ID A0A0J5GS04_9BACI Unreviewed; 402 AA.
AC A0A0J5GS04;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=AB685_16985 {ECO:0000313|EMBL:KMJ57117.1};
OS Bacillus sp. LL01.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1665556 {ECO:0000313|EMBL:KMJ57117.1, ECO:0000313|Proteomes:UP000036436};
RN [1] {ECO:0000313|EMBL:KMJ57117.1, ECO:0000313|Proteomes:UP000036436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL01 {ECO:0000313|EMBL:KMJ57117.1,
RC ECO:0000313|Proteomes:UP000036436};
RA Vilo C., Galetovic A., Araya J., Gomez Silva B., Dong Q.;
RT "Draft Genome Sequence of a Bacillus Bacterium from the Atacama Desert
RT Wetlands Metagenome.";
RL Submitted (JUN-2015) 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:KMJ57117.1}.
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DR EMBL; LFEL01000006; KMJ57117.1; -; Genomic_DNA.
DR RefSeq; WP_047971802.1; NZ_LFEL01000006.1.
DR AlphaFoldDB; A0A0J5GS04; -.
DR REBASE; 127363; M2.BspLL01ORF16980P.
DR PATRIC; fig|1665556.3.peg.5391; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000036436; 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 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; 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 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}; 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 101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 402 AA; 46254 MW; F8B8E7C6AFE0EC12 CRC64;
MNFIDIFAGC GGLSEGFKQN PHYTMLGAVE WEKPQVNNLR KHLKNNYKMN DADERVIHFD
IQRTEELING WDNDVEYDSH VGLDALIGDT NVDLIIGGPP CQAYSVAGRI RDGNGMRNDY
RNFLFESYMK LVRHYQPNIF VFENVPGILS ARPNGETLVT DLIRDEIINS GYEIADDLKS
FAQFDLSEYG VPQKRKRVII IGVRKGYKNN IQEALHQFYL DILPQYRENI RTVQDAISNL
PSIIPAESDY ILNGKRYSHV FKNNIPNHIP RYHNRRDINT FKILCEDIEA GTNQYITTHA
LKELYTKITG HKSNIHKYHV LRWNQPSNTI PAHLYKDGLR HIHPDSTQSR SITVREAARL
QTFPDDYKFI SSLGDNYKMI GNAVPPLFAE KLASALVEFI NI
//
