ID A0A0N7Z3W3_9CYAN Unreviewed; 531 AA.
AC A0A0N7Z3W3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=NIES2104_09360 {ECO:0000313|EMBL:GAP94425.1};
OS Leptolyngbya sp. NIES-2104.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP94425.1, ECO:0000313|Proteomes:UP000052243};
RN [1] {ECO:0000313|EMBL:GAP94425.1, ECO:0000313|Proteomes:UP000052243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP94425.1,
RC ECO:0000313|Proteomes:UP000052243};
RX PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA Kawachi M.;
RT "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL DNA Res. 22:403-412(2015).
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 -!- 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 {ECO:0000256|RuleBase:RU363039}.
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:GAP94425.1}.
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DR EMBL; BBWW01000001; GAP94425.1; -; Genomic_DNA.
DR RefSeq; WP_058996036.1; NZ_BBWW01000001.1.
DR AlphaFoldDB; A0A0N7Z3W3; -.
DR STRING; 1552121.NIES2104_09360; -.
DR InParanoid; A0A0N7Z3W3; -.
DR OrthoDB; 9810191at2; -.
DR Proteomes; UP000052243; 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: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; 2.
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 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}.
FT DOMAIN 12..143
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 145..369
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 402..523
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
FT MOTIF 17..27
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT MOTIF 306..310
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ SEQUENCE 531 AA; 60732 MW; FEE2BF69D7A26D64 CRC64;
MTLSLEKPNF ALTTPLYYVN DLPHIGSAYP TIAADAMARF QRLLGKPVRF VTGSDEHGQK
IQRTAESLGR KPQEHCDLVV EGFKRLWTQL DIQYDRFIRT TEERHHAIVK EFFQRVWDNG
DIYLSQQKGW YCVSCEEFKE ERELLEGNRC SIHTTKEVEW RDEENYFFRL SNYQEKLEKL
YAEHPEFIEP DIRRNEVLSF VSQGLRDFSV SRVNFDWGFP IPTDPKHTIY VWFDALLGYI
TALLDPDQEP TLENATSKWY PFNVHIIGKD ILRFHAVYFP AMLMSAGLPL PYKVFGHGFL
VRDGVKMGKS SGNAIDPVAL VERYGVDAFR YYFLKGIEFG RDGVFDETRF VDMCNADLAD
GFGNLLNRSL GLIHKNSGGV VPDVEISEDH PLRSIAEGLS DRVANAYDSL AFNVACEEVL
TLIRLGNKYI NEQAPWSLYK AGKNQEAEEV LYAVLESVRL AAYLLAPIIP RTSTAVYQQL
GLNVDFNDAS LIDVSITFPN QARWGILRAK QALQKPQPVF QKLELPVESS P
//
