NTM1A_XENTR
ID NTM1A_XENTR Reviewed; 224 AA.
AC B1H2P7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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;
GN Name=ntmt1; Synonyms=mettl11a;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2008) 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 = 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; BC161081; AAI61081.1; -; mRNA.
DR RefSeq; NP_001120381.1; NM_001126909.1.
DR RefSeq; XP_012823473.1; XM_012968019.2.
DR AlphaFoldDB; B1H2P7; -.
DR SMR; B1H2P7; -.
DR PaxDb; B1H2P7; -.
DR PRIDE; B1H2P7; -.
DR Ensembl; ENSXETT00000030922; ENSXETP00000030922; ENSXETG00000014162.
DR GeneID; 100145456; -.
DR KEGG; xtr:100145456; -.
DR CTD; 28989; -.
DR Xenbase; XB-GENE-994935; ntmt1.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_055356_3_1_1; -.
DR InParanoid; B1H2P7; -.
DR OMA; PVRMYCL; -.
DR OrthoDB; 1528533at2759; -.
DR PhylomeDB; B1H2P7; -.
DR TreeFam; TF314174; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000014162; Expressed in skeletal muscle tissue and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
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:0018011; P:N-terminal peptidyl-alanine methylation; IBA:GO_Central.
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:0035568; P:N-terminal peptidyl-proline methylation; IBA:GO_Central.
DR GO; GO:0035572; P:N-terminal peptidyl-serine dimethylation; ISS:UniProtKB.
DR GO; GO:0035570; P:N-terminal peptidyl-serine methylation; IBA:GO_Central.
DR GO; GO:0035573; P:N-terminal peptidyl-serine trimethylation; ISS:UniProtKB.
DR GO; GO:0006480; P:N-terminal protein amino acid methylation; IBA:GO_Central.
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 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"
FT /id="PRO_0000399778"
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; 25458 MW; FE83F2A7CD929D86 CRC64;
MSTELVEDEA QFYCKAQKYW KNVPATVDGM LGGYGHISNI DLNGSKKFLQ RFLRQEGSNK
TGNMYALDCG AGIGRITKRL LLPLFKKVDM VDVTDEFLSK AKSYLGEEGS RVGNYFCCGL
QEFSPEPNRY DVIWIQWVIG HLTDEHLVDF LKRCSLGLRP NGIIVIKDNV TQDVSIMDDV
DSSICRDIDL VRKLIKQAGL SLLAVERQEN FPDEIYHVFS FAMR
