ID NT1AA_XENLA Reviewed; 224 AA.
AC Q4KL94;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 27-NOV-2024, entry version 65.
DE RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1-A;
DE EC=2.1.1.244 {ECO:0000250|UniProtKB:Q9BV86};
DE AltName: Full=Alpha N-terminal protein methyltransferase 1A-A;
DE AltName: Full=Methyltransferase-like protein 11A-A;
DE AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1A-A;
DE Short=NTM1A-A;
GN Name=ntmt1-a; Synonyms=mettl11a-a, MGC116538;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Distributive alpha-N-methyltransferase that methylates the N-
CC terminus of target proteins containing the N-terminal motif
CC [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved.
CC Specifically catalyzes mono-, di- or tri-methylation of the exposed
CC alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]-
CC Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys
CC motif. Required during mitosis for normal bipolar spindle formation and
CC chromosome segregation via its action on target proteins.
CC {ECO:0000250|UniProtKB:Q9BV86}.
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 Evidence={ECO:0000250|UniProtKB:Q9BV86};
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 Evidence={ECO:0000250|UniProtKB:Q9BV86};
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 Evidence={ECO:0000250|UniProtKB:Q9BV86};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BV86}.
CC Note=Predominantly nuclear. {ECO:0000250|UniProtKB:Q9BV86}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family.
CC {ECO:0000305}.
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DR EMBL; BC099343; AAH99343.1; -; mRNA.
DR RefSeq; NP_001090080.1; NM_001096611.1.
DR AlphaFoldDB; Q4KL94; -.
DR SMR; Q4KL94; -.
DR DNASU; 735155; -.
DR GeneID; 735155; -.
DR KEGG; xla:735155; -.
DR AGR; Xenbase:XB-GENE-994939; -.
DR CTD; 735155; -.
DR Xenbase; XB-GENE-994939; ntmt1.L.
DR OrthoDB; 5471049at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 735155; Expressed in oocyte and 19 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008276; F:protein methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0018011; P:N-terminal peptidyl-alanine methylation; IEA:TreeGrafter.
DR GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; ISS:UniProtKB.
DR GO; GO:0018016; P:N-terminal peptidyl-proline dimethylation; ISS:UniProtKB.
DR GO; GO:0035572; P:N-terminal peptidyl-serine dimethylation; ISS:UniProtKB.
DR GO; GO:0035573; P:N-terminal peptidyl-serine trimethylation; ISS:UniProtKB.
DR GO; GO:0007051; P:spindle organization; ISS:UniProtKB.
DR CDD; cd02440; AdoMet_MTases; 1.
DR FunFam; 3.40.50.150:FF:000025; N-terminal Xaa-Pro-Lys N-methyltransferase 1; 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:SF1; N-TERMINAL XAA-PRO-LYS N-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 2: Evidence at transcript level;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..224
FT /note="N-terminal Xaa-Pro-Lys N-methyltransferase 1-A"
FT /id="PRO_0000399776"
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 92..94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 120..121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
SQ SEQUENCE 224 AA; 25399 MW; 57933F098217D705 CRC64;
MSTELVEDET QFYGKAQNYW KNVPPTVDGM LGGYGHISNV DLNGSKKFLQ RFLRQEGSNK
TGNACALDCG AGIGRITKRL LLPLFKTVDM VDVTDEFLNK AKSFLGEEGK RVGNYFCCGL
QEFSPEPNRY DVIWIQWVIG HLTDEHLVNF LQRCRLGLRP NGIIVIKDNV TQDASIMDDV
DSSICREIDL VRKLIKQAGL SILAVERQEN FPDEIYHVFS FAMR
//
