CAS1B_THET8
ID CAS1B_THET8 Reviewed; 325 AA.
AC Q53WG8;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
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}; OrderedLocusNames=TTHB193;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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; AP008227; BAD71989.1; -; Genomic_DNA.
DR RefSeq; WP_011229111.1; NC_006462.1.
DR RefSeq; YP_145432.1; NC_006462.1.
DR PDB; 6KDV; X-ray; 3.11 A; A/B/C/D=1-325.
DR PDB; 6KE1; X-ray; 3.39 A; A/B=1-325.
DR PDBsum; 6KDV; -.
DR PDBsum; 6KE1; -.
DR AlphaFoldDB; Q53WG8; -.
DR SMR; Q53WG8; -.
DR EnsemblBacteria; BAD71989; BAD71989; BAD71989.
DR GeneID; 3169280; -.
DR KEGG; ttj:TTHB193; -.
DR PATRIC; fig|300852.9.peg.2144; -.
DR HOGENOM; CLU_077904_0_0_0; -.
DR OMA; IWVGEAG; -.
DR PhylomeDB; Q53WG8; -.
DR Proteomes; UP000000532; Plasmid pTT27.
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; cd09719; Cas1_I-E; 1.
DR Gene3D; 1.20.120.920; -; 1.
DR Gene3D; 3.100.10.20; -; 1.
DR HAMAP; MF_01470; Cas1; 1.
DR InterPro; IPR033641; Cas1_I-E.
DR InterPro; IPR002729; CRISPR-assoc_Cas1.
DR InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR InterPro; IPR019851; CRISPR-assoc_Cas1_ECOLI.
DR InterPro; IPR042211; CRISPR-assoc_Cas1_N.
DR Pfam; PF01867; Cas_Cas1; 1.
DR TIGRFAMs; TIGR00287; cas1; 1.
DR TIGRFAMs; TIGR03638; cas1_ECOLI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; DNA-binding; Endonuclease; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nuclease; Plasmid; Reference proteome.
FT CHAIN 1..325
FT /note="CRISPR-associated endonuclease Cas1 2"
FT /id="PRO_0000417091"
FT REGION 283..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 212
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:6KDV"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6KDV"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:6KDV"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:6KDV"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6KDV"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:6KDV"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6KDV"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:6KDV"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6KDV"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6KE1"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:6KDV"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:6KDV"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:6KDV"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:6KDV"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6KDV"
FT HELIX 141..160
FT /evidence="ECO:0007829|PDB:6KDV"
FT HELIX 179..201
FT /evidence="ECO:0007829|PDB:6KDV"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6KDV"
FT HELIX 218..242
FT /evidence="ECO:0007829|PDB:6KDV"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6KDV"
FT HELIX 247..262
FT /evidence="ECO:0007829|PDB:6KDV"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:6KDV"
SQ SEQUENCE 325 AA; 35724 MW; 3DC2C79B20B9F519 CRC64;
MPPVSSARNL KELPKFRDGL SYLYVEHAVV EREAGGIGIY DQEGLTLAPV AGLGVLFLGP
GTRITHAAVR LLAENGCTVA WVGEGMARFY AQGLGDTRSA ARFYRQARAW ADPALHLEVV
MRLYRMRFSE PLPEGLTLEQ VRGLEGVRVR NAYARWSRET GVPWYGRSYD RGNWRAADPV
NRALSAGASY LYGLAHAAIV SLGFSPALGF IHTGKLLSFV YDIADLYKAD YLVPAAFRTV
AESEEAVERR VRRALREAIQ EGRLLERMAE DLLNLFRGLG LPEEEDPVEE DPTRPGGLWD
LEGEVEGGVA YGGDDPGEGA EEPEG
