ID   MTBR_BPRH1              Reviewed;         503 AA.
AC   P09915;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Orphan methyltransferase M.Rho11sI {ECO:0000303|PubMed:12654995};
DE            Short=M.Rho11sI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Bsu P11s;
DE   AltName: Full=Cytosine-specific methyltransferase Rho11sI;
DE   AltName: Full=Modification methylase Rho11sI;
OS   Bacillus phage rho11s (Bacteriophage rho-11s).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Lambdavirus; unclassified Lambdavirus.
OX   NCBI_TaxID=10735;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=3109889; DOI=10.1002/j.1460-2075.1987.tb04869.x;
RA   Behrens B., Noyer-Weidner M., Pawlek B., Lauster R., Balganesh T.S.,
RA   Trautner T.A.;
RT   "Organization of multispecific DNA methyltransferases encoded by temperate
RT   Bacillus subtilis phages.";
RL   EMBO J. 6:1137-1142(1987).
RN   [2]
RP   SEQUENCE REVISION TO 476.
RA   Trautner T.A.;
RL   Submitted (SEP-1987) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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 methyltransferase that methylates C-? within the sequences
CC       5'-GGCC-3' and 5'-GAGCTC-3' (Probable). A methyltransferase that
CC       methylates C-1 within the sequences 5'-GGCC-3' and C-2 in 5'-GCNGC-3'
CC       (PubMed:12654995). Modification confers resistance against restriction
CC       enzymes that recognize these sequences (Probable).
CC       {ECO:0000303|PubMed:12654995, ECO:0000305, ECO:0000305|PubMed:3109889}.
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:0000255|PROSITE-ProRule:PRU10018};
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; X05242; CAA28869.1; -; Genomic_DNA.
DR   PIR; A28137; CTBPRH.
DR   SMR; P09915; -.
DR   REBASE; 2835; M.Rho11sI.
DR   REBASE; 7238; M.Rho11sII.
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:0099018; P:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 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   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 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   DNA-binding; Host-virus interaction; Methyltransferase;
KW   Restriction-modification system evasion by virus; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..503
FT                   /note="Orphan methyltransferase M.Rho11sI"
FT                   /id="PRO_0000087869"
FT   DOMAIN          4..500
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   503 AA;  57130 MW;  AAAFB8FE01B8129E CRC64;
     MSKLRVMSLF SGIGAFEAAL RNIGVEYELV GFSEIDKYAI KSYCAIHNAD EQLNFGDVSK
     IDKKKLPEFD LLVGGSPCQS FSVAGYRKGF EDTRGTLFFQ YIDTLKEKQP RYFVFENVKG
     LINHDKGNTL NIMAESFSEV GYRIDLELLN SKFFNVPQNR ERIYIIGVRE DLIENDEWVV
     EKGRNDVLSK GKKRLKELNI KSFNFKWSAQ DIVGRRLREI LEEYVDEKYY LSEEKTSKLI
     EQIEKPKEKD VVFVGGINVG KRWLNNGKTY SRNFKQGNRV YDSNGIATTL TSQSVGGLGG
     QTSLYKVEDP IMIGHIDLKG HDAIKRVYSP DGVSPTLTTM GEGHREPKIA VEYVGNINPS
     GKGMNDQVYN SNGLSPTLTT NKGEGVKISV PNPEIRPVLT PEREEKRQNG RRFKEDDEPA
     FTVNTIDRHG VAIGEYPKYR IRKLTPLECW RLQAFDEEDF EKALSVGISN SQLYKQAGNS
     ITVTVLESIF KELIHTYVNE ESE