ID A0A0U3MSN9_9MOLU Unreviewed; 406 AA.
AC A0A0U3MSN9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN ORFNames=ASO20_02230 {ECO:0000313|EMBL:ALV23455.1};
OS Mycoplasma sp. (ex Biomphalaria glabrata).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1749074 {ECO:0000313|EMBL:ALV23455.1, ECO:0000313|Proteomes:UP000063836};
RN [1] {ECO:0000313|Proteomes:UP000063836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Swain M.T., Geyer K., Niazi U., Hoffmann K.F.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALV23455.1, ECO:0000313|Proteomes:UP000063836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Barreiro1 {ECO:0000313|EMBL:ALV23455.1};
RA Adema C.M.;
RT "Whole genome analysis of Biomphalaria glabrata (Mollusca, Lophotrochozoa),
RT a snail intermediate host for transmission of schistosomiasis.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC Evidence={ECO:0000256|ARBA:ARBA00001893};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC subfamily. {ECO:0000256|ARBA:ARBA00010203}.
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DR EMBL; CP013128; ALV23455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3MSN9; -.
DR STRING; 1749074.ASO20_02230; -.
DR REBASE; 136862; M.MspBgORF2230P.
DR KEGG; myg:ASO20_02230; -.
DR PATRIC; fig|1749074.3.peg.426; -.
DR OrthoDB; 9800801at2; -.
DR Proteomes; UP000063836; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR017985; MeTrfase_CN4_CS.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000063836};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 28..98
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
SQ SEQUENCE 406 AA; 47580 MW; 1BB1690B7D000554 CRC64;
MAKIFKYKGD EKFTLDTLIN LKDIDVDWSR TGDKNASSLH SISSYLAMFA PAMPRYFIEK
LTQENDLVYD PFSGRGTTAL KSREMNRRFV GSDLNPYALV LSRSKIATCT KQEAINYVNN
LEINFKVWKD NENNVNKFNN ENFSELRYFY SKSVLTQLIF LRENYGINWR NFSDVQNFVF
GITLGIMHGK LKKDGTTIYF SLDMPNTISM APNYVKKFAA AKNLIKPDVN IFELIRNRIN
QKYDELLSKK FKSNIYEINA LENNKDIENN SIKLLITSPP YLSVVNYTNS NWLKLWLLGY
ERSNLRNEIK LSDRLNFEKY TNFMIDFLEN VYDKIQIGGY IVLIVGDVHN EKLIEKVWEI
IQNKVKFNLK EIYWDDKYLQ THKITNMLNG KKGKATTIEK VLLLRK
//
