CCRM_BRUSI
ID CCRM_BRUSI Reviewed; 377 AA.
AC B0CKH7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Type II methyltransferase M.Bsu23445ORF519P {ECO:0000303|PubMed:12654995};
DE Short=M.Bsu23445ORF519P {ECO:0000303|PubMed:12654995};
GN Name=ccrM; OrderedLocusNames=BSUIS_A0519;
OS Brucella suis (strain ATCC 23445 / NCTC 10510).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=470137;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23445 / NCTC 10510;
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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'-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; CP000911; ABY37607.1; -; Genomic_DNA.
DR RefSeq; WP_004689516.1; NC_010169.1.
DR AlphaFoldDB; B0CKH7; -.
DR SMR; B0CKH7; -.
DR REBASE; 16913; M.Bsu23445ORF519P.
DR EnsemblBacteria; ABY37607; ABY37607; BSUIS_A0519.
DR GeneID; 45123969; -.
DR GeneID; 55590245; -.
DR KEGG; bmt:BSUIS_A0519; -.
DR HOGENOM; CLU_024927_5_1_5; -.
DR OMA; WRKANPM; -.
DR Proteomes; UP000008545; 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_0000363190"
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