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Database: UniProt
Entry: K9XMG3_STAC7
LinkDB: K9XMG3_STAC7
Original site: K9XMG3_STAC7 
ID   K9XMG3_STAC7            Unreviewed;       527 AA.
AC   K9XMG3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01228};
DE            EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_01228};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228};
DE            Short=MetRS {ECO:0000256|HAMAP-Rule:MF_01228};
GN   Name=metG {ECO:0000256|HAMAP-Rule:MF_01228};
GN   OrderedLocusNames=Sta7437_0056 {ECO:0000313|EMBL:AFZ33678.1};
OS   Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC   Stanieria.
OX   NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ33678.1, ECO:0000313|Proteomes:UP000010473};
RN   [1] {ECO:0000313|Proteomes:UP000010473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:0000256|ARBA:ARBA00003314,
CC       ECO:0000256|HAMAP-Rule:MF_01228}.
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:0000256|HAMAP-
CC         Rule:MF_01228};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363039}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}.
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DR   EMBL; CP003653; AFZ33678.1; -; Genomic_DNA.
DR   RefSeq; WP_015191351.1; NC_019748.1.
DR   AlphaFoldDB; K9XMG3; -.
DR   STRING; 111780.Sta7437_0056; -.
DR   KEGG; scs:Sta7437_0056; -.
DR   PATRIC; fig|111780.3.peg.54; -.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_9_4_3; -.
DR   OMA; SDMHGTP; -.
DR   OrthoDB; 9810191at2; -.
DR   Proteomes; UP000010473; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00398; metG; 1.
DR   PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_01228};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01228}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01228};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01228};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_01228}; Reference proteome {ECO:0000313|Proteomes:UP000010473}.
FT   DOMAIN          9..148
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          153..367
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          402..510
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           14..24
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   MOTIF           303..307
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ   SEQUENCE   527 AA;  60787 MW;  0C0B4D205392B544 CRC64;
     MKDRFKFALT TPLYYVNDVP HIGSAYTTMV ADVIARFQRL QGNSVLLITG TDEHGQKIER
     TAAEQGLEPQ VHCDRIVASF QSLWEKLNIQ YDRFSRTTAV RHEAIVKEFF ERVWQKGDIY
     LDQQQGWYCV SCEEFKEERD LLEGGFCPLH PNKQVEWRDE ENYFFKLSQY QTQLETLYAQ
     NLDFIQPESR RNEVLNFVSQ GLKDFSISRV NLDWGFPLPS DPNHTIYVWF DALLGYVTAL
     LEPEQEPTLA NALSQWWPIN LHLIGKDILR FHAVYWPAML MSAELPLPKR IFGHGFLTKD
     GKKMSKTLGN TVDPFALVNK YSSDAVRYYF LKGIDFGKDG DFNETRFVEL LNADLADNLG
     NLLNRTLGML KKYCQSNGPQ LTEADLDLEH PLKKIGTGLS DRVFQAYEAL QFSQACEEIF
     NLIRASNKHI DESAPWSLYK QGKQKEVEQI LYAVLESVRL SAYLLSPIIP NLSNDIYQQL
     GFSFDFNHKT HNLADDILIH HSQWGKLTAN QNLSKARPIF SKLELPS
//
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