NTM1B_RAT
ID NTM1B_RAT Reviewed; 283 AA.
AC D3ZVR1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 2;
DE EC=2.1.1.299 {ECO:0000250|UniProtKB:Q5VVY1};
DE AltName: Full=Alpha N-terminal protein methyltransferase 1B;
DE AltName: Full=Methyltransferase-like protein 11B;
DE AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1B;
DE Short=NTM1B;
GN Name=Ntmt2; Synonyms=Mettl11b {ECO:0000312|RGD:1564106};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-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
CC monomethylation of exposed alpha-amino group of Ala or Ser residue in
CC the [Ala/Ser]-Pro-Lys motif and Pro in the Pro-Pro-Lys motif.
CC Predominantly functions as a mono-methyltransferase but is also able to
CC di-/tri-methylate the GPKRIA peptide and di-methylate the PPKRIA
CC peptide (in vitro). May activate NTMT1 by priming its substrates for
CC trimethylation. {ECO:0000250|UniProtKB:Q5VVY1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-
CC methionine = H(+) + N-terminal N-methyl-L-alanyl-L-prolyl-L-lysyl-
CC [protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54096,
CC Rhea:RHEA-COMP:13785, Rhea:RHEA-COMP:13786, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138057,
CC ChEBI:CHEBI:138058; EC=2.1.1.299;
CC Evidence={ECO:0000250|UniProtKB:Q5VVY1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54097;
CC Evidence={ECO:0000250|UniProtKB:Q5VVY1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-
CC methionine = H(+) + N-terminal N-methyl-L-prolyl-L-prolyl-L-lysyl-
CC [protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54100,
CC Rhea:RHEA-COMP:13787, Rhea:RHEA-COMP:13788, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138059,
CC ChEBI:CHEBI:138060; EC=2.1.1.299;
CC Evidence={ECO:0000250|UniProtKB:Q5VVY1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54101;
CC Evidence={ECO:0000250|UniProtKB:Q5VVY1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-
CC methionine = H(+) + N-terminal N-methyl-L-seryl-L-prolyl-L-lysyl-
CC [protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54104,
CC Rhea:RHEA-COMP:13789, Rhea:RHEA-COMP:13790, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138061,
CC ChEBI:CHEBI:138062; EC=2.1.1.299;
CC Evidence={ECO:0000250|UniProtKB:Q5VVY1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54105;
CC Evidence={ECO:0000250|UniProtKB:Q5VVY1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5VVY1}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family.
CC {ECO:0000305}.
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DR EMBL; CH473958; EDM09375.1; -; Genomic_DNA.
DR RefSeq; XP_001074994.2; XM_001074994.5.
DR RefSeq; XP_222824.5; XM_222824.8.
DR AlphaFoldDB; D3ZVR1; -.
DR SMR; D3ZVR1; -.
DR STRING; 10116.ENSRNOP00000068028; -.
DR PaxDb; D3ZVR1; -.
DR PRIDE; D3ZVR1; -.
DR Ensembl; ENSRNOT00000076404; ENSRNOP00000068028; ENSRNOG00000025415.
DR GeneID; 289167; -.
DR UCSC; RGD:1564106; rat.
DR CTD; 149281; -.
DR RGD; 1564106; Mettl11b.
DR eggNOG; KOG3178; Eukaryota.
DR GeneTree; ENSGT00390000008371; -.
DR HOGENOM; CLU_055356_3_0_1; -.
DR InParanoid; D3ZVR1; -.
DR OMA; RKYDVIW; -.
DR OrthoDB; 1528533at2759; -.
DR PhylomeDB; D3ZVR1; -.
DR TreeFam; TF314174; -.
DR PRO; PR:D3ZVR1; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000234681; Chromosome 13.
DR Bgee; ENSRNOG00000025415; Expressed in esophagus and 5 other tissues.
DR ExpressionAtlas; D3ZVR1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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:0006480; P:N-terminal protein amino acid methylation; 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 SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..283
FT /note="N-terminal Xaa-Pro-Lys N-methyltransferase 2"
FT /id="PRO_0000399780"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VVY1"
FT BINDING 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VVY1"
FT BINDING 146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VVY1"
FT BINDING 174..175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VVY1"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VVY1"
SQ SEQUENCE 283 AA; 32312 MW; 51D969AADB30C17C CRC64;
MAHLGAHFAF RSRWQKTDDE LCRHSMSFIL HKAIRNDFFQ SYLYLLEKIP LVKLYALTSQ
VIDGEMQFYA RAKLFYQEVP ATEEGMMGNF IELSNPDIQA SREFLRKFVG GPGRAGTGCA
LDCGSGIGRV SKHVLLPVFS SVELVDMMES FLLEAQSYLQ VNENKVESYH CYSLQEFTPH
LGRYDVIWIQ WVSGYLTDKD LLAFLSRCRD GLKENGVIIL KDNVAREGCI FDLSDSSVTR
DMDILRSLIR KSGLVVLGQE KQEGFPEQCV PVWMFALHSD RHS
