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Reviewed, UniProtKB/Swiss-Prot P25262 (MTB1_HERAU)

Last modified June 16, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Modification methylase HgiBI
      Short name=M.HgiBI
    EC=2.1.1.37
Alternative name(s):
    Cytosine-specific methyltransferase HgiBI
Gene names
Name: hgiBIM
OrganismHerpetosiphon aurantiacus (Herpetosiphon giganteus)
Taxonomic identifier65 [NCBI]
Taxonomic lineageBacteriaChloroflexiHerpetosiphonalesHerpetosiphonaceaeHerpetosiphon

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

This methylase recognizes the double-stranded sequence GGWCC, causes specific methylation on C-? on both strands, and protects the DNA from cleavage by the HgiBI endonuclease.

Catalytic activity

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

Sequence similarities

Belongs to the C5-methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Modification methylase HgiBI
PRO_0000087885

Sites

Active site751 By similarity

Sequences

Sequence LengthMass (Da)Tools
P25262-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 70A658159D8D23AD

FASTA43749,627
        10         20         30         40         50         60 
MQQFRFIDLF AGIGGFRLGL EAVGGVCVAS AEIDQQAIKV YRQNWPTDGV DHNLGDITAI 

        70         80         90        100        110        120 
QQLPAHDVLV GGVPCQPWSI AGKNQAFDDP RGQLWADVIR LVQINQPKAF IFENVKGLVD 

       130        140        150        160        170        180 
PRNRLCLEII LDSFKDLGYS VFYKLLNSFD FGVAQNRDRV FIVGIQQKLD LNGFSFPEYT 

       190        200        210        220        230        240 
ESEQRLYHIL DNLEVPETKL ESIPIQRNLF GERIDVGYNK LTPRGAFNDF FILNDIRNGP 

       250        260        270        280        290        300 
TSIHSWEIYP TTEREKQICM IIMRNRRNSR YGDCDGNPMS YQDIAELVAG LAEKELQTLV 

       310        320        330        340        350        360 
EKRILRQYPD GKYEFFNRRL SGGIDGTYRI FLPNARFFGT LTARGMHDEI AEISVSGANA 

       370        380        390        400        410        420 
EEYKHNFIQQ VLIPKRYRKI TVSEAARLQG FPGSFQFHSN QSANFRLIGN SVAPPVIVAL 

       430 
GKALQCVKLF EQELCEV 

« Hide

References

[1]"Isolation and genetic structure of the AvaII isoschizomeric restriction-modification system HgiBI from Herpetosiphon giganteus Hpg5: M.HgiBI reveals high homology to M.BanI."
Duesterhoeft A., Erdmann D., Kroeger M.
Nucleic Acids Res. 19:3207-3211(1991) [PubMed: 2062638] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: HPG5.
[2]"Organization and gene expression within restriction-modification systems of Herpetosiphon giganteus."
Kroeger M., Blum E., Deppe E., Duesterhoeft A., Erdmann D., Kilz S., Meyer-Rogge S., Moestl D.
Gene 157:43-47(1995) [PubMed: 7607523] [Abstract]
Cited for: DISCUSSION OF SEQUENCE.

Cross-references

Sequence databases

X55137 Genomic DNA. Translation: CAA38927.1.
PIRS22307.

3D structure databases

HSSPHSSP built from PDB template 6MHT based on UniProtKB P05102.
ModBaseSearch...

Protein family/group databases

REBASE3414. M.HgiBI.

Enzyme and pathway databases

BRENDA2.1.1.37. 291850.

Family and domain databases

InterProIPR001525. C5_DNA_meth.
IPR018117. C5_DNA_meth_AS.
[Graphical view]
PANTHERPTHR10629. C5_DNA_meth. 1 hit.
PfamPF00145. DNA_methylase. 1 hit.
[Graphical view]
PRINTSPR00105. C5METTRFRASE.
TIGRFAMsTIGR00675. dcm. 1 hit.
PROSITEPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTB1_HERAU
AccessionPrimary (citable) accession number: P25262
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents