NTM1A_AILME
ID NTM1A_AILME Reviewed; 223 AA.
AC D2H163;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1;
DE EC=2.1.1.244 {ECO:0000250|UniProtKB:Q9BV86};
DE AltName: Full=Alpha N-terminal protein methyltransferase 1A;
DE AltName: Full=Methyltransferase-like protein 11A;
DE AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1A;
DE Short=NTM1A;
DE Contains:
DE RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed;
GN Name=NTMT1; Synonyms=METTL11A; ORFNames=PANDA_003235;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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. Some of the substrates may be primed by NTMT2-mediated
CC monomethylation. Catalyzes the trimethylation of the N-terminal Gly in
CC CENPA (after removal of Met-1). Responsible for the N-terminal
CC methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required
CC during mitosis for normal bipolar spindle formation and chromosome
CC segregation via its action on RCC1. {ECO:0000250|UniProtKB:Q9BV86}.
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:0000250|UniProtKB:Q9BV86};
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:0000250|UniProtKB:Q9BV86};
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: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; GL192421; EFB25068.1; -; Genomic_DNA.
DR RefSeq; XP_002915248.1; XM_002915202.3.
DR RefSeq; XP_019650819.1; XM_019795260.1.
DR RefSeq; XP_019650820.1; XM_019795261.1.
DR RefSeq; XP_019650821.1; XM_019795262.1.
DR RefSeq; XP_019650822.1; XM_019795263.1.
DR AlphaFoldDB; D2H163; -.
DR SMR; D2H163; -.
DR STRING; 9646.ENSAMEP00000016883; -.
DR Ensembl; ENSAMET00000031878; ENSAMEP00000022635; ENSAMEG00000026209.
DR GeneID; 100464977; -.
DR KEGG; aml:100464977; -.
DR CTD; 28989; -.
DR eggNOG; KOG3178; Eukaryota.
DR GeneTree; ENSGT00390000008371; -.
DR InParanoid; D2H163; -.
DR OrthoDB; 1528533at2759; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0016571; P:histone methylation; ISS:UniProtKB.
DR GO; GO:0018012; P:N-terminal peptidyl-alanine trimethylation; IEA:Ensembl.
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 Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR008576; MeTrfase_NTM1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12753; PTHR12753; 1.
DR Pfam; PF05891; Methyltransf_PK; 1.
DR PIRSF; PIRSF016958; DUF858_MeTrfase_lik; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Acetylation; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..223
FT /note="N-terminal Xaa-Pro-Lys N-methyltransferase 1"
FT /id="PRO_0000423226"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT CHAIN 2..223
FT /note="N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-
FT terminally processed"
FT /id="PRO_0000399774"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 91..93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 119..120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT MOD_RES 2
FT /note="N-acetylthreonine; in N-terminal Xaa-Pro-Lys N-
FT methyltransferase 1, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
SQ SEQUENCE 223 AA; 25284 MW; 6161C15BE8D7E5F1 CRC64;
MTSEVIEDEK QFYLKAKTYW KEVPPTVDGM LGGYGHISSI DISSSRKFLQ RFLREGPNKT
GTSCALDCGA GIGRITKRLL LPLFGVVDMV DVTEDFLIKA RTYLGEEGKR VRNYFCCGLQ
DFSPEPNSYD VIWIQWVIGH LTDQHLAEFL RRCKQGLRPN GIIVIKDNMA QEGVILDDVD
SSVCRDLDVV HRIVRSAGLS LLAEERQENL PDEIYHVYSL ALR
