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Database: UniProt
Entry: F3NDK1_9ACTN
LinkDB: F3NDK1_9ACTN
Original site: F3NDK1_9ACTN 
ID   F3NDK1_9ACTN            Unreviewed;       547 AA.
AC   F3NDK1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
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=SGM_1215 {ECO:0000313|EMBL:EGG48488.1};
OS   Streptomyces griseoaurantiacus M045.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG48488.1, ECO:0000313|Proteomes:UP000003022};
RN   [1] {ECO:0000313|EMBL:EGG48488.1, ECO:0000313|Proteomes:UP000003022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M045 {ECO:0000313|EMBL:EGG48488.1,
RC   ECO:0000313|Proteomes:UP000003022};
RX   PubMed=21551298; DOI=10.1128/JB.05053-11;
RA   Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT   "Draft genome sequence of the marine bacterium Streptomyces
RT   griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT   with a pABA core component.";
RL   J. Bacteriol. 193:3417-3418(2011).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01228};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-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 2A 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:EGG48488.1}.
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DR   EMBL; AEYX01000022; EGG48488.1; -; Genomic_DNA.
DR   RefSeq; WP_006138791.1; NZ_AEYX01000022.1.
DR   AlphaFoldDB; F3NDK1; -.
DR   STRING; 996637.SGM_1215; -.
DR   eggNOG; COG0143; Bacteria.
DR   Proteomes; UP000003022; 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; 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; 1.
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   Metal-binding {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:UP000003022};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   DOMAIN          14..376
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          389..543
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
FT   MOTIF           21..31
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   MOTIF           313..317
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ   SEQUENCE   547 AA;  60698 MW;  A76AE5DF7988CB46 CRC64;
     MAATGSEKQG AKAYYVSTPI YYVNDAPHLG HAYTTVAGDV LTRWHRQRGE KVWYLTGTDE
     HGQKIMRTAE ANGVTPQAWA DKLVTEAWEP LWEHLDIAND DFIRTTQKRH TDRVQEFVQD
     LHDKGEIYKG GYEGPYCVGC EEYKLPGELL DGEGEFAGQK LCPIHKKPVE ILSEENYFFR
     LSEYTDKLLA HYEANPDFIQ PESARNEVVN FVRQGLQDLS ISRSTFDWGI PIPWDEKHVI
     YVWIDALLNY ATAVGYNENQ EKFEETFPAD VHLVGKDILR FHAVIWPAML MAQGLPLPGK
     VAANGWLMVG GEKMSKSNLT GIKPQDLTTH FGVDAYRWYF LRAIAFGQDG SFSWEDFSAR
     YTSELANDYG NLASRVAAMV GKYFDGELPA STADGEAEAA VRAGLAKAVA EADRRIGEEL
     DFQGGILAVF DFVKQVNGYL TEQEPWKVAK TAFSDAAGAA GSEEGRARLA TILYTAAEAL
     RAVAVLLNPV MPETSQKLWE SLGAEPSLGA LADQRVQEAA DWGRLPAGAK ITKGAVLFPR
     LEEPPTA
//
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