CAS1_AQUAE
ID CAS1_AQUAE Reviewed; 316 AA.
AC O66692;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=aq_369;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-316.
RA Ebihara A., Yokoyama S., Kuramitsu S.;
RT "Crystal structure of uncharacterized conserved protein from Aquifex
RT aeolicus.";
RL Submitted (MAY-2007) 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; AE000657; AAC06657.1; -; Genomic_DNA.
DR PIR; H70332; H70332.
DR RefSeq; NP_213252.1; NC_000918.1.
DR RefSeq; WP_010880190.1; NC_000918.1.
DR PDB; 2YZS; X-ray; 2.00 A; A/B=2-316.
DR PDBsum; 2YZS; -.
DR AlphaFoldDB; O66692; -.
DR SMR; O66692; -.
DR STRING; 224324.aq_369; -.
DR EnsemblBacteria; AAC06657; AAC06657; aq_369.
DR KEGG; aae:aq_369; -.
DR PATRIC; fig|224324.8.peg.298; -.
DR eggNOG; COG1518; Bacteria.
DR HOGENOM; CLU_052779_2_0_0; -.
DR InParanoid; O66692; -.
DR OMA; NTIMFET; -.
DR OrthoDB; 1581397at2; -.
DR EvolutionaryTrace; O66692; -.
DR Proteomes; UP000000798; 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; Reference proteome.
FT CHAIN 1..316
FT /note="CRISPR-associated endonuclease Cas1"
FT /id="PRO_0000417072"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 206
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 221
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 97..119
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 136..158
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 173..194
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 257..272
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:2YZS"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 286..301
FT /evidence="ECO:0007829|PDB:2YZS"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:2YZS"
SQ SEQUENCE 316 AA; 36887 MW; DE65231D147C463F CRC64;
MGRVYYINSH GTLSRHENTL RFENAEVKKD IPVEDVEEIF VFAELSLNTK LLNFLASKGI
PLHFFNYYGY YTGTFYPRES SVSGHLLIKQ VEHYLDAQKR LYLAKSFVIG SILNLEYVYK
ISADTYLNKV KETNSIPELM SVEAEFRKLC YKKLEEVTGW ELEKRTKRPP QNPLNALISF
GNSLTYAKVL GEIYKTQLNP TVSYLHEPST KRFSLSLDVA EVFKPIFVDN LIIRLIQENK
IDKTHFSTEL NMTFLNEIGR KVFLKAFNEL LETTIFYPKL NRKVSHRTLI KLELYKLIKH
LLEEEVYLPL NYGGLK
