ID N1NZ30_YEASC Unreviewed; 324 AA.
AC N1NZ30;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Mht1p {ECO:0000313|EMBL:EIW08658.1};
GN ORFNames=CENPK1137D_428 {ECO:0000313|EMBL:EIW08658.1};
OS Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=889517 {ECO:0000313|EMBL:EIW08658.1};
RN [1] {ECO:0000313|EMBL:EIW08658.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CEN.PK113-7D {ECO:0000313|EMBL:EIW08658.1};
RA Nijkamp J.F., van den Broek M.A., Datema E., de Kok S., Bosman L.,
RA Luttink M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA Klaassen P., Platt D., Paddon C.J., Koetter P., van Ham R.C.,
RA Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT "De novo sequencing, assembly and analysis of the genome of the laboratory
RT strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT biotechnology.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505-2};
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DR EMBL; CM001533; EIW08658.1; -; Genomic_DNA.
DR AlphaFoldDB; N1NZ30; -.
DR HOGENOM; CLU_004914_3_2_1; -.
DR Proteomes; UP000013192; Chromosome XII.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR PANTHER; PTHR11103:SF18; HOMOCYSTEINE S-METHYLTRANSFERASE 1-RELATED; 1.
DR PANTHER; PTHR11103; SLR1189 PROTEIN; 1.
DR Pfam; PF02574; S-methyl_trans; 1.
DR PIRSF; PIRSF037505; Betaine_HMT; 2.
DR SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR PROSITE; PS50970; HCY; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037505-2, ECO:0000256|PROSITE-
KW ProRule:PRU00333};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00333};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333};
KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2, ECO:0000256|PROSITE-
KW ProRule:PRU00333}.
FT DOMAIN 6..320
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 324 AA; 36744 MW; BD3F282F61F45B0F CRC64;
MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV
VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEKRY
LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL
KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS
FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETM VKKFVDNGAR
IIGGCCRTSP KDIAEIASAV DKYS
//
