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Database: UniProt
Entry: A0A1H6WHX7_9RHOB
LinkDB: A0A1H6WHX7_9RHOB
Original site: A0A1H6WHX7_9RHOB 
ID   A0A1H6WHX7_9RHOB        Unreviewed;       382 AA.
AC   A0A1H6WHX7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=SAMN05444007_103368 {ECO:0000313|EMBL:SEJ12082.1};
OS   Cribrihabitans marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cribrihabitans.
OX   NCBI_TaxID=1227549 {ECO:0000313|EMBL:SEJ12082.1, ECO:0000313|Proteomes:UP000199379};
RN   [1] {ECO:0000313|EMBL:SEJ12082.1, ECO:0000313|Proteomes:UP000199379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29340 {ECO:0000313|EMBL:SEJ12082.1,
RC   ECO:0000313|Proteomes:UP000199379};
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|ARBA:ARBA00000743,
CC         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; FNYD01000003; SEJ12082.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6WHX7; -.
DR   STRING; 1227549.SAMN05444007_103368; -.
DR   Proteomes; UP000199379; 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; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199379};
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   ACT_SITE        74
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   382 AA;  42392 MW;  275B1B01F6B10000 CRC64;
     MSRTFYEFFA GGGMARAGLG SGWKCLLAND FDRKKGLTYG KNWGDDHLVV DDIRNIGPED
     MPGKPDLVWG SFPCQDLSLA GGGAGLRGDR SGTFWPFISH IQSLRDEGRA PAIIALENVL
     GTLTSHSGKD FAAICEALKN LGYNYGAMVV DASLFVPQSR PRLFVIGVRS DISTPPVQTS
     EEPLAPWHTT GLKNAYKRLP DVLQEGWIWW RMPKPPKREQ SFGDLIEENP ASCKWHTKAE
     TTTLLSMMSE VNLAKVETAK AARKRMVGTI YKRTRHEHGI KVQRAEIRFD DIAGCLRTPA
     GGSSRQLIMV IEGEKIRSRL ISTRETARLM GLPDSYELPD RYNEAYHLTG DGVAVPVVRH
     IAKHVLQPLL LAHETTVSRE VV
//
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