CAS4_THETK
ID CAS4_THETK Reviewed; 190 AA.
AC G4RJY5;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=CRISPR-associated exonuclease Cas4;
DE EC=3.1.12.1 {ECO:0000250|UniProtKB:Q97TX9};
GN Name=cas4; OrderedLocusNames=TTX_1245;
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
RN [2]
RP SUBUNIT, INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX PubMed=22408157; DOI=10.1128/jb.00206-12;
RA Plagens A., Tjaden B., Hagemann A., Randau L., Hensel R.;
RT "Characterization of the CRISPR/Cas subtype I-A system of the
RT hyperthermophilic crenarchaeon Thermoproteus tenax.";
RL J. Bacteriol. 194:2491-2500(2012).
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 -!- SUBUNIT: Can form a Cascis complex with Cas1/2 and Csa1.
CC {ECO:0000269|PubMed:22408157}.
CC -!- INDUCTION: Slightly induced by 20 J/m2 ultraviolet light. Member of the
CC csa1-cas1/2-cas4 operon. {ECO:0000269|PubMed:22408157}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated exonuclease Cas4 family.
CC {ECO:0000305}.
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DR EMBL; FN869859; CCC81880.1; -; Genomic_DNA.
DR RefSeq; WP_014127135.1; NC_016070.1.
DR AlphaFoldDB; G4RJY5; -.
DR SMR; G4RJY5; -.
DR STRING; 768679.TTX_1245; -.
DR EnsemblBacteria; CCC81880; CCC81880; TTX_1245.
DR GeneID; 11262125; -.
DR KEGG; ttn:TTX_1245; -.
DR PATRIC; fig|768679.9.peg.1258; -.
DR eggNOG; arCOG00786; Archaea.
DR HOGENOM; CLU_102055_2_0_2; -.
DR OMA; RQYLYCP; -.
DR OrthoDB; 84826at2157; -.
DR Proteomes; UP000002654; 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 1: Evidence at protein level;
KW 4Fe-4S; Antiviral defense; Exonuclease; Hydrolase; Iron; Iron-sulfur;
KW Manganese; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..190
FT /note="CRISPR-associated exonuclease Cas4"
FT /id="PRO_0000422225"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 74
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 87
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 171
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 174
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 180
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
SQ SEQUENCE 190 AA; 21116 MW; 648DE105DE64C9AB CRC64;
MSLCINPSLI RQYLYCPMAA YYIAAGAPEP PTLRMQRGRE IQQEAAQAAA KALGAERAEY
SVHITAPPLC GTVDAVLWIN GRPSPLEVKA AARPRRIPIH HKAQAAAYIA MVQRAYGRAV
ATAYIYYAES GQIAQIRMAK DLQELLNYAV SRLQQILQGK PPVLNPNPAK CQNCWYRKWC
SHLPTTVEKI
