ID   CSA1_THETK              Reviewed;         278 AA.
AC   G4RJY8;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=CRISPR-associated exonuclease Csa1;
GN   Name=csa1; OrderedLocusNames=TTX_1248;
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) (By
CC       similarity). A ssDNA exonuclease with 5' to 3' and perhaps 3' to 5'
CC       activity. {ECO:0000250|UniProtKB:Q97YD4}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q97YD4};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. May not be required for
CC       nuclease activity. {ECO:0000250|UniProtKB:Q97YD4};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q97YD4};
CC       Note=Mn(2+) required for nuclease activity.
CC       {ECO:0000250|UniProtKB:Q97YD4};
CC   -!- SUBUNIT: Can form a Cascis complex with Cas4 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 protein Csa1 family.
CC       {ECO:0000305}.
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DR   EMBL; FN869859; CCC81883.1; -; Genomic_DNA.
DR   RefSeq; WP_014127138.1; NC_016070.1.
DR   AlphaFoldDB; G4RJY8; -.
DR   STRING; 768679.TTX_1248; -.
DR   EnsemblBacteria; CCC81883; CCC81883; TTX_1248.
DR   GeneID; 11262128; -.
DR   KEGG; ttn:TTX_1248; -.
DR   PATRIC; fig|768679.9.peg.1261; -.
DR   eggNOG; arCOG04195; Archaea.
DR   HOGENOM; CLU_905009_0_0_2; -.
DR   OMA; FAYGYCP; -.
DR   OrthoDB; 88132at2157; -.
DR   Proteomes; UP000002654; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; 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   InterPro; IPR009260; CRISPR-ass_Csa1.
DR   Pfam; PF06023; Csa1; 1.
DR   PIRSF; PIRSF009226; UCP009226; 1.
DR   TIGRFAMs; TIGR01896; cas_AF1879; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Antiviral defense; Iron; Iron-sulfur; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..278
FT                   /note="CRISPR-associated exonuclease Csa1"
FT                   /id="PRO_0000422232"
FT   BINDING         55
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         266
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         270
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         276
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
SQ   SEQUENCE   278 AA;  30102 MW;  5F3390785ABD9A22 CRC64;
     MLTLLEIARL LRRAKVTQGP AEVSPELRGW AYDRQPVKPP AYLGLALSDF AYGYCPTGRS
     LYLKYVLGER PQPTKPLAEG QALHAVLFKA LEDFRRYVYS GAPMSPPGEG MPEDLRAKAE
     ALYRYIAVRL TGEYQYVLAS RLARSRDAAA FYAAPIAAQI AVDGAPLGLS YVVADGVALG
     AVVEFKFGPS QNVDVALAGY AMAIEAEYGV PIDYGIHVQI AVDGQVEYRA SAYVLGDAPR
     AKFLEARDEA IDVVASARDP GPAPQCPKTC PYYSVCRS