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Database: UniProt
Entry: A0A171C263_9ACTN
LinkDB: A0A171C263_9ACTN
Original site: A0A171C263_9ACTN 
ID   A0A171C263_9ACTN        Unreviewed;       326 AA.
AC   A0A171C263;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=STXM2123_5840 {ECO:0000313|EMBL:GAT85139.1};
OS   Streptomyces sp. F-3.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT85139.1, ECO:0000313|Proteomes:UP000078145};
RN   [1] {ECO:0000313|EMBL:GAT85139.1, ECO:0000313|Proteomes:UP000078145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.;
RT   "Streptomyces sp. F-3 geneom sequencing.";
RL   Submitted (MAY-2016) 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:GAT85139.1}.
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DR   EMBL; BDDR01000069; GAT85139.1; -; Genomic_DNA.
DR   RefSeq; WP_067400305.1; NZ_BDDR01000069.1.
DR   AlphaFoldDB; A0A171C263; -.
DR   STRING; 1840095.STXM2123_5840; -.
DR   OrthoDB; 1550386at2; -.
DR   Proteomes; UP000078145; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078145}.
FT   BINDING         152
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         217
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         233
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ   SEQUENCE   326 AA;  36733 MW;  6AEF38730A9A36F7 CRC64;
     MPAATRTYWL TEPCRIRRED NSIRVERADG TPVRIPVTDI QDLVAFDHVD VNTSAMSLLS
     RNGITLHVLD HYGNHAGHFA PAESMASAAV VRRQVEITAD TTQRMTIARA LVQATAHNLR
     WVLDTDLLNP ALETLNAKLP DCGDPDAVMG QEGNFRRTAW AVLDTQLPAW LRLDGRTRRP
     PTNAGNAFVS YLDSIVYAQV LTALRSTPLH PAIGFLHADT DRRRNTLALY LAEPFKPLFT
     ERLLRRAAAQ KTLKPSDFET EVGRASLSRN GRKKVAGMVK EELATTVFHR SLKRKVSYEE
     LIHLEALKLV RLCLEGKPYK PFRPWW
//
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