ID A0A094CCS0_9PEZI Unreviewed; 648 AA.
AC A0A094CCS0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=V497_08739 {ECO:0000313|EMBL:KFY51946.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY51946.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY51946.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY51946.1}.
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DR EMBL; JPJZ01001549; KFY51946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CCS0; -.
DR STRING; 1420910.A0A094CCS0; -.
DR HOGENOM; CLU_436879_0_0_1; -.
DR OrthoDB; 2787189at2759; -.
DR Proteomes; UP000029268; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03198};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03198};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03198};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 298..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 85..87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
SQ SEQUENCE 648 AA; 71539 MW; 2EA4ABAC1A6A39FE CRC64;
MIPRVPSPDY SPLSIGVDFT PLPVYKAAST TSIDFDGLLP APLQLHEDLK GGCGGQLWPA
GMVLSKYMLR EHKDDLKDAT ILELGAGGGL VGLAVALGCN ISEPIIITDQ INMMPLMEQN
IKLNKLESRV TPLVLNWGEP LPDILSSRPA THILAADCVY FEPAFPLLLL TLSELLKACD
QAVIYFCFKK RRRADAQFMK AARKLFAIEE IEDQDKAVWS REQLFIDNFT TIDNNFITKK
TKMTVTMSDY EDRMLKYAEL TATYTQRMAA AAWCSLAVGL AALVATIYFS YREDARKEKN
GNQHQHQQHT TPIVSGNMTF SFGPATSERS AQPFQDIGRQ PVPPGNAQPP PQVLARGHAT
ISDNMRGGGK GTDNDSSSTS EASPAEDSRP SRLRRRPTRY GSEDVLPSTS SPPPLPDSPM
ESQLPRGPDA VKRPRSLTDT LHTEGKSGGM EARFAKSKEF MNQYHKKEPA NAQYVDDVQS
LEGEHSDNES KDSLNGFDAR SEPHLKTGVF SRFQKTLKVQ QQEEFQDPGL LLDIERIMRR
IEGRTPMPLK FKDAVGCKFT FPLDIARTWP AGLPPRRCAW AACSRWTLRF NRPKRRQYSP
TGVEICRGAG YGYHYAHVAD ARAAEASAAE ASAAEAAAAA AAAAVEKF
//
