ID A0A1E5RQD6_HANUV Unreviewed; 252 AA.
AC A0A1E5RQD6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=AWRI3580_g2106 {ECO:0000313|EMBL:OEJ89060.1};
OS Hanseniaspora uvarum (Yeast) (Kloeckera apiculata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=29833 {ECO:0000313|EMBL:OEJ89060.1, ECO:0000313|Proteomes:UP000095358};
RN [1] {ECO:0000313|Proteomes:UP000095358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3580 {ECO:0000313|Proteomes:UP000095358};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
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:OEJ89060.1}.
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DR EMBL; LPNN01000004; OEJ89060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5RQD6; -.
DR STRING; 29833.A0A1E5RQD6; -.
DR VEuPathDB; FungiDB:AWRI3580_g2106; -.
DR OrthoDB; 5470823at2759; -.
DR Proteomes; UP000095358; 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:OEJ89060.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095358};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03223};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03223, ECO:0000313|EMBL:OEJ89060.1}.
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT BINDING 86..88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT BINDING 138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
SQ SEQUENCE 252 AA; 29015 MW; A4F22356A8C47684 CRC64;
MSDNESLFDN NLFEEPEDFR PPPPQEHFTK YERKSETADP KEIQLKLIGS SPLWGHLLWN
AGIYTANHLD TFAKEICEGK NILELGAAAG LPSIIAGLNK ANKVVCTDYP DLELINNIKD
NVAKYNKHNN VVVEGYIWGN EYDDIVKHLP ATAENKFDLI IMSDLVFNHT EHHKLLKTGK
DLLAKGGKIL VVFSPHRPWL LQDDLQFFET CKEEPYGFKV EKFDLVNWKP MFDEDEETVE
IRSRVYSFYL TL
//
