ID   CAS2A_SYNY3             Reviewed;          94 AA.
AC   Q6ZEI1;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=CRISPR-associated endoribonuclease Cas2 1 {ECO:0000255|HAMAP-Rule:MF_01471};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01471};
GN   Name=cas2-1 {ECO:0000255|HAMAP-Rule:MF_01471}; OrderedLocusNames=ssr7017;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OG   Plasmid pSYSA.
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=14686584; DOI=10.1093/dnares/10.5.221;
RA   Kaneko T., Nakamura Y., Sasamoto S., Watanabe A., Kohara M., Matsumoto M.,
RA   Shimpo S., Yamada M., Tabata S.;
RT   "Structural analysis of four large plasmids harboring in a unicellular
RT   cyanobacterium, Synechocystis sp. PCC 6803.";
RL   DNA Res. 10:221-228(2003).
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; AP004311; BAD01919.1; -; Genomic_DNA.
DR   PDB; 7CR6; X-ray; 3.72 A; E/F=1-94.
DR   PDB; 7CR8; X-ray; 3.70 A; E/F/M/N/U/V/e/f/m/n/u/v=1-94.
DR   PDBsum; 7CR6; -.
DR   PDBsum; 7CR8; -.
DR   AlphaFoldDB; Q6ZEI1; -.
DR   SMR; Q6ZEI1; -.
DR   EnsemblBacteria; BAD01919; BAD01919; BAD01919.
DR   KEGG; syn:ssr7017; -.
DR   InParanoid; Q6ZEI1; -.
DR   OMA; GKWTQYS; -.
DR   PhylomeDB; Q6ZEI1; -.
DR   Proteomes; UP000001425; Plasmid pSYSA.
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   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Plasmid; Reference proteome.
FT   CHAIN           1..94
FT                   /note="CRISPR-associated endoribonuclease Cas2 1"
FT                   /id="PRO_0000417733"
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"
SQ   SEQUENCE   94 AA;  10838 MW;  9812C9C310560FBA CRC64;
     MLYLIIYDVP ATKAGNKRRT RLFDLLSGYG KWRQFSVFEC FLSVKQFAKL QTAMEKLIKL
     DEDAVCIYVL DENTVQRTIT YGTPQPEKPG SIII