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Database: UniProt
Entry: A5U150
LinkDB: A5U150
Original site: A5U150 
ID   A5U150_MYCTA            Unreviewed;       519 AA.
AC   A5U150;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   11-DEC-2019, entry version 100.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01228};
DE            EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_01228};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228};
DE            Short=MetRS {ECO:0000256|HAMAP-Rule:MF_01228};
GN   Name=metG {ECO:0000256|HAMAP-Rule:MF_01228,
GN   ECO:0000313|EMBL:ABQ72750.1};
GN   OrderedLocusNames=MRA_1016 {ECO:0000313|EMBL:ABQ72750.1};
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947 {ECO:0000313|EMBL:ABQ72750.1, ECO:0000313|Proteomes:UP000001988};
RN   [1] {ECO:0000313|EMBL:ABQ72750.1, ECO:0000313|Proteomes:UP000001988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra {ECO:0000313|Proteomes:UP000001988};
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
RN   [2] {ECO:0000213|PDB:5XET, ECO:0000213|PDB:5XGQ}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
RX   PubMed=30002848; DOI=10.1107/S2052252518008217;
RA   Wang W., Qin B., Wojdyla J.A., Wang M., Gao X., Cui S.;
RT   "Structural characterization of free-state and product-state Mycobacterium
RT   tuberculosis methionyl-tRNA synthetase reveals an induced-fit ligand-
RT   recognition mechanism.";
RL   IUCrJ 5:478-490(2018).
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_01228,
CC       ECO:0000256|SAAS:SAAS01102718}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01228, ECO:0000256|SAAS:SAAS01159305};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228,
CC       ECO:0000256|SAAS:SAAS01102710}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 2B subfamily. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}.
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DR   EMBL; CP000611; ABQ72750.1; -; Genomic_DNA.
DR   RefSeq; WP_003911321.1; NZ_CP016972.1.
DR   PDB; 5XET; X-ray; 2.38 A; C=1-519.
DR   PDB; 5XGQ; X-ray; 1.90 A; A/B=1-519.
DR   PDBsum; 5XET; -.
DR   PDBsum; 5XGQ; -.
DR   SMR; A5U150; -.
DR   STRING; 419947.MRA_1016; -.
DR   EnsemblBacteria; ABQ72750; ABQ72750; MRA_1016.
DR   KEGG; mra:MRA_1016; -.
DR   eggNOG; ENOG4105CKH; Bacteria.
DR   eggNOG; COG0143; LUCA.
DR   HOGENOM; HOG000200401; -.
DR   KO; K01874; -.
DR   OMA; SDMHGTP; -.
DR   OrthoDB; 761140at2; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; -; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:5XET, ECO:0000213|PDB:5XGQ};
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159323,
KW   ECO:0000313|EMBL:ABQ72750.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159304};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228, ECO:0000256|SAAS:SAAS01102725};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01228, ECO:0000256|RuleBase:RU363039,
KW   ECO:0000256|SAAS:SAAS01159317};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159262};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159279}.
FT   DOMAIN          4..137
FT                   /note="tRNA-synt_1g"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          150..362
FT                   /note="tRNA-synt_1g"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   REGION          500..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           11..21
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   MOTIF           299..303
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   COMPBIAS        501..519
FT                   /note="Pro-rich"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  58093 MW;  B8DAE2553B5EFB49 CRC64;
     MKPYYVTTAI AYPNAAPHVG HAYEYIATDA IARFKRLDRY DVRFLTGTDE HGLKVAQAAA
     AAGVPTAALA RRNSDVFQRM QEALNISFDR FIRTTDADHH EASKELWRRM SAAGDIYLDN
     YSGWYSVRDE RFFVESETQL VDGTRLTVET GTPVTWTEEQ TYFFRLSAYT DKLLAHYHAN
     PDFIAPETRR NEVISFVSGG LDDLSISRTS FDWGVQVPEH PDHVMYVWVD ALTNYLTGAG
     FPDTDSELFR RYWPADLHMI GKDIIRFHAV YWPAFLMSAG IELPRRIFAH GFLHNRGEKM
     SKSVGNIVDP VALAEALGVD QVRYFLLREV PFGQDGSYSD EAIVTRINTD LANELGNLAQ
     RSLSMVAKNL DGRVPNPGEF ADADAALLAT ADGLLERVRG HFDAQAMHLA LEAIWLMLGD
     ANKYFSVQQP WVLRKSESEA DQARFRTTLY VTCEVVRIAA LLIQPVMPES AGKILDLLGQ
     APNQRSFAAV GVRLTPGTAL PPPTGVFPRY QPPQPPEGK
//
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