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P17743 (T2C2_HAEIF) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. 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:
Type-2 restriction enzyme HincII

Short name=R.HincII
EC=3.1.21.4
Alternative name(s):
Endonuclease HincII
Type II restriction enzyme 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: UniProtKB-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 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-258.
[3]"Ca2+ binding in the active site of HincII: implications for the catalytic mechanism."
Etzkorn C., Horton N.C.
Biochemistry 43:13256-13270(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-257.
[4]"Mechanistic insights from the structures of HincII bound to cognate DNA cleaved from addition of Mg2+ and Mn2+."
Etzkorn C., Horton N.C.
J. Mol. Biol. 343:833-849(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-257.
[5]"DNA-induced conformational changes in type II restriction endonucleases: the structure of unliganded HincII."
Little E.J., Horton N.C.
J. Mol. Biol. 351:76-88(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-257.
[6]"Alteration of sequence specificity of the type II restriction endonuclease HincII through an indirect readout mechanism."
Joshi H.K., Etzkorn C., Chatwell L., Bitinaite J., Horton N.C.
J. Biol. Chem. 281:23852-23869(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-258.
[7]"DNA distortion and specificity in a sequence-specific endonuclease."
Babic A.C., Little E.J., Manohar V.M., Bitinaite J., Horton N.C.
J. Mol. Biol. 383:186-204(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 2-258.
[8]"Early interrogation and recognition of DNA sequence by indirect readout."
Little E.J., Babic A.C., Horton N.C.
Structure 16:1828-1837(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52124 Genomic DNA. Translation: CAA36370.1.
PIRS10323.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KC6X-ray2.60A/B/C/D2-258[»]
1TW8X-ray2.80A/B/C/D2-258[»]
1TX3X-ray2.50A/B/C/D2-258[»]
1XHUX-ray2.95A/B/C/D2-258[»]
1XHVX-ray2.50A/B/C/D2-258[»]
2AUDX-ray2.10A2-258[»]
2GIEX-ray2.60A/B/C/D2-258[»]
2GIGX-ray1.83A/B2-258[»]
2GIHX-ray2.50A/B2-258[»]
2GIIX-ray2.30A/B2-258[»]
2GIJX-ray1.93A/B2-258[»]
3E3YX-ray2.13A/B2-258[»]
3E40X-ray2.10A/B2-258[»]
3E41X-ray2.73A/B2-258[»]
3E42X-ray2.68A/B2-258[»]
3E43X-ray2.73A/B2-258[»]
3E44X-ray2.52A/B2-258[»]
3E45X-ray2.78A/B2-258[»]
3EBCX-ray2.55A/B1-258[»]
ProteinModelPortalP17743.
SMRP17743. Positions 2-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48338N.

Protein family/group databases

REBASE1148. HincII.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.600.10. 1 hit.
InterProIPR011337. DNA_rep_MutH/RE_typeII.
IPR011335. Restrct_endonuc-II-like.
IPR015307. Restrct_endonuc_II_HincII.
[Graphical view]
PfamPF09226. Endonuc-HincII. 1 hit.
[Graphical view]
SUPFAMSSF52980. SSF52980. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP17743.

Entry information

Entry nameT2C2_HAEIF
AccessionPrimary (citable) accession number: P17743
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references