SYM_THET8
ID SYM_THET8 Reviewed; 618 AA.
AC P23395; Q5SIR6;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Methionine--tRNA ligase;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=metG; Synonyms=metS; OrderedLocusNames=TTHA1298;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1993699; DOI=10.1016/s0021-9258(18)49984-x;
RA Nureki O., Muramatsu T., Suzuki K., Kohda D., Matsuzawa H., Ohta T.,
RA Miyazawa T., Yokoyama S.;
RT "Methionyl-tRNA synthetase gene from an extreme thermophile, Thermus
RT thermophilus HB8. Molecular cloning, primary-structure analysis, expression
RT in Escherichia coli, and site-directed mutagenesis.";
RL J. Biol. Chem. 266:3268-3277(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10673435; DOI=10.1016/s0969-2126(00)00095-2;
RA Sugiura I., Nureki O., Ugaji-Yoshikawa Y., Kuwabara S., Shimada A.,
RA Tateno M., Lorber B., Giege R., Moras D., Yokoyama S., Konno M.;
RT "The 2.0-A crystal structure of Thermus thermophilus methionyl-tRNA
RT synthetase reveals two RNA-binding modules.";
RL Structure 8:197-208(2000).
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.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 2A subfamily. {ECO:0000305}.
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DR EMBL; M64273; AAA27510.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71121.1; -; Genomic_DNA.
DR RefSeq; WP_011228577.1; NC_006461.1.
DR RefSeq; YP_144564.1; NC_006461.1.
DR PDB; 1A8H; X-ray; 2.00 A; A=1-500.
DR PDB; 1WOY; X-ray; 2.00 A; A=1-500.
DR PDB; 2D54; X-ray; 2.00 A; A=1-502.
DR PDB; 2D5B; X-ray; 1.80 A; A=1-500.
DR PDB; 3VU8; X-ray; 2.20 A; A=1-502.
DR PDBsum; 1A8H; -.
DR PDBsum; 1WOY; -.
DR PDBsum; 2D54; -.
DR PDBsum; 2D5B; -.
DR PDBsum; 3VU8; -.
DR AlphaFoldDB; P23395; -.
DR SMR; P23395; -.
DR STRING; 300852.55772680; -.
DR ChEMBL; CHEMBL1641341; -.
DR EnsemblBacteria; BAD71121; BAD71121; BAD71121.
DR GeneID; 3169329; -.
DR KEGG; ttj:TTHA1298; -.
DR PATRIC; fig|300852.9.peg.1276; -.
DR eggNOG; COG0073; Bacteria.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_9_4_0; -.
DR OMA; SDMHGTP; -.
DR PhylomeDB; P23395; -.
DR EvolutionaryTrace; P23395; -.
DR PRO; PR:P23395; -.
DR Proteomes; UP000000532; 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-KW.
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; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR004495; Met-tRNA-synth_bsu_C.
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; 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 PANTHER; PTHR43326; PTHR43326; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR TIGRFAMs; TIGR00399; metG_C_term; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..618
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139258"
FT DOMAIN 518..618
FT /note="tRNA-binding"
FT MOTIF 12..22
FT /note="'HIGH' region"
FT MOTIF 297..301
FT /note="'KMSKS' region"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 615..618
FT /note="AVVK -> RW (in Ref. 1; AAA27510)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 20..38
FT /evidence="ECO:0007829|PDB:2D5B"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 67..84
FT /evidence="ECO:0007829|PDB:2D5B"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:2D5B"
FT STRAND 117..127
FT /evidence="ECO:0007829|PDB:2D5B"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:2D5B"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1A8H"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:2D5B"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:2D5B"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:2D5B"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:2D5B"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2D5B"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:2D5B"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:2D5B"
FT TURN 237..242
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:2D5B"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 268..276
FT /evidence="ECO:0007829|PDB:2D5B"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:2D5B"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 317..327
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 354..367
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 400..421
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:2D5B"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 431..452
FT /evidence="ECO:0007829|PDB:2D5B"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 457..466
FT /evidence="ECO:0007829|PDB:2D5B"
FT HELIX 475..479
FT /evidence="ECO:0007829|PDB:2D5B"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:2D54"
SQ SEQUENCE 618 AA; 70693 MW; 920A449052C62558 CRC64;
MEKVFYVTTP IYYVNAEPHL GHAYTTVVAD FLARWHRLDG YRTFFLTGTD EHGETVYRAA
QAAGEDPKAF VDRVSGRFKR AWDLLGIAYD DFIRTTEERH KKVVQLVLKK VYEAGDIYYG
EYEGLYCVSC ERFYTEKELV EGLCPIHGRP VERRKEGNYF FRMEKYRPWL QEYIQENPDL
IRPEGYRNEV LAMLAEPIGD LSISRPKSRV PWGIPLPWDE NHVTYVWFDA LLNYVSALDY
PEGEAYRTFW PHAWHLIGKD ILKPHAVFWP TMLKAAGIPM YRHLNVGGFL LGPDGRKMSK
TLGNVVDPFA LLEKYGRDAL RYYLLREIPY GQDTPVSEEA LRTRYEADLA DDLGNLVQRT
RAMLFRFAEG RIPEPVAGEE LAEGTGLAGR LRPLVRELKF HVALEEAMAY VKALNRYINE
KKPWELFKKE PEEARAVLYR VVEGLRIASI LLTPAMPDKM AELRRALGLK EEVRLEEAER
WGLAEPRPIP EEAPVLFPKK EAKVEAKPKE EAWIGIEDFA KVELRVAEVL AAEKHPNADR
LLVLRLSLGN EERTVVSGIA KWYRPEELVG KKVVLVANLK PAKLRGIESQ GMILAAQEGE
ALALVTVEGE VPPGAVVK
