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Database: UniProt
Entry: H3ZK33_THELN
LinkDB: H3ZK33_THELN
Original site: H3ZK33_THELN 
ID   H3ZK33_THELN            Unreviewed;       322 AA.
AC   H3ZK33;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=OCC_00662 {ECO:0000313|EMBL:EHR79723.1};
OS   Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523849 {ECO:0000313|EMBL:EHR79723.1, ECO:0000313|Proteomes:UP000015502};
RN   [1] {ECO:0000313|EMBL:EHR79723.1, ECO:0000313|Proteomes:UP000015502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
RC   {ECO:0000313|Proteomes:UP000015502};
RX   PubMed=22493191; DOI=10.1128/JB.00123-12;
RA   Gardner A.F., Kumar S., Perler F.B.;
RT   "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT   litoralis NS-C.";
RL   J. Bacteriol. 194:2375-2376(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 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; CP006670; EHR79723.1; -; Genomic_DNA.
DR   RefSeq; WP_004066414.1; NC_022084.1.
DR   AlphaFoldDB; H3ZK33; -.
DR   STRING; 523849.OCC_00662; -.
DR   PaxDb; 523849-OCC_00662; -.
DR   GeneID; 16548337; -.
DR   KEGG; tlt:OCC_00662; -.
DR   HOGENOM; CLU_052779_2_0_2; -.
DR   OrthoDB; 2216at2157; -.
DR   Proteomes; UP000015502; 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         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         214
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         229
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ   SEQUENCE   322 AA;  37345 MW;  20F8E5DD9C846496 CRC64;
     MRKKSITLLS DGALTRRENT LYFENAQGKK PLAVEGIYDI YIYGHVNISS QALHFLAQKG
     IAVHFFNYYG HYDGSFYPRE SLHSGDLLIK QAEHYLNKEK RLKLAKLFVT GSAKNMELNL
     KRWKINASFG ELLKELESAR KITEVMNVEA RIRQEYYNLW DEVLPDGFKI VRRTRRPPEN
     EMNALISFLN SRLYATIVSE LYNTQLAPTV SYLHEPSERR FSLALDLSEI FKPIIADRIA
     NRLVKQGIIK EGHFREELNG VLLTKEGMKT VLKAYNEELG KSVKHPGLKK NVTKQRLIRL
     EAYKLIKHLV GIKDYEPLVA WF
//
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