ID A0A094C7K2_9PEZI Unreviewed; 617 AA.
AC A0A094C7K2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Protein-lysine N-methyltransferase EFM5 {ECO:0000256|HAMAP-Rule:MF_03187};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03187};
DE AltName: Full=Elongation factor methyltransferase 5 {ECO:0000256|HAMAP-Rule:MF_03187};
GN Name=EFM5 {ECO:0000256|HAMAP-Rule:MF_03187};
GN ORFNames=V496_09751 {ECO:0000313|EMBL:KFY49869.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY49869.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY49869.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
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 trimethylates elongation factor 1-alpha at 'Lys-
CC 79'. {ECO:0000256|HAMAP-Rule:MF_03187}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_03187}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM5 family. {ECO:0000256|HAMAP-Rule:MF_03187}.
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:KFY49869.1}.
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DR EMBL; JPJY01001902; KFY49869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094C7K2; -.
DR STRING; 1420909.A0A094C7K2; -.
DR HOGENOM; CLU_505396_0_0_1; -.
DR OrthoDB; 141210at2759; -.
DR Proteomes; UP000029302; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd05271; NDUFA9_like_SDR_a; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_03187; Methyltr_EFM5; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR019369; Efm5/EEF1AKMT1.
DR InterPro; IPR041370; Mlase_EEF1AKMT1/ZCCHC4.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR PANTHER; PTHR12126:SF11; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 9, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12126; NADH-UBIQUINONE OXIDOREDUCTASE 39 KDA SUBUNIT-RELATED; 1.
DR Pfam; PF10237; N6-adenineMlase; 1.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03187};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03187}; Reference proteome {ECO:0000313|Proteomes:UP000029302};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03187}.
FT DOMAIN 58..283
FT /note="NmrA-like"
FT /evidence="ECO:0000259|Pfam:PF05368"
SQ SEQUENCE 617 AA; 69414 MW; 962653EF81495A9D CRC64;
MKSCSPSSTA ALRAAARPKS YISPIASRNV SDISITRTGK PIIKVQGGRS SLGGHTATVF
GATGFLGRYI VNRLARQGCT VIIPYREEMA KRHLKVTGDL GRVIFMEYDL RNTESLEESV
RHSDIVYNLV GRSYPTKNFD LEDVHVEGAE RIADAVAKYD VDRFVHVSSY NADANSTSEF
YRTKARGESV VRSIFPETTI VRPAPMFGFE DRLLHKLAGV TNLLTSNNME ERYKPVHVID
VGHALEKMLN DDSTASQTYE LFGPKDYSTA EIAELVDKEI HKHRRHINLP KSILKPAATI
LNKALWWPVL SGDEIEREFI DQHIDPTAKT FKDLDIEPAD LANLTFHYLQ SYRSAAFYDL
PPATEQGKFR MSEIQDDDSD IPVLSGSALE ALKEFYADRD AKEKELENLK AKKNTGDILS
MDTFTENWND SQFWYSQETA DIFARELLAK CDNKSKIAVI SAPSAFVQLK NIIASTSMTA
DKIPEIYLLE FDERFSIFPE FVFYDYKYPL KLPPSMKGSI DHIICDPPFL SEDCQTKAAL
TARWLSKPSG TSQGEATSDP ASRVIVCTGE RMNSLVNKLY GPLGVHTTTF EPVHAKGLSN
EFYCYANFEC ANWKWKD
//
