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Database: UniProt
Entry: NTM1_DICDI
LinkDB: NTM1_DICDI
Original site: NTM1_DICDI 
ID   NTM1_DICDI              Reviewed;         270 AA.
AC   Q55DH6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-NOV-2024, entry version 86.
DE   RecName: Full=Alpha N-terminal protein methyltransferase 1;
DE            EC=2.1.1.244;
DE   AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1;
DE            Short=NTM1;
GN   ORFNames=DDB_G0269658;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Alpha-N-methyltransferase that methylates the N-terminus of
CC       target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys
CC       when the initiator Met is cleaved. Specifically catalyzes mono-, di- or
CC       tri-methylation of exposed alpha-amino group of Ala or Ser residue in
CC       the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the
CC       Pro-Pro-Lys motif (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC         L-methionine = N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-
CC         [protein] + 3 S-adenosyl-L-homocysteine + 3 H(+);
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC         L-methionine = N-terminal N,N,N-trimethyl-L-seryl-L-prolyl-L-lysyl-
CC         [protein] + 3 S-adenosyl-L-homocysteine + 3 H(+);
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-
CC         L-methionine = N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L-lysyl-
CC         [protein] + 2 S-adenosyl-L-homocysteine + 2 H(+);
CC         Xref=Rhea:RHEA:54736, Rhea:RHEA-COMP:13787, Rhea:RHEA-COMP:13974,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138059, ChEBI:CHEBI:138318; EC=2.1.1.244;
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000005; EAL72179.1; -; Genomic_DNA.
DR   RefSeq; XP_646155.1; XM_641063.1.
DR   AlphaFoldDB; Q55DH6; -.
DR   SMR; Q55DH6; -.
DR   PaxDb; 44689-DDB0190440; -.
DR   EnsemblProtists; EAL72179; EAL72179; DDB_G0269658.
DR   GeneID; 8617106; -.
DR   KEGG; ddi:DDB_G0269658; -.
DR   dictyBase; DDB_G0269658; -.
DR   VEuPathDB; AmoebaDB:DDB_G0269658; -.
DR   eggNOG; KOG3178; Eukaryota.
DR   HOGENOM; CLU_055356_3_1_1; -.
DR   InParanoid; Q55DH6; -.
DR   OMA; PVRMYCL; -.
DR   PhylomeDB; Q55DH6; -.
DR   PRO; PR:Q55DH6; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006480; P:N-terminal protein amino acid methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   FunFam; 3.40.50.150:FF:000365; Unplaced genomic scaffold supercont1.14, whole genome shotgun sequence; 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   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..270
FT                   /note="Alpha N-terminal protein methyltransferase 1"
FT                   /id="PRO_0000399785"
FT   BINDING         114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..139
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         165..166
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  31043 MW;  77293519AB1AF60D CRC64;
     MTIKNEEQQQ QTNKLKYPKN LLSSGLDGEG NTYINIEDLW KKELEGKDNK MEDKWYKSAD
     EYWKGVEATV DGMLGGLAQV SPIDVVASKV FIQDFIKGTD SRPPINLNLA LDCGAGIGRV
     AKEFLLPIGF KNVDLVEQNK LFLDKAKSDN FKDDNRVENY YAVGLQDFTF EKKYDCIWIQ
     WVIGHLHDLD FIEFLKKCMD SLTPNGIICI KDNCAKKRFI MDKEDNSVSR TEDHLKYLFD
     QAGCKLLKSM VQPNFPKELF PVLMFALERK
//
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