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Reviewed, UniProtKB/Swiss-Prot P17743 (T2C2_HAEIN)

Last modified June 16, 2009. Version 67. 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:
    Type-2 restriction enzyme HincII
      Short name=R.HincII
    EC=3.1.21.4
Alternative name(s):
    Type II restriction enzyme HincII
    Endonuclease HincII
Gene names
Name: hincIIR
OrganismHaemophilus influenzae
Taxonomic identifier727 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Recognizes the double-stranded sequence GTYRAC and cleaves after Y-3.

Catalytic activity

Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.

Ontologies

Keywords
   Biological processRestriction system
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Gene Ontology (GO)
   Biological processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionDNA binding

Inferred from electronic annotation. Source: InterPro

Type II site-specific deoxyribonuclease activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 258257Type-2 restriction enzyme HincII
PRO_0000077319

Secondary structure

........................................... 258
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17743-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9FE82017F7C15A47

FASTA25829,871
        10         20         30         40         50         60 
MSFIKPIYQD INSILIGQKV KRPKSGTLSG HAAGEPFEKL VYKFLKENLS DLTFKQYEYL 

        70         80         90        100        110        120 
NDLFMKNPAI IGHEARYKLF NSPTLLFLLS RGKAATENWS IENLFEEKQN DTADILLVKD 

       130        140        150        160        170        180 
QFYELLDVKR RNISKSAQAP NIISAYKLAQ TCAKMIDNKE FDLFDINYLE VDSELNGEDL 

       190        200        210        220        230        240 
VCVSTSFAEL FKSEPSELYI NWAAAMQIQF HVRDLDQGFN GTREEWAKSY LKHFVTQAEQ 

       250 
RAISMIDKFV KPFKKYIL 

« 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.
[2]"Sequence selectivity and degeneracy of a restriction endonuclease mediated by DNA intercalation."
Horton N.C., Dorner L.F., Perona J.J.
Nat. Struct. Biol. 9:42-47(2002) [PubMed: 11742344] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

X52124 Genomic DNA. Translation: CAA36370.1.
PIRS10323.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1KC6X-ray2.60A/B/C/D2-258[»]
1XHUX-ray2.95A/B/C/D2-257[»]
1XHVX-ray2.50A/B/C/D2-257[»]
ModBaseSearch...

Protein family/group databases

REBASE1148. HincII.

Enzyme and pathway databases

BRENDA3.1.21.4. 109.

Family and domain databases

InterProIPR011337. Restrict_endonuc_II/DNA_repair.
IPR015307. Restrict_endonuc_II_HincII.
[Graphical view]
Gene3DG3DSA:3.40.600.10. Restrict_endonuc_II/DNA_repair. 1 hit.
PfamPF09226. Endonuc-HincII. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameT2C2_HAEIN
AccessionPrimary (citable) accession number: P17743
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 67 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

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