ID E1MBI1_9ACTO Unreviewed; 424 AA.
AC E1MBI1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=HMPREF9278_0599 {ECO:0000313|EMBL:EFN94135.1};
OS Mobiluncus mulieris FB024-16.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=866770 {ECO:0000313|EMBL:EFN94135.1, ECO:0000313|Proteomes:UP000004387};
RN [1] {ECO:0000313|EMBL:EFN94135.1, ECO:0000313|Proteomes:UP000004387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB024-16 {ECO:0000313|EMBL:EFN94135.1,
RC ECO:0000313|Proteomes:UP000004387};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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 -!- 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:EFN94135.1}.
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DR EMBL; AEGV01000006; EFN94135.1; -; Genomic_DNA.
DR RefSeq; WP_004016016.1; NZ_AEGV01000006.1.
DR AlphaFoldDB; E1MBI1; -.
DR REBASE; 42997; M.Mmu24ORF599P.
DR GeneID; 66606779; -.
DR Proteomes; UP000004387; Unassembled WGS sequence.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR CDD; cd04762; HTH_MerR-trunc; 1.
DR Gene3D; 1.10.1660.10; -; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
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; PF00376; MerR; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00552; HTH_MERR_1; 1.
DR PROSITE; PS50937; HTH_MERR_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 DOMAIN 3..49
FT /note="HTH merR-type"
FT /evidence="ECO:0000259|PROSITE:PS50937"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 424 AA; 47619 MW; 8DA3BFD4C229AECC CRC64;
MDLLSISQAS AQVGVSIDTL RRWDKSGIIR ATRDSRGKRF FDRQEIEALI AKRDCRVHGD
ETRRHFRVLN DPKPNGFTSV DLFAGAGGTA LGLENAGFRH VLLSELDKDA VATLRLNRPN
WNVSAGDVAS LDFRAFAGKV DLVEGGFPCQ AFSYAGHSRG FEDTRGTLFF EFARAVSEIT
PKVFIGENVR GLLRHDSGRT LQTMLHTLTE IRGKHGERYR VGYRLMRAQY HDVPQKRERL
MLAGVRSDIG DELFFPRERN YIVSLWDAIG DRPQSPGQTY PQRKREVLSL VPPGGYWRDL
PDDIAREYLG GSYHLSGGKT GMARRLSWDE PSLTLTCSPA QKQTERCHPE ETRPLNVREY
ARIQTFPDDW KFSGGMSAQY KQIGNAVPVN LAYYMGKCAA ATLGDSRPEI LDFAAPASPQ
DYVN
//
