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Reviewed, UniProtKB/Swiss-Prot P17744 (MTHC_HAEIN)

Last modified September 22, 2009. Version 56. 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 HincII
      Short name=M.HincII
    EC=2.1.1.72
Alternative name(s):
    Adenine-specific methyltransferase HincII
Gene names
Name: hincIIM
OrganismHaemophilus influenzae
Taxonomic identifier727 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length502 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 GTYRAC, causes specific methylation on A-5 on both strands, and protects the DNA from cleavage by the HincII endonuclease.

Catalytic activity

S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

Sequence similarities

Belongs to the N(4)/N(6)-methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 502502Modification methylase HincII
PRO_0000087973

Sequences

Sequence LengthMass (Da)Tools
P17744-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 2536FA72B2F1720A

FASTA50258,776
        10         20         30         40         50         60 
MDESKKISLG QFFTPTHIVK YMIGLMTKNK NASILEPSSG NGVFLDSLIQ LGYTNLTSYE 

        70         80         90        100        110        120 
IDGDIISHPF VINSSFITSY DKPQYDSIIG NPPYVRWKNL SELQKKELKD NSIWKMYCNS 

       130        140        150        160        170        180 
LCDYFYIFII KSILQLKVGG ELIFICPDYF FSTKNAEGLR KFLINNGSFE KIILFNESKV 

       190        200        210        220        230        240 
FHGVSSSVVI FKYIKGKNID NINIINIDSK SPIKSEDIES LGESYYIPRF SSSDVWVTSP 

       250        260        270        280        290        300 
NHIKVALDKF ESYCKTIKKV QQKSLFDDLS FLDKAFQMND INYSELELLN SICVAKAKHL 

       310        320        330        340        350        360 
DAFCFSGYTR YKLILDDNNE DKLITYFPNF FYEFNNYKDY LLKRYSYNKY LPYWEVAFLR 

       370        380        390        400        410        420 
NFSLFSKNEK KIFVPCKERI SKKSNFRFSL VDEFIYPTQD VTALYKKENV KESIEYITAY 

       430        440        450        460        470        480 
LNSKAVFLWM KYKGVVKGNV VEFSEKPLTN IPFRRIDWQL KSEKKIHDDI TNLVRKYLSN 

       490        500 
KEFSILHEIN LNLEKLGIKV EI 

« Hide

References

[1]"Cloning, nucleotide sequence, and expression of the HincII restriction-modification system."
Ito H., Sadaoka A., Kotani H., Hiraoka N., Nakamura T.
Nucleic Acids Res. 18:3903-3911(1990) [PubMed: 2374714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RC.

Cross-references

Sequence databases

X52124 Genomic DNA. Translation: CAA36369.1.

3D structure databases

HSSPHSSP built from PDB template 2ADM based on UniProtKB P14385.
ModBaseSearch...

Protein family/group databases

REBASE3425. M.HincII.

Enzyme and pathway databases

BRENDA2.1.1.72. 109.

Family and domain databases

InterProIPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
[Graphical view]
PfamPF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSPR00507. N12N6MTFRASE.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTHC_HAEIN
AccessionPrimary (citable) accession number: P17744
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: September 22, 2009
This is version 56 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