ID   CAS2_ACIET              Reviewed;         102 AA.
AC   B9M9X6;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=Dtpsy_0058;
OS   Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Diaphorobacter.
OX   NCBI_TaxID=535289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TPSY;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT   "Complete sequence of Diaphorobacter sp. TPSY.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001392; ACM31547.1; -; Genomic_DNA.
DR   RefSeq; WP_012655174.1; NC_011992.1.
DR   AlphaFoldDB; B9M9X6; -.
DR   SMR; B9M9X6; -.
DR   STRING; 535289.Dtpsy_0058; -.
DR   EnsemblBacteria; ACM31547; ACM31547; Dtpsy_0058.
DR   KEGG; dia:Dtpsy_0058; -.
DR   eggNOG; COG3512; Bacteria.
DR   HOGENOM; CLU_150500_1_0_4; -.
DR   OMA; TDKQFGM; -.
DR   OrthoDB; 1841250at2; -.
DR   Proteomes; UP000000450; 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   HAMAP; MF_01471; Cas2; 1.
DR   InterPro; IPR021127; CRISPR_associated_Cas2.
DR   InterPro; IPR019199; Virulence_VapD/CRISPR_Cas2.
DR   Pfam; PF09827; CRISPR_Cas2; 1.
DR   TIGRFAMs; TIGR01573; cas2; 1.
PE   3: Inferred from homology;
KW   Antiviral defense; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease.
FT   CHAIN           1..102
FT                   /note="CRISPR-associated endoribonuclease Cas2"
FT                   /id="PRO_0000417701"
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   102 AA;  11656 MW;  F9D5B3D4EE86ECA7 CRC64;
     MRMLVFFDLP VVSKADRRAY TVFRRFLLND GYDMIQFSVY GRILNGTDAA QKHMQRLLAN
     LPSEGSVRVL TVTEKQFASM KLLVGLPLFQ EKKVNAAQIA LF