GenomeNet

Database: UniProt
Entry: NTM1_CAEEL
LinkDB: NTM1_CAEEL
Original site: NTM1_CAEEL 
ID   NTM1_CAEEL              Reviewed;         234 AA.
AC   Q9N4D9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   27-NOV-2024, entry version 131.
DE   RecName: Full=Alpha N-terminal protein methyltransferase 1 {ECO:0000250|UniProtKB:Q9BV86};
DE            EC=2.1.1.244 {ECO:0000250|UniProtKB:Q9BV86};
DE   AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1 {ECO:0000250|UniProtKB:Q9BV86};
DE            Short=NTM1 {ECO:0000250|UniProtKB:Q9BV86};
GN   Name=homt-1 {ECO:0000312|WormBase:Y74C9A.3};
GN   ORFNames=Y74C9A.3 {ECO:0000312|WormBase:Y74C9A.3};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=17573073; DOI=10.1016/j.neuropharm.2007.04.017;
RA   Tanaka D., Furusawa K., Kameyama K., Okamoto H., Doi M.;
RT   "Melatonin signaling regulates locomotion behavior and homeostatic states
RT   through distinct receptor pathways in Caenorhabditis elegans.";
RL   Neuropharmacology 53:157-168(2007).
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. {ECO:0000250|UniProtKB:Q9BV86}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC         L-methionine = N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-
CC         [protein] + 3 S-adenosyl-L-homocysteine + 3 H(+);
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         Evidence={ECO:0000250|UniProtKB:Q9BV86};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC         L-methionine = N-terminal N,N,N-trimethyl-L-seryl-L-prolyl-L-lysyl-
CC         [protein] + 3 S-adenosyl-L-homocysteine + 3 H(+);
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         Evidence={ECO:0000250|UniProtKB:Q9BV86};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-
CC         L-methionine = N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L-lysyl-
CC         [protein] + 2 S-adenosyl-L-homocysteine + 2 H(+);
CC         Xref=Rhea:RHEA:54736, Rhea:RHEA-COMP:13787, Rhea:RHEA-COMP:13974,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138059, ChEBI:CHEBI:138318; EC=2.1.1.244;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV86};
CC   -!- TISSUE SPECIFICITY: Expressed in uterine cells and PVT neurons of the
CC       tail. {ECO:0000269|PubMed:17573073}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FO080986; CCD68263.1; -; Genomic_DNA.
DR   RefSeq; NP_490660.1; NM_058260.4.
DR   AlphaFoldDB; Q9N4D9; -.
DR   SMR; Q9N4D9; -.
DR   BioGRID; 37096; 3.
DR   STRING; 6239.Y74C9A.3.1; -.
DR   PaxDb; 6239-Y74C9A.3; -.
DR   PeptideAtlas; Q9N4D9; -.
DR   EnsemblMetazoa; Y74C9A.3.1; Y74C9A.3.1; WBGene00022277.
DR   GeneID; 171590; -.
DR   KEGG; cel:CELE_Y74C9A.3; -.
DR   UCSC; Y74C9A.3.1; c. elegans.
DR   AGR; WB:WBGene00022277; -.
DR   CTD; 171590; -.
DR   WormBase; Y74C9A.3; CE28146; WBGene00022277; homt-1.
DR   eggNOG; KOG3178; Eukaryota.
DR   GeneTree; ENSGT00390000008371; -.
DR   HOGENOM; CLU_055356_3_1_1; -.
DR   InParanoid; Q9N4D9; -.
DR   OMA; PVRMYCL; -.
DR   OrthoDB; 5471049at2759; -.
DR   PhylomeDB; Q9N4D9; -.
DR   PRO; PR:Q9N4D9; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00022277; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006480; P:N-terminal protein amino acid methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   FunFam; 3.40.50.150:FF:000025; N-terminal Xaa-Pro-Lys N-methyltransferase 1; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR008576; MeTrfase_NTM1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12753; AD-003 - RELATED; 1.
DR   PANTHER; PTHR12753:SF0; ALPHA N-TERMINAL PROTEIN METHYLTRANSFERASE 1; 1.
DR   Pfam; PF05891; Methyltransf_PK; 1.
DR   PIRSF; PIRSF016958; DUF858_MeTrfase_lik; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..234
FT                   /note="Alpha N-terminal protein methyltransferase 1"
FT                   /id="PRO_0000399783"
FT   BINDING         71
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT   BINDING         93..95
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT   BINDING         120..121
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT   BINDING         136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV86"
SQ   SEQUENCE   234 AA;  26632 MW;  988CDEE1C7CEE4E6 CRC64;
     MSSSSSSRIH NGEDVYEKAE EYWSRASQDV NGMLGGFEAL HAPDISASKR FIEGLKKKNL
     FGYFDYALDC GAGIGRVTKH LLMPFFSKVD MEDVVEELIT KSDQYIGKHP RIGDKFVEGL
     QTFAPPERRY DLIWIQWVSG HLVDEDLVDF FKRCAKGLKP GGCIVLKDNV TNHEKRLFDD
     DDHSWTRTEP ELLKAFADSQ LDMVSKALQT GFPKEIYPVK MYALKPQHTG FTNN
//
DBGET integrated database retrieval system