NTM1_ARATH
ID NTM1_ARATH Reviewed; 276 AA.
AC Q5PP70; F4KA87; Q9FI20;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Alpha N-terminal protein methyltransferase 1;
DE EC=2.1.1.244;
DE AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1;
DE Short=NTM1;
GN OrderedLocusNames=At5g44450; ORFNames=MFC16.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Alpha-N-methyltransferase that methylates the N-terminus of
CC target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys
CC when the initiator Met is cleaved. Specifically catalyzes mono-, di- or
CC tri-methylation of exposed alpha-amino group of Ala or Ser residue in
CC the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the
CC Pro-Pro-Lys motif (By similarity). {ECO:0000250}.
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 -!- 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 -!- 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 -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09152.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB017065; BAB09152.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95110.2; -; Genomic_DNA.
DR EMBL; BT020227; AAV74221.1; -; mRNA.
DR EMBL; BT020502; AAW39003.1; -; mRNA.
DR RefSeq; NP_199258.4; NM_123812.5.
DR AlphaFoldDB; Q5PP70; -.
DR SMR; Q5PP70; -.
DR STRING; 3702.AT5G44450.1; -.
DR PaxDb; Q5PP70; -.
DR PRIDE; Q5PP70; -.
DR ProteomicsDB; 248955; -.
DR DNASU; 834472; -.
DR EnsemblPlants; AT5G44450.1; AT5G44450.1; AT5G44450.
DR GeneID; 834472; -.
DR Gramene; AT5G44450.1; AT5G44450.1; AT5G44450.
DR KEGG; ath:AT5G44450; -.
DR Araport; AT5G44450; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_055356_1_0_1; -.
DR InParanoid; Q5PP70; -.
DR OMA; PVRMYCL; -.
DR PhylomeDB; Q5PP70; -.
DR PRO; PR:Q5PP70; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5PP70; baseline and differential.
DR Genevisible; Q5PP70; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008276; F:protein methyltransferase activity; IEA:UniProt.
DR GO; GO:0006480; P:N-terminal protein amino acid methylation; IEA:InterPro.
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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..276
FT /note="Alpha N-terminal protein methyltransferase 1"
FT /id="PRO_0000399786"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 118..120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 149..150
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 276 AA; 31247 MW; 7930421C67BFA7A3 CRC64;
MDICGVDSEG KEFNSVQEMW REEIGEGDET KKTQWYRDGV SYWEGVEASV DGVLGGYGHV
NDADIIGSEV FLKTLLQERL VNNVGANQHL VALDCGSGIG RITKNLLIRY FNEVDLLEPV
AQFLDAAREN LASAGSETHK ATNFFCVPLQ EFTPAAGRYD VIWVQWCIGH LTDNDFVSFF
NRAKGYLKPG GFFVVKENLA KNGFVLDKED HSITRSDPYF KQLFRQCGLH LYRTKDQKGL
PQELFAVKMY ALTVDTPPKI HRTRSKTRSN RPQIIK
