CAS1C_THEYD
ID CAS1C_THEYD Reviewed; 325 AA.
AC B5YIU9;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=CRISPR-associated endonuclease Cas1 3 {ECO:0000255|HAMAP-Rule:MF_01470};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01470};
GN Name=cas1-3 {ECO:0000255|HAMAP-Rule:MF_01470}; Synonyms=cas1_2;
GN OrderedLocusNames=THEYE_A2036;
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; ACI20555.1; -; Genomic_DNA.
DR RefSeq; WP_012545291.1; NC_011296.1.
DR RefSeq; YP_002249823.1; NC_011296.1.
DR AlphaFoldDB; B5YIU9; -.
DR SMR; B5YIU9; -.
DR STRING; 289376.THEYE_A2036; -.
DR EnsemblBacteria; ACI20555; ACI20555; THEYE_A2036.
DR KEGG; tye:THEYE_A2036; -.
DR PATRIC; fig|289376.4.peg.1984; -.
DR eggNOG; COG1518; Bacteria.
DR HOGENOM; CLU_052779_2_0_0; -.
DR InParanoid; B5YIU9; -.
DR OMA; NTIMFET; -.
DR OrthoDB; 1581397at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004520; F:endodeoxyribonuclease 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; cd09722; Cas1_I-B; 1.
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; IPR019858; CRISPR-assoc_Cas1_HMARI/TNEAP.
DR InterPro; IPR042211; CRISPR-assoc_Cas1_N.
DR PANTHER; PTHR43219; PTHR43219; 1.
DR Pfam; PF01867; Cas_Cas1; 1.
DR TIGRFAMs; TIGR00287; cas1; 1.
DR TIGRFAMs; TIGR03641; cas1_HMARI; 1.
PE 3: Inferred from homology;
KW Antiviral defense; DNA-binding; Endonuclease; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..325
FT /note="CRISPR-associated endonuclease Cas1 3"
FT /id="PRO_0000417088"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 217
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
SQ SEQUENCE 325 AA; 38754 MW; 3F1EAA66247F3628 CRC64;
MRNYYIFSNG RIRRKENTIY IENEQGDRKA IPIEDVDTIH IFGEVDLNTK LLNFICQQGK
TVHFYNYYGF YSGSLMPRER NVSGHIVVKQ VEHFLDPERR FYLAYSFVEG AIFHMVRNLR
EYKNTDEFQE KIKKELSNAV ETTKISELMG CEGRARDFYY EAFNTFLKSD FSMGKREKRP
PRNPINALIS FANSMIYTTV LNEIYHTQLN PTVSYLHEPS ERRYSLSLDI AEIFKPLLAD
AIIFKLINNN MIKLDDFEED VNYCYLNESG RKKFIREFDQ KLSTTIKHRK LKRNVSYRTI
IRIECYKLIK HFIGDEVYAP FKAWW
