ID S5R8E1_9PROT Unreviewed; 576 AA.
AC S5R8E1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00098};
DE EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_00098};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00098};
DE Short=MetRS {ECO:0000256|HAMAP-Rule:MF_00098};
GN Name=metG {ECO:0000256|HAMAP-Rule:MF_00098,
GN ECO:0000313|EMBL:AGS06845.1};
GN ORFNames=SSDC_00760 {ECO:0000313|EMBL:AGS06845.1};
OS Candidatus Profftella armatura.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Profftella.
OX NCBI_TaxID=669502 {ECO:0000313|EMBL:AGS06845.1, ECO:0000313|Proteomes:UP000015216};
RN [1] {ECO:0000313|EMBL:AGS06845.1, ECO:0000313|Proteomes:UP000015216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC {ECO:0000313|EMBL:AGS06845.1,
RC ECO:0000313|Proteomes:UP000015216};
RX PubMed=23850282; DOI=10.1016/j.cub.2013.06.027;
RA Nakabachi A., Ueoka R., Oshima K., Teta R., Mangoni A., Gurgui M.,
RA Oldham N.J., van Echten-Deckert G., Okamura K., Yamamoto K., Inoue H.,
RA Ohkuma M., Hongoh Y., Miyagishima S.Y., Hattori M., Piel J., Fukatsu T.;
RT "Defensive bacteriome symbiont with a drastically reduced genome.";
RL Curr. Biol. 23:1478-1484(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_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;
CC Evidence={ECO:0000256|ARBA:ARBA00001234, ECO:0000256|HAMAP-
CC Rule:MF_00098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00098};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00098};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00098}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00098}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 1 subfamily. {ECO:0000256|ARBA:ARBA00008258,
CC ECO:0000256|HAMAP-Rule:MF_00098}.
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DR EMBL; CP003468; AGS06845.1; -; Genomic_DNA.
DR AlphaFoldDB; S5R8E1; -.
DR STRING; 669502.SSDC_00760; -.
DR KEGG; ssdc:SSDC_00760; -.
DR PATRIC; fig|669502.6.peg.149; -.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_7_0_4; -.
DR OrthoDB; 9810191at2; -.
DR Proteomes; UP000015216; Chromosome.
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 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; IPR001412; aa-tRNA-synth_I_CS.
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; 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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00098};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00098};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00098};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00098};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00098};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00098}; Reference proteome {ECO:0000313|Proteomes:UP000015216};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00098}.
FT DOMAIN 14..420
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT MOTIF 21..31
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT MOTIF 355..359
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
SQ SEQUENCE 576 AA; 68064 MW; EAB5991934782772 CRC64;
MKKHDSEFKD VRRIFVTTAL PYANGELHIG HIMEYIQADI WVRFQCMQQD NGKSRQVYFI
CADDAHGAAI MIAAEKAGMT PKEFINNISS NRKKYLDGFY IKFDNWYSTD SIENIDLVQK
IYDTLYNKAK LIINKKINQF FDPIKNIFLP DRYIKGECPI CNAKDQYGDF CECCSSIYTP
TKLINPYSIL SGTKPIIKSS KHFFFKLSDK RCIDFLRKWA IHDKRLQPEI VNKIKEWLEK
DNKFNDWDIS RDAPYFGIKI PNTLEKYFYV WLDAPIGYLA SLKNFFEKGG PKKKYNELRN
FDEFISSPNT EQYHFIGKDI FYFHILFWPA ILKFSGRKLP NNIFVHGFMT INGKKMSKSN
KIGISPLYYL KIGMNPEWLR YYIASKLNNK IEDIDFNSQS FISCVNSDLI GKYINIASRS
SSFIEKYFKG YLNMKWVKDN DTFLSKLRVV SSSIQKYYEN RNFNKVLYIV IEQTNFINIF
FDQNKPWKLA KNNIYHEKLH KISSRLLEAF RILTIYLKPI LPNLAKSVET FLNISPLQWI
NIFTPLTQNH KINKYRHLMT RVDKNIVDNL LKNKNI
//
