ID   CCRM_BRUA4              Reviewed;         377 AA.
AC   A6WWI2;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 92.
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.OanORF605P {ECO:0000303|PubMed:12654995};
DE            Short=M.OanORF605P {ECO:0000303|PubMed:12654995};
GN   Name=ccrM; OrderedLocusNames=Oant_0605;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 /
RC   NBRC 15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
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; CP000758; ABS13336.1; -; Genomic_DNA.
DR   RefSeq; WP_012090866.1; NC_009667.1.
DR   AlphaFoldDB; A6WWI2; -.
DR   SMR; A6WWI2; -.
DR   STRING; 439375.Oant_0605; -.
DR   REBASE; 15992; M.OanORF605P.
DR   KEGG; oan:Oant_0605; -.
DR   eggNOG; COG2189; Bacteria.
DR   HOGENOM; CLU_024927_5_1_5; -.
DR   Proteomes; UP000002301; Chromosome 1.
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; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..377
FT                   /note="DNA methyltransferase CcrM"
FT                   /id="PRO_0000363194"
FT   DOMAIN          271..373
FT                   /note="RAMA"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   377 AA;  42079 MW;  0D0B34E4710E708B CRC64;
     MSLVRLAHEL PIEAPRTAWL DSIIKGDCVA ALERLPDHSV DVIFADPPYN LQLGGDLHRP
     DQSMVSAVDD HWDQFESFQA YDAFTRAWLM ACRRVLKPNG TIWVIGSYHN IFRVGSQLQD
     LGFWLLNDVI WRKTNPMPNF RGRRFQNAHE TLIWASRDQK GKGYTFNYEA MKAANDDVQM
     RSDWLFPICT GSERLKDENG DKVHPTQKPE ALLARIMMAS SKPGDVILDP FFGSGTTGAV
     AKRLGRHFVG IEREQSYIDA ATARIDAVEP LGKAELTVMT GKRAEPRVAF TSVLEAGLLR
     PGTVLCDERR RFAAIVRADG TLAANGEAGS IHRIGAKVQG FDACNGWTFW HYEENGALKP
     IDALRKVIRD QMAVAGA
//