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 27-MAR-2024, entry version 93.
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; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; 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 KEGG; amr:AM1_F0085; -.
DR HOGENOM; CLU_009710_1_2_3; -.
DR OrthoDB; 9810191at2; -.
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; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 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 NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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
//
