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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
 
 
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