CAS2_STRMU
ID CAS2_STRMU Reviewed; 109 AA.
AC Q8DTE5;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=SMU_1403c;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59068.1; -; Genomic_DNA.
DR RefSeq; NP_721762.1; NC_004350.2.
DR AlphaFoldDB; Q8DTE5; -.
DR SMR; Q8DTE5; -.
DR STRING; 210007.SMU_1403c; -.
DR PRIDE; Q8DTE5; -.
DR DNASU; 1029503; -.
DR EnsemblBacteria; AAN59068; AAN59068; SMU_1403c.
DR KEGG; smu:SMU_1403c; -.
DR PATRIC; fig|210007.7.peg.1248; -.
DR eggNOG; COG3512; Bacteria.
DR HOGENOM; CLU_150500_1_1_9; -.
DR OMA; TDKQFGM; -.
DR Proteomes; UP000002512; 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; Reference proteome.
FT CHAIN 1..109
FT /note="CRISPR-associated endoribonuclease Cas2"
FT /id="PRO_0000417729"
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 109 AA; 12634 MW; 7AE5EEB400A9A560 CRC64;
MRMILMFDMP TDTAEERKAY RKFRKFLLSE GFIMHQFSVY SKLLLNNSAN TAMIARLKEN
NPKKGNITLL TVTEKQFARM IYLNGERDTS IANSDSRLVF LGEAFPDET