVETRL MTPDEAVKRG AMALFGEKYG DEVRVVSMGA
     GDAGRSAYSI ELCGGTHVAR TGDIGAFRIL AESGVAAGIR RIEAVTGEAA LAATEAETDL
     LEEAAAALKV APAELPARIA ALLEEKKRFE RQVAELQRKL ATGGAAAEIE EVAGIKFAAR
     NLGEVSPRDL KSLADSILKS MGSGIAALVS TAESKASIVV AVSPDLTSAN NAVTLVQAAS
     GVVGGKGGGG RPDMAQAGGP DASKADEALA AVRALIKP
//