CAS1_THEMA
ID CAS1_THEMA Reviewed; 319 AA.
AC Q9X2B7; G4FGI5;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=CRISPR-associated endonuclease Cas1;
DE EC=3.1.-.-;
GN Name=cas1; OrderedLocusNames=TM_1797;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), AND SUBUNIT.
RA Beloglazova N., Skarina T., Petit P., Flick R., Brown G., Savchenko A.,
RA Yakunin A.F.;
RT "Crystal structure and nuclease activity of TM1797, a Cas1 protein from
RT Thermotoga maritima.";
RL Submitted (JAN-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 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 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer (Probable). Forms a heterotetramer with a Cas2
CC homodimer (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD36860.1; -; Genomic_DNA.
DR PIR; B72210; B72210.
DR RefSeq; NP_229594.1; NC_000853.1.
DR RefSeq; WP_004082344.1; NZ_CP011107.1.
DR PDB; 4XTK; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-319.
DR PDBsum; 4XTK; -.
DR AlphaFoldDB; Q9X2B7; -.
DR SMR; Q9X2B7; -.
DR STRING; 243274.THEMA_05205; -.
DR EnsemblBacteria; AAD36860; AAD36860; TM_1797.
DR KEGG; tma:TM1797; -.
DR eggNOG; COG1518; Bacteria.
DR InParanoid; Q9X2B7; -.
DR OMA; AYKLIKH; -.
DR OrthoDB; 1581397at2; -.
DR EvolutionaryTrace; Q9X2B7; -.
DR Proteomes; UP000008183; 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..319
FT /note="CRISPR-associated endonuclease Cas1"
FT /id="PRO_0000417089"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4XTK"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:4XTK"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:4XTK"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4XTK"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:4XTK"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:4XTK"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4XTK"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 96..120
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 141..160
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 181..201
FT /evidence="ECO:0007829|PDB:4XTK"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:4XTK"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 265..279
FT /evidence="ECO:0007829|PDB:4XTK"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:4XTK"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:4XTK"
SQ SEQUENCE 319 AA; 37705 MW; 8507C7996A0B4CA7 CRC64;
MESVYLFSSG TLKRKANTIC LETESGRKYI PVENVMDIKV FGEVDLNKRF LEFLSQKRIP
IHFFNREGYY VGTFYPREYL NSGFLILKQA EHYINQEKRM LIAREIVSRS FQNMVDFLKK
RKVRADSLTR YKKKAEEASN VSELMGIEGN AREEYYSMID SLVSDERFRI EKRTRRPPKN
FANTLISFGN SLLYTTVLSL IYQTHLDPRI GYLHETNFRR FSLNLDIAEL FKPAVVDRLF
LNLVNTRQIN EKHFDEISEG LMLNDEGKSL FVKNYEQALR ETVFHKKLNR YVSMRSLIKM
ELHKLEKHLI GEQVFGSEE
