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CAS1_PYRHO
ID   CAS1_PYRHO              Reviewed;         322 AA.
AC   O58938;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=CRISPR-associated endonuclease Cas1 {ECO:0000255|HAMAP-Rule:MF_01470};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01470};
GN   Name=cas1 {ECO:0000255|HAMAP-Rule:MF_01470}; OrderedLocusNames=PH1245;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), AND SUBUNIT.
RA   Petit P., Brown G., Savchenko A., Yakunin A.F.;
RT   "Structure determination and overall comparison of three Cas1 proteins.";
RL   Submitted (DEC-2010) to the PDB data bank.
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; BA000001; BAA30345.1; -; Genomic_DNA.
DR   PIR; G71068; G71068.
DR   RefSeq; WP_010885333.1; NC_000961.1.
DR   PDB; 4WJ0; X-ray; 2.85 A; A/B=1-322.
DR   PDBsum; 4WJ0; -.
DR   AlphaFoldDB; O58938; -.
DR   SMR; O58938; -.
DR   STRING; 70601.3257662; -.
DR   EnsemblBacteria; BAA30345; BAA30345; BAA30345.
DR   GeneID; 1443568; -.
DR   KEGG; pho:PH1245; -.
DR   eggNOG; arCOG01452; Archaea.
DR   OMA; AYKLIKH; -.
DR   OrthoDB; 70037at2157; -.
DR   EvolutionaryTrace; O58938; -.
DR   Proteomes; UP000000752; 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   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; DNA-binding; Endonuclease; Hydrolase;
KW   Magnesium; Manganese; Metal-binding; Nuclease.
FT   CHAIN           1..322
FT                   /note="CRISPR-associated endonuclease Cas1"
FT                   /id="PRO_0000417109"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT   BINDING         214
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT   BINDING         229
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   STRAND          12..17
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   STRAND          20..27
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   STRAND          37..42
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           50..58
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   STRAND          62..66
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   STRAND          72..78
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           85..96
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           98..122
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           129..132
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           133..138
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           142..160
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           166..168
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           181..202
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           222..234
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           236..245
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           251..253
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           265..279
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   TURN            286..288
FT                   /evidence="ECO:0007829|PDB:4WJ0"
FT   HELIX           294..309
FT                   /evidence="ECO:0007829|PDB:4WJ0"
SQ   SEQUENCE   322 AA;  37755 MW;  F9FE7ED7D36D55B4 CRC64;
     MRKKPLTIFS DGTLTRRENT LYFESAKGRK PLAIEGIYDI YIYGHVNITS QALHYIAQKG
     ILIHFFNHYG YYDGTFYPRE TLLSGDLIIR QAEHYLNKEK RLFLAKSFVT GGTKNMERNL
     KNWGIKAKLS DYLDELNDAR KITEIMNVEA RIRQEYYAKW DENLPEEFKI VKRTRRPPKN
     EMNALISFLN SRLYATIITE IYNTQLAPTI SYLHEPSERR FSLSLDLSEI FKPIIADRVA
     NRLVKKGSLK KEHFREDLNG VLLTEEGMKI VTKAYNEELQ KSVKHPKIGS NVTRQRLIRL
     EAYKLIKHLV GVEEYKPLVA WF
 
 
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