ID A0A0V8S7Z4_9CELL Unreviewed; 595 AA.
AC A0A0V8S7Z4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00098};
DE EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_00098};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00098};
DE Short=MetRS {ECO:0000256|HAMAP-Rule:MF_00098};
GN Name=metG {ECO:0000256|HAMAP-Rule:MF_00098};
GN ORFNames=ATM99_00040 {ECO:0000313|EMBL:KSW16378.1};
OS Cellulomonas sp. B6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW16378.1, ECO:0000313|Proteomes:UP000054319};
RN [1] {ECO:0000313|EMBL:KSW16378.1, ECO:0000313|Proteomes:UP000054319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B6 {ECO:0000313|EMBL:KSW16378.1,
RC ECO:0000313|Proteomes:UP000054319};
RA Piccinni F.E., Campos E.;
RT "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas strain
RT Isolated from Decaying Forest Soil.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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_00098}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00098};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00098};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00098}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00098}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 1 subfamily. {ECO:0000256|ARBA:ARBA00008258,
CC ECO:0000256|HAMAP-Rule:MF_00098}.
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:KSW16378.1}.
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DR EMBL; LNTD01000203; KSW16378.1; -; Genomic_DNA.
DR RefSeq; WP_062103805.1; NZ_LNTD01000203.1.
DR AlphaFoldDB; A0A0V8S7Z4; -.
DR STRING; 1295626.ATM99_00040; -.
DR OrthoDB; 9810191at2; -.
DR Proteomes; UP000054319; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
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 InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 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_00098};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00098}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00098};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00098};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00098};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00098}; Reference proteome {ECO:0000313|Proteomes:UP000054319};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00098}.
FT DOMAIN 7..410
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 421..529
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
FT MOTIF 11..21
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT MOTIF 347..351
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
SQ SEQUENCE 595 AA; 66811 MW; 1969A2918E7EAE09 CRC64;
MSRILSAVAW PYANGPRHIG HVAGFGIPSD VFSRYMRMAG HDVLMVSGTD EHGTPILVQA
DKEGVTAQEL ADRYNRVIVE DLTQLGLSYD LFTRTTTRNH YAVVQEMFRT VHKNGYMVER
TTMGAVSPST GRTLPDRYIE GTCPICGYDG ARGDQCDNCG NQLDAIELKN PRSKINGETP
KFVESEHFFL DLPAFVDALG DWLRTRTEWR PNVLKFSLNL LDDVRPRAMT RDIDWGIPVP
LDGWEQNPGK RLYVWFDAVI GYLSASIEWA RRTGDPEAWR QFWNDTDARS YYFMGKDNIT
FHSQIWPAEL LGYAGRGSKG GAPGPYGLLN LPTEVVSSEF LNVEGKQFST SRGLVILVRD
MLARYQPDAL RYYISVAGPE TQDVDFTWAE FKRRTNDELV AGWGNLVNRT ASMVHKNFGE
IPTPGPRLAV DEALTAEITT AFGRVGDLVG THRQRQALQE AMRVVGEANR YVSETEPWKL
KNDRERLATV LHTTTQAVSD LNTLLAPFLP HSAQAVHEAL GGTGTFSPQP RIEEVTDLDD
DTRHYPVITG DYRSVRGTWQ PRAVVPGTKV DKPTPVFTKL DDAIVEEELE RLRQS
//
