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Database: UniProt
Entry: A0A0A2L210_PENIT
LinkDB: A0A0A2L210_PENIT
Original site: A0A0A2L210_PENIT 
ID   A0A0A2L210_PENIT        Unreviewed;       249 AA.
AC   A0A0A2L210;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Protein-lysine N-methyltransferase EFM6 {ECO:0000256|HAMAP-Rule:MF_03198};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03198};
DE   AltName: Full=Elongation factor methyltransferase 6 {ECO:0000256|HAMAP-Rule:MF_03198};
GN   Name=EFM6 {ECO:0000256|HAMAP-Rule:MF_03198};
GN   ORFNames=PITC_003530 {ECO:0000313|EMBL:KGO73166.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO73166.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO73166.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO73166.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC       methyltransferase that methylates elongation factor 1-alpha.
CC       {ECO:0000256|HAMAP-Rule:MF_03198}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. METTL21 family. EFM6 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_03198}.
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:KGO73166.1}.
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DR   EMBL; JQGA01000835; KGO73166.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2L210; -.
DR   STRING; 40296.A0A0A2L210; -.
DR   HOGENOM; CLU_055721_2_1_1; -.
DR   OMA; IYITDQE; -.
DR   OrthoDB; 2787189at2759; -.
DR   PhylomeDB; A0A0A2L210; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_03198; Methyltr_EFM6; 1.
DR   InterPro; IPR033684; EFM6.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN; 1.
DR   PANTHER; PTHR14614:SF98; PROTEIN-LYSINE N-METHYLTRANSFERASE EFM6; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         68
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         95..97
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         119
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         165
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
SQ   SEQUENCE   249 AA;  27489 MW;  8D8C898EE927162B CRC64;
     MIEIPMPTLS DSESSPPSSP GGLRISESLA PPRELKAAVT TDISFDGLLK EPLLLKEDLK
     DGCGGQLWPA GMTLAKYLLS RHAADLSDKT IVELGAGGGL VGLAVARGCH LEQPIYITDQ
     EPMFSLMKSN IQLNNLGANA TAAILNWGEP IPDQIPSKPD VILAADCVYF EPAFPLLITT
     LQDLLGPDTV CYFCYKRRRR ADMRFMKMAK KAFEMEQIRN DPGAEAYNRE NIFLYTIRAK
     RLDQKSETR
//
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