CAS6_THET8
ID CAS6_THET8 Reviewed; 211 AA.
AC Q53WG9;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=CRISPR-associated endoribonuclease Cse3;
DE EC=3.1.-.-;
DE AltName: Full=Cse3 endoRNase;
DE AltName: Full=Cse3 endoribonuclease;
GN Name=cse3; Synonyms=cas6 {ECO:0000305}; OrderedLocusNames=TTHB192;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=16672237; DOI=10.1110/ps.062131106;
RA Ebihara A., Yao M., Masui R., Tanaka I., Yokoyama S., Kuramitsu S.;
RT "Crystal structure of hypothetical protein TTHB192 from Thermus
RT thermophilus HB8 reveals a new protein family with an RNA recognition
RT motif-like domain.";
RL Protein Sci. 15:1494-1499(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) IN COMPLEX WITH RNA, FUNCTION AS AN
RP ENDORIBONUCLEASE, SUBUNIT, RNA-BINDING, AND MUTAGENESIS OF TYR-23; GLU-24;
RP HIS-26; ARG-27; SER-34; GLU-38; ASN-102; ARG-158 AND LYS-160.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=21572442; DOI=10.1038/nsmb.2043;
RA Sashital D.G., Jinek M., Doudna J.A.;
RT "An RNA-induced conformational change required for CRISPR RNA cleavage by
RT the endoribonuclease Cse3.";
RL Nat. Struct. Mol. Biol. 18:680-687(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH RNA, FUNCTION AS AN
RP ENDORIBONUCLEASE, SUBUNIT, RNA-BINDING, AND MUTAGENESIS OF TYR-23; ARG-27;
RP ARG-157 AND ARG-158.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=21572444; DOI=10.1038/nsmb.2042;
RA Gesner E.M., Schellenberg M.J., Garside E.L., George M.M., Macmillan A.M.;
RT "Recognition and maturation of effector RNAs in a CRISPR interference
RT pathway.";
RL Nat. Struct. Mol. Biol. 18:688-692(2011).
CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC repeat), is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain sequences complementary to
CC antecedent mobile elements and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). This
CC enzyme processes pre-crRNA into individual crRNA units, but may not
CC actually undergo enzyme turnover, retaining the crRNA product
CC (PubMed:21572442). Generates a 2',3'-cyclic phosphodiester.
CC {ECO:0000269|PubMed:21572442, ECO:0000269|PubMed:21572444}.
CC -!- SUBUNIT: Probably part of the Cascade ribonucleoprotein complex
CC (Probable). Monomer, retains crRNA after it is processed.
CC {ECO:0000269|PubMed:21572442, ECO:0000269|PubMed:21572444,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated protein Cas6/Cse3/CasE
CC family. Subtype I-E/Ecoli subfamily. {ECO:0000305}.
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DR EMBL; AP008227; BAD71988.1; -; Genomic_DNA.
DR RefSeq; WP_011229112.1; NC_006462.1.
DR RefSeq; YP_145431.1; NC_006462.1.
DR PDB; 1WJ9; X-ray; 1.90 A; A=1-211.
DR PDB; 2Y8W; X-ray; 1.80 A; A=1-211.
DR PDB; 2Y8Y; X-ray; 1.44 A; A=1-211.
DR PDB; 2Y9H; X-ray; 2.50 A; A/C/E/G/I/K/M/O=1-211.
DR PDB; 3QRP; X-ray; 2.35 A; A=1-211.
DR PDB; 3QRQ; X-ray; 3.19 A; A=1-211.
DR PDB; 3QRR; X-ray; 3.10 A; A=1-211.
DR PDBsum; 1WJ9; -.
DR PDBsum; 2Y8W; -.
DR PDBsum; 2Y8Y; -.
DR PDBsum; 2Y9H; -.
DR PDBsum; 3QRP; -.
DR PDBsum; 3QRQ; -.
DR PDBsum; 3QRR; -.
DR AlphaFoldDB; Q53WG9; -.
DR SMR; Q53WG9; -.
DR PRIDE; Q53WG9; -.
DR EnsemblBacteria; BAD71988; BAD71988; BAD71988.
DR GeneID; 3167898; -.
DR KEGG; ttj:TTHB192; -.
DR PATRIC; fig|300852.9.peg.2143; -.
DR HOGENOM; CLU_080982_0_0_0; -.
DR OMA; EQAGWPT; -.
DR PhylomeDB; Q53WG9; -.
DR EvolutionaryTrace; Q53WG9; -.
DR Proteomes; UP000000532; Plasmid pTT27.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR010179; CRISPR-assoc_prot_Cse3.
DR Pfam; PF08798; CRISPR_assoc; 1.
DR SMART; SM01101; CRISPR_assoc; 1.
DR TIGRFAMs; TIGR01907; casE_Cse3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Nuclease;
KW Plasmid; Reference proteome; RNA-binding.
FT CHAIN 1..211
FT /note="CRISPR-associated endoribonuclease Cse3"
FT /id="PRO_0000417969"
FT SITE 23
FT /note="Stabilizes transition-state intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 23
FT /note="Y->F: 97% loss of cleavage activity."
FT /evidence="ECO:0000269|PubMed:21572442,
FT ECO:0000269|PubMed:21572444"
FT MUTAGEN 24
FT /note="E->A: 71% loss of cleavage activity."
FT /evidence="ECO:0000269|PubMed:21572442"
FT MUTAGEN 26
FT /note="H->A: 99.8% loss of cleavage activity, binds RNA
FT normally."
FT /evidence="ECO:0000269|PubMed:21572442"
FT MUTAGEN 27
FT /note="R->A: 86% loss of cleavage activity."
FT /evidence="ECO:0000269|PubMed:21572442,
FT ECO:0000269|PubMed:21572444"
FT MUTAGEN 34
FT /note="S->A: 41% loss of cleavage activity."
FT /evidence="ECO:0000269|PubMed:21572442"
FT MUTAGEN 38
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:21572442"
FT MUTAGEN 102
FT /note="N->A: No effect on cleavage, increases enzyme
FT turnover."
FT /evidence="ECO:0000269|PubMed:21572442"
FT MUTAGEN 157
FT /note="R->A: 85% loss of cleavage activity."
FT /evidence="ECO:0000269|PubMed:21572444"
FT MUTAGEN 158
FT /note="R->A: 64% loss of cleavage activity
FT (PubMed:21572442); 99% loss of cleavage activity
FT (PubMed:21572444)."
FT /evidence="ECO:0000269|PubMed:21572442,
FT ECO:0000269|PubMed:21572444"
FT MUTAGEN 160
FT /note="K->A: 45% loss of cleavage activity."
FT /evidence="ECO:0000269|PubMed:21572442"
FT STRAND 1..8
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT HELIX 34..38
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2Y8W"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT STRAND 143..156
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:3QRP"
FT STRAND 169..183
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2Y8Y"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:2Y8Y"
SQ SEQUENCE 211 AA; 23725 MW; 0AD90E0358E0E6FB CRC64;
MWLTKLVLNP ASRAARRDLA NPYEMHRTLS KAVSRALEEG RERLLWRLEP ARGLEPPVVL
VQTLTEPDWS VLDEGYAQVF PPKPFHPALK PGQRLRFRLR ANPAKRLAAT GKRVALKTPA
EKVAWLERRL EEGGFRLLEG ERGPWVQILQ DTFLEVRRKK DGEEAGKLLQ VQAVLFEGRL
EVVDPERALA TLRRGVGPGK ALGLGLLSVA P
