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
//