MTC9_CITFR
ID MTC9_CITFR Reviewed; 300 AA.
AC P14243;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Type II methyltransferase M.Cfr9I {ECO:0000303|PubMed:8163180};
DE Short=M.Cfr9I {ECO:0000303|PubMed:2690010};
DE EC=2.1.1.113;
DE AltName: Full=Modification methylase Cfr9I;
DE AltName: Full=N(4)- cytosine-specific methyltransferase Cfr9I;
GN Name=cfr9IM {ECO:0000303|PubMed:2690010};
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=RFL9;
RX PubMed=2690010; DOI=10.1093/nar/17.23.9823;
RA Klimasauskas S., Timinskas A., Menkevicius S., Butkiene D., Butkus V.,
RA Janulaitis A.;
RT "Sequence motifs characteristic of DNA[cytosine-N4]methyltransferases:
RT similarity to adenine and cytosine-C5 DNA-methylases.";
RL Nucleic Acids Res. 17:9823-9832(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 258-300.
RC STRAIN=RFL9;
RX PubMed=8163180; DOI=10.1016/0378-1119(94)90132-5;
RA Lubys A., Menkevicius S., Timinskas A., Butkus V., Janulaitis A.;
RT "Cloning and analysis of translational control for genes encoding the Cfr9I
RT restriction-modification system.";
RL Gene 141:85-89(1994).
RN [3]
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, recognizes the double-stranded
CC sequence 5'-CCCGGG-3', methylates C-2 on both strands, and protects the
CC DNA from cleavage by the Cfr9I endonuclease.
CC {ECO:0000303|PubMed:8163180, ECO:0000305|PubMed:2690010}.
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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC subfamily. {ECO:0000305}.
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DR EMBL; X17022; CAA34887.1; -; Genomic_DNA.
DR EMBL; X74517; CAA52629.1; -; Genomic_DNA.
DR PIR; S07540; S07540.
DR AlphaFoldDB; P14243; -.
DR SMR; P14243; -.
DR REBASE; 3346; M.Cfr9I.
DR KEGG; ag:CAA34887; -.
DR BRENDA; 2.1.1.113; 1398.
DR PRO; PR:P14243; -.
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 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..300
FT /note="Type II methyltransferase M.Cfr9I"
FT /id="PRO_0000087927"
FT REGION 109..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 33781 MW; 972B291C551CBF2F CRC64;
MPSKKSSSPL SVEKLHRSEP LELNGATLFE GDALSVLRRL PSGSVRCIVT SPPYWGLRDY
GIDEQIGLES SMTQFLNRLV TIFSEAKRVL TDDGTLWVNI GDGYTSGNRG YRAPDKKNPA
RAMAVRPDTP EGLKPKDLIG IPWRLAFALQ EDGWYLRSDI VWNKPNAMPE SVKDRPTRSH
EFLFMLTKSE KYYYDWEAVR EEKDSGGFRN RRTVWNVNTK PFAGAHFATF PTELIRPCIL
ASTKPGDYVL DPFFGSGTVG VVCQQEDRQY VGIELNPEYV DIAVNRLQGE DTNVIRIAAA
