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Database: UniProt
Entry: A0A133XXL3_9ACTN
LinkDB: A0A133XXL3_9ACTN
Original site: A0A133XXL3_9ACTN 
ID   A0A133XXL3_9ACTN        Unreviewed;       673 AA.
AC   A0A133XXL3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN   ORFNames=HMPREF3192_00101 {ECO:0000313|EMBL:KXB35695.1};
OS   Atopobium deltae.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Atopobium.
OX   NCBI_TaxID=1393034 {ECO:0000313|EMBL:KXB35695.1, ECO:0000313|Proteomes:UP000070675};
RN   [1] {ECO:0000313|Proteomes:UP000070675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00019 {ECO:0000313|Proteomes:UP000070675};
RA   Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA   O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA   Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 1 subfamily. {ECO:0000256|ARBA:ARBA00008258}.
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:KXB35695.1}.
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DR   EMBL; LSCR01000001; KXB35695.1; -; Genomic_DNA.
DR   RefSeq; WP_066304377.1; NZ_KQ959483.1.
DR   AlphaFoldDB; A0A133XXL3; -.
DR   STRING; 1393034.HMPREF3192_00101; -.
DR   PATRIC; fig|1393034.3.peg.96; -.
DR   OrthoDB; 9810191at2; -.
DR   Proteomes; UP000070675; 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:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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; IPR029038; MetRS_Zn.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
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|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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070675}.
FT   DOMAIN          16..254
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          311..468
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
SQ   SEQUENCE   673 AA;  76328 MW;  6911E69BF5C86833 CRC64;
     MSVDMSKRPS FPKRAVITAG MPYGNKNLHF GHIGGVFVPA DFFARFLRDR IGASNVVFVS
     GTDCYGSPIM EGYRKLKEQQ NYEGSILDYV QENHDAQKHA LNAYHISLDL YSGSGLEPAK
     SFHNKMSQRV ITRLYERGYL HKLSTMQFYD PQAEQFLNGR QVMGRCPIRG CKSEKAYADE
     CDLGHQFDPE ELIAPVSQLT GATPELRPVA NWYFDLPKFH ADLEKVMRDW DADPQVRSVV
     TKTARESLAQ PCIYIQTRYR DEFEAIREQL PSHSLTEATQ NQSSFSVSFA DWEARDTARS
     VLEEKSIRFR TGKTLLPFRI TGNIDWGIPA PELEGLRDLT VWCWPESLWA PISFTQTALA
     CDTNGHFSSH DWSDWWRADD AAVYQFIGQD NIYFYCVVQP ALWNALAWDW FQDTPVANYH
     ILFMNKKASS SGAIKPPMAE ELLENYTAEQ LRCHWLSLAL DQKAVSFAPK TYDISVSHVD
     KKTGEEILVK DDPRVVDPAL KESAFLTNIF NRLARSCFYG AQNACGGMLP DATPSQEVLD
     ECTSALLDFE QAASVFDAHT ALSIAEKFTR DANKRWDSAS KAGREDQALY VQALADAFAQ
     LRCATLLMHP AAPDGCELIC QYLNFDPEQF FSWDNAFKTP QELAQLAGQN PAEHVLRTLR
     ARFDFFSKHK TQK
//
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