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Database: UniProt
Entry: A7TPD2_VANPO
LinkDB: A7TPD2_VANPO
Original site: A7TPD2_VANPO 
ID   A7TPD2_VANPO            Unreviewed;       271 AA.
AC   A7TPD2;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   05-JUN-2019, entry version 50.
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=Kpol_1009p6 {ECO:0000313|EMBL:EDO15860.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294)
OS   (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
OC   Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO15860.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M.,
RA   Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two
RT   yeast species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein
CC       methyltransferase that trimethylates the N-terminal glycine 'Gly-
CC       2' of elongation factor 1-alpha, before also catalyzing the mono-
CC       and dimethylation of 'Lys-3'. {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
CC       methyltransferase superfamily. EFM7 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03223}.
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DR   EMBL; DS480441; EDO15860.1; -; Genomic_DNA.
DR   RefSeq; XP_001643718.1; XM_001643668.1.
DR   STRING; 36033.XP_001643718.1; -.
DR   EnsemblFungi; EDO15860; EDO15860; Kpol_1009p6.
DR   GeneID; 5543972; -.
DR   KEGG; vpo:Kpol_1009p6; -.
DR   eggNOG; KOG2920; Eukaryota.
DR   eggNOG; ENOG4111NE8; LUCA.
DR   InParanoid; A7TPD2; -.
DR   KO; K17878; -.
DR   OMA; FYTHHRP; -.
DR   OrthoDB; 1588190at2759; -.
DR   PhylomeDB; A7TPD2; -.
DR   Proteomes; UP000000267; 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:0000183; P:chromatin silencing at rDNA; IEA:EnsemblFungi.
DR   GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03223; Methyltr_EFM7; 1.
DR   InterPro; IPR025784; EFM7.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51560; SAM_MT_NNT1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000267};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03223};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03223};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000267};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03223};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03223}.
FT   REGION        1     28       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A7TPD2}.
FT   REGION       90     92       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03223}.
FT   BINDING      64     64       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03223}.
FT   BINDING     112    112       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03223}.
FT   BINDING     159    159       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03223}.
FT   BINDING     183    183       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03223}.
SQ   SEQUENCE   271 AA;  30814 MW;  296A6C9CF3D3EECD CRC64;
     MSDTESLTGA TGLFEEPEDF RPPPPKPHFA AYQREYISED SKSKQEKLDL RLVGSSPLWG
     HLLWNAGIYT AKHLDKHPEL VQDKTVLELG AASALPSLIS ALIGAKKVIS TDYPDADLLA
     NIQYNVDHLV FNGEELSNDP AVLKSQLDER NLVVEGYIWG NEYTPLVDHI GGDSSKFDLV
     ILSDLVFNHT EHHKLLKTTK DMMAKDGKAL VVFSPHRPWL LENDLSFFET AKEYNLEPTK
     IEMVNWKPMF EEDDETIEIR SRVYAYYLTH K
//
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