SYM_HELPJ
ID SYM_HELPJ Reviewed; 656 AA.
AC Q9ZKG9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Methionine--tRNA ligase;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=metG; OrderedLocusNames=jhp_0967;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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:0000250}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 2A subfamily. {ECO:0000305}.
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DR EMBL; AE001439; AAD06543.1; -; Genomic_DNA.
DR PIR; H71867; H71867.
DR RefSeq; WP_001172571.1; NC_000921.1.
DR AlphaFoldDB; Q9ZKG9; -.
DR SMR; Q9ZKG9; -.
DR STRING; 85963.jhp_0967; -.
DR EnsemblBacteria; AAD06543; AAD06543; jhp_0967.
DR KEGG; hpj:jhp_0967; -.
DR eggNOG; COG0073; Bacteria.
DR eggNOG; COG0143; Bacteria.
DR OMA; SDMHGTP; -.
DR Proteomes; UP000000804; 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; 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; 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; PF09334; tRNA-synt_1g; 2.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..656
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139222"
FT DOMAIN 555..656
FT /note="tRNA-binding"
FT MOTIF 11..21
FT /note="'HIGH' region"
FT MOTIF 301..305
FT /note="'KMSKS' region"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 656 AA; 75433 MW; 8F22F3BA1F9B9756 CRC64;
MQKSLITTPI YYVNDIPHIG HAYTTLIADT LKKYYTLQGE EVFFLTGTDE HGQKIEQSAR
LRNQSPKAYA DSISAIFKNQ WDFFNLDYDG FIRTTDSEHQ KCVQNAFEIM FEKGDIYKGT
YSGYYCVSCE SYCAVSKVDN TDSKVLCPDC LRETTLLEEE SYFFKLSAYE KPLLEFYAKN
PEAILPIYRK NEVTSFIEQG LLDLSITRTS FEWGIPLPKK MNDPKHVVYV WLDALLNYAS
ALGYLNGLDN KMAHFERARH IVGKDILRFH AIYWPAFLMS LNLPLFKQLC VHGWWTIEGV
KMSKSLGNVL DAQKLAMEYG IEELRYFLLR EVPFGQDGDF SKKALVERIN ANLNNDLGNL
LNRLLGMAKK YFNYSLKSTK ITAYYPKELE KAHQILDNAN SFVPKMQLHK ALEELFNIYD
FLNKLIAKEE PWVLHKNNES EKLEALLSLI ANTLLQSSFL LYAFMPKSAM KLASAFRVEI
TPNNYERFFK AKKLQDMVLQ DTEPLFSKIE KIEKIEKIEK IEKIEKGEEA LAEKAEKKEK
EKAPPTQENY ISIEDFKKVE IKVGLIKEAQ RIEKSNKLLR LKVDLGENRL RQIISGIALD
YEPESLVGQM VCVVANLKPA KLMGEMSEGM ILAVRDNDNL ALISPTREKI AGSLIS
