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N-terminal Xaa-Pro-Lys N-methyltransferase 1 (EC 2.1.1.244) (Alpha N-terminal protein methyltransferase 1A) (Methyltransferase-like protein 11A) (X-Pro-Lys N-terminal protein methyltransferase 1A) (NTM1A) [Cleaved into: N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed]

 NTM1A_BOVIN             Reviewed;         223 AA.
Q2T9N3;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 70.
RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1;
EC=2.1.1.244 {ECO:0000250|UniProtKB:Q9BV86};
AltName: Full=Alpha N-terminal protein methyltransferase 1A;
AltName: Full=Methyltransferase-like protein 11A;
AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1A;
Short=NTM1A;
Contains:
RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed;
Name=NTMT1; Synonyms=METTL11A;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Distributive alpha-N-methyltransferase that methylates
the N-terminus of target proteins containing the N-terminal motif
[Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved.
Specifically catalyzes mono-, di- or tri-methylation of the
exposed alpha-amino group of the Ala, Gly or Ser residue in the
[Ala/Gly/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in
the Pro-Pro-Lys motif. Some of the substrates may be primed by
METTL11B-mediated monomethylation. Catalyzes the trimethylation of
the N-terminal Gly in CENPA (after removal of Met-1). Responsible
for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1,
RPL23A and SET. Required during mitosis for normal bipolar spindle
formation and chromosome segregation via its action on RCC1.
{ECO:0000250|UniProtKB:Q9BV86}.
-!- CATALYTIC ACTIVITY: 3 S-adenosyl-L-methionine + N-terminal-
(A,S)PK-[protein] = 3 S-adenosyl-L-homocysteine + N-terminal-
N,N,N-trimethyl-N-(A,S)PK-[protein].
{ECO:0000250|UniProtKB:Q9BV86}.
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + N-terminal-PPK-
[protein] = 2 S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-
N-PPK-[protein]. {ECO:0000250|UniProtKB:Q9BV86}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BV86}.
Note=Predominantly nuclear. {ECO:0000250|UniProtKB:Q9BV86}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1
family. {ECO:0000305}.
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EMBL; BC111344; AAI11345.1; -; mRNA.
RefSeq; NP_001033306.1; NM_001038217.2.
UniGene; Bt.29263; -.
ProteinModelPortal; Q2T9N3; -.
SMR; Q2T9N3; -.
STRING; 9913.ENSBTAP00000020514; -.
PaxDb; Q2T9N3; -.
PRIDE; Q2T9N3; -.
GeneID; 617042; -.
KEGG; bta:617042; -.
CTD; 28989; -.
eggNOG; KOG3178; Eukaryota.
eggNOG; ENOG410XS7T; LUCA.
HOVERGEN; HBG054992; -.
InParanoid; Q2T9N3; -.
KO; K16219; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; ISS:UniProtKB.
GO; GO:0008276; F:protein methyltransferase activity; ISS:UniProtKB.
GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
GO; GO:0018011; P:N-terminal peptidyl-alanine methylation; IBA:GO_Central.
GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; ISS:UniProtKB.
GO; GO:0018016; P:N-terminal peptidyl-proline dimethylation; ISS:UniProtKB.
GO; GO:0035568; P:N-terminal peptidyl-proline methylation; IBA:GO_Central.
GO; GO:0035572; P:N-terminal peptidyl-serine dimethylation; ISS:UniProtKB.
GO; GO:0035570; P:N-terminal peptidyl-serine methylation; IBA:GO_Central.
GO; GO:0035573; P:N-terminal peptidyl-serine trimethylation; ISS:UniProtKB.
GO; GO:0007051; P:spindle organization; ISS:UniProtKB.
InterPro; IPR008576; MeTrfase_NTM1.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR12753; PTHR12753; 1.
Pfam; PF05891; Methyltransf_PK; 1.
PIRSF; PIRSF016958; DUF858_MeTrfase_lik; 1.
SUPFAM; SSF53335; SSF53335; 1.
2: Evidence at transcript level;
Acetylation; Complete proteome; Methyltransferase; Nucleus;
Reference proteome; S-adenosyl-L-methionine; Transferase.
CHAIN 1 223 N-terminal Xaa-Pro-Lys N-
methyltransferase 1.
/FTId=PRO_0000423227.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:Q9BV86}.
CHAIN 2 223 N-terminal Xaa-Pro-Lys N-
methyltransferase 1, N-terminally
processed.
/FTId=PRO_0000245581.
REGION 91 93 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9BV86}.
REGION 119 120 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9BV86}.
BINDING 69 69 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:Q9BV86}.
BINDING 74 74 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q9BV86}.
BINDING 135 135 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:Q9BV86}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9BV86}.
MOD_RES 2 2 N-acetylthreonine; in N-terminal Xaa-Pro-
Lys N-methyltransferase 1, N-terminally
processed.
{ECO:0000250|UniProtKB:Q9BV86}.
SEQUENCE 223 AA; 25289 MW; 8CAD33132D956E23 CRC64;
MTSEVIEDEK QFYSKAKTYW KEVPATVDGM LGGYGHISSI DINSSRKFLQ RFLREGQNKT
GTSYALDCGA GIGRITKRLL LPLFGVVDMV DVTEDFLVKA KTYLGEEGKR VRNFFCCGLQ
DFSPEPQSYD VIWIQWVIGH LTDQHLAEFL RRCKRGLRPN GIIVIKDNMA QEGVILDDVD
SSVCRALDVV HRIVRSAGLS LLAQERQENL PDEIYHVYSL ALR


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