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 03-AUG-2022, entry version 120.
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 = 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 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 = 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 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 = 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 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}.
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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; -.
DR EPD; Q9N4D9; -.
DR PaxDb; Q9N4D9; -.
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 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; 1528533at2759; -.
DR PhylomeDB; Q9N4D9; -.
DR PRO; PR:Q9N4D9; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022277; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; 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; IBA:GO_Central.
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..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
