ID   CAS2_PYRFU              Reviewed;          85 AA.
AC   Q8U1T8;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=CRISPR-associated endoribonuclease Cas2 {ECO:0000255|HAMAP-Rule:MF_01471};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01471};
GN   Name=cas2 {ECO:0000255|HAMAP-Rule:MF_01471}; OrderedLocusNames=PF1117;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS).
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RG   Southeast collaboratory for structural genomics (SECSG);
RA   Chen L.Q., Fu Z.-Q., Hwang J., Chang J., Chen L., Wang Y., Zhang H.,
RA   Liu Z.-J., Rose J.P., Wang B.C.;
RT   "Crystal structure of hypothetical protein Pf1117 from Pyrococcus
RT   furiosus.";
RL   Submitted (AUG-2006) to the PDB data bank.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01471}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01471};
CC   -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas1 homodimer.
CC       {ECO:0000255|HAMAP-Rule:MF_01471}.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2
CC       protein family. {ECO:0000255|HAMAP-Rule:MF_01471}.
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DR   EMBL; AE009950; AAL81241.1; -; Genomic_DNA.
DR   RefSeq; WP_014835332.1; NZ_CP023154.1.
DR   PDB; 2I0X; X-ray; 2.70 A; A=1-85.
DR   PDB; 4TNO; X-ray; 2.14 A; A=1-85.
DR   PDBsum; 2I0X; -.
DR   PDBsum; 4TNO; -.
DR   AlphaFoldDB; Q8U1T8; -.
DR   SMR; Q8U1T8; -.
DR   STRING; 186497.PF1117; -.
DR   EnsemblBacteria; AAL81241; AAL81241; PF1117.
DR   GeneID; 41712926; -.
DR   KEGG; pfu:PF1117; -.
DR   PATRIC; fig|186497.12.peg.1178; -.
DR   eggNOG; arCOG04194; Archaea.
DR   HOGENOM; CLU_161124_0_1_2; -.
DR   OMA; LTHVQNS; -.
DR   OrthoDB; 118787at2157; -.
DR   PhylomeDB; Q8U1T8; -.
DR   EvolutionaryTrace; Q8U1T8; -.
DR   Proteomes; UP000001013; Chromosome.
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   TIGRFAMs; TIGR01573; cas2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..85
FT                   /note="CRISPR-associated endoribonuclease Cas2"
FT                   /id="PRO_0000417751"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01471"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:4TNO"
FT   TURN            11..13
FT                   /evidence="ECO:0007829|PDB:4TNO"
FT   HELIX           14..21
FT                   /evidence="ECO:0007829|PDB:4TNO"
FT   TURN            22..24
FT                   /evidence="ECO:0007829|PDB:4TNO"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:4TNO"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:4TNO"
FT   HELIX           39..52
FT                   /evidence="ECO:0007829|PDB:4TNO"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:2I0X"
FT   STRAND          59..67
FT                   /evidence="ECO:0007829|PDB:4TNO"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:4TNO"
SQ   SEQUENCE   85 AA;  9979 MW;  0BEFD67576A39068 CRC64;
     MYIVVVYDVG VERVNKVKKF LRMHLNWVQN SVFEGEVTLA EFERIKEGLK KIIDENSDSV
     IIYKLRSMPP RETLGIEKNP IEEII