ID   CAS2B_SACS2             Reviewed;          88 AA.
AC   Q97Y85;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=CRISPR-associated endoribonuclease Cas2 2;
DE            EC=3.1.-.-;
GN   Name=cas22; OrderedLocusNames=SSO8090;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   FUNCTION AS A SSRNA-SPECIFIC ENDORIBONUCLEASE.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=18482976; DOI=10.1074/jbc.m803225200;
RA   Beloglazova N., Brown G., Zimmerman M.D., Proudfoot M., Makarova K.S.,
RA   Kudritska M., Kochinyan S., Wang S., Chruszcz M., Minor W., Koonin E.V.,
RA   Edwards A.M., Savchenko A., Yakunin A.F.;
RT   "A novel family of sequence-specific endoribonucleases associated with the
RT   clustered regularly interspaced short palindromic repeats.";
RL   J. Biol. Chem. 283:20361-20371(2008).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RA   Proudfoot M., Brown M., Singer A.U., Skarina T., Tan K., Kagan O.,
RA   Edwards A.M., Joachimiak A., Savchenko A., Yakunin A.F.;
RT   "Structure of the RNase SSO8090 from Sulfolobus solfataricus.";
RL   Submitted (OCT-2008) 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 (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:18482976}.
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}.
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DR   EMBL; AE006641; AAK54438.1; -; Genomic_DNA.
DR   RefSeq; WP_009990820.1; NC_002754.1.
DR   PDB; 3EXC; X-ray; 2.25 A; X=1-88.
DR   PDBsum; 3EXC; -.
DR   AlphaFoldDB; Q97Y85; -.
DR   SMR; Q97Y85; -.
DR   STRING; 273057.SSO8090; -.
DR   EnsemblBacteria; AAK54438; AAK54438; SSO8090.
DR   GeneID; 44130269; -.
DR   KEGG; sso:SSO8090; -.
DR   PATRIC; fig|273057.12.peg.1479; -.
DR   eggNOG; arCOG04194; Archaea.
DR   HOGENOM; CLU_161124_2_0_2; -.
DR   InParanoid; Q97Y85; -.
DR   OMA; IDIFPIC; -.
DR   PhylomeDB; Q97Y85; -.
DR   EvolutionaryTrace; Q97Y85; -.
DR   Proteomes; UP000001974; 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..88
FT                   /note="CRISPR-associated endoribonuclease Cas2 2"
FT                   /id="PRO_0000416952"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:3EXC"
FT   HELIX           12..24
FT                   /evidence="ECO:0007829|PDB:3EXC"
FT   STRAND          28..31
FT                   /evidence="ECO:0007829|PDB:3EXC"
FT   STRAND          34..38
FT                   /evidence="ECO:0007829|PDB:3EXC"
FT   HELIX           44..54
FT                   /evidence="ECO:0007829|PDB:3EXC"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:3EXC"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:3EXC"
FT   HELIX           69..73
FT                   /evidence="ECO:0007829|PDB:3EXC"
SQ   SEQUENCE   88 AA;  10224 MW;  870148D1138A7930 CRC64;
     MKLLVVYDVS DDSKRNKLAN NLKKLGLERI QRSAFEGDID SQRVKDLVRV VKLIVDTNTD
     IVHIIPLGIR DWERRIVIGR EGLEEWLV