SYM_YERPB
ID SYM_YERPB Reviewed; 675 AA.
AC B2JZK3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00098};
DE EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_00098};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00098};
DE Short=MetRS {ECO:0000255|HAMAP-Rule:MF_00098};
GN Name=metG {ECO:0000255|HAMAP-Rule:MF_00098}; OrderedLocusNames=YPTS_1644;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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: Homodimer. {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; CP001048; ACC88613.1; -; Genomic_DNA.
DR RefSeq; WP_012413632.1; NZ_CP009780.1.
DR AlphaFoldDB; B2JZK3; -.
DR SMR; B2JZK3; -.
DR KEGG; ypb:YPTS_1644; -.
DR PATRIC; fig|502801.10.peg.1015; -.
DR OMA; SDMHGTP; -.
DR BioCyc; YPSE502801:YPTS_RS08400-MON; -.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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 CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR Gene3D; 2.20.28.20; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR004495; Met-tRNA-synth_bsu_C.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002547; tRNA-bd_dom.
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 Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF57770; SSF57770; 1.
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; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..675
FT /note="Methionine--tRNA ligase"
FT /id="PRO_1000093745"
FT DOMAIN 573..675
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT MOTIF 15..25
FT /note="'HIGH' region"
FT MOTIF 332..336
FT /note="'KMSKS' region"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT BINDING 162
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 675 AA; 75650 MW; 8307E106EBC60B3B CRC64;
MAQVAKKILV TCALPYANGS IHLGHMLEHI QADIWVRFQR MRGNQVHFIC ADDAHGTPIM
LKAQQMGIEP EQMIAEMSQE HQQDFAGFAI SYDNYHSTHS DENRELSSLI YGRLKANGYI
KNRTISQLYD PEKGMFLPDR FVKGTCPKCK APEQYGDNCE VCGATYSPTE LIDPKSAVSG
ATPVMRESEH FFFDLPAFSD MLQAWTRSGA LQEQVANKMQ EWFDSGLQQW DITRDAPYFG
FEVPDAPGKY FYVWLDAPIG YMGAFKNLCD KRGDLDFDEF WGKDAKTDLY HFIGKDIVYF
HSLFWPAMLE GSNFRKPTNL FVHGYVTVNG AKMSKSRGTF IKAGTYLKYL DADCLRYYYA
AKLSSRIDDI DLNLEDFVQR VNADIVNKVV NLASRNAGFI NKRFAGQLAD QLADPVLYKT
FTDAATSIAD AYNNRESGKA IREIMALADV ANRYVDEQAP WVVAKQEGRD ADLHAICSMG
INLFRVLMTY LKPVLPSLTE RTEAFLNTEL TWDSIEQPLL GHSITAFKAL FNRIDLDKVN
EMVASSKEDM APATRVTGPL ADDPIQETIS FDDFAKVDMR IALIQQAEFV EGSDKLLKLT
LELGGETRQI FSGIRSAYPD PKALEGRMTV MVANLAPRKM RFGVSEGMVM AAGPGGSDIF
LLSPDSGAQP GMQVK
