CS3HD_PYRFU
ID CS3HD_PYRFU Reviewed; 237 AA.
AC Q8U336;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=CRISPR-associated endonuclease Cas3-HD;
DE EC=3.1.-.-;
DE AltName: Full=CRISPR-associated ss-nucleic acid exo- and endonuclease Cas3-HD;
GN Name=cas3; Synonyms=cas3''; OrderedLocusNames=PF0639;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION AS A NUCLEASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=22009198; DOI=10.1038/emboj.2011.377;
RA Beloglazova N., Petit P., Flick R., Brown G., Savchenko A., Yakunin A.F.;
RT "Structure and activity of the Cas3 HD nuclease MJ0384, an effector enzyme
RT of the CRISPR interference.";
RL EMBO J. 30:4616-4627(2011).
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). Cas3
CC plus Cascade participate in CRISPR interference, the third stage of
CC CRISPR immunity. Acts as a ssDNA and ssRNA nuclease, probably with both
CC exo- and endonuclease activities. Activity is higher for DNA than RNA.
CC Templates include 2',3'-cAMP and 2',3'-cGMP.
CC {ECO:0000269|PubMed:22009198}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22009198};
CC Note=ssDNase activity requires Mg(2+), ssRNase activity does not
CC require cations. {ECO:0000269|PubMed:22009198};
CC -!- ACTIVITY REGULATION: Both ssDNase and ssRNase are inhibited by EDTA.
CC {ECO:0000269|PubMed:22009198}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:22009198};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22009198}.
CC -!- DOMAIN: Proteins of this family have an N-terminal nuclease domain and
CC a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the
CC domains are swapped, in others they are encoded separately.
CC -!- SIMILARITY: Belongs to the CRISPR-associated nuclease Cas3-HD family.
CC {ECO:0000305}.
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DR EMBL; AE009950; AAL80763.1; -; Genomic_DNA.
DR RefSeq; WP_011011759.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U336; -.
DR SMR; Q8U336; -.
DR STRING; 186497.PF0639; -.
DR DNASU; 1468483; -.
DR EnsemblBacteria; AAL80763; AAL80763; PF0639.
DR GeneID; 41712441; -.
DR KEGG; pfu:PF0639; -.
DR PATRIC; fig|186497.12.peg.669; -.
DR eggNOG; arCOG01442; Archaea.
DR HOGENOM; CLU_1052127_0_0_2; -.
DR OMA; HEPILMG; -.
DR OrthoDB; 79895at2157; -.
DR PhylomeDB; Q8U336; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3210.30; -; 1.
DR InterPro; IPR006483; CRISPR-assoc_Cas3_HD.
DR InterPro; IPR038257; CRISPR-assoc_Cas3_HD_sf.
DR Pfam; PF18019; HD_6; 1.
DR TIGRFAMs; TIGR01596; cas3_HD; 1.
DR PROSITE; PS51643; HD_CAS3; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Endonuclease; Exonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..237
FT /note="CRISPR-associated endonuclease Cas3-HD"
FT /id="PRO_0000417606"
FT DOMAIN 4..215
FT /note="HD Cas3-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00974"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 237 AA; 27077 MW; 020E658972409BBB CRC64;
MSCKAFQGQT LREHIEAMLA AWEIVKNKYI PSIIRVMKTV GVKFTEEDAD KFMKTLIILH
DVGKCSEVYQ KHLSNNEPLR GFRHELVSAY YAYNILKDMF KDETIAFIGA LVVMMHHEPI
LMGQIRSLDK EELTPEVVLD KLRTFNGVME GTESFIKSMI KEKLGVIPKV PSPTQEDVLR
EVIRLSVLAR HRPDSGKLRM VVGALLIPLV LCDYKGAKER EGESPKFAEV LRVEMMK
