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UniProtKB/Swiss-Prot entry P06530


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MTBR_BACSU
Primary accession number P06530
Secondary accession numbers None
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on January 1, 1988 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 60)
Name and origin of the protein
Protein name Modification methylase BsuRI
Synonyms M.BsuRI
EC 2.1.1.37
Cytosine-specific methyltransferase BsuRI
Gene name
Name: hsdRM
Synonyms: hsdM
From
Bacillus subtilis [TaxID: 1423] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=R;
DOI=10.1093/nar/13.18.6403; PubMed=2997708 [NCBI, ExPASy, EBI, Israel, Japan]
Kiss A., Posfai G., Keller C.C., Venetianer P., Roberts R.J.;
"Nucleotide sequence of the BsuRI restriction-modification system.";
Nucleic Acids Res. 13:6403-6421(1985).
Comments
  • FUNCTION: This methylase recognizes the double-stranded sequence GGCC, causes specific methylation on C-3 on both strands, and protects the DNA from cleavage by the BsuRI endonuclease.
  • CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
  • SUBUNIT: Monomer.
  • SIMILARITY: Belongs to the C5-methyltransferase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X02988; CAA26731.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B23488; XYBSR1.
3D structure databases
HSSP P20589; 1DCT. [HSSP ENTRY / PDB]
ModBase P06530.
Protein family/group databases
REBASE 3340; M.BsuRI.
Ontologies
GO
GO:0003886; Molecular function: DNA (cytosine-5-)-methyltransferase activity (inferred from electronic annotation from EC).
GO:0009307; Biological process: DNA restriction-modification system (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001525; C5_DNA_meth.
Graphical view of domain structure.
PANTHER PTHR10629; C5_DNA_meth; 1.
Pfam PF00145; DNA_methylase; 1.
Pfam graphical view of domain structure.
PRINTS PR00105; C5METTRFRASE.
TIGRFAMs TIGR00675; dcm; 1.
PROSITE PS00094; C5_MTASE_1; 1.
PS00095; C5_MTASE_2; 1.
BLOCKS P06530.
ProtoNet P06530.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Methyltransferase; Restriction system; S-adenosyl-L-methionine; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   436  436     Modification methylase BsuRI. PRO_0000087864
ACT_SITE   157   157        By similarity. 
Sequence information
Length: 436 AA [This is the length of the unprocessed precursor] Molecular weight: 49635 Da [This is the MW of the unprocessed precursor] CRC64: 07EE0B2CA9140B19 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTLKIDIKGR GKYKPASDYS IDDVKNVLME KIFEESSRII NSDDDLEIIE KVDFRTDKIN 

        70         80         90        100        110        120 
VLSLFSGCGG LDLGFELAGL AAVIGEQAAM EAFKDKDRFN ELRNKSIFHT IYTNDLFKEA 

       130        140        150        160        170        180 
NQTYKTNFPG HVIQHEKDIR QVKYFPKCNL ILGGFPCPGF SEAGPRLIDD DRNFLYLHFI 

       190        200        210        220        230        240 
RSLIQAQPEI FVAENVKGMM TLGKGEVLNQ IIEDFASAGY RVQFKLLNAR DYGVPQLRER 

       250        260        270        280        290        300 
VIIEGVRKDI SFNYKYPSPT HGEETGLKPF KTLRDSIGDL VTDPGPYFTG SYSSIYMSRN 

       310        320        330        340        350        360 
RKKSWDEQSF TIQASGRQAP LHPGGLSMKK IGKDKWVFPD GEENHRRLSV KEIARVQTFP 

       370        380        390        400        410        420 
DWFQFSQGTN SQTSINNRLD KQYKQIGNAV PVLLAKAVAS PIANWAINYL ESSPNNKIKN 

       430 
RERKLSIRTF LRIKTS 

P06530 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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