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 27-MAR-2024, entry version 77. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GeneID; 58776344; -. DR KEGG; bmt:BSUIS_A0519; -. DR HOGENOM; CLU_024927_5_1_5; -. 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; 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..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 //