ID Q81BE5_BACCR Unreviewed; 196 AA.
AC Q81BE5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=CRISPR-associated endoribonuclease Cas2 {ECO:0000256|HAMAP-Rule:MF_01471};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01471};
GN Name=cas2 {ECO:0000256|HAMAP-Rule:MF_01471};
GN OrderedLocusNames=BC_3220 {ECO:0000313|EMBL:AAP10162.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP10162.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP10162.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(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:0000256|HAMAP-
CC Rule:MF_01471}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01471};
CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas1 homodimer.
CC {ECO:0000256|HAMAP-Rule:MF_01471}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2
CC protein family. {ECO:0000256|HAMAP-Rule:MF_01471}.
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DR EMBL; AE016877; AAP10162.1; -; Genomic_DNA.
DR RefSeq; NP_832961.1; NC_004722.1.
DR RefSeq; WP_000819859.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81BE5; -.
DR KEGG; bce:BC3220; -.
DR PATRIC; fig|226900.8.peg.3302; -.
DR HOGENOM; CLU_121791_0_0_9; -.
DR OrthoDB; 2356842at2; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01471; Cas2; 1.
DR InterPro; IPR021127; CRISPR_associated_Cas2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13671; AAA_33; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|HAMAP-Rule:MF_01471};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_01471};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01471};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01471};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01471};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01471};
KW Reference proteome {ECO:0000313|Proteomes:UP000001417}.
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01471"
SQ SEQUENCE 196 AA; 22722 MW; 429A8656B307489D CRC64;
MKRFVIITVG KTHSGKTTFA KALEKELSHS FVMDQDNQAE FINTHYEKLQ PAEGANTFKH
GLSKFIVDYA KEHTNLHLII CNSNRSKNGR FYLLNELFPQ NEYVRILVHF DIPDDVLYER
VARSTRSTNI FRGGYSSFKE VLDRQQTESL HDDVVDPIEN EADYLFVIRN SKDVNSTILK
IVHLAKEYSP TPNKRL
//
