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
//