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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). 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi32 – 321Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi62 – 621Manganese; via tele nitrogen1 Publication
Metal bindingi99 – 991Manganese1 Publication
Metal bindingi113 – 1131Manganese1 Publication
Metal bindingi114 – 1141Manganese; via carbonyl oxygen1 Publication
Metal bindingi188 – 1881Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi191 – 1911Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi197 – 1971Iron-sulfur (4Fe-4S)1 Publication

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB
  2. DNA binding Source: UniProtKB-KW
  3. manganese ion binding Source: UniProtKB
  4. single-stranded DNA 5'-3' exodeoxyribonuclease activity Source: UniProtKB

GO - Biological processi

  1. defense response to virus Source: UniProtKB-KW
  2. DNA catabolic process, exonucleolytic Source: UniProtKB
  3. 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

BioCyciSSOL273057:GCH2-1-MONOMER.

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
ProteomesiUP000001974: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321C → A: Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-188; A-191 and A-197. 1 Publication
Mutagenesisi99 – 991D → A: Abolishes nuclease activity. 2 Publications
Mutagenesisi113 – 1131E → A: Impairs exonuclease activity. 1 Publication
Mutagenesisi115 – 1151K → A: Abolishes exonuclease activity. 1 Publication
Mutagenesisi148 – 1481Y → A: Nearly abolishes exonuclease activity. 1 Publication
Mutagenesisi188 – 1881C → A: Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-32; A-191 and A-197. 1 Publication
Mutagenesisi191 – 1911C → A: Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-32; A-188 and A-197. 1 Publication
Mutagenesisi197 – 1971C → A: Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-32; A-188 and A-191. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 202202CRISPR-associated exonuclease Cas4PRO_0000422224Add
BLAST

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

202
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1616Combined sources
Beta strandi23 – 253Combined sources
Helixi26 – 294Combined sources
Helixi33 – 419Combined sources
Helixi43 – 464Combined sources
Helixi47 – 515Combined sources
Helixi53 – 7220Combined sources
Beta strandi75 – 8713Combined sources
Beta strandi90 – 10213Combined sources
Beta strandi110 – 1156Combined sources
Helixi126 – 13914Combined sources
Beta strandi142 – 1509Combined sources
Beta strandi153 – 1597Combined sources
Helixi165 – 17612Combined sources
Beta strandi180 – 1845Combined sources
Helixi188 – 1903Combined sources
Helixi194 – 1963Combined sources

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1468.
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.
RefSeqiNP_341578.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK43340; AAK43340; SSO0001.
GeneIDi1455258.
KEGGisso:SSO0001.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK43340.1.
PIRiA90139.
RefSeqiNP_341578.1. NC_002754.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi273057.SSO0001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK43340; AAK43340; SSO0001.
GeneIDi1455258.
KEGGisso:SSO0001.

Phylogenomic databases

eggNOGiCOG1468.
HOGENOMiHOG000223327.
InParanoidiQ97TX9.
KOiK07464.
OMAiWECRYCP.

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-1-MONOMER.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. "The CRISPR associated protein Cas4 is a 5' to 3' DNA exonuclease with an iron-sulfur cluster."
    Zhang J., Kasciukovic T., White M.F.
    PLoS ONE 7:E47232-E47232(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN EXONUCLEASE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-99.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  3. "Toroidal structure and DNA cleavage by the CRISPR-associated [4Fe-4S] cluster containing Cas4 nuclease SSO0001 from Sulfolobus solfataricus."
    Lemak S., Beloglazova N., Nocek B., Skarina T., Flick R., Brown G., Popovic A., Joachimiak A., Savchenko A., Yakunin A.F.
    J. Am. Chem. Soc. 135:17476-17487(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S) AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, DNA-BINDING, SUBUNIT, MUTAGENESIS OF CYS-32; ASP-99; LYS-115; TYR-148; CYS-188; CYS-191 AND CYS-197.

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: February 4, 2015
This is version 60 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

External Data

Dasty 3

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 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.