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Database: UniProt
Entry: T1AXF2_9ZZZZ
LinkDB: T1AXF2_9ZZZZ
Original site: T1AXF2_9ZZZZ 
ID   T1AXF2_9ZZZZ            Unreviewed;       185 AA.
AC   T1AXF2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
DE   Flags: Fragment;
GN   ORFNames=B1B_07393 {ECO:0000313|EMBL:EQD62147.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD62147.1};
RN   [1] {ECO:0000313|EMBL:EQD62147.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mendez C., Richter M., Ferrer M., Sanchez J.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EQD62147.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA   Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA   Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA   Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA   Ferrer M.;
RT   "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT   along an acid mine drainage.";
RL   ISME J. 8:1259-1274(2014).
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};
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:EQD62147.1}.
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DR   EMBL; AUZY01004707; EQD62147.1; -; Genomic_DNA.
DR   AlphaFoldDB; T1AXF2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR   InterPro; IPR023458; Met-tRNA_ligase_1.
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   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; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000313|EMBL:EQD62147.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          4..185
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   NON_TER         185
FT                   /evidence="ECO:0000313|EMBL:EQD62147.1"
SQ   SEQUENCE   185 AA;  20766 MW;  ACA45D4230B27BE8 CRC64;
     MQRILVNCAL PYANSPLHLG HIAGSYLGAD IFVRALRLMG EDVLFVCGTD EYGTPITIQA
     DREHVTPSEI ADRYHAEHER SFEKIQIRFD IFSRTTSAAH KENASELFTR LYNGGYLTKG
     SMISPYCKTC GKFMPDRYIE GTCPYCGNTR ARGDQCDSCG RILDPQDLIE PRCIVSGDAP
     EFRET
//
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