NTM1_YEAST
ID NTM1_YEAST Reviewed; 232 AA.
AC P38340; D6VQQ8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Alpha N-terminal protein methyltransferase 1;
DE EC=2.1.1.244;
DE AltName: Full=Translation associated element 1;
DE AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1;
DE Short=NTM1;
GN Name=TAE1; Synonyms=NTM1; OrderedLocusNames=YBR261C; ORFNames=YBR1729;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8465606; DOI=10.1002/yea.320090210;
RA Doignon F., Biteau N., Crouzet M., Aigle M.;
RT "The complete sequence of a 19,482 bp segment located on the right arm of
RT chromosome II from Saccharomyces cerevisiae.";
RL Yeast 9:189-199(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=19055778; DOI=10.1186/1471-2164-9-583;
RA Alamgir M., Eroukova V., Jessulat M., Xu J., Golshani A.;
RT "Chemical-genetic profile analysis in yeast suggests that a previously
RT uncharacterized open reading frame, YBR261C, affects protein synthesis.";
RL BMC Genomics 9:583-583(2008).
RN [7]
RP FUNCTION.
RX PubMed=20481588; DOI=10.1021/bi100428x;
RA Webb K.J., Lipson R.S., Al-Hadid Q., Whitelegge J.P., Clarke S.G.;
RT "Identification of protein N-terminal methyltransferases in yeast and
RT humans.";
RL Biochemistry 49:5225-5235(2010).
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. Responsible for the N-terminal methylation of the
CC ribosomal proteins RPL12A, RPL12B, RPS25A and RPS25B.
CC {ECO:0000269|PubMed:20481588}.
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 -!- 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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Defects in both translation efficiency and
CC fidelity. {ECO:0000269|PubMed:19055778}.
CC -!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family.
CC {ECO:0000305}.
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DR EMBL; X70529; CAA49926.1; -; Genomic_DNA.
DR EMBL; Z36130; CAA85224.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07378.1; -; Genomic_DNA.
DR PIR; S32963; S32963.
DR RefSeq; NP_009820.1; NM_001178609.1.
DR PDB; 7D8D; X-ray; 1.05 A; A=1-232.
DR PDB; 7D8F; X-ray; 1.15 A; A=1-232.
DR PDBsum; 7D8D; -.
DR PDBsum; 7D8F; -.
DR AlphaFoldDB; P38340; -.
DR SMR; P38340; -.
DR BioGRID; 32957; 219.
DR DIP; DIP-4951N; -.
DR IntAct; P38340; 43.
DR STRING; 4932.YBR261C; -.
DR iPTMnet; P38340; -.
DR MaxQB; P38340; -.
DR PaxDb; P38340; -.
DR PRIDE; P38340; -.
DR EnsemblFungi; YBR261C_mRNA; YBR261C; YBR261C.
DR GeneID; 852564; -.
DR KEGG; sce:YBR261C; -.
DR SGD; S000000465; TAE1.
DR VEuPathDB; FungiDB:YBR261C; -.
DR eggNOG; KOG3178; Eukaryota.
DR GeneTree; ENSGT00390000008371; -.
DR HOGENOM; CLU_055356_3_1_1; -.
DR InParanoid; P38340; -.
DR OMA; PVRMYCL; -.
DR BioCyc; YEAST:G3O-29185-MON; -.
DR BRENDA; 2.1.1.244; 984.
DR PRO; PR:P38340; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38340; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0018016; P:N-terminal peptidyl-proline dimethylation; IDA:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..232
FT /note="Alpha N-terminal protein methyltransferase 1"
FT /id="PRO_0000119292"
FT BINDING 71
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 123..124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:7D8D"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:7D8D"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:7D8D"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:7D8D"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:7D8D"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:7D8D"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:7D8D"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:7D8F"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:7D8D"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:7D8D"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:7D8D"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:7D8D"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:7D8D"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:7D8D"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:7D8D"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:7D8D"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:7D8D"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:7D8D"
FT STRAND 161..172
FT /evidence="ECO:0007829|PDB:7D8D"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:7D8D"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:7D8D"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:7D8D"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:7D8D"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:7D8D"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:7D8D"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:7D8D"
SQ SEQUENCE 232 AA; 26068 MW; 66699F37B0013088 CRC64;
MDVPADSHIK YEDAIDYWTD VDATVDGVLG GYGEGTVVPT MDVLGSNNFL RKLKSRMLPQ
ENNVKYAVDI GAGIGRVSKT MLHKHAAKID LVEPVKPFIE QMHVELAELK DKGQIGQIYE
VGMQDWTPDA GKYWLIWCQW CVGHLPDAEL VAFLKRCIVG LQPNGTIVVK ENNTPTDTDD
FDETDSSVTR SDAKFRQIFE EAGLKLIASE RQRGLPRELY PVRMYALKPM PN
