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Database: UniProt
Entry: A0A0S8AH03_9BACT
LinkDB: A0A0S8AH03_9BACT
Original site: A0A0S8AH03_9BACT 
ID   A0A0S8AH03_9BACT        Unreviewed;       280 AA.
AC   A0A0S8AH03;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Methionyl-tRNA synthetase {ECO:0000313|EMBL:KPJ97932.1};
DE   Flags: Fragment;
GN   ORFNames=AMK71_12235 {ECO:0000313|EMBL:KPJ97932.1};
OS   Nitrospira bacterium SG8_35_4.
OC   Bacteria; Nitrospirota; Nitrospiria.
OX   NCBI_TaxID=1704025 {ECO:0000313|EMBL:KPJ97932.1, ECO:0000313|Proteomes:UP000050997};
RN   [1] {ECO:0000313|EMBL:KPJ97932.1, ECO:0000313|Proteomes:UP000050997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_35_4 {ECO:0000313|EMBL:KPJ97932.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363039}.
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:KPJ97932.1}.
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DR   EMBL; LJTM01000257; KPJ97932.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8AH03; -.
DR   PATRIC; fig|1704025.3.peg.1656; -.
DR   Proteomes; UP000050997; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
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   PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363039}.
FT   DOMAIN          6..150
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          156..280
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   NON_TER         280
FT                   /evidence="ECO:0000313|EMBL:KPJ97932.1"
SQ   SEQUENCE   280 AA;  32600 MW;  D84B31509BEC17AF CRC64;
     MEHSKFYITT PIYYVNDVPH IGHAYTTIAA DILARYHRLR GKKVFFLTGT DEHGQKVEKA
     AALKSRTPKE HADIMVENFK ALWEKLNISN DAFIRTTDEE HVKTVQGIIQ LLWDRGEIEK
     RKYSGWYCTP DERFWTEKEI VEGNCPDCGR PVEEIQEENY FFLMSKYQKT LIAHIESADP
     PYILPETRKN EVLGFLKNNE LGDLCITRPK SRLSWGVPIP FDNDFVTYVW FDALLNYFSA
     TRYLAPGAEN AKLGDFWWPA DHHLVGKDIL TTHAVYWSTM
//
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