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Database: UniProt
Entry: A0A0Q0UHW2_9CORY
LinkDB: A0A0Q0UHW2_9CORY
Original site: A0A0Q0UHW2_9CORY 
ID   A0A0Q0UHW2_9CORY        Unreviewed;       609 AA.
AC   A0A0Q0UHW2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
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   ECO:0000313|EMBL:KQB85992.1};
GN   ORFNames=Clow_01734 {ECO:0000313|EMBL:KQB85992.1};
OS   Corynebacterium lowii.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB85992.1, ECO:0000313|Proteomes:UP000050488};
RN   [1] {ECO:0000313|EMBL:KQB85992.1, ECO:0000313|Proteomes:UP000050488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML 130206 {ECO:0000313|EMBL:KQB85992.1,
RC   ECO:0000313|Proteomes:UP000050488};
RA   Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S.,
RA   Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H.,
RA   Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.;
RT   "Corynebacteirum lowii and Corynebacterium oculi species nova, derived from
RT   human clinical disease and and emended description of Corynebacterium
RT   mastiditis.";
RL   Submitted (OCT-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:KQB85992.1}.
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DR   EMBL; LKEV01000005; KQB85992.1; -; Genomic_DNA.
DR   RefSeq; WP_055178323.1; NZ_LKEV01000005.1.
DR   AlphaFoldDB; A0A0Q0UHW2; -.
DR   STRING; 1544413.Clow_01734; -.
DR   PATRIC; fig|1544413.3.peg.1743; -.
DR   OrthoDB; 9810191at2; -.
DR   Proteomes; UP000050488; 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:UP000050488};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00098}.
FT   DOMAIN          5..411
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          422..528
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
FT   MOTIF           12..22
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   MOTIF           348..352
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT   BINDING         351
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
SQ   SEQUENCE   609 AA;  67415 MW;  6955880456E666AF CRC64;
     MTKTVLVSVA WPYANGPRHI GHVAGFGVPS DVFARYQRMQ GAEVLMVSGT DEHGTPLLVQ
     ADKEGVSVKE LADRYNRQIV QDLAGLGLSY DLFTRTTTRN HYAVVQELFK GLHENGYMIK
     QTTMGAVSPK TGRTLPDRYI EGTCPICGSE GARGDQCDNC GNQLDPVDLI KPVSKIDGET
     PEFIETEHFL LDLPSLAEAL EKWLSTRESW RPNVLKFSLN LLRDLHPRAM TRDIDWGIPV
     PVEGWQDNNA KKLYVWFDAV VGYLSASIEW AWRSGEPEAW KKFWQNPEAE AYYFMGKDNI
     TFHSQIWPAE LLGYAGKGSK GGSLHPYGEL NLPTEVVSSE FLTMSGSKFS SSKGVVIYVK
     DFLEEFGPDP LRYFIAVAGP ENTDTDFTWD EFVRRINNEL ANGWGNLVNR TVSMAHKNFG
     EVPAPGALTA EDEAILNLAH ESLATVGEHL EQSKFKAGIN AAMHVVGEAN AYIASQEPWK
     LAKDEAQRER LATVLWTALQ VVSDCNVMLT PYLPATAQQV HETLGREGIW AAQPQVSEVT
     DDMPVELVGV GLPEEGQSYP VISGDYAAQQ ARWERVEVVP GTALAKPKPL IQKLDPELAQ
     TGPAWAPVE
//
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