CAS1A_ARCFU
ID CAS1A_ARCFU Reviewed; 345 AA.
AC O28401;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
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}; OrderedLocusNames=AF_1878;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), FUNCTION AS A NUCLEASE, COFACTOR,
RP SUBUNIT, AND MUTAGENESIS OF GLU-168; HIS-239 AND GLU-254.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=24211577; DOI=10.1016/j.bbrc.2013.10.122;
RA Kim T.Y., Shin M., Huynh Thi Yen L., Kim J.S.;
RT "Crystal structure of Cas1 from Archaeoglobus fulgidus and characterization
RT of its nucleolytic activity.";
RL Biochem. Biophys. Res. Commun. 441:720-725(2013).
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 sequences complementary to
CC antecedent mobile elements and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA).
CC Involved in the integration of spacer DNA into the CRISPR cassette (By
CC similarity). Acts as a dsDNA and ssRNA nuclease, binds to linear and
CC circular dsDNA and linear ssRNA and ssDNA. {ECO:0000250,
CC ECO:0000269|PubMed:24211577}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:24211577};
CC -!- SUBUNIT: Forms a heterotetramer with a Cas2 homodimer (By similarity).
CC Homodimer. {ECO:0000250, ECO:0000269|PubMed:24211577}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01470}.
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DR EMBL; AE000782; AAB89374.1; -; Genomic_DNA.
DR PIR; E69484; E69484.
DR RefSeq; WP_010879371.1; NC_000917.1.
DR PDB; 4N06; X-ray; 2.40 A; A/B=1-345.
DR PDBsum; 4N06; -.
DR AlphaFoldDB; O28401; -.
DR SMR; O28401; -.
DR STRING; 224325.AF_1878; -.
DR DNASU; 1485099; -.
DR EnsemblBacteria; AAB89374; AAB89374; AF_1878.
DR GeneID; 24795623; -.
DR KEGG; afu:AF_1878; -.
DR eggNOG; arCOG01452; Archaea.
DR HOGENOM; CLU_052779_0_0_2; -.
DR OMA; YYVGSFY; -.
DR OrthoDB; 70037at2157; -.
DR PhylomeDB; O28401; -.
DR Proteomes; UP000002199; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; DNA-binding; Endonuclease; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nuclease; Reference proteome;
KW RNA-binding.
FT CHAIN 1..345
FT /note="CRISPR-associated endonuclease Cas1 1"
FT /id="PRO_0000417093"
FT BINDING 168
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305"
FT BINDING 239
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305"
FT BINDING 254
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305"
FT MUTAGEN 168
FT /note="E->A: Binds but no longer cleaves ssRNA."
FT /evidence="ECO:0000269|PubMed:24211577"
FT MUTAGEN 239
FT /note="H->A: Binds but no longer cleaves ssRNA."
FT /evidence="ECO:0000269|PubMed:24211577"
FT MUTAGEN 254
FT /note="E->A: Binds but no longer cleaves ssRNA."
FT /evidence="ECO:0000269|PubMed:24211577"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 96..123
FT /evidence="ECO:0007829|PDB:4N06"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 129..150
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 157..182
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 206..228
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:4N06"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 257..270
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4N06"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:4N06"
FT HELIX 317..332
FT /evidence="ECO:0007829|PDB:4N06"
SQ SEQUENCE 345 AA; 39046 MW; 2BCE7D693786D106 CRC64;
MRLVVDGFGK YLGIENGLIV VKEKGKALRK VRPEDLKQVL IIGKAAISSD AIKLLLKNRV
DVVFLDFNGE ILGRLSHPLI GTAKTRREQY LAYGDKRGVH LAKEFIKAKM ANQMAILTNL
AKARKDSNPE VAESLLKAKK EIDACLNELD GVEAEMIDKV RERLLGIEGK ASKHYWDAIS
LVIPEEYRFN GRRGIEIGSP RYAKDIVNAM LNYGYSILLA ECVKAVELAG LDPYAGFLHV
DVSGRSSLAI DLMENFRQQV VDRVVLRLIS YRQIKPEDCE KRNMVCQLSD NARRLLLASL
LERLDSKTQY RGRNLAYSSI ILLHARDVVA FLRGERRYEG FVQKW
