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Database: UniProt
Entry: A0A1G4JAU5_9SACH
LinkDB: A0A1G4JAU5_9SACH
Original site: A0A1G4JAU5_9SACH 
ID   A0A1G4JAU5_9SACH        Unreviewed;       231 AA.
AC   A0A1G4JAU5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Alpha N-terminal protein methyltransferase 1 {ECO:0000256|ARBA:ARBA00039449};
DE            EC=2.1.1.244 {ECO:0000256|ARBA:ARBA00039112};
DE   AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1 {ECO:0000256|ARBA:ARBA00043129};
GN   ORFNames=LADA_0E01068G {ECO:0000313|EMBL:SCU86932.1};
OS   Lachancea dasiensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU86932.1, ECO:0000313|Proteomes:UP000190274};
RN   [1] {ECO:0000313|Proteomes:UP000190274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Devillers H.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC         L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-
CC         L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:54712, Rhea:RHEA-COMP:13785, Rhea:RHEA-COMP:13971,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138057, ChEBI:CHEBI:138315; EC=2.1.1.244;
CC         Evidence={ECO:0000256|ARBA:ARBA00035913};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-
CC         L-methionine = 2 H(+) + N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L-
CC         lysyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54736,
CC         Rhea:RHEA-COMP:13787, Rhea:RHEA-COMP:13974, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138059,
CC         ChEBI:CHEBI:138318; EC=2.1.1.244;
CC         Evidence={ECO:0000256|ARBA:ARBA00036157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC         L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-seryl-L-prolyl-
CC         L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:54724, Rhea:RHEA-COMP:13789, Rhea:RHEA-COMP:13973,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138061, ChEBI:CHEBI:138317; EC=2.1.1.244;
CC         Evidence={ECO:0000256|ARBA:ARBA00036171};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family.
CC       {ECO:0000256|ARBA:ARBA00009059}.
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DR   EMBL; LT598455; SCU86932.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4JAU5; -.
DR   STRING; 1266660.A0A1G4JAU5; -.
DR   OrthoDB; 5471049at2759; -.
DR   Proteomes; UP000190274; Chromosome E.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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   InterPro; IPR008576; MeTrfase_NTM1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12753; AD-003 - RELATED; 1.
DR   PANTHER; PTHR12753:SF0; ALPHA N-TERMINAL PROTEIN METHYLTRANSFERASE 1; 1.
DR   Pfam; PF05891; Methyltransf_PK; 1.
DR   PIRSF; PIRSF016958; DUF858_MeTrfase_lik; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000190274};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR016958-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   BINDING         70
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
FT   BINDING         75
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
FT   BINDING         122..123
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
FT   BINDING         138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
SQ   SEQUENCE   231 AA;  25956 MW;  8B9FFD0D0F12D3F0 CRC64;
     MDKPDAHINY EDAVDYWTSV PATVDGVLGG YGEGTIVPTM DVMGSNHFLR KLKSRMIVAD
     NHKKVGCDIG AGIGRVTRDM LQKHCDVVDL VEPVKPFVDQ MEVELAPLAK EGRLGQIYAV
     GMQDWVPEEG KYWLIWCQWC VGHLPDVELV QFFERCKKAL QPNGTIVVKE NNTQTGEDDF
     DATDSSVTRS DDKFKLLFEK AGLKLIATER QKGLPKELYP VRLYALKPLQ S
//
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