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Protein

CRISPR-associated exonuclease Cas4

Gene

cas4

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). This protein is a 5' to 3' partially processive exonuclease that cleaves off single mononucleotides. Has a marked preference for ssDNA, although in vitro it also acts on dsDNA and ssRNA. Has low endonuclease activity with circular ssDNA. Binds ssDNA and can unwind dsDNA; unwinding does not require ATP.By similarity2 Publications

Catalytic activityi

Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.2 Publications

Cofactori

Protein has several cofactor binding sites:

pH dependencei

Optimum pH is 9-10.1 Publication

Temperature dependencei

Optimum temperature is 65-70 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi32Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi62Manganese; via tele nitrogen1 Publication1
Metal bindingi99Manganese1 Publication1
Metal bindingi113Manganese1 Publication1
Metal bindingi114Manganese; via carbonyl oxygen1 Publication1
Metal bindingi188Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi191Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi197Iron-sulfur (4Fe-4S)1 Publication1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • manganese ion binding Source: UniProtKB
  • single-stranded DNA 5'-3' exodeoxyribonuclease activity Source: UniProtKB

GO - Biological processi

  • defense response to virus Source: UniProtKB-KW
  • DNA catabolic process, exonucleolytic Source: UniProtKB
  • DNA duplex unwinding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Antiviral defense

Keywords - Ligandi

4Fe-4S, DNA-binding, Iron, Iron-sulfur, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.12.1. 6163.

Names & Taxonomyi

Protein namesi
Recommended name:
CRISPR-associated exonuclease Cas4 (EC:3.1.12.12 Publications)
Gene namesi
Name:cas4
Ordered Locus Names:SSO0001
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001974 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi32C → A: Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-188; A-191 and A-197. 1 Publication1
Mutagenesisi99D → A: Abolishes nuclease activity. 2 Publications1
Mutagenesisi113E → A: Impairs exonuclease activity. 1 Publication1
Mutagenesisi115K → A: Abolishes exonuclease activity. 1 Publication1
Mutagenesisi148Y → A: Nearly abolishes exonuclease activity. 1 Publication1
Mutagenesisi188C → A: Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-32; A-191 and A-197. 1 Publication1
Mutagenesisi191C → A: Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-32; A-188 and A-197. 1 Publication1
Mutagenesisi197C → A: Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-32; A-188 and A-191. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004222241 – 202CRISPR-associated exonuclease Cas4Add BLAST202

Interactioni

Subunit structurei

Homodecamer, formed by the assembly of dimers into a decameric toroid, with the active sites oriented towards the central tunnel.2 Publications

Protein-protein interaction databases

STRINGi273057.SSO0001.

Structurei

Secondary structure

1202
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 16Combined sources16
Beta strandi23 – 25Combined sources3
Helixi26 – 29Combined sources4
Helixi33 – 41Combined sources9
Helixi43 – 46Combined sources4
Helixi47 – 51Combined sources5
Helixi53 – 72Combined sources20
Beta strandi75 – 87Combined sources13
Beta strandi90 – 102Combined sources13
Beta strandi105 – 107Combined sources3
Beta strandi110 – 115Combined sources6
Helixi126 – 139Combined sources14
Beta strandi142 – 150Combined sources9
Beta strandi153 – 159Combined sources7
Helixi165 – 176Combined sources12
Beta strandi180 – 184Combined sources5
Helixi188 – 190Combined sources3
Helixi194 – 196Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IC1X-ray2.35A/B/C/D/F/G/H/I/J/K1-202[»]
SMRiQ97TX9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG00790. Archaea.
COG1468. LUCA.
HOGENOMiHOG000223327.
InParanoidiQ97TX9.
KOiK07464.
OMAiWECRYCP.

Family and domain databases

InterProiIPR013343. CRISPR-assoc_prot_Cas4.
[Graphical view]
TIGRFAMsiTIGR00372. cas4. 1 hit.

Sequencei

Sequence statusi: Complete.

Q97TX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITEFLLKKK LEEHLSHVKE ENTIYVTDLV RCPRRVRYES EYKELAISQV
60 70 80 90 100
YAPSAILGDI LHLGLESVLK GNFNAETEVE TLREINVGGK VYKIKGRADA
110 120 130 140 150
IIRNDNGKSI VIEIKTSRSD KGLPLIHHKM QLQIYLWLFS AEKGILVYIT
160 170 180 190 200
PDRIAEYEIN EPLDEATIVR LAEDTIMLQN SPRFNWECKY CIFSVICPAK

LT
Length:202
Mass (Da):23,239
Last modified:October 1, 2001 - v1
Checksum:iC1E8868ACC093382
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK43340.1.
PIRiA90139.
RefSeqiWP_009989652.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK43340; AAK43340; SSO0001.
GeneIDi27426297.
KEGGisso:SSO0001.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK43340.1.
PIRiA90139.
RefSeqiWP_009989652.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IC1X-ray2.35A/B/C/D/F/G/H/I/J/K1-202[»]
SMRiQ97TX9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO0001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK43340; AAK43340; SSO0001.
GeneIDi27426297.
KEGGisso:SSO0001.

Phylogenomic databases

eggNOGiarCOG00790. Archaea.
COG1468. LUCA.
HOGENOMiHOG000223327.
InParanoidiQ97TX9.
KOiK07464.
OMAiWECRYCP.

Enzyme and pathway databases

BRENDAi3.1.12.1. 6163.

Family and domain databases

InterProiIPR013343. CRISPR-assoc_prot_Cas4.
[Graphical view]
TIGRFAMsiTIGR00372. cas4. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCAS4_SULSO
AccessioniPrimary (citable) accession number: Q97TX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2013
Last sequence update: October 1, 2001
Last modified: November 2, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.