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Database: UniProt
Entry: D3D4C5_9ACTN
LinkDB: D3D4C5_9ACTN
Original site: D3D4C5_9ACTN 
ID   D3D4C5_9ACTN            Unreviewed;       369 AA.
AC   D3D4C5;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=FrEUN1fDRAFT_4647 {ECO:0000313|EMBL:EFC82258.1};
OS   Parafrankia sp. EUN1f.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Parafrankia.
OX   NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC82258.1, ECO:0000313|Proteomes:UP000004777};
RN   [1] {ECO:0000313|EMBL:EFC82258.1, ECO:0000313|Proteomes:UP000004777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EUN1f {ECO:0000313|EMBL:EFC82258.1,
RC   ECO:0000313|Proteomes:UP000004777};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A.,
RA   Fernandez M., Tisa L.;
RT   "The draft genome of Frankia sp. EUN1f.";
RL   Submitted (JAN-2010) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFC82258.1}.
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DR   EMBL; ADGX01000079; EFC82258.1; -; Genomic_DNA.
DR   RefSeq; WP_006542508.1; NZ_ADGX01000079.1.
DR   AlphaFoldDB; D3D4C5; -.
DR   Proteomes; UP000004777; Unassembled WGS sequence.
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; cd09719; Cas1_I-E; 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; IPR033641; Cas1_I-E.
DR   InterPro; IPR002729; CRISPR-assoc_Cas1.
DR   InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR   InterPro; IPR019851; CRISPR-assoc_Cas1_ECOLI.
DR   InterPro; IPR042211; CRISPR-assoc_Cas1_N.
DR   NCBIfam; TIGR00287; cas1; 1.
DR   NCBIfam; TIGR03638; cas1_ECOLI; 1.
DR   PANTHER; PTHR34353:SF3; CRISPR-ASSOCIATED ENDONUCLEASE CAS1; 1.
DR   PANTHER; PTHR34353; CRISPR-ASSOCIATED ENDONUCLEASE CAS1 1; 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   REGION          323..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         158
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         225
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         238
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ   SEQUENCE   369 AA;  40329 MW;  1019AD996B0B7CEA CRC64;
     MSVTRAPQTA KHRLGRPTLA MLPRVADSLS FLYLESVQVT QDDTGVLAYV ETPHGVEKTY
     LPTAALSCLL LGPGTSITQP ALATLARHDT SVVCVGAGGI RSYANIQPAG LTTRWLEQQA
     RTWADDTLRV QVAARMYRTR FATDVPESTT LAQLRGMEGQ RVKAYYKLLA QKHRIPRFRR
     NYDPAKWDTQ DPVNLALSAA NTCLYGIVHA AVCALGCSPA LGYIHSGTQL AFVYDIADLY
     KAKTTIPLAF ALHDSPDPER AARSRLREEF RLIRLLPNII NDIQTMLDLS RDLDTDDDPG
     DRASLTADMV HLWDPDLGAL PAGVNYSNDT PAAGNDTDAP RPSPPAGTID NGDLEDDDVL
     INLGDPWPQ
//
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