SYM_COXB1
ID SYM_COXB1 Reviewed; 546 AA.
AC B6J4V8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=CbuK_0316;
OS Coxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain Q154)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434924;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CbuK_Q154;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
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; CP001020; ACJ19623.1; -; Genomic_DNA.
DR RefSeq; WP_005770550.1; NC_011528.1.
DR AlphaFoldDB; B6J4V8; -.
DR SMR; B6J4V8; -.
DR KEGG; cbc:CbuK_0316; -.
DR HOGENOM; CLU_009710_7_0_6; -.
DR OMA; SDMHGTP; -.
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; IPR001412; aa-tRNA-synth_I_CS.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Zinc.
FT CHAIN 1..546
FT /note="Methionine--tRNA ligase"
FT /id="PRO_1000093709"
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 546 AA; 62243 MW; 9156A0B31B96728C CRC64;
MTTEKRQILV TAALPYANGP IHLGHMVEHI QADIWVRFQR LKGNDCLFIC GEDAHGTAIM
ITAQKQGLPP EALVAKMHKE HARDLGGFLI EYDNFYTTHS PENRELAELI YTRLKDKGDI
FAKTISQAYD PVKEIFLPDR FIRGTCPRCG AKDQYGDVCE VCGATYSPTE LIDPVSALSG
AKPIEKNSEH FFFSLNRYTQ LLKKWIDAGH LQPQVANKLK EWFSEDLKPW DISRDAPYFG
FEIPHAANKY FYVWLDAPIG YMASLKNLSK QRPSVNFDAY WKEGSQTELY HFVGKDIVYF
HALFWPAMLS SAGFRLPTAI YVHGYLTVNG QKMSKSRGTF ITAHHYLDHL SPEYLRYYYA
AKLSAQVEDI DLNLDDFIQR VNADLIGKYV NLASRCAGFI TKNFGGKLAN ELPEPDLYES
FLQTEQTITD YYESLNYSKA VRVIMSLADR ANQYIDAKKP WALAKEINQE AQVQAVCTQG
LNLFKILTTY LKPILPVTAK KVEQFLNCDE LNFANLKTPL LDHSVNPFEP LMQRLLPETA
AQLTHE
