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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
 
 
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