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Protein

Modification methylase BspRI

Gene

bspRIM

Organism
Lysinibacillus sphaericus (Bacillus sphaericus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei156 – 1561S-methylcysteine intermediate

GO - Molecular functioni

  1. DNA (cytosine-5-)-methyltransferase activity Source: UniProtKB-EC
  2. DNA binding Source: InterPro

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

Protein family/group databases

REBASEi3322. M.BspRI.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase BspRI (EC:2.1.1.37)
Short name:
M.BspRI
Alternative name(s):
Cytosine-specific methyltransferase BspRI
Gene namesi
Name:bspRIM
OrganismiLysinibacillus sphaericus (Bacillus sphaericus)
Taxonomic identifieri1421 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Modification methylase BspRIPRO_0000087862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei156 – 1561S-methylcysteine; by autocatalysis1 Publication
Modified residuei181 – 1811S-methylcysteine; by autocatalysis1 Publication

Post-translational modificationi

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

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP13906.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 408351SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase C5-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PRINTSiPR00105. C5METTRFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00675. dcm. 1 hit.
PROSITEiPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13906-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAIKINEKGR GKFKPAPTYE KEEVRQLLME KINEEMEAVA TATSDISNDE
60 70 80 90 100
IQYKSDKFNV LSLFCGAGGL DLGFELAGLE QSLGTDKALE AFKDRDVYNA
110 120 130 140 150
IRHESVFHTV YANDIFSEAL QTYEKNMPNH VFIHEKDIRK IKEFPSANLV
160 170 180 190 200
IGGFPCPGFS EAGPRLVDDE RNFLYIHFIR CLMQVQPEIF VAENVKGMMT
210 220 230 240 250
LGGGEVFRQI VEDFGAAGYR VEARLLNARD YGVPQIRERV IIVGVRNDID
260 270 280 290 300
FNYEYPEITH GNEEGLKPYV TLEEAIGDLS LDPGPYFTGS YSTIFMSRNR
310 320 330 340 350
KKKWTDQSFT IQASGRQAPI HPGGLPMEKV DKNKWIFPDG EENHRRLSVK
360 370 380 390 400
EIKRIQTFPD WYEFSDGGNM KVSVNNRLDK QYKQIGNAVP VFLARAVAKS
410 420
IAQFAADYLK DNHPHEAPQM KLFI
Length:424
Mass (Da):48,212
Last modified:June 15, 2010 - v3
Checksum:i1DED6A45DB0A4FCF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15758 Genomic DNA. Translation: CAA33764.2.
PIRiS07792.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15758 Genomic DNA. Translation: CAA33764.2.
PIRiS07792.

3D structure databases

ProteinModelPortaliP13906.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi3322. M.BspRI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PRINTSiPR00105. C5METTRFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00675. dcm. 1 hit.
PROSITEiPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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. Cited for: SEQUENCE REVISION TO 322, PARTIAL PROTEIN SEQUENCE, METHYLATION AT CYS-156 AND 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.

Entry informationi

Entry nameiMTB1_LYSSH
AccessioniPrimary (citable) accession number: P13906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 15, 2010
Last modified: January 7, 2015
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.