CAS1A_THEYD
ID CAS1A_THEYD Reviewed; 318 AA.
AC B5YJS2;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=CRISPR-associated endonuclease Cas1 1 {ECO:0000255|HAMAP-Rule:MF_01470};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01470};
GN Name=cas1-1 {ECO:0000255|HAMAP-Rule:MF_01470};
GN OrderedLocusNames=THEYE_A0644;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) 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:0000255|HAMAP-Rule:MF_01470}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01470};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01470};
CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas2 homodimer.
CC {ECO:0000255|HAMAP-Rule:MF_01470}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01470}.
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DR EMBL; CP001147; ACI21534.1; -; Genomic_DNA.
DR RefSeq; WP_012546247.1; NC_011296.1.
DR RefSeq; YP_002248487.1; NC_011296.1.
DR AlphaFoldDB; B5YJS2; -.
DR SMR; B5YJS2; -.
DR STRING; 289376.THEYE_A0644; -.
DR EnsemblBacteria; ACI21534; ACI21534; THEYE_A0644.
DR KEGG; tye:THEYE_A0644; -.
DR PATRIC; fig|289376.4.peg.638; -.
DR eggNOG; COG1518; Bacteria.
DR HOGENOM; CLU_052779_1_1_0; -.
DR InParanoid; B5YJS2; -.
DR OMA; YYVGSFY; -.
DR OrthoDB; 1581397at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
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; -; 1.
DR Gene3D; 3.100.10.20; -; 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 Pfam; PF01867; Cas_Cas1; 1.
DR TIGRFAMs; TIGR00287; cas1; 1.
PE 3: Inferred from homology;
KW Antiviral defense; DNA-binding; Endonuclease; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..318
FT /note="CRISPR-associated endonuclease Cas1 1"
FT /id="PRO_0000417086"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 240
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
SQ SEQUENCE 318 AA; 36548 MW; 79540871E9482BA3 CRC64;
MSTVFIDRKD IEIRVDGNSI SFYAKGKKDG SLPLSPLKRV VIVGNVKIET SVLYKLVNHG
ITVLFLTGKL KYSGILNGPL HNNGLLRVKQ YQKSLSGFSL KFAKELIKRK IVSQRDFLSE
IREIKKALAM QADRAIEILN KAISNIEVTP ISIDSLRGIE GAASSIYFIT YSKIFPNSLK
FVRRIKRPPK DPVNAMLSLC YTLLHYEIVR EIQLIGLDPT IGFYHQFEYG RESLACDLVE
LFRVNVDRFV YELFKAKHLG NRDFMKDEES GGVYLKKTGR KKFYPLYEQW VQQQRTIWRG
EVQGFARRIL EEKDIISG
