ID   SYA_ALCBS               Reviewed;         863 AA.
AC   Q0VNK2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
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=ABO_1798;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL17246.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_693518.1; -.
DR   GeneID; 4211293; -.
DR   GenomeReviews; AM286690_GR; ABO_1798.
DR   KEGG; abo:ABO_1798; -.
DR   NMPDR; fig|393595.12.peg.1802; -.
DR   HOGENOM; Q0VNK2; -.
DR   BioCyc; ABOR393595:ABO_1798-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    863       Alanyl-tRNA synthetase.
FT                                /FTId=PRO_0000347483.
SQ   SEQUENCE   863 AA;  93888 MW;  E7D0C86144E21574 CRC64;
     MKSAELRQAF LDYFASQGHT KVSSSSLVPA NDPTLLFTNA GMNQFKDVFL GRESRDYTRA
     TSSQRCVRAG GKHNDLENVG YTARHHTFFE MLGNFSFGDY FKREAIKFAW EFLTGTLGLP
     EERLWVTVHV SDDEAADIWL KEMGVSAERF SRLDEDNFWQ MGDTGPCGPS SEIFYDHGAD
     VPGGPPGSAD EDLDRYIEIW NLVFMQYDRQ PDGELQPLPK PSVDTGMGLE RIAAVLQGVH
     SNYEIDLFQA LLQAAAKATG CTDLEEKSLR VIADHIRSAS FLICDGVIPS NEGRGYVLRR
     IIRRALRHGH KLGQDKPFFS TLVAALVAEM GEAYPELGRE QARIEKALLA EEEQFGRTLA
     AGMKVLESAI EQLDGRVLPG DVLFNLYDTH GFPPDLTADV ARERDLSVDM DGFEAAMAAQ
     RERARGAGSF ANDYSDRLNI DAITDFSGYE KLADDNTVVA LYKDGAAVDT LNAGEEGMVV
     LDRTPFYAES GGQVGDTGAL IADEARFMVT DTRKRQAAHV HVGKQVSGSL TIGGKVSACV
     DVDRRLAVMR NHSATHLMHA ALRNVLGEHV QQKGSLVSAD YLRFDFSHGE AVSEAQREEI
     EILVNRQILA NTAVTTELMD IESAREAGAM ALFGEKYDDQ VRVLSMGSDG FSKELCGGTH
     VNRTGDIGLF RITLEASAAA GVRRIEAVTG EHALAVMRRQ ERALSEIAAT VKSSLDNAAD
     RVRSQAQKVR ELEKEIERLK QKLASGAGGD LTSEVQDING VKVLATQIDG ADGKTLRVTM
     DKLKDKLGSA VIVLAAVEGE KVALVAGVTK DLTTKYKAGD LLKFVAEQVD GRGGGRPDMA
     QGGGNNPAAL PGALESVKAW VAE
//