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Database: UniProt
Entry: G3A060_9RALS
LinkDB: G3A060_9RALS
Original site: G3A060_9RALS 
ID   G3A060_9RALS            Unreviewed;       307 AA.
AC   G3A060;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=RALSY_10527 {ECO:0000313|EMBL:CCA84552.1};
OS   Ralstonia syzygii R24.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA84552.1};
RN   [1] {ECO:0000313|EMBL:CCA84552.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA84552.1};
RX   PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA   Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA   Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT   "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT   solanacearum strains form a single genomic species despite divergent
RT   lifestyles.";
RL   PLoS ONE 6:e24356-e24356(2011).
RN   [2] {ECO:0000313|EMBL:CCA84552.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA84552.1};
RA   Genoscope - CEA;
RL   Submitted (APR-2011) 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|ARBA:ARBA00038592, 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; FR854086; CCA84552.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3A060; -.
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   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; IPR042211; CRISPR-assoc_Cas1_N.
DR   InterPro; IPR019855; CRISPR-assoc_Cas1_NMENI.
DR   NCBIfam; TIGR00287; cas1; 1.
DR   NCBIfam; TIGR03639; cas1_NMENI; 1.
DR   PANTHER; PTHR34353; CRISPR-ASSOCIATED ENDONUCLEASE CAS1 1; 1.
DR   PANTHER; PTHR34353:SF2; 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|ARBA:ARBA00023211, 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         148
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         205
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   307 AA;  33732 MW;  8CFACCE8C3649A87 CRC64;
     MIGRIVEIAT NNRYLGLDRG FMVVKSADEE VGRVPLDDLA AVIIAAHGIT HSSNLLVALA
     ERGVPFVLTA ANMQPVAMLW SVDGNYQQAG RMEAQLGASL PQNKRLWQQV VRSKLQMQAV
     VLESVGVPSA PLSALVSKVR SGDPENYEAQ GARRYWVLLF GDTFRRDRQQ EGINTLLNYG
     YTVLRAATAR AVIAAGLHPS VGLHHSNTQN AMRLVDDLME PFRPLIDLQV HACWRAGDIA
     LDRETKKRLA DVMYLDMPSP QGITPVMGAV QRLCTSLAQL YLGERKELEL PLCPTPIDLA
     AMFVPLA
//
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