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Database: UniProt
Entry: A0A139SS96_9BACT
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ID   A0A139SS96_9BACT        Unreviewed;       521 AA.
AC   A0A139SS96;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ORFNames=AXK12_01690 {ECO:0000313|EMBL:KXU37417.1};
OS   Cephaloticoccus capnophilus.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC   Cephaloticoccus.
OX   NCBI_TaxID=1548208 {ECO:0000313|EMBL:KXU37417.1, ECO:0000313|Proteomes:UP000071392};
RN   [1] {ECO:0000313|EMBL:KXU37417.1, ECO:0000313|Proteomes:UP000071392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CV41 {ECO:0000313|EMBL:KXU37417.1,
RC   ECO:0000313|Proteomes:UP000071392};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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: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       MetG type 2B subfamily. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXU37417.1}.
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DR   EMBL; LSZP01000008; KXU37417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139SS96; -.
DR   STRING; 1548208.AXK12_01690; -.
DR   OrthoDB; 9810191at2; -.
DR   Proteomes; UP000071392; Unassembled WGS sequence.
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; 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; 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; PF19303; Anticodon_3; 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:UP000071392}.
FT   DOMAIN          5..136
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          152..357
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          371..514
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
FT   MOTIF           11..21
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ   SEQUENCE   521 AA;  59138 MW;  5676B03D9C41879D CRC64;
     MPDFYITTAI DYVNGPPHLG HAYEKVLTDV IARVRRMRGD RVYFLTGVDE HGQKVQQSAR
     ARGVAPQQFC DEIAAEFRAL LPRLDVSNDD FIRTTEARHK RVVCDLLQRL YDKGEIYKAE
     YRGYYSTRQE QFLQEKDRNP DGTWPELFGE VTEITESNYF FKLSAYQDWL VRFLTENEAF
     VFPKFRQKQV LEFLKEPLND LCISRPKERL EWGIPLPFDA DFVTYVWFDA LTNYYSAVAD
     KEPAIWPATW HVIGKDILVP PHAVYWPIML KAADIPLPRG IIAHGWWSIR GDKMAKSTGN
     FVEPNAFVDS YGTDALRYFL MREMVVGQDS DFSETQFQAR YNADLANNLG NLLNRTLNMI
     NRFADGVVPA PEGAAEAAAP EAELRALWEE TRAAIPAHWD GFQFHLALER TITFVSATNA
     YIEKRAPWKL GKSSEPADRA LLVRTLATMA EALRLAAVLL RPIIPGSVAK IEAALGYTPP
     ETDWAAECEW GTRLSGAKVA ESLVLFPRIQ ATTSAEAAPK K
//
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