ID   CS3HD_THETK             Reviewed;         226 AA.
AC   G4RJZ4;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=CRISPR-associated endonuclease Cas3-HD;
DE            EC=3.1.-.-;
DE   AltName: Full=CRISPR-associated ssDNA/ssRNA endonuclease Cas3-HD;
GN   Name=cas3'; Synonyms=cas3''; OrderedLocusNames=TTX_1254;
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). Cas3
CC       plus Cascade participate in CRISPR interference, the third stage of
CC       CRISPR immunity. Acts as a ssDNA and ssRNA nuclease, probably with both
CC       exo- and endonuclease activities. Activity is higher for DNA than RNA
CC       (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer (By similarity). Can form a Cascade complex with Csa5,
CC       Cas7, Cas5a, Cas3 and Cas8a2. {ECO:0000250,
CC       ECO:0000269|PubMed:22408157}.
CC   -!- INDUCTION: Repressed by 5 J/m2 ultraviolet light and 50 mM NaCl,
CC       slightly induced by 20 J/m2 ultraviolet light, 100 and 150 mM Nacl.
CC       Member of the csa5-cas7-cas5a-cas3-cas3'-cas8a2 operon.
CC       {ECO:0000269|PubMed:22408157}.
CC   -!- DOMAIN: Proteins of this family have an N-terminal nuclease domain and
CC       a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the
CC       domains are swapped, in others they are encoded separately.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated nuclease Cas3-HD family.
CC       {ECO:0000305}.
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DR   EMBL; FN869859; CCC81889.1; -; Genomic_DNA.
DR   RefSeq; WP_014127144.1; NC_016070.1.
DR   AlphaFoldDB; G4RJZ4; -.
DR   SMR; G4RJZ4; -.
DR   STRING; 768679.TTX_1254; -.
DR   EnsemblBacteria; CCC81889; CCC81889; TTX_1254.
DR   GeneID; 11262134; -.
DR   KEGG; ttn:TTX_1254; -.
DR   PATRIC; fig|768679.9.peg.1267; -.
DR   eggNOG; arCOG01442; Archaea.
DR   HOGENOM; CLU_1076128_0_0_2; -.
DR   OMA; HEPMILA; -.
DR   OrthoDB; 87017at2157; -.
DR   Proteomes; UP000002654; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3210.30; -; 1.
DR   InterPro; IPR006483; CRISPR-assoc_Cas3_HD.
DR   InterPro; IPR038257; CRISPR-assoc_Cas3_HD_sf.
DR   TIGRFAMs; TIGR01596; cas3_HD; 1.
DR   PROSITE; PS51643; HD_CAS3; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..226
FT                   /note="CRISPR-associated endonuclease Cas3-HD"
FT                   /id="PRO_0000422228"
FT   DOMAIN          9..204
FT                   /note="HD Cas3-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00974"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   226 AA;  25029 MW;  2413B564DE607DFD CRC64;
     MSCCAYFRGR DCLQTYEDHI TQALEACERL RPYYGRWMEK AFGTADAAAL AVEFHDLGKL
     AKAYIAGNRA RYRHEVLGAY FALKTLQTEA RYYVAAAVAL HHEPMILAAY AGELGERAIH
     VSTLRAMLKD SDLSLGCTPN YSYRPEVAAA LREWASRPPT ADDVADAFQE LAVYLSGGAP
     EEARVKRLRV AGLLHVLTVC DNWGARGRPG EGTFISRYMT VSELGL