ID   CAS2A_THET2             Reviewed;          94 AA.
AC   Q745W0;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=CRISPR-associated endoribonuclease Cas2 1;
DE            EC=3.1.-.-;
GN   Name=cas2a; OrderedLocusNames=TT_P0195;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OG   Plasmid pTT27.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
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).
CC       Functions as a ssRNA-specific endoribonuclease. Involved in the
CC       integration of spacer DNA into the CRISPR cassette (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas1 homodimer.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2
CC       protein family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017222; AAS82525.1; -; Genomic_DNA.
DR   RefSeq; WP_011174371.1; NC_005838.1.
DR   AlphaFoldDB; Q745W0; -.
DR   SMR; Q745W0; -.
DR   STRING; 262724.TT_P0195; -.
DR   EnsemblBacteria; AAS82525; AAS82525; TT_P0195.
DR   GeneID; 3169570; -.
DR   KEGG; tth:TT_P0195; -.
DR   eggNOG; COG1343; Bacteria.
DR   HOGENOM; CLU_161124_3_3_0; -.
DR   OMA; GKWTQYS; -.
DR   OrthoDB; 1951170at2; -.
DR   Proteomes; UP000000592; Plasmid pTT27.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-UniRule.
DR   GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-UniRule.
DR   CDD; cd09725; Cas2_I_II_III; 1.
DR   HAMAP; MF_01471; Cas2; 1.
DR   InterPro; IPR021127; CRISPR_associated_Cas2.
DR   InterPro; IPR019199; Virulence_VapD/CRISPR_Cas2.
DR   PANTHER; PTHR34405; PTHR34405; 1.
DR   Pfam; PF09827; CRISPR_Cas2; 1.
DR   PIRSF; PIRSF032582; Cas2; 1.
DR   TIGRFAMs; TIGR01573; cas2; 1.
PE   3: Inferred from homology;
KW   Antiviral defense; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease; Plasmid.
FT   CHAIN           1..94
FT                   /note="CRISPR-associated endoribonuclease Cas2 1"
FT                   /id="PRO_0000418430"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   94 AA;  11114 MW;  3B16EDB398EA08D0 CRC64;
     MRELYLVIAY DTPDDRRRAR LAKLLKGFGE RRQYSVFEAR LTREQWAHLK GKLEALVNKE
     EDVLAVYFLP PEAVGRTWRI GHEGLKRLED PDFV