ID A0A0E3NUD9_9EURY Unreviewed; 708 AA.
AC A0A0E3NUD9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=MSMTP_0485 {ECO:0000313|EMBL:AKB23954.1};
OS Methanosarcina sp. MTP4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434100 {ECO:0000313|EMBL:AKB23954.1, ECO:0000313|Proteomes:UP000033049};
RN [1] {ECO:0000313|EMBL:AKB23954.1, ECO:0000313|Proteomes:UP000033049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTP4 {ECO:0000313|EMBL:AKB23954.1,
RC ECO:0000313|Proteomes:UP000033049};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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|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: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC 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|HAMAP-Rule:MF_00098}.
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DR EMBL; CP009505; AKB23954.1; -; Genomic_DNA.
DR RefSeq; WP_048177625.1; NZ_CP009505.1.
DR AlphaFoldDB; A0A0E3NUD9; -.
DR STRING; 1434100.MSMTP_0485; -.
DR GeneID; 24855698; -.
DR KEGG; metm:MSMTP_0485; -.
DR PATRIC; fig|1434100.4.peg.621; -.
DR HOGENOM; CLU_009710_1_2_2; -.
DR OrthoDB; 371856at2157; -.
DR Proteomes; UP000033049; Chromosome.
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:0000049; F:tRNA binding; 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 CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR004495; Met-tRNA-synth_bsu_C.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00398; metG; 1.
DR NCBIfam; TIGR00399; metG_C_term; 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 Pfam; PF01588; tRNA_bind; 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; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS50886; TRBD; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00098};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW 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:UP000033049};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00098};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00098};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00098}.
FT DOMAIN 606..708
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT REGION 558..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 16..26
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT MOTIF 330..334
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT COMPBIAS 560..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 150
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 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
SQ SEQUENCE 708 AA; 79488 MW; 9AB67D729A3B8900 CRC64;
MSKSSDKPVL VTCGLPYANG KAHVGHLRTY VPADIFVRAL KKEGRDVTFV CGSDTHGTPI
VVNAEQLGIT PGELVETYHK HFDETFKQLG VNFDAFGTTD DPENHNRTLE IVNKLIEKDY
VYPKTIEIAY CPKCDRFLPD RYVEGTCPHC GETARGDECD QGCGKHLEPG ELKSPVCTIC
GGPAEYRKQE HFFFKLSEFS DYLMNYLSNE LGGTTNARNY ALGWVKQGLE DWCITRNLEW
GVKFPGHDDL VVYVWVDAPI GYMAFTEEWA AQANDSWEKY WKGDGEIIHF IGGDITYHHC
IFWPAMLKGA DYSVPTDVVA SGMVKIEDKT FSKTRGYVVW VGEDYLDHGF HPDILRYYLA
SYTSHTKELN FSWRVLQEKI NTELVAVLGN FLYRTMLFAF KNYGKIPEGE IEPEVKEKIE
TAINEVNAAM EEYEFKKAVD TAMALASFGN IYFQSHEPWK LIKEDKEACG QVLYNCLQLG
KALTLLFEPV LPGSMENAWK GLGLEGDVHE AQYSDALVPL KAGSGFAKPK ILFTKLEDDK
IGEMEEISSE RVRIAIAKQT GPKEGKEEKE VAKSEGKPPA TEEKAEAKPE EEGEEEENLP
QIEYDDFAKL DIRVGKVLVV EKIKKSKKLL RIEVDIGEPE PRQIVAGMAP YYDPEELVGK
NIIVLANLKP TKLCGVKSNG MMLAADDGGE IVAALMPDKE LKPGSRIR
//