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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//