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P13906 (MTB1_LYSSH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Modification methylase BspRI

Short name=M.BspRI
EC=2.1.1.37
Alternative name(s):
Cytosine-specific methyltransferase BspRI
Gene names
Name:bspRIM
OrganismLysinibacillus sphaericus (Bacillus sphaericus)
Taxonomic identifier1421 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 BspRI endonuclease.

Catalytic activity

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.

Subunit structure

Monomer.

Post-translational modification

In the absence of DNA, can self-methylate two cysteine residues.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Contains 1 SAM-dependent MTase C5-type domain.

Ontologies

Keywords
   Biological processRestriction system
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMMethylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA (cytosine-5-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Modification methylase BspRI
PRO_0000087862

Regions

Domain58 – 408351SAM-dependent MTase C5-type

Sites

Active site1561S-methylcysteine intermediate

Amino acid modifications

Modified residue1811S-methylcysteine; by autocatalysis Ref.2

Sequences

Sequence LengthMass (Da)Tools
P13906 [UniParc].

Last modified June 15, 2010. Version 3.
Checksum: 1DED6A45DB0A4FCF

FASTA42448,212
        10         20         30         40         50         60 
MAIKINEKGR GKFKPAPTYE KEEVRQLLME KINEEMEAVA TATSDISNDE IQYKSDKFNV 

        70         80         90        100        110        120 
LSLFCGAGGL DLGFELAGLE QSLGTDKALE AFKDRDVYNA IRHESVFHTV YANDIFSEAL 

       130        140        150        160        170        180 
QTYEKNMPNH VFIHEKDIRK IKEFPSANLV IGGFPCPGFS EAGPRLVDDE RNFLYIHFIR 

       190        200        210        220        230        240 
CLMQVQPEIF VAENVKGMMT LGGGEVFRQI VEDFGAAGYR VEARLLNARD YGVPQIRERV 

       250        260        270        280        290        300 
IIVGVRNDID FNYEYPEITH GNEEGLKPYV TLEEAIGDLS LDPGPYFTGS YSTIFMSRNR 

       310        320        330        340        350        360 
KKKWTDQSFT IQASGRQAPI HPGGLPMEKV DKNKWIFPDG EENHRRLSVK EIKRIQTFPD 

       370        380        390        400        410        420 
WYEFSDGGNM KVSVNNRLDK QYKQIGNAVP VFLARAVAKS IAQFAADYLK DNHPHEAPQM 


KLFI 

« Hide

References

[1]"Structure of the Bacillus sphaericus R modification methylase gene."
Posfai G., Kiss A., Erdei S., Posfai J., Venetianer P.
J. Mol. Biol. 170:597-610(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Self-methylation of BspRI DNA-methyltransferase."
Szilak L., Finta C., Patthy A., Venetianer P., Kiss A.
Nucleic Acids Res. 22:2876-2881(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 322, PARTIAL PROTEIN SEQUENCE, AUTOMETHYLATION AT CYS-181.
[3]Rasko T., Der A., Klement E., Posfai E., Medzihradszky K.F., Marshak D.R., Roberts R.J., Kiss A.
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 394.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15758 Genomic DNA. Translation: CAA33764.2.
PIRS07792.

3D structure databases

ProteinModelPortalP13906.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE3322. M.BspRI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR10629. PTHR10629. 1 hit.
PfamPF00145. DNA_methylase. 2 hits.
[Graphical view]
PRINTSPR00105. C5METTRFRASE.
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR00675. dcm. 1 hit.
PROSITEPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTB1_LYSSH
AccessionPrimary (citable) accession number: P13906
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 15, 2010
Last modified: June 11, 2014
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries