CAS2C_THEYD
ID CAS2C_THEYD Reviewed; 88 AA.
AC B5YIU7;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=CRISPR-associated endoribonuclease Cas2 3 {ECO:0000255|HAMAP-Rule:MF_01471};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01471};
GN Name=cas2-3 {ECO:0000255|HAMAP-Rule:MF_01471};
GN OrderedLocusNames=THEYE_A2034;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001147; ACI21703.1; -; Genomic_DNA.
DR RefSeq; WP_012546411.1; NC_011296.1.
DR RefSeq; YP_002249821.1; NC_011296.1.
DR AlphaFoldDB; B5YIU7; -.
DR SMR; B5YIU7; -.
DR STRING; 289376.THEYE_A2034; -.
DR EnsemblBacteria; ACI21703; ACI21703; THEYE_A2034.
DR KEGG; tye:THEYE_A2034; -.
DR PATRIC; fig|289376.4.peg.1982; -.
DR eggNOG; COG1343; Bacteria.
DR HOGENOM; CLU_161124_0_1_0; -.
DR InParanoid; B5YIU7; -.
DR OMA; KKYFTWV; -.
DR OrthoDB; 1951170at2; -.
DR Proteomes; UP000000718; 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 3: Inferred from homology;
KW Antiviral defense; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Reference proteome.
FT CHAIN 1..88
FT /note="CRISPR-associated endoribonuclease Cas2 3"
FT /id="PRO_0000417735"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01471"
SQ SEQUENCE 88 AA; 10480 MW; F6125887858012BF CRC64;
MPYLIVTYDI AEERVNKVRK ILKKYFMWVQ NSVFEGEITE GKLLKCKLEL EKVIDKEVDS
VYFYSLENRL NYRKTVLGIE KEITGNIL
