ID W9Y3C9_9EURO Unreviewed; 305 AA.
AC W9Y3C9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=A1O3_03950 {ECO:0000313|EMBL:EXJ86993.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ86993.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ86993.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ86993.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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}.
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:EXJ86993.1}.
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DR EMBL; AMGY01000003; EXJ86993.1; -; Genomic_DNA.
DR RefSeq; XP_007732272.1; XM_007734082.1.
DR AlphaFoldDB; W9Y3C9; -.
DR STRING; 1182542.W9Y3C9; -.
DR GeneID; 19168072; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_055356_2_1_1; -.
DR OrthoDB; 5471049at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR016958-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
FT BINDING 173..174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
FT BINDING 210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
SQ SEQUENCE 305 AA; 33780 MW; 6B9E390D7EB85A9A CRC64;
MPPTKRARIS HSPDPQDIDY ESGKLQSQPG PENPAIETPG HAMDTDSNIS IPDQVAYWSK
ITPSVDGMLG GYPQVSRIDL QFSRNFLRKL QRLDKSDRAR PSANAPHDQA EYAFQHCLEP
GAGIGRVTLN LLAGICSKID IIEPVKRFTD VLTAEDSPVV RSGQLQRVYN VPLQTWTADS
IPSYSAPGLD AEATPAATST TGRYDLIYNQ WCLNHLSMAD LVSYLTKLIP LLRANGWIIV
KENLSTDAFA ADIFDEEDSS VTRSDQNWRI GFEQAGLKLV KTELQTGFPK ALGLLPVRMY
ALRPR
//
