NTM1B_DANRE
ID NTM1B_DANRE Reviewed; 278 AA.
AC B8JM82;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 61.
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; ORFNames=si:ch211-214d2.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAX14472.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CU571309; CAX14472.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B8JM82; -.
DR SMR; B8JM82; -.
DR STRING; 7955.ENSDARP00000120895; -.
DR PaxDb; B8JM82; -.
DR PRIDE; B8JM82; -.
DR ZFIN; ZDB-GENE-081104-175; ntmt2.
DR eggNOG; KOG3178; Eukaryota.
DR InParanoid; B8JM82; -.
DR PhylomeDB; B8JM82; -.
DR TreeFam; TF314174; -.
DR PRO; PR:B8JM82; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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..278
FT /note="N-terminal Xaa-Pro-Lys N-methyltransferase 2"
FT /id="PRO_0000399781"
FT BINDING 123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VVY1"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VVY1"
FT BINDING 145
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"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VVY1"
SQ SEQUENCE 278 AA; 32383 MW; 884DD76B83173BE7 CRC64;
MEFSGTHQAF RNRWAKTDDE MCKHSMSFHL HKTLRKEFFA SYLYLLEQIP LVKLYALTCE
YIKGEKQFYY RAQNFYKDVP PSEEGMMGDF VEISDIDLEG SRQFLKKFVG PGKAGTKCAL
DCGCGIGRVS KGVLFPVFES MEMLDMMEEF ILHAHECYLG DYADRVESYY LYNLQEFIPP
RKKYDVIWMQ WVACHLTDKD LMEFLMRAKE SLRPNGVIII KDNMARQGCK LDPIDSSIIR
HLDIMNGIIQ RAGLNILDVE KQEGFPEAIV PVWMIAMR
