ID   CS1F2_THETK             Reviewed;         264 AA.
AC   G4RJY6;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=CRISPR-associated endonuclease Cas1/endonuclease Cas2 fusion;
DE            EC=3.1.-.-;
GN   Name=cas2; Synonyms=cas1; OrderedLocusNames=TTX_1246;
OS   Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS   / Kra 1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Thermoproteus.
OX   NCBI_TaxID=768679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX   PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA   Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA   Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA   Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA   Hensel R.;
RT   "The complete genome sequence of Thermoproteus tenax: a physiologically
RT   versatile member of the Crenarchaeota.";
RL   PLoS ONE 6:E24222-E24222(2011).
RN   [2]
RP   SUBUNIT, INDUCTION, AND OPERON STRUCTURE.
RC   STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX   PubMed=22408157; DOI=10.1128/jb.00206-12;
RA   Plagens A., Tjaden B., Hagemann A., Randau L., Hensel R.;
RT   "Characterization of the CRISPR/Cas subtype I-A system of the
RT   hyperthermophilic crenarchaeon Thermoproteus tenax.";
RL   J. Bacteriol. 194:2491-2500(2012).
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 (By
CC       similarity). Can form a Cascis complex with Cas4 and Csa1.
CC       {ECO:0000250, ECO:0000269|PubMed:22408157}.
CC   -!- INDUCTION: Slightly induced by 20 J/m2 ultraviolet light. Member of the
CC       csa1-cas1/2-cas4 operon. {ECO:0000269|PubMed:22408157}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated
CC       endonuclease Cas1 family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the CRISPR-associated
CC       endoribonuclease Cas2 protein family. {ECO:0000305}.
CC   -!- CAUTION: Neither Cas1 nor Cas2 are fully present in this fusion
CC       protein, however as this is the only copy of these proteins in this
CC       organism they are probably functional. The Cas1 section is much smaller
CC       than usual and it is quite atypical. {ECO:0000305}.
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DR   EMBL; FN869859; CCC81881.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4RJY6; -.
DR   SMR; G4RJY6; -.
DR   STRING; 768679.TTX_1246; -.
DR   EnsemblBacteria; CCC81881; CCC81881; TTX_1246.
DR   KEGG; ttn:TTX_1246; -.
DR   PATRIC; fig|768679.9.peg.1259; -.
DR   eggNOG; arCOG01452; Archaea.
DR   eggNOG; arCOG04194; Archaea.
DR   HOGENOM; CLU_1052197_0_0_2; -.
DR   Proteomes; UP000002654; Chromosome.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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   HAMAP; MF_01471; Cas2; 1.
DR   InterPro; IPR002729; CRISPR-assoc_Cas1.
DR   InterPro; IPR021127; CRISPR_associated_Cas2.
DR   InterPro; IPR019199; Virulence_VapD/CRISPR_Cas2.
DR   PANTHER; PTHR34405; PTHR34405; 1.
DR   Pfam; PF01867; Cas_Cas1; 1.
DR   Pfam; PF09827; CRISPR_Cas2; 1.
DR   TIGRFAMs; TIGR01573; cas2; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease; Reference proteome.
FT   CHAIN           1..264
FT                   /note="CRISPR-associated endonuclease Cas1/endonuclease
FT                   Cas2 fusion"
FT                   /id="PRO_0000422226"
FT   REGION          1..104
FT                   /note="CRISPR-associated endonuclease Cas1"
FT   REGION          108..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..264
FT                   /note="CRISPR-associated endonuclease Cas2"
FT   BINDING         182
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   264 AA;  28671 MW;  DE5DB4F0C6367AF9 CRC64;
     MDEVLLLTGG ISITTRALRA LLATGATVAV FSPRGEPLGI FMRPVGDATG AKRRCQYKAA
     EDGRGLQYAK SWVFKKILGQ RDNIKAWRRR LRGYSQYAES LAKALPGAGL HGAMETPRRR
     RRGQDGGQAG VRGRPTHPPV PPGAGRRSPG GAPRGQEASL RRDPQRGQSS GALHMYVIVV
     YDITENDVRA KVADILRAYG LARIQRSAYV GRLPPALVKE LAERLARAVR GANADIAIFK
     VDKRTIDTSL RIPPRPPAGH VALH