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Database: UniProt
Entry: T1C8P0_9ZZZZ
LinkDB: T1C8P0_9ZZZZ
Original site: T1C8P0_9ZZZZ 
ID   T1C8P0_9ZZZZ            Unreviewed;       268 AA.
AC   T1C8P0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=site-specific DNA-methyltransferase (cytosine-N(4)-specific) {ECO:0000256|ARBA:ARBA00012185};
DE            EC=2.1.1.113 {ECO:0000256|ARBA:ARBA00012185};
GN   ORFNames=B1B_00679 {ECO:0000313|EMBL:EQD78522.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD78522.1};
RN   [1] {ECO:0000313|EMBL:EQD78522.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mendez C., Richter M., Ferrer M., Sanchez J.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EQD78522.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA   Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA   Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA   Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA   Ferrer M.;
RT   "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT   along an acid mine drainage.";
RL   ISME J. 8:1259-1274(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQD78522.1}.
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DR   EMBL; AUZY01000505; EQD78522.1; -; Genomic_DNA.
DR   AlphaFoldDB; T1C8P0; -.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   PANTHER; PTHR13370:SF33; TYPE II METHYLTRANSFERASE M.MJAV; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EQD78522.1};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          26..252
FT                   /note="DNA methylase N-4/N-6"
FT                   /evidence="ECO:0000259|Pfam:PF01555"
SQ   SEQUENCE   268 AA;  29522 MW;  95B8FD3887CFCBF7 CRC64;
     MTPEGPTVRL IEGDAAELPR LAPGSIHLVV TSPPYPMIAQ WDGSFAAQGA DDFDGMHALL
     DRAWQSCHRV LVPGGLLAIS IGDAVRTRDG EFRLWPNHAR VLTGAARIGF RPLPYLLWKK
     PLNKPNAFLG SGFLPPNAYV TLDCEFLLLF RKGGLRRFAA HDPRRSASRL TRAERDRWFS
     QVWSDVRGAR QAGPDGRTGA FPPEIPRRLI RMFSVLGDTV LDPFAGTGTT LWVAAELGRR
     AIGVERDPTV HRRSAARGAA LGFRVETE
//
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