ID C4ZCR2_AGARV Unreviewed; 672 AA.
AC C4ZCR2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN OrderedLocusNames=EUBREC_0628 {ECO:0000313|EMBL:ACR74417.1};
OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS / VPI 0990) (Eubacterium rectale).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR74417.1, ECO:0000313|Proteomes:UP000001477};
RN [1] {ECO:0000313|EMBL:ACR74417.1, ECO:0000313|Proteomes:UP000001477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC 0990 {ECO:0000313|Proteomes:UP000001477};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001107; ACR74417.1; -; Genomic_DNA.
DR RefSeq; WP_012741533.1; NC_012781.1.
DR AlphaFoldDB; C4ZCR2; -.
DR STRING; 515619.EUBREC_0628; -.
DR REBASE; 21024; M.EreORF628P.
DR PaxDb; 515619-EUBREC_0628; -.
DR KEGG; ere:EUBREC_0628; -.
DR HOGENOM; CLU_408686_0_0_9; -.
DR Proteomes; UP000001477; Chromosome.
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; 3.90.120.10; 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; IPR031303; C5_meth_CS.
DR InterPro; IPR019059; Restrct_endonuc_II_HaeIII.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00675; dcm; 1.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF09556; RE_HaeIII; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 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}; 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 ACT_SITE 77
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 672 AA; 76927 MW; B538B58DD792170B CRC64;
MNIISLFSGC GGLDLGFESA GFNIPVANEF DKTIWATFKA NHPNTHLIEG DIRQVTKEDI
EQYIDGEIDG IIGGPPCQSW SEAGSLKGIK DARGQLFFDY IRILKEFQPK FFLAENVSGM
LANRHSEAVQ NILNLFDGAG YDVSFTLVNA KDYGVAEERK RVFYIGFRKD LNIDFGFPKG
STKEDDKKIT LRDIIWDLQD TAVPSGEKNH HNPEAINNNE YYTGAYSPIF MSRNRVKSWD
EQAFTVQASG RQCQLHPQAP KMVKVGQNDC RFVEGKEHLY RRMTIREVAR VQGFPDNFKF
IYEDTNTAYK MIGNAVPVNL AYEIAVAIKK YLEGNSADVV VDDDVIDAKE VNEKKVSTKS
NDQGRAYEYA WIKTLYKALC EMRKTKIVDN SSLHANEKAW MLMDEEMQQT FMISAEAAIN
EVLEMEPRLS ENDNDELTLE FQKDGAGVKG DVRDIVIRRD DIEWEIGLSI KHNHDAVKHS
RLSHKLDFGK EWFDIPCSNE YWGAVNPIFD MLKSEKENGS RWSEIVQKDE NVYVPLLQAF
MDEVNRAYKE DKNMPEKMIE YLIGKEDYYK IVSHDSKRLT LIHTFNMHDT LNKSSKDKVS
EIEVPVVELP TRLIDIGFKP KSNNTVEMIL DNGWQLSFRI HSASTKVEPS LKFDVQFISM
PVSVCTIKCV WK
//
