MTBS_BPSPR
ID MTBS_BPSPR Reviewed; 439 AA.
AC P00476;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Orphan methyltransferase M.SPRI {ECO:0000303|PubMed:12654995};
DE Short=M.SPRI {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase SPRI;
DE AltName: Full=Modification methylase SPRI;
OS Bacillus phage SPR (Bacteriophage SPR).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Lambdavirus; unclassified Lambdavirus.
OX NCBI_TaxID=10725;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6092231; DOI=10.1016/0378-1119(84)90165-3;
RA Buhk H.-J., Behrens B., Tailor R., Wilke K., Prada J.J., Gunthert U.,
RA Noyer-Weidner M., Jentsch S., Trautner T.A.;
RT "Restriction and modification in Bacillus subtilis: nucleotide sequence,
RT functional organization and product of the DNA methyltransferase gene of
RT bacteriophage SPR.";
RL Gene 29:51-61(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6096817; DOI=10.1093/nar/12.23.9039;
RA Posfai G., Baldauf F., Erdei S., Posfai J., Venetianer P., Kiss A.;
RT "Structure of the gene coding for the sequence-specific DNA-
RT methyltransferase of the B. subtilis phage SPR.";
RL Nucleic Acids Res. 12:9039-9049(1984).
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 the C-1 in the sequence
CC 5'-GGCC-3' and both cytosines in the sequence 5'-CCGG-3' (Probable). A
CC methyltransferase that methylates C-3 within the sequence 5'-GGCC-3',
CC C-1 in 5'-CCGG-3' and C-2 in 5'-CCWGG-3'. Modification confers
CC resistance against restriction enzymes that recognize these sequences
CC (PubMed:12654995). {ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:6092231}.
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 -!- SUBUNIT: Monomer.
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; K02124; AAA32604.1; -; Genomic_DNA.
DR PIR; A91516; CTBPSR.
DR SMR; P00476; -.
DR REBASE; 2834; M.SPRI.
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..439
FT /note="Orphan methyltransferase M.SPRI"
FT /id="PRO_0000087868"
FT DOMAIN 4..436
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 413
FT /note="T -> A (in Ref. 2; AAA32604)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="I -> V (in Ref. 2; AAA32604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 49881 MW; 407DCF178D32D5BE CRC64;
MGKLRVMSLF SGIGAFEAAL RNIGVGYELV GFSEIDKYAV KSFCAIHNVD EQLNFGDVSK
IDKKKLPEFD LLVGGSPCQS FSVAGHRKGF EDTRGTLFFQ YVETLKEKQP KFFVFENVKG
LINHDKGNTL NVMAEAFSEV GYRIDLELLN SKFFNVPQNR ERLYIIGIRE DLIKNEEWSL
DFKRKDILQK GKQRLVELDI KSFNFRWTAQ SAATKRLKDL LEEYVDEKYY LNEDKTNSLI
KELSTSRLNE NLTVEQVGNI NPSGNGMNGN VYNSSGLSPT ITTNKGEGLK IAVEYSRKSG
LGRELAVSHT LSASDWRGLN RNQKQNAVVE VRPVLTPERG EKRQNGRRFK DDGEPAFTVN
TIDRHGVAVG EYPKYRIRRL TPLECFRLQA FDDEDFEKAF AAGISNSQLY KQTGNSITVT
VLESIFKELI HTYINKESE
