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Database: UniProt
Entry: A0A1G6D736_9FIRM
LinkDB: A0A1G6D736_9FIRM
Original site: A0A1G6D736_9FIRM 
ID   A0A1G6D736_9FIRM        Unreviewed;       719 AA.
AC   A0A1G6D736;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=SAMN02910317_02046 {ECO:0000313|EMBL:SDB40879.1};
OS   Ruminococcaceae bacterium FB2012.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX   NCBI_TaxID=1520817 {ECO:0000313|EMBL:SDB40879.1, ECO:0000313|Proteomes:UP000199364};
RN   [1] {ECO:0000313|EMBL:SDB40879.1, ECO:0000313|Proteomes:UP000199364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB2012 {ECO:0000313|EMBL:SDB40879.1,
RC   ECO:0000313|Proteomes:UP000199364};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC         Evidence={ECO:0000256|RuleBase:RU000417};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01016, ECO:0000256|RuleBase:RU000416}.
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DR   EMBL; FMXS01000010; SDB40879.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6D736; -.
DR   STRING; 1520817.SAMN02910317_02046; -.
DR   Proteomes; UP000199364; Unassembled WGS sequence.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 3.30.70.1270; Api92-like domains; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR040809; LPD28.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR041329; YubB_C.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF00145; DNA_methylase; 2.
DR   Pfam; PF18406; DUF1281_C; 1.
DR   Pfam; PF18843; LPD28; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01016}; Reference proteome {ECO:0000313|Proteomes:UP000199364};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01016};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01016}.
FT   DOMAIN          519..593
FT                   /note="YubB ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18406"
FT   DOMAIN          615..706
FT                   /note="Large polyvalent protein associated"
FT                   /evidence="ECO:0000259|Pfam:PF18843"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   719 AA;  81048 MW;  9E9CCCE7DEC7EEED CRC64;
     MPLIRFFDVF AGIGGFRSGL EKAGGFECVG YCEIDKYAKA AYEAIYDTRG EVYYEDIRKI
     DPEKLPDFEC LCGGFPCQSF SIAGKRRGFN DTRGTMFFEI ARIAAVKKPK YMLLENVPGL
     LNHDGGRTFK TILDALDDLG YDVTWQVLNS ADHYVAQARK RVFIVCFLRE KCSGRVLSYR
     EANPKTLVKR IPGREGERVY DPEGLGITLN ANAGGFAGRT GLYLFTEDAA LPIKSLTKSG
     YQLAYPGDSI DLAYPDMNSR RGRVGDNIAH TVTPSATQGY YDVKCIDMNY GAEITELARC
     IPARQDGGVG HHKGEKSGVL ELTAPIPILT PEKEQVRQQG RRTKDPDDPM FTITVTDRHG
     VVYNGAIRKL LPIECWRLQG FRDSQFLKAQ NAGISRAQLY KQAGNAVTTN VIEVLGRFIQ
     AIDKEEFKTM PNHVKNTLSF SGDPKKISEM KEKIKSDEYG LGTIDFEKII PMPDSIYRGD
     LGKAEMEKYG KNNWYDWRVG HWGTKWPAYG FDETVDYSQN DTIEFQTAWF APHPVIEQLA
     KMYPDITINH KWADEDLGMN CGEHEYADGE RIREFYPEIS KDRLDFALDM WNLDPAELGL
     AVNGYGNDYV QLRGESFELI EVEGQKALFA NHRMTKADIP QGLYVYHLRE GDNGEFSTIE
     PQVLVNHAGS AVTKKPIDFK GADHIDFDED SSPNFLGEEA TFEDLIEMSD QVEDMEVIQ
//
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