ID   MT36_OCEIH              Reviewed;         460 AA.
AC   Q8EL95;
DT   30-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Putative type II methyltransferase M.OihORF3336P {ECO:0000303|PubMed:12654995};
DE            Short=M.OihORF3336P {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase;
DE   AltName: Full=Putative modification methylase OB3336;
GN   OrderedLocusNames=OB3336;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: A methylase, recognizes the double-stranded sequence 5'-
CC       ACCGGT-3', methylates C-? on both strands. No endonuclease has been
CC       identified for this methylase. {ECO:0000303|PubMed:12654995}.
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   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; BA000028; BAC15292.1; -; Genomic_DNA.
DR   RefSeq; WP_011067734.1; NC_004193.1.
DR   AlphaFoldDB; Q8EL95; -.
DR   SMR; Q8EL95; -.
DR   STRING; 221109.22779025; -.
DR   REBASE; 11861; M.Ret42ORF108P.
DR   REBASE; 203433; M.Bam1267ORF4054P.
DR   REBASE; 6390; M.OihORF3336P.
DR   EnsemblBacteria; BAC15292; BAC15292; BAC15292.
DR   KEGG; oih:OB3336; -.
DR   eggNOG; COG0270; Bacteria.
DR   HOGENOM; CLU_006958_2_4_9; -.
DR   OMA; YAIDLFC; -.
DR   OrthoDB; 1178320at2; -.
DR   PhylomeDB; Q8EL95; -.
DR   PRO; PR:Q8EL95; -.
DR   Proteomes; UP000000822; Chromosome.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..460
FT                   /note="Putative type II methyltransferase M.OihORF3336P"
FT                   /id="PRO_0000087915"
FT   DOMAIN          15..458
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   460 AA;  52508 MW;  5483B86933CDBD0C CRC64;
     MHQIYSATST DKKLPEVVDL FSGCGGLALG FQLAGFNIRK GIELDRDASD VASFNLHWRQ
     GKHDRHLNND ITLLSANEFY NDLDRKNDLI VIGGPPCQAY SKIGRAKLKS LGEERRQEND
     ARGKLYENFL DYALHVDANV IVMENVPEAV NYGGVNIPDT VCDILINKGY DAIWTVLNAA
     DFGVPQTRVR LFVMAIKKDI GKIKFIPEPT HKPHINVKRQ SVNVRWMQSE IRNSKYYKQP
     NIPDETLSDW VTVGDAIGDL PNLFPVYNQK YKNYKPMMMK EYKSPPQNTF QKLMRINNKV
     DKVTGNMFRN TKRDFSIFDK MEEGDNYLDA HNIAMSLLRK EMRKSGITKE NEFEYRLLKD
     RIVPPYSTEK FVEKWRKLSS DKPSHTLVAH LSTDTYSHLH PREPRGISVR EAARLQSFPD
     DFLFDCSMGA AFKQIGNAVP PLLAKAIAEA MKKNIQGGCI