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Database: UniProt
Entry: A0A1I6MGH7_9RHOB
LinkDB: A0A1I6MGH7_9RHOB
Original site: A0A1I6MGH7_9RHOB 
ID   A0A1I6MGH7_9RHOB        Unreviewed;       324 AA.
AC   A0A1I6MGH7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=SAMN05444714_1747 {ECO:0000313|EMBL:SFS14742.1};
OS   Yoonia litorea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Yoonia.
OX   NCBI_TaxID=1123755 {ECO:0000313|EMBL:SFS14742.1, ECO:0000313|Proteomes:UP000198926};
RN   [1] {ECO:0000313|EMBL:SFS14742.1, ECO:0000313|Proteomes:UP000198926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29433 {ECO:0000313|EMBL:SFS14742.1,
RC   ECO:0000313|Proteomes:UP000198926};
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; FOZM01000001; SFS14742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6MGH7; -.
DR   STRING; 1123755.SAMN05444714_1747; -.
DR   OrthoDB; 9813719at2; -.
DR   Proteomes; UP000198926; 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; IPR031303; C5_meth_CS.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000198926};
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        79
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   324 AA;  35553 MW;  732DEFD179145CDB CRC64;
     MTKPLSSIEL CAGGGGQALG LERAGFGHDA LVENDQWARA TLKLNRPTWN VLEGEQCDLT
     KFDATPFRGV DLVAGGVPCP PFSKAGKQLG ADDERDLFPH AVRVIDEVRP KAVMLENVRG
     FLDAVFHDYR NELKSQLKKL GYTRVEWHLY NACDFGVSQL RPRVVIVAMH DDYADNFDWP
     VGKATTPPTV GELLYEMMAS KGWRGAKKWR DNADEIAPTI VGGSKKHGGP DLGPTRAKRA
     WEALGVNGKT IAEEAPERDF VGLPRLTVQM AARVQGFPED WQFAGRKTNA YRQVGNAFPP
     PVAEAVALNV KAAITSTKRL YAVA
//
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