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Database: UniProt
Entry: N9VBB8_9GAMM
LinkDB: N9VBB8_9GAMM
Original site: N9VBB8_9GAMM 
ID   N9VBB8_9GAMM            Unreviewed;       304 AA.
AC   N9VBB8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=G114_07715 {ECO:0000313|EMBL:ENY72542.1};
OS   Aeromonas diversa CDC 2478-85.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1268237 {ECO:0000313|EMBL:ENY72542.1, ECO:0000313|Proteomes:UP000023775};
RN   [1] {ECO:0000313|EMBL:ENY72542.1, ECO:0000313|Proteomes:UP000023775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2478-85 {ECO:0000313|EMBL:ENY72542.1,
RC   ECO:0000313|Proteomes:UP000023775};
RX   PubMed=23792745; DOI=10.1128/genomeA.00330-13;
RA   Farfan M., Spataro N., Sanglas A., Albarral V., Loren J.G., Bosch E.,
RA   Fuste M.C.;
RT   "Draft Genome Sequence of the Aeromonas diversa Type Strain.";
RL   Genome Announc. 1:S69-S82(2013).
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:ENY72542.1}.
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DR   EMBL; APVG01000015; ENY72542.1; -; Genomic_DNA.
DR   RefSeq; WP_005351117.1; NZ_CDCE01000025.1.
DR   AlphaFoldDB; N9VBB8; -.
DR   PATRIC; fig|1268237.3.peg.1522; -.
DR   eggNOG; COG1518; Bacteria.
DR   Proteomes; UP000023775; 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; 2.
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          277..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         140
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         207
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         220
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ   SEQUENCE   304 AA;  33042 MW;  8A4701146184B49D CRC64;
     MLPPLKPLPI KDRRAMLFLK YGQLDVIDGA FVLVDKEGVR THIPIGTVAC LMLEPGTRVS
     HAAVKLAATA GTLLVWVGEA GVRLYAAGQP GGARSDRLLY QAKLALDEDL RLKVVRKMFE
     LRFGEPPPSR RSVDQLRGIE GARVRETYKL LAARYGVKWQ GRRYDPKDWD KGDLPNKCIS
     AATSCLYGIT EAAILAAGYA PAIGFIHSGK PLSFVYDIAD IIKFETVVPQ AFEIAARGDA
     NPDRAVRLAC RDSFNKQRTL EKLIPLIEEV LLAGGITPPE APADAQPPAI PEPAGMGDAG
     HRSQ
//
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