ID   CCRM_BRUO2              Reviewed;         386 AA.
AC   A5VP58;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
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.BovORF495P {ECO:0000303|PubMed:12654995};
DE            Short=M.BovORF495P {ECO:0000303|PubMed:12654995};
GN   Name=ccrM; Synonyms=babI; OrderedLocusNames=BOV_0495;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX   PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA   Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA   de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA   Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA   Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT   "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT   range and tissue tropism.";
RL   PLoS ONE 4:E5519-E5519(2009).
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; CP000708; ABQ61978.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5VP58; -.
DR   SMR; A5VP58; -.
DR   REBASE; 15978; M.BovORF495P.
DR   KEGG; bov:BOV_0495; -.
DR   HOGENOM; CLU_024927_5_1_5; -.
DR   Proteomes; UP000006383; 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; Vaccinia Virus protein VP39; 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   PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   Pfam; PF18755; RAMA; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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..386
FT                   /note="DNA methyltransferase CcrM"
FT                   /id="PRO_0000363192"
FT   DOMAIN          280..382
FT                   /note="RAMA"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   386 AA;  43292 MW;  8662138DB587B6CC CRC64;
     MRSQVIEYPM SLVRLAHELP IEAPRTAWLD SIIKGDCVSA LERLPDHSVD VIFADPPYNL
     QLGGDLHRPD QSMVSAVDDH WDQFESFQAY DAFTRAWLLA CRRVLKPNGT IWVIGSYHNI
     FRVGTQLQDL GFWLLNDIVW RKTNPMPNFR GRRFQNAHET LIWASRDQKG KGYTFNYEAM
     KAANDDVQMR SDWLFPICTG SERLKDENGD KVHPTQKPEA LLARIMMASS KPGDVILDPF
     FGSGTTGAVA KRLGRHFVGI EREQPYIDAA TARINAVEPL GKAELTVMTG KRAEPRVAFT
     SVMEAGLLRP GTVLCDERRR FAAIVRADGT LTANGEAGSI HRIGARVQGF DACNGWTFWH
     FEENGVLKPI DALRKIIREQ MAAAGA
//