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Protein

CRISPR-associated endoribonuclease Cse3

Gene

cse3

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 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). This enzyme processes pre-crRNA into individual crRNA units, but may not actually undergo enzyme turnover, retaining the crRNA product (PubMed:21572442). Generates a 2',3'-cyclic phosphodiester.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei23 – 231Stabilizes transition-state intermediateCurated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Antiviral defense

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-2215-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
CRISPR-associated endoribonuclease Cse3 (EC:3.1.-.-)
Alternative name(s):
Cse3 endoRNase
Cse3 endoribonuclease
Gene namesi
Name:cse3
Synonyms:cas6Curated
Ordered Locus Names:TTHB192
Encoded oniPlasmid pTT270 Publication
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Plasmid pTT27

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231Y → F: 97% loss of cleavage activity. 2 Publications
Mutagenesisi24 – 241E → A: 71% loss of cleavage activity. 1 Publication
Mutagenesisi26 – 261H → A: 99.8% loss of cleavage activity, binds RNA normally. 1 Publication
Mutagenesisi27 – 271R → A: 86% loss of cleavage activity. 2 Publications
Mutagenesisi34 – 341S → A: 41% loss of cleavage activity. 1 Publication
Mutagenesisi38 – 381E → A: No effect. 1 Publication
Mutagenesisi102 – 1021N → A: No effect on cleavage, increases enzyme turnover. 1 Publication
Mutagenesisi157 – 1571R → A: 85% loss of cleavage activity. 1 Publication
Mutagenesisi158 – 1581R → A: 64% loss of cleavage activity (PubMed:21572442); 99% loss of cleavage activity (PubMed:21572444). 2 Publications
Mutagenesisi160 – 1601K → A: 45% loss of cleavage activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211CRISPR-associated endoribonuclease Cse3PRO_0000417969Add
BLAST

Interactioni

Subunit structurei

Probably part of the Cascade ribonucleoprotein complex (Probable). Monomer, retains crRNA after it is processed.Curated2 Publications

Structurei

Secondary structure

211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 88Combined sources
Helixi13 – 208Combined sources
Helixi22 – 309Combined sources
Helixi31 – 333Combined sources
Helixi34 – 385Combined sources
Beta strandi45 – 484Combined sources
Beta strandi52 – 543Combined sources
Beta strandi58 – 658Combined sources
Helixi69 – 713Combined sources
Beta strandi76 – 794Combined sources
Beta strandi83 – 853Combined sources
Beta strandi94 – 1018Combined sources
Beta strandi104 – 1063Combined sources
Turni108 – 1103Combined sources
Beta strandi113 – 1153Combined sources
Helixi119 – 13214Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi143 – 15614Combined sources
Turni161 – 1633Combined sources
Beta strandi169 – 18315Combined sources
Helixi185 – 19410Combined sources
Beta strandi196 – 1983Combined sources
Helixi200 – 2023Combined sources
Beta strandi207 – 2104Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJ9X-ray1.90A1-211[»]
2Y8WX-ray1.80A1-211[»]
2Y8YX-ray1.44A1-211[»]
2Y9HX-ray2.50A/C/E/G/I/K/M/O1-211[»]
3QRPX-ray2.35A1-211[»]
3QRQX-ray3.19A1-211[»]
3QRRX-ray3.10A1-211[»]
ProteinModelPortaliQ53WG9.
SMRiQ53WG9. Positions 1-211.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53WG9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000015851.
KOiK19126.
OMAiYEMHRTL.
OrthoDBiEOG6Z6FX3.

Family and domain databases

InterProiIPR010179. CRISPR-assoc_prot_Cse3.
[Graphical view]
PfamiPF08798. CRISPR_assoc. 1 hit.
[Graphical view]
SMARTiSM01101. CRISPR_assoc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01907. casE_Cse3. 1 hit.

Sequencei

Sequence statusi: Complete.

Q53WG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLTKLVLNP ASRAARRDLA NPYEMHRTLS KAVSRALEEG RERLLWRLEP
60 70 80 90 100
ARGLEPPVVL VQTLTEPDWS VLDEGYAQVF PPKPFHPALK PGQRLRFRLR
110 120 130 140 150
ANPAKRLAAT GKRVALKTPA EKVAWLERRL EEGGFRLLEG ERGPWVQILQ
160 170 180 190 200
DTFLEVRRKK DGEEAGKLLQ VQAVLFEGRL EVVDPERALA TLRRGVGPGK
210
ALGLGLLSVA P
Length:211
Mass (Da):23,725
Last modified:May 24, 2005 - v1
Checksum:i0AD90E0358E0E6FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008227 Genomic DNA. Translation: BAD71988.1.
RefSeqiWP_011229112.1. NC_006462.1.
YP_145431.1. NC_006462.1.

Genome annotation databases

EnsemblBacteriaiBAD71988; BAD71988; BAD71988.
GeneIDi3167898.
KEGGittj:TTHB192.
PATRICi23959324. VBITheThe93045_2143.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008227 Genomic DNA. Translation: BAD71988.1.
RefSeqiWP_011229112.1. NC_006462.1.
YP_145431.1. NC_006462.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJ9X-ray1.90A1-211[»]
2Y8WX-ray1.80A1-211[»]
2Y8YX-ray1.44A1-211[»]
2Y9HX-ray2.50A/C/E/G/I/K/M/O1-211[»]
3QRPX-ray2.35A1-211[»]
3QRQX-ray3.19A1-211[»]
3QRRX-ray3.10A1-211[»]
ProteinModelPortaliQ53WG9.
SMRiQ53WG9. Positions 1-211.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71988; BAD71988; BAD71988.
GeneIDi3167898.
KEGGittj:TTHB192.
PATRICi23959324. VBITheThe93045_2143.

Phylogenomic databases

HOGENOMiHOG000015851.
KOiK19126.
OMAiYEMHRTL.
OrthoDBiEOG6Z6FX3.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-2215-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ53WG9.

Family and domain databases

InterProiIPR010179. CRISPR-assoc_prot_Cse3.
[Graphical view]
PfamiPF08798. CRISPR_assoc. 1 hit.
[Graphical view]
SMARTiSM01101. CRISPR_assoc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01907. casE_Cse3. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 reveals a new protein family with an RNA recognition motif-like domain."
    Ebihara A., Yao M., Masui R., Tanaka I., Yokoyama S., Kuramitsu S.
    Protein Sci. 15:1494-1499(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "An RNA-induced conformational change required for CRISPR RNA cleavage by the endoribonuclease Cse3."
    Sashital D.G., Jinek M., Doudna J.A.
    Nat. Struct. Mol. Biol. 18:680-687(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) IN COMPLEX WITH RNA, FUNCTION AS AN ENDORIBONUCLEASE, SUBUNIT, RNA-BINDING, MUTAGENESIS OF TYR-23; GLU-24; HIS-26; ARG-27; SER-34; GLU-38; ASN-102; ARG-158 AND LYS-160.
    Strain: HB8 / ATCC 27634 / DSM 579.
  4. "Recognition and maturation of effector RNAs in a CRISPR interference pathway."
    Gesner E.M., Schellenberg M.J., Garside E.L., George M.M., Macmillan A.M.
    Nat. Struct. Mol. Biol. 18:688-692(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH RNA, FUNCTION AS AN ENDORIBONUCLEASE, SUBUNIT, RNA-BINDING, MUTAGENESIS OF TYR-23; ARG-27; ARG-157 AND ARG-158.
    Strain: HB8 / ATCC 27634 / DSM 579.

Entry informationi

Entry nameiCAS6_THET8
AccessioniPrimary (citable) accession number: Q53WG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: May 24, 2005
Last modified: December 9, 2015
This is version 72 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, Plasmid, 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.