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Protein

CRISPR-associated endoribonuclease Cse3

Gene

cse3

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Sitei23Stabilizes transition-state intermediateCurated1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease, RNA-binding
Biological processAntiviral defense

Enzyme and pathway databases

BioCyciTTHE300852:G1GKC-2172-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)DescriptionActionsGraphical viewLength
Mutagenesisi23Y → F: 97% loss of cleavage activity. 2 Publications1
Mutagenesisi24E → A: 71% loss of cleavage activity. 1 Publication1
Mutagenesisi26H → A: 99.8% loss of cleavage activity, binds RNA normally. 1 Publication1
Mutagenesisi27R → A: 86% loss of cleavage activity. 2 Publications1
Mutagenesisi34S → A: 41% loss of cleavage activity. 1 Publication1
Mutagenesisi38E → A: No effect. 1 Publication1
Mutagenesisi102N → A: No effect on cleavage, increases enzyme turnover. 1 Publication1
Mutagenesisi157R → A: 85% loss of cleavage activity. 1 Publication1
Mutagenesisi158R → A: 64% loss of cleavage activity (PubMed:21572442); 99% loss of cleavage activity (PubMed:21572444). 2 Publications1
Mutagenesisi160K → A: 45% loss of cleavage activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004179691 – 211CRISPR-associated endoribonuclease Cse3Add BLAST211

Proteomic databases

PRIDEiQ53WG9

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1211
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 8Combined sources8
Helixi13 – 20Combined sources8
Helixi22 – 30Combined sources9
Helixi31 – 33Combined sources3
Helixi34 – 38Combined sources5
Beta strandi45 – 48Combined sources4
Beta strandi52 – 54Combined sources3
Beta strandi58 – 65Combined sources8
Helixi69 – 71Combined sources3
Beta strandi76 – 79Combined sources4
Beta strandi83 – 85Combined sources3
Beta strandi94 – 101Combined sources8
Beta strandi104 – 106Combined sources3
Turni108 – 110Combined sources3
Beta strandi113 – 115Combined sources3
Helixi119 – 132Combined sources14
Beta strandi135 – 137Combined sources3
Beta strandi143 – 156Combined sources14
Turni161 – 163Combined sources3
Beta strandi169 – 183Combined sources15
Helixi185 – 194Combined sources10
Beta strandi196 – 198Combined sources3
Helixi200 – 202Combined sources3
Beta strandi207 – 210Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53WG9

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000015851
KOiK19126
OMAiEQAGWPT

Family and domain databases

InterProiView protein in InterPro
IPR010179 CRISPR-assoc_prot_Cse3
PfamiView protein in Pfam
PF08798 CRISPR_assoc, 1 hit
SMARTiView protein in SMART
SM01101 CRISPR_assoc, 1 hit
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
PATRICifig|300852.9.peg.2143

Entry informationi

Entry nameiCAS6_THET8
AccessioniPrimary (citable) accession number: Q53WG9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: May 24, 2005
Last modified: May 23, 2018
This is version 78 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Plasmid, Reference proteome

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