ID A0A017HBM2_9RHOB Unreviewed; 547 AA.
AC A0A017HBM2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN ORFNames=Lokhon_01846 {ECO:0000313|EMBL:EYD71776.1};
OS Limimaricola hongkongensis DSM 17492.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1122180 {ECO:0000313|EMBL:EYD71776.1, ECO:0000313|Proteomes:UP000025047};
RN [1] {ECO:0000313|EMBL:EYD71776.1, ECO:0000313|Proteomes:UP000025047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17492 {ECO:0000313|EMBL:EYD71776.1,
RC ECO:0000313|Proteomes:UP000025047};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (MAR-2013) 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 -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016}.
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:EYD71776.1}.
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DR EMBL; APGJ01000006; EYD71776.1; -; Genomic_DNA.
DR RefSeq; WP_017928675.1; NZ_KK088652.1.
DR AlphaFoldDB; A0A017HBM2; -.
DR STRING; 1122180.Lokhon_01846; -.
DR REBASE; 128644; M.Lho17492ORF1846P.
DR PATRIC; fig|1122180.6.peg.1827; -.
DR eggNOG; COG0270; Bacteria.
DR HOGENOM; CLU_014695_0_0_5; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000025047; 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; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF50; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT3; 1.
DR Pfam; PF00145; DNA_methylase; 2.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:UP000025047};
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 96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 547 AA; 59218 MW; BA9DFD08FC232DC9 CRC64;
MDGGLFTGFP TAAPGADLPP LIADSFAGGG GASTGIEMAL GRSPGVAINH DEMALAMHGA
NHPETRHLTS SVYAIDPRDL VRPGQRVGLA WFSPDCKHHS KAKGGKPLEK NIRDLAWVVV
HWAELVRPEV ICLENVEEFQ DWCPLGPDHR PVAAQRGATF RLWVGRLRKL GYKVEWRELR
ACDFGAPTIR KRLFLVARCD GRPIIWPTPT HGAPDSAEVL AGKRKPWRTA AEIIDWSIPC
PSIFDTSEEI MRKHGVRAIR PLAENTLKRV ARGIQRFVIE ARQPFLVTYA QHGGAMRSGF
DPVHTITASL KDQNALIIPT LVQTGYGERE GQQPRSLDLH KPIGTMVAGG AKHALVAAFL
AQHNAGAKME RHAGRPATAP ISTLTTRGTQ QNVVAATMMN LRGTAEAQLA GRSIEVPAPT
VTSGGNHAGL VAAFMTKYYG QGEGQDIGEP CHTLTTRDRF GVVTVEIGGE PYAITDIGMR
MLTPREQFRA QGFPDSYIID RGADGRPMPK THQTQKCGNS VCPPVAAALI RANCAHLAAD
RVKETAA
//