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Database: UniProt
Entry: E9E816_METAQ
LinkDB: E9E816_METAQ
Original site: E9E816_METAQ 
ID   E9E816_METAQ            Unreviewed;       891 AA.
AC   E9E816;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN   ORFNames=MAC_06014 {ECO:0000313|EMBL:EFY87887.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY87887.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY87887.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
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; GL698519; EFY87887.1; -; Genomic_DNA.
DR   RefSeq; XP_007812354.1; XM_007814163.1.
DR   AlphaFoldDB; E9E816; -.
DR   STRING; 655827.E9E816; -.
DR   GeneID; 19250325; -.
DR   KEGG; maw:MAC_06014; -.
DR   eggNOG; KOG0436; Eukaryota.
DR   eggNOG; KOG4135; Eukaryota.
DR   HOGENOM; CLU_009710_5_1_1; -.
DR   InParanoid; E9E816; -.
DR   OMA; TFIVCEP; -.
DR   OrthoDB; 166496at2759; -.
DR   Proteomes; UP000002499; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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; cd00814; MetRS_core; 1.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR007344; GrpB/CoaE.
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; IPR043519; NT_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00398; metG; 1.
DR   PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF13302; Acetyltransf_3; 1.
DR   Pfam; PF04229; GrpB; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS51186; GNAT; 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:UP000002499}.
FT   DOMAIN          585..770
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   891 AA;  101257 MW;  ECB25F0BEF74BEA7 CRC64;
     MVLADVLKRW QQIKGKETFF LTGTDEHGMK IQRAAAKEGI APKEFCDNYS NKFRELAAAG
     DISYDAFIRT TDLEHKEAVS EFWLQLKHTL PEHLELYKGT HEGWYAVSDE CFYPEDLVRP
     DIVPQTGKKI MVSDETGSEV EWVKEETWFF PLTKYKDALL KFYDENPNWI TPAHRMNEVR
     NWVENHLEDL SITRPAARLS WGIPDPEDHN QTIYVWVDAL INYITQAGYG RKWHSSSDNT
     GLWPADMQII GKDILRFHAI YWPALLMALD LPLPKQLLCH NHWTMSNRKM SKSLGNVVNP
     FFAVQRWDID PLRYFLMRNG SFTKDMSYSN QLIGSVYAKE LQANIGNLLY RIARPKVTSK
     WSTLEAVGAF RRGAFGEIPG HTSQQLFVSL DDHLEKITSA FFEEMEKFNT GGAIREVFNL
     LRETNRYVSD TEPWNLVKSP NPQSRILLNL VIYNCAEALR IAGILLQPIM PTKASLLLNE
     LGVREDRRTL EFASKGKDPE YGTEAKTGDS AARLKKWDTI FPPTPNANDS DAEIMEQLSS
     ALHDKTKNKM NQVAELLAME ARMGEEAVAK MLSEMHAARN AKMGDILVAL QEATASQPLT
     LEEEYENQQS WRTAHEKLTF IICQALPTAD RASPSIKAKV VDADDRMIGD INFFIYQDDD
     PEETLQNRKA NVALRGEIDV MIASTEHRRQ GFGSASVQAL LMYLRENMKH ILKEYTCSLK
     LGQEVDLAEL MVKIQEGNIG SRRLFENLGF NQVGDVNYFG EVTLLIAWAK VENLVDGLLN
     SGEVYREVRA QTETWTAKAT QSKVKQATSE EIMEHYNFDP ERVKRVSYCE KKYPLEIQEP
     DPSWPVQFQA LESSIEAALG LKAICISHVG STGVPGLSAK NIIDSDLTVA D
//
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