ID   SYM_ALCBS               Reviewed;         686 AA.
AC   Q0VP51;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Methionyl-tRNA synthetase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionine--tRNA ligase;
DE            Short=MetRS;
GN   Name=metG; OrderedLocusNames=ABO_1599;
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   -!- FUNCTION: Is required not only for elongation of protein synthesis
CC       but also for the initiation of all mRNA translation through
CC       initiator tRNA(fMet) aminoacylation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP +
CC       diphosphate + L-methionyl-tRNA(Met).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. MetG type 1 subfamily.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain.
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DR   EMBL; AM286690; CAL17047.1; -; Genomic_DNA.
DR   RefSeq; YP_693319.1; -.
DR   GeneID; 4211503; -.
DR   GenomeReviews; AM286690_GR; ABO_1599.
DR   KEGG; abo:ABO_1599; -.
DR   HOGENOM; Q0VP51; -.
DR   OMA; Q0VP51; CEAVPES.
DR   BioCyc; ABOR393595:ABO_1599-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00098; -; 1.
DR   InterPro; IPR015413; aa-tRNA-synt_I.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002304; Met-tRNA-synth_Ia.
DR   InterPro; IPR004495; Met-tRNA-synth_Ia_bsu_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR014758; tRNA-synt_met_N.
DR   InterPro; IPR002547; tRNA_bd.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   TIGRFAMs; TIGR00399; metG_C_term; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   RNA-binding; tRNA-binding; Zinc.
FT   CHAIN         1    686       Methionyl-tRNA synthetase.
FT                                /FTId=PRO_0000331776.
FT   DOMAIN      584    686       tRNA-binding.
FT   MOTIF        22     32       "HIGH" region.
FT   MOTIF       337    341       "KMSKS" region.
FT   METAL       153    153       Zinc (By similarity).
FT   METAL       156    156       Zinc (By similarity).
FT   METAL       166    166       Zinc (By similarity).
FT   METAL       169    169       Zinc (By similarity).
FT   BINDING     340    340       ATP (By similarity).
SQ   SEQUENCE   686 AA;  76792 MW;  12B533D19987EF81 CRC64;
     MEIDAVPMSD TPRKILVTSA LPYANGPIHL GHLLEYIQTD IWVRFQKLRG QQCIYVCADD
     AHGTAIMLKA EENGVTPEQQ IAQVKADHER DFADFQVNFD NYYSTHSPEN RALSEMVFQR
     NKDAGYILEK TITQLYDPQK GMFLADRFVK GTCPKCKSED QYGDNCEVCG ATYTPAELIE
     PYSSVSGATP VEKETTQLFF DLPKFEALLR EWTRSGALQE QVANKLQEWI EDLQPWDISR
     EAPYFGFEIP GYPGKYFYVW LDAPIGYMAS FQNYCDREGL SFDDYWGKES TAELYHFIGK
     DIINFHGLFW PAMLDGAGLR KPTAIYSHGF VTVNGAKMSK SRGTFIKART YLDHLSPEYL
     RYYFAAKLSS RVDDFDLNLE DFAQRVNSDL VGKLVNIASR TGNFVKKFGG TLSTELDNMM
     LVREVQEAGP RIADFYEKRE FGKAMREIMA LADHANVYIA DKAPWSLSKE EGKEQEVLAI
     CSTAINVFRL LVIYLKPVLP ALAERAEAFM QVEPLTWADS EQLLLGHEIA KFKPLLSRVD
     MAQVESMLED SKESTPAPAA AKPKKAATQK ADAADNDETI SIDDFLKVKL RVARVAKAAH
     VDGADKLLQL TLDVGELGQR NVFAGIKARY APEELEGKLV VLVANLAPRK MKFGISEGMV
     LAAGPGGDDI HILSPDSGAE PGMEVR
//