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Database: UniProt
Entry: W8PI96_9EURY
LinkDB: W8PI96_9EURY
Original site: W8PI96_9EURY 
ID   W8PI96_9EURY            Unreviewed;       326 AA.
AC   W8PI96;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=CRISPR-associated endonuclease Cas1 {ECO:0000256|HAMAP-Rule:MF_01470};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01470};
GN   Name=cas1 {ECO:0000256|HAMAP-Rule:MF_01470};
GN   ORFNames=BD01_0210 {ECO:0000313|EMBL:AHL21839.1};
OS   Thermococcus nautili.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=195522 {ECO:0000313|EMBL:AHL21839.1, ECO:0000313|Proteomes:UP000019434};
RN   [1] {ECO:0000313|EMBL:AHL21839.1, ECO:0000313|Proteomes:UP000019434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30-1 {ECO:0000313|EMBL:AHL21839.1,
RC   ECO:0000313|Proteomes:UP000019434};
RA   Oberto J., Gaudin M., Cossu M., Gorlas A., Slesarev A., Marguet E.,
RA   Forterre P.;
RT   "Genome Sequence of an Hyperthermophilic Archaeon, Thermococcus nautili 30-
RT   1, producing viral vesicles.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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 spacers, sequences complementary to
CC       antecedent mobile elements, and target invading nucleic acids. CRISPR
CC       clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as
CC       a dsDNA endonuclease. Involved in the integration of spacer DNA into
CC       the CRISPR cassette. {ECO:0000256|HAMAP-Rule:MF_01470}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01470};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01470};
CC   -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas2 homodimer.
CC       {ECO:0000256|HAMAP-Rule:MF_01470}.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01470}.
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DR   EMBL; CP007264; AHL21839.1; -; Genomic_DNA.
DR   RefSeq; WP_042689018.1; NZ_CP007264.1.
DR   AlphaFoldDB; W8PI96; -.
DR   STRING; 195522.BD01_0210; -.
DR   GeneID; 24958473; -.
DR   KEGG; tnu:BD01_0210; -.
DR   eggNOG; arCOG01452; Archaea.
DR   HOGENOM; CLU_052779_2_0_2; -.
DR   OrthoDB; 2216at2157; -.
DR   Proteomes; UP000019434; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004520; F:DNA endonuclease 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   CDD; cd09722; Cas1_I-B; 1.
DR   Gene3D; 1.20.120.920; CRISPR-associated endonuclease Cas1, C-terminal domain; 1.
DR   Gene3D; 3.100.10.20; CRISPR-associated endonuclease Cas1, N-terminal domain; 1.
DR   HAMAP; MF_01470; Cas1; 1.
DR   InterPro; IPR002729; CRISPR-assoc_Cas1.
DR   InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR   InterPro; IPR019858; CRISPR-assoc_Cas1_HMARI/TNEAP.
DR   InterPro; IPR042211; CRISPR-assoc_Cas1_N.
DR   NCBIfam; TIGR00287; cas1; 1.
DR   NCBIfam; TIGR03641; cas1_HMARI; 1.
DR   PANTHER; PTHR43219; CRISPR-ASSOCIATED ENDONUCLEASE CAS1; 1.
DR   PANTHER; PTHR43219:SF2; CRISPR-ASSOCIATED ENDONUCLEASE CAS1; 1.
DR   Pfam; PF01867; Cas_Cas1; 1.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01470};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01470};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01470};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01470}.
FT   BINDING         153
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         218
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         233
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ   SEQUENCE   326 AA;  38462 MW;  C790794FEFF9E9FC CRC64;
     MRKRSLTLLS DGTLFRRENT LYFENERGRK PLAVEGIYDI YIYGHVTITS QALHYLAQKG
     ISVHFFNHYG HYDGSFYPRE SLNSGDLVIR QAEHYLDREK RLKLARLFVR GSALNMERNL
     RRWKVNDGFS EELRELLEEL EGARKITEVM NVEARIREAY YSRWDGHLPE GFKIVKRTRR
     PPENEMNALI SFLNSRLYAT IVSELYNTQL VPTVSYLHEP GERRFSLALD LSEIFKPIVA
     DRLATRLVTK RMLSKEHFRE ELNGVLLTKE GMKKVLSEYE KELTKSVKHP ELKRNVTKKR
     LIRLEAYKLI KHLVGVKEYE PLVAWF
//
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