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Protein

Type-2 restriction enzyme HincII

Gene

hincIIR

Organism
Haemophilus influenzae
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Restriction system

Enzyme and pathway databases

BRENDAi3.1.21.4. 2529.

Protein family/group databases

REBASEi1148. HincII.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme HincII (EC:3.1.21.4)
Short name:
R.HincII
Alternative name(s):
Endonuclease HincII
Type II restriction enzyme HincII
Gene namesi
Name:hincIIR
OrganismiHaemophilus influenzae
Taxonomic identifieri727 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000773192 – 258Type-2 restriction enzyme HincIIAdd BLAST257

Interactioni

Protein-protein interaction databases

DIPiDIP-48338N.
STRINGi71421.HI0512.

Structurei

Secondary structure

1258
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 7Combined sources3
Helixi8 – 15Combined sources8
Beta strandi19 – 21Combined sources3
Beta strandi24 – 26Combined sources3
Beta strandi30 – 32Combined sources3
Turni33 – 36Combined sources4
Helixi37 – 48Combined sources12
Turni50 – 52Combined sources3
Beta strandi53 – 55Combined sources3
Helixi56 – 65Combined sources10
Helixi73 – 78Combined sources6
Helixi83 – 89Combined sources7
Helixi93 – 98Combined sources6
Beta strandi101 – 103Combined sources3
Beta strandi114 – 119Combined sources6
Beta strandi122 – 132Combined sources11
Turni133 – 135Combined sources3
Beta strandi141 – 144Combined sources4
Helixi145 – 158Combined sources14
Beta strandi162 – 176Combined sources15
Beta strandi179 – 189Combined sources11
Helixi190 – 192Combined sources3
Helixi195 – 197Combined sources3
Beta strandi200 – 202Combined sources3
Turni203 – 206Combined sources4
Beta strandi207 – 209Combined sources3
Helixi212 – 214Combined sources3
Helixi223 – 249Combined sources27
Helixi251 – 256Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP17743.
SMRiP17743.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17743.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4106KR2. Bacteria.
ENOG410YBKR. LUCA.

Family and domain databases

Gene3Di3.40.600.10. 1 hit.
InterProiIPR011337. DNA_rep_MutH/RE_typeII.
IPR011335. Restrct_endonuc-II-like.
IPR015307. Restrct_endonuc_II_HincII.
[Graphical view]
PfamiPF09226. Endonuc-HincII. 1 hit.
[Graphical view]
SUPFAMiSSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17743-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFIKPIYQD INSILIGQKV KRPKSGTLSG HAAGEPFEKL VYKFLKENLS
60 70 80 90 100
DLTFKQYEYL NDLFMKNPAI IGHEARYKLF NSPTLLFLLS RGKAATENWS
110 120 130 140 150
IENLFEEKQN DTADILLVKD QFYELLDVKR RNISKSAQAP NIISAYKLAQ
160 170 180 190 200
TCAKMIDNKE FDLFDINYLE VDSELNGEDL VCVSTSFAEL FKSEPSELYI
210 220 230 240 250
NWAAAMQIQF HVRDLDQGFN GTREEWAKSY LKHFVTQAEQ RAISMIDKFV

KPFKKYIL
Length:258
Mass (Da):29,871
Last modified:January 23, 2007 - v3
Checksum:i9FE82017F7C15A47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52124 Genomic DNA. Translation: CAA36370.1.
PIRiS10323.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52124 Genomic DNA. Translation: CAA36370.1.
PIRiS10323.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP17743.
SMRiP17743.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48338N.
STRINGi71421.HI0512.

Protein family/group databases

REBASEi1148. HincII.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4106KR2. Bacteria.
ENOG410YBKR. LUCA.

Enzyme and pathway databases

BRENDAi3.1.21.4. 2529.

Miscellaneous databases

EvolutionaryTraceiP17743.

Family and domain databases

Gene3Di3.40.600.10. 1 hit.
InterProiIPR011337. DNA_rep_MutH/RE_typeII.
IPR011335. Restrct_endonuc-II-like.
IPR015307. Restrct_endonuc_II_HincII.
[Graphical view]
PfamiPF09226. Endonuc-HincII. 1 hit.
[Graphical view]
SUPFAMiSSF52980. SSF52980. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiT2C2_HAEIF
AccessioniPrimary (citable) accession number: P17743
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 99 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries

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 one 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.