CAS1B_THEYD
ID CAS1B_THEYD Reviewed; 330 AA.
AC B5YL10;
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 2 {ECO:0000255|HAMAP-Rule:MF_01470};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01470};
GN Name=cas1-2 {ECO:0000255|HAMAP-Rule:MF_01470}; Synonyms=cas1_1;
GN OrderedLocusNames=THEYE_A1101;
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; ACI20636.1; -; Genomic_DNA.
DR RefSeq; WP_012545370.1; NC_011296.1.
DR RefSeq; YP_002248925.1; NC_011296.1.
DR AlphaFoldDB; B5YL10; -.
DR SMR; B5YL10; -.
DR STRING; 289376.THEYE_A1101; -.
DR EnsemblBacteria; ACI20636; ACI20636; THEYE_A1101.
DR KEGG; tye:THEYE_A1101; -.
DR PATRIC; fig|289376.4.peg.1079; -.
DR eggNOG; COG1518; Bacteria.
DR HOGENOM; CLU_052779_2_0_0; -.
DR InParanoid; B5YL10; -.
DR OMA; AYKLIKH; -.
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..330
FT /note="CRISPR-associated endonuclease Cas1 2"
FT /id="PRO_0000417087"
FT BINDING 156
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 222
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
SQ SEQUENCE 330 AA; 39190 MW; BF7CAC5C1087D91A CRC64;
MKKSLYIISD GELKRKDNTL YFETSEERKY IPVENTREIL IFGEVSMNKR LLEFLTESEI
IIHFFNYYGY YIGSFYPREH LNSGYMILKQ AEHYLDTGKR LNLAEKFVSG AIENIKKVLI
YYHNRGKELS EIISKIQEIA TNIPDCSTTD ELMAIEGNIR DYYYQSFDII LDNEHFIFET
RTKRPPKNRI NALISFANSL VYTTCLSEIY QTHLDPRIGY LHATNFRRFT LNLDVAEIFK
PIIADRAIFS IVNKRIVKPQ HFEKKLDGIV LNDKGKQILL QEMDERLRST IQHKKLGRHV
SYRQLIRLEL YKIQKHLMEE EEYKPFVTGW
