ID   CCRM_BRUAB              Reviewed;         377 AA.
AC   P0C116; O30570; Q57EN0;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
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 orphan methyltransferase M.BabAORF513P {ECO:0000303|PubMed:12654995};
DE            Short=M.BabAORF513P {ECO:0000303|PubMed:12654995};
GN   Name=ccrM; Synonyms=babI, babIM; OrderedLocusNames=BruAb1_0513;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX73904.1; -; Genomic_DNA.
DR   RefSeq; WP_002969465.1; NC_006932.1.
DR   AlphaFoldDB; P0C116; -.
DR   SMR; P0C116; -.
DR   REBASE; 11024; M.BabAORF513P.
DR   EnsemblBacteria; AAX73904; AAX73904; BruAb1_0513.
DR   GeneID; 3788634; -.
DR   KEGG; bmb:BruAb1_0513; -.
DR   HOGENOM; CLU_024927_5_1_5; -.
DR   OMA; WRKANPM; -.
DR   Proteomes; UP000000540; 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_0000087985"
FT   DOMAIN          271..373
FT                   /note="RAMA"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   377 AA;  42202 MW;  657C88A25580B39D CRC64;
     MSLVRLAHEL PIEAPRTAWL DSIIKGDCVS ALERLPDHSV DVIFADPPYN LQLGGDLHRP
     DQSMVSAVDD HWDQFESFQA YDAFTRAWLL ACRRVLKPNG TIWVIGSYHN IFRVGTQLQD
     LGFWLLNDIV WRKTNPMPNF RGRRFQNAHE TLIWASREQK GKGYTFNYEA MKAANDDVQM
     RSDWLFPICT GSERLKDENG DKVHPTQKPE ALLARIMMAS SKPGDVILDP FFGSGTTGAV
     AKRLGRHFVG IEREQPYIDA ATARINAVEP LGKAELTVMT GKRAEPRVAF TSVMEAGLLR
     PGTVLCDERR RFAAIVRADG TLTANGEAGS IHRIGARVQG FDACNGWTFW HFEENGVLKP
     IDALRKIIRE QMAAAGA