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Database: UniProt
Entry: Q6FTV8_CANGA
LinkDB: Q6FTV8_CANGA
Original site: Q6FTV8_CANGA 
ID   Q6FTV8_CANGA            Unreviewed;       750 AA.
AC   Q6FTV8;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN   OrderedLocusNames=CAGL0F08459g {ECO:0000313|CGD:CAL0131210,
GN   ECO:0000313|EMBL:CAG59260.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG59260.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG59260.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
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DR   EMBL; CR380952; CAG59260.1; -; Genomic_DNA.
DR   RefSeq; XP_446336.1; XM_446336.1.
DR   AlphaFoldDB; Q6FTV8; -.
DR   STRING; 284593.Q6FTV8; -.
DR   EnsemblFungi; CAGL0F08459g-T; CAGL0F08459g-T-p1; CAGL0F08459g.
DR   GeneID; 2887794; -.
DR   KEGG; cgr:CAGL0F08459g; -.
DR   CGD; CAL0131210; CAGL0F08459g.
DR   VEuPathDB; FungiDB:CAGL0F08459g; -.
DR   eggNOG; KOG1247; Eukaryota.
DR   HOGENOM; CLU_009710_4_1_1; -.
DR   InParanoid; Q6FTV8; -.
DR   OMA; HLNTTEY; -.
DR   Proteomes; UP000002428; Chromosome F.
DR   GO; GO:0017102; C:methionyl glutamyl tRNA synthetase complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd10290; GST_C_MetRS_N_fungi; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 1.20.1050.110; -; 1.
DR   Gene3D; 3.40.30.170; -; 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; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR018285; Met-tRNA-synth_N.
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; PF09635; MetRS-N; 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.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   DOMAIN          11..130
FT                   /note="Methionyl-tRNA synthetase N-terminal
FT                   heteromerisation"
FT                   /evidence="ECO:0000259|Pfam:PF09635"
FT   DOMAIN          197..588
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          611..749
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
SQ   SEQUENCE   750 AA;  85254 MW;  0445A1BC50603217 CRC64;
     MASQVSFDKV KGRDAKVVLA NNLKIALAIE LAKGLKLSIN EDRSEPLLTA GELVLRDANA
     ILRYALDDFE GIHSEQYHYA LSSVEAYLYH QQSSEEHATE LVNKMIDNYL KLDKDSKLDA
     VTLISFANAY ALRPTQINDA FKDDLPEALK KAIQTATKYT PRSSSEFKNT GEKHIAEGYL
     VSKQGSEILP KEGERNILIT SALPYVNNVP HLGNIVGSVL SADIFARYCK SRNYNTLFIC
     GTDEYGTATE TKAIEEGVSP RELCDKYHKI HSDVYKWFQI GFDYFGRTTT EQQTEIAQDI
     FLKLDKNGYL GEESMKQLYC PVHNSFLADR YVEGECPKCH YEDARGDQCD KCGGLLDPFE
     LINPRCKLDN AIPEPKTSDH IFLALDKLEP EIKKWVEKAS TEGEWSKNSK TITNSWLKDG
     LKPRCITRDL VWGTPVPLEK YKDKVLYVWF DATIGYVSIT ANYTKNWEQW WKKPEDVKLY
     QFMGKDNVPF HTVVFPGSQL GTNDEWTMLH HLNTTEYLQY EGGKFSKSRG VGVFGNNAQD
     SGISPSVWRY YLASVRPESS DSHFSWDDFV ARNNSELLAN LGNFVNRIIK FVNAKYNGVI
     PKFDTKNLPN YDSLVSDINE ILRNYVKEME TAHERRGLEI AMSLSARGNQ FLQENKLDNS
     LFSQHPEKSD AVVGVGLNIV YAVASLIYPF MPETAETINR MLNAPALKID EEFHIALLGG
     HNINKAEYLF QRIDEKKIDE WRAKYGGQDK
//
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