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SYM1_ACAM1
ID   SYM1_ACAM1              Reviewed;         558 AA.
AC   A8ZQ66;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Methionine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00098};
DE            EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_00098};
DE   AltName: Full=Methionyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00098};
DE            Short=MetRS 1 {ECO:0000255|HAMAP-Rule:MF_00098};
GN   Name=metG1 {ECO:0000255|HAMAP-Rule:MF_00098}; OrderedLocusNames=AM1_F0085;
OS   Acaryochloris marina (strain MBIC 11017).
OG   Plasmid pREB6.
OC   Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC   Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017;
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
CC   -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC       also for the initiation of all mRNA translation through initiator
CC       tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC         methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC         Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00098};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00098};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00098}.
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DR   EMBL; CP000843; ABW33099.1; -; Genomic_DNA.
DR   RefSeq; WP_012168149.1; NC_009931.1.
DR   AlphaFoldDB; A8ZQ66; -.
DR   SMR; A8ZQ66; -.
DR   EnsemblBacteria; ABW33099; ABW33099; AM1_F0085.
DR   KEGG; amr:AM1_F0085; -.
DR   HOGENOM; CLU_009710_1_2_3; -.
DR   OMA; YMRMAGH; -.
DR   OrthoDB; 761140at2; -.
DR   Proteomes; UP000000268; Plasmid pREB6.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.20.28.20; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR023458; Met-tRNA_ligase_1.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR029038; MetRS_Zn.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR45765; PTHR45765; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF57770; SSF57770; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Plasmid; Protein biosynthesis; Reference proteome;
KW   Zinc.
FT   CHAIN           1..558
FT                   /note="Methionine--tRNA ligase 1"
FT                   /id="PRO_0000331770"
FT   MOTIF           10..20
FT                   /note="'HIGH' region"
FT   MOTIF           332..336
FT                   /note="'KMSKS' region"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
SQ   SEQUENCE   558 AA;  64196 MW;  A6481D3ED2FF1293 CRC64;
     MRYLITSALP YINGIKHLGN LVGSMLPADI YARFLRQEGE EVLYICATDE HGTPAEIAAI
     DAGLEVAEFC AKQYHKQKEI YKRFGLSFDY FGRTSAPENH ELTQYFYQQL AKQNFIEERE
     ISQFYALDDQ RFLPDRYVTG TCPHCGYEQA RGDQCENCTK VLTPTELIKP RSTISGSTHL
     ELRTSRHLFL RLDKLSDEVR NWVDKQTQWS TLTKSIALKW LNEGLKSRCI TRDLVWGVPV
     PTEGFERKVF YVWFDAPIGY ISATKAWGDI TNNDWECWWK ESDDVHYTQF MAKDNLPFHT
     IMWPATILGS REPWKMVDYI KGFNWLNYYG GKFSTSSQRG VFLDQALEIA SADNWRYMLI
     ANAPESADSA FTWEQFQKQV NKELADNLGN FVNRILKFTA SRFGMTLPEG GTPGDAEAEL
     QVTCNELVEK LRKYLHNLEF RRATETLNAL WRTGNQYIDV RAPWVLFKTD QDETAMVIRT
     CVNLIRLYAI SSAPFIPHTT QALFDALQLT DVERRHTMTE ASDLTLLAAG RSFMVPAPLF
     QKIDDDLVAE LKAQYGGE
 
 
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