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Database: UniProt
Entry: A0A421J7Q1_9ASCO
LinkDB: A0A421J7Q1_9ASCO
Original site: A0A421J7Q1_9ASCO 
ID   A0A421J7Q1_9ASCO        Unreviewed;       253 AA.
AC   A0A421J7Q1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Protein N-terminal and lysine N-methyltransferase EFM7 {ECO:0000256|HAMAP-Rule:MF_03223};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03223};
DE   AltName: Full=Elongation factor methyltransferase 7 {ECO:0000256|HAMAP-Rule:MF_03223};
GN   Name=EFM7 {ECO:0000256|HAMAP-Rule:MF_03223};
GN   ORFNames=JA9_000290 {ECO:0000313|EMBL:RLV84697.1};
OS   Meyerozyma sp. JA9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV84697.1, ECO:0000313|Proteomes:UP000286412};
RN   [1] {ECO:0000313|EMBL:RLV84697.1, ECO:0000313|Proteomes:UP000286412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA9 {ECO:0000313|EMBL:RLV84697.1,
RC   ECO:0000313|Proteomes:UP000286412};
RA   Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT   "Physiological and comparative genomic analysis of newly identified yeasts
RT   Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT   production.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein methyltransferase
CC       that trimethylates the N-terminal glycine 'Gly-2' of elongation factor
CC       1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
CC       {ECO:0000256|HAMAP-Rule:MF_03223}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03223}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. EFM7 family. {ECO:0000256|HAMAP-Rule:MF_03223}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLV84697.1}.
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DR   EMBL; NSDU01000017; RLV84697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421J7Q1; -.
DR   STRING; 2028340.A0A421J7Q1; -.
DR   Proteomes; UP000286412; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_03223; Methyltr_EFM7; 1.
DR   InterPro; IPR025784; EFM7.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN; 1.
DR   PANTHER; PTHR14614:SF10; PROTEIN N-TERMINAL AND LYSINE N-METHYLTRANSFERASE EFM7; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51560; SAM_MT_NNT1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03223};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03223,
KW   ECO:0000313|EMBL:RLV84697.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286412};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03223};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03223, ECO:0000313|EMBL:RLV84697.1}.
FT   BINDING         57
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         84..86
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         106
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         164
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
SQ   SEQUENCE   253 AA;  29108 MW;  B2A89FC12981A3E2 CRC64;
     MSDDEIDVGL FEEPEGFLPP PPEPHFATYE RKINGAKPST IEMRLVGKSP LWGHMLWNAG
     IYTADYLDKH SKELVRGKRV LELGAAAGLP SLVCGLNEAA YVLSTDYPDP DLIANIQYNV
     DHTPDAKNIE VRGYIWGNDI GAMMFNEENK AAKEDEKFDL IILSDLIFNH NQHHNLLKSC
     KQLLNASGLI FVVFSPHRAH LLHEDLRFFE TCKEYGFKSK QNDMQIWNPM FEEEEETAEI
     RSRVYSYFLE WDR
//
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