ID   CAS4_AERPE              Reviewed;         199 AA.
AC   Q9YCL9;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=CRISPR-associated exonuclease Cas4;
DE            EC=3.1.12.1 {ECO:0000250|UniProtKB:Q97TX9};
GN   Name=cas4; OrderedLocusNames=APE_1239.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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). This
CC       may be a 5' to 3' ssDNA exonuclease (By similarity).
CC       {ECO:0000250|UniProtKB:Q97TX9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=exonucleolytic cleavage in the 5'- to 3'-direction to yield
CC         nucleoside 3'-phosphates.; EC=3.1.12.1;
CC         Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC       Note=Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also
CC       utilise Cu(2+). {ECO:0000250|UniProtKB:Q97TX9};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. It may be important for
CC       protein stability, since mutation of the Cys that bind the cofactor
CC       leads to a colorless, insoluble protein.
CC       {ECO:0000250|UniProtKB:Q97TX9};
CC   -!- SIMILARITY: Belongs to the CRISPR-associated exonuclease Cas4 family.
CC       {ECO:0000305}.
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DR   EMBL; BA000002; BAA80228.2; -; Genomic_DNA.
DR   PIR; F72596; F72596.
DR   AlphaFoldDB; Q9YCL9; -.
DR   SMR; Q9YCL9; -.
DR   STRING; 272557.APE_1239.1; -.
DR   EnsemblBacteria; BAA80228; BAA80228; APE_1239.1.
DR   KEGG; ape:APE_1239.1; -.
DR   eggNOG; arCOG00786; Archaea.
DR   OMA; RQYLYCP; -.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR   GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR   Gene3D; 3.90.320.10; -; 1.
DR   InterPro; IPR013343; CRISPR-assoc_prot_Cas4.
DR   InterPro; IPR022765; Dna2/Cas4_DUF83.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   Pfam; PF01930; Cas_Cas4; 1.
DR   TIGRFAMs; TIGR00372; cas4; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Antiviral defense; Exonuclease; Hydrolase; Iron; Iron-sulfur;
KW   Manganese; Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..199
FT                   /note="CRISPR-associated exonuclease Cas4"
FT                   /id="PRO_0000417890"
FT   BINDING         13
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         91
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         92
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         179
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         182
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         188
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
SQ   SEQUENCE   199 AA;  22699 MW;  CF544C2685BFA1CB CRC64;
     MRPVSMLKEY AYCPRVAYYM EVLRPSYRPT EPMNLSREIY SVDHVRGILR SSGFRIVKEE
     WAVPLRSKRL GLQGVADGVV VEGSLGIIVV EAKLSVRSNR WLHTRGRHVI FQAAAYALAL
     EETRGYSVDY LAIVSLEDSK TYVVKMSPSL RRDVIRLADD MNKTLDDGLE PPPKPGRKCV
     ACRFRRVCQP WVAERGSER