ID F4HL47_PYRSN Unreviewed; 322 AA.
AC F4HL47;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 OrderedLocusNames=PNA2_1813 {ECO:0000313|EMBL:AEC52728.1};
OS Pyrococcus sp. (strain NA2).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=342949 {ECO:0000313|EMBL:AEC52728.1, ECO:0000313|Proteomes:UP000008293};
RN [1] {ECO:0000313|EMBL:AEC52728.1, ECO:0000313|Proteomes:UP000008293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA2 {ECO:0000313|EMBL:AEC52728.1,
RC ECO:0000313|Proteomes:UP000008293};
RX PubMed=21602357; DOI=10.1128/JB.05150-11;
RA Lee H.S., Bae S.S., Kim M.S., Kwon K.K., Kang S.G., Lee J.H.;
RT "Complete genome sequence of hyperthermophilic Pyrococcus sp. strain NA2,
RT isolated from a deep-sea hydrothermal vent area.";
RL J. Bacteriol. 193:3666-3667(2011).
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; CP002670; AEC52728.1; -; Genomic_DNA.
DR RefSeq; WP_013749278.1; NC_015474.1.
DR AlphaFoldDB; F4HL47; -.
DR STRING; 342949.PNA2_1813; -.
DR GeneID; 10555303; -.
DR KEGG; pyn:PNA2_1813; -.
DR PATRIC; fig|342949.8.peg.1828; -.
DR eggNOG; arCOG01452; Archaea.
DR HOGENOM; CLU_052779_2_0_2; -.
DR OrthoDB; 2216at2157; -.
DR Proteomes; UP000008293; 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; 37854 MW; EEB7CFEBD0BDFA7C CRC64;
MRKKHLTIFS DGTLLRKENT LYFESSKGKK PLAIEGIYDI YIYGHVNITS QALHYLAQKG
IVVHFFNHYG FYDGSFYPRE TLLSGELIIR QAEHYLDKEK RLFLAKAFVW GGAKNMERNF
KNWSIDFDFS SHLEELKGVN KITEVMNVEA RIRQEYYGRW DETLPEGFKI GKRTRRPPKN
EMNALISFLN SRLYATIITE LYNTQLAPTI SYLHEPSERR FSLALDLSEI FKPIIVDRIA
NRLVKKGVIK EEHFRKDLNG VLLSDEGMRI VTRAYNEELQ KSTKHQKLGK NVTRQRLIRL
EAYKLIKHLV GVEEYRPLVA WF
//
