MTBP_BPPHT
ID MTBP_BPPHT Reviewed; 443 AA.
AC P68586; P05795;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Orphan methyltransferase M.Phi3TI {ECO:0000303|PubMed:12654995};
DE Short=M.Phi3TI {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase Phi3TI;
DE AltName: Full=Modification methylase Phi3TI;
GN Name=mtbP;
OS Bacillus phage phi3T (Bacteriophage phi-3T).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Spbetavirus; unclassified Spbetavirus.
OX NCBI_TaxID=10736;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3087819; DOI=10.1016/0378-1119(86)90153-8;
RA Tran-Betcke A., Behrens B., Noyer-Weidner M., Trautner T.A.;
RT "DNA methyltransferase genes of Bacillus subtilis phages: comparison of
RT their nucleotide sequences.";
RL Gene 42:89-96(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-91 AND 125-443.
RX PubMed=3142766; DOI=10.1002/j.1460-2075.1988.tb03110.x;
RA Wilke K., Rauhut E., Noyer-Weidner M., Lauster R., Pawlek B., Behrens B.,
RA Trautner T.A.;
RT "Sequential order of target-recognizing domains in multispecific DNA-
RT methyltransferases.";
RL EMBO J. 7:2601-2609(1988).
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-1 within the sequences
CC 5'-GGCC-3' and 5'-GCNGC-3' (PubMed:12654995). Modification confers
CC resistance against restriction enzymes that recognize these sequences
CC (Probable). {ECO:0000303|PubMed:12654995, ECO:0000305}.
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; M13488; AAA32352.1; -; Genomic_DNA.
DR PIR; A24465; CTBPPT.
DR SMR; P68586; -.
DR REBASE; 2633; M.Phi3TI.
DR PRO; PR:P68586; -.
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; 2.
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..443
FT /note="Orphan methyltransferase M.Phi3TI"
FT /id="PRO_0000087866"
FT DOMAIN 4..440
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"
FT CONFLICT 40
FT /note="I -> V (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="V -> L (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 50510 MW; 2BF02005159E9879 CRC64;
MSKLRVMSLF SGIGAFEAAL RNIGVDYELI GFSEIDKYAI KSYCAIHNVS ETLNVGDISK
AKKDNIPYFD LLTSGFPCPT FSVAGGRDGM EYKCSNCSHE HLITYEDYKK GVKCPKCEAV
SKAKDERGTL FFETALLAEE KKPKFVILEN VKGLINSGNG QVLRIISETM NNIGYRIDLE
LLNSKFFNVP QNRERVYIIG IREDLVENEQ WVVGQKRNDV LSKGKKRLQE INIKSFNFKW
PLQDTVTKRL REILEDFVDE KYYLNEEKTK KLVEQLGTAP LQKQEVREPL MVGHVDLKGH
DAIKRVYSPE GLSPTLTTMG GGHREPKIAE KQKEVRAVLT PEREEKRQNG RRFKENGEPA
FTVNTIDRHG VAIGEYPKYK IRKLSPLECW RLQAFDDEDF EKAFAAGISN SQLYKQAGNS
ITVSVLESIF QELIHTYVNK ESE
