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Database: UniProt
Entry: A0A166SB10_9RHOB
LinkDB: A0A166SB10_9RHOB
Original site: A0A166SB10_9RHOB 
ID   A0A166SB10_9RHOB        Unreviewed;       570 AA.
AC   A0A166SB10;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   ORFNames=A3721_19020 {ECO:0000313|EMBL:KZY02958.1};
OS   Sulfitobacter sp. HI0023.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1822225 {ECO:0000313|EMBL:KZY02958.1, ECO:0000313|Proteomes:UP000077323};
RN   [1] {ECO:0000313|EMBL:KZY02958.1, ECO:0000313|Proteomes:UP000077323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0023 {ECO:0000313|EMBL:KZY02958.1,
RC   ECO:0000313|Proteomes:UP000077323};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-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_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}.
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:KZY02958.1}.
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DR   EMBL; LWEQ01000161; KZY02958.1; -; Genomic_DNA.
DR   RefSeq; WP_067922335.1; NZ_LWEQ01000161.1.
DR   AlphaFoldDB; A0A166SB10; -.
DR   OrthoDB; 9810191at2; -.
DR   Proteomes; UP000077323; 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: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; 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; 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   NCBIfam; TIGR00398; metG; 1.
DR   PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   Pfam; PF19303; Anticodon_3; 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.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {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:UP000077323};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00098}.
FT   DOMAIN          4..407
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          419..570
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
FT   COILED          433..460
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           11..21
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   MOTIF           344..348
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         347
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
SQ   SEQUENCE   570 AA;  63642 MW;  C5E7AB33A7C09980 CRC64;
     MTRHLITSAL PYINGIKHLG NLVGSQLPAD LFARYLRARG HEVLFLCATD EHGTPAELAA
     AKAGLPVAEY CAQLHEQQAE IAAGFGLSFD HFGRSSSAQN HRLTQHFAGA LADAGLIEEV
     TQRQVYSVAD ARFLPDRYIE GTCPNCGYDS ARGDQCDNCT KQLDPTDLIE PRSTISGSTE
     LETRETKHLF LRQSRMKDDL DSWIRGKEDW PVLTTSIAKK WLHDGDGLQD RGITRDLDWG
     VPVRKGDAPW PGMEGKVFYV WFDAPIEYIA AAQEWVDAGK GSDWESWWRT DRGADDVRYT
     QFMGKDNVPF HTLSFPATIM GSGEPWKLVD YIKSFNYLNY DGGQFSTSRG RGVFQDQALS
     LLPADYWRWW LLSHAPETSD AEFTWENFQA SVNKDLADVL GNFVSRITKF CRSKFGETVP
     EAGAYGPAEE ALIADLTERV ARYEAQMDAI EVRKSAQELR AIWAAGNEYL QAQAPWTTFK
     TDPDRAAAQV RLALNLIPLY AVLSAPFVPE AARTMLEAMG APDAGWPGNV KTTLGQLPPG
     HAFTVPEVLF AKITDEQRED WETRFAGTRD
//
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