MTC1_CITFR
ID MTC1_CITFR Reviewed; 376 AA.
AC Q04845;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Type II methyltransferase M.CfrBI {ECO:0000303|PubMed:12654995};
DE Short=M.CfrBI {ECO:0000303|PubMed:8335262};
DE EC=2.1.1.113 {ECO:0000269|PubMed:8335262};
DE AltName: Full=Modification methylase CfrBI;
DE AltName: Full=N(4)- cytosine-specific methyltransferase CfrBI;
GN Name=cfrBIM {ECO:0000303|PubMed:8335262};
OS Citrobacter freundii.
OG Plasmid pZE8.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=4111;
RX PubMed=8335262; DOI=10.1016/0378-1119(93)90698-3;
RA Zakharova M.V., Kravetz A.N., Beletzkaja I.V., Repyk A.V., Solonin A.S.;
RT "Cloning and sequences of the genes encoding the CfrBI restriction-
RT modification system from Citrobacter freundii.";
RL Gene 129:77-81(1993).
RN [2]
RP NOMENCLATURE, AND SUBTYPE.
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 beta subtype methylase that recognizes the double-stranded
CC sequence 5'-CCWWGG-3', methylates C-1 on both strands, and protects the
CC DNA from cleavage by the CfrBI endonuclease.
CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:8335262}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC Evidence={ECO:0000269|PubMed:8335262};
CC -!- DISRUPTION PHENOTYPE: Loss of methyltransferase activity.
CC {ECO:0000269|PubMed:8335262}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC subfamily. {ECO:0000305}.
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DR EMBL; X57945; CAA41012.1; -; Genomic_DNA.
DR PIR; JN0745; JN0745.
DR AlphaFoldDB; Q04845; -.
DR SMR; Q04845; -.
DR REBASE; 3548; M.CfrBI.
DR BRENDA; 2.1.1.113; 1398.
DR PRO; PR:Q04845; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR017985; MeTrfase_CN4_CS.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Methyltransferase; Plasmid; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..376
FT /note="Type II methyltransferase M.CfrBI"
FT /id="PRO_0000087926"
SQ SEQUENCE 376 AA; 43358 MW; 2EE9E08E36616A21 CRC64;
MTVKNNYLNR GYLVTSTTQA KKIAKLHLEK LDLADKFSFG LPEVDDRYHV WRVPLVATGH
RIGEIVINSK TSTIDYKKSS KSPFLIKKAM EVVHTPKKVK KEKKIISKSP LNNMLLQGNC
AETLKKLPDE SVNLVFTSPP YYNAKPEYSE YHTYDEYLSL LRSVIKECHR VLSEGRFFVI
NVSPVLIRRA SRNEASKRIA VPFDLHRLFI EEGYEFIDDI HWVKPEGAGW ALGRGRRFAA
DRNPLQYKPV PVTEYILVYR KKTDKLIDWN IRNHHSKEDV FDSKIGDDYE KTNLWKINPS
RNRKHPATFP YGLAERVIKY YSFKNDVILD PFAGSGTTAK AAIDLGRRFV MCEISKQYID
LIIEGTMLGG DLKIIN
