CCRM_BRUSU
ID CCRM_BRUSU Reviewed; 377 AA.
AC Q8G242; G0K740;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=DNA methyltransferase CcrM {ECO:0000250|UniProtKB:Q2YMK2};
DE Short=M.CcrM;
DE EC=2.1.1.72;
DE AltName: Full=Adenine-specific methyltransferase BabI;
DE AltName: Full=Probable type II methyltransferase M.Bsu1330ORF492P/M.Bsu1330ORF491P {ECO:0000303|PubMed:12654995};
DE Short=M.Bsu1330ORF492P/M.Bsu1330ORF491P {ECO:0000303|PubMed:12654995};
GN Name=ccrM; Synonyms=babI; OrderedLocusNames=BR0491, BS1330_I0492;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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 that recognizes the double-stranded
CC sequence 5'-GANTC-3' and methylates A-2 on both strands
CC (PubMed:12654995) (By similarity). CcrM-mediated methylation has
CC important cellular functions. Contributes to the accurate cell-cycle
CC control of DNA replication and cellular morphology (By similarity).
CC {ECO:0000250|UniProtKB:O30569, ECO:0000250|UniProtKB:Q2YMK2,
CC ECO:0000303|PubMed:12654995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE014291; AAN29434.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM17847.1; -; Genomic_DNA.
DR RefSeq; WP_004689516.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8G242; -.
DR SMR; Q8G242; -.
DR REBASE; 39483; M.Bsu1330ORF492P.
DR REBASE; 40994; M.Bsu1330ORF491P.
DR EnsemblBacteria; AEM17847; AEM17847; BS1330_I0492.
DR GeneID; 45123969; -.
DR GeneID; 55590245; -.
DR KEGG; bms:BR0491; -.
DR KEGG; bsi:BS1330_I0492; -.
DR PATRIC; fig|204722.22.peg.1353; -.
DR HOGENOM; CLU_024927_5_1_5; -.
DR OMA; WRKANPM; -.
DR Proteomes; UP000007104; Chromosome I.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR040843; RAMA.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF18755; RAMA; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..377
FT /note="DNA methyltransferase CcrM"
FT /id="PRO_0000363189"
FT DOMAIN 271..373
FT /note="RAMA"
FT /evidence="ECO:0000255"
SQ SEQUENCE 377 AA; 42188 MW; 7E9D36B9F52BA83D CRC64;
MSLVRLAHEL PIEAPRTAWL DSIIKGDCVS ALERLPDHSV DVIFADPPYN LQLGGDLHRP
DQSMVSAVDD HWDQFESFQA YDAFTRAWLL ACRRVLKPNG TIWVIGSYHN IFRVGTQLQD
LGFWLLNDIV WRKTNPMPNF RGRRFQNAHE TLIWASRDQK GKGYTFNYEA MKAANDDVQM
RSDWLFPICT GSERLKDENG DKVHPTQKPE ALLARIMMAS SKPGDVILDP FFGSGTTGAV
AKRLGRHFVG IEREQPYIDA ATARINAVEP LGKAELTVMT GKRAEPRVAF TSVMEAGLLR
PGTVLCDERR RFAAIVRADG TLTANGEAGS IHRIGARVQG FDACNGWTFW HFEENGVLKP
IDALRKIIRE QMAAAGA
