ID A0A0G0XD66_9BACT Unreviewed; 546 AA.
AC A0A0G0XD66;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=UU81_C0048G0001 {ECO:0000313|EMBL:KKS22810.1};
OS Microgenomates group bacterium GW2011_GWC1_41_8.
OC Bacteria.
OX NCBI_TaxID=1618519 {ECO:0000313|EMBL:KKS22810.1, ECO:0000313|Proteomes:UP000034304};
RN [1] {ECO:0000313|EMBL:KKS22810.1, ECO:0000313|Proteomes:UP000034304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 Vsr family. {ECO:0000256|ARBA:ARBA00029466}.
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:KKS22810.1}.
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DR EMBL; LCCB01000048; KKS22810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0XD66; -.
DR PATRIC; fig|1618519.3.peg.952; -.
DR Proteomes; UP000034304; Unassembled WGS sequence.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR CDD; cd00221; Vsr; 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 Gene3D; 3.40.960.10; VSR Endonuclease; 1.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR004603; DNA_mismatch_endonuc_vsr.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00675; dcm; 1.
DR NCBIfam; TIGR00632; vsr; 1.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR Pfam; PF00145; DNA_methylase; 2.
DR Pfam; PF03852; Vsr; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
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 256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 546 AA; 62544 MW; 1FADDC6D2C117538 CRC64;
MADVLTITQR SYNMSRIKSG NTAPELRLQE LLVSEGFGNF ETHPKSVPGR PDFYFSNHKS
AIFVDGCFWH ACKDCYKAPQ TNEEFWKMKI GTNVQRDETV NKKLNDLGIA VIRVKEHELK
KDAALVMQNI GKELSKRVQP RVLDLFAGAG GLSEGFIRAG CEMVGHIEME KNSCSTLLTR
MIYHALRKKG ELEDYKKYIT GRITREKLIE KYGLQKERDS VICAAIGKDN YGDLIEQVRT
RLNGKSLDII VGGPPCQAYS YIGRARDIKK MRTDERNFLY KYYIEFLKAL KPKIFVFENV
PGLLSAGEGR YLLHMRQLML SAGYATDYRI LNAADYGVPQ NRKRVILVGW RKDSNLKSYP
EFPVVNREYK VKDFFSDLPK IKSGGGKPIK KFSRKNKLLQ DLGIRNPDFE FLMDHITRPH
TDRDLEIYHL AVLAKQKGEN IKYNTLPERL KTHNNEISFL DRFKVVDADA PGSHTVVAHI
AKDGHFYIHP DLKQNRSLSV REAARLQTFP DDYKFEGERG PQLKQIGNAV PPILSEIIAK
ELIKHL
//
