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Database: UniProt
Entry: Q53VY2
LinkDB: Q53VY2
Original site: Q53VY2 
ID   CAS3_THET8              Reviewed;         920 AA.
AC   Q53VY2;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   16-OCT-2019, entry version 85.
DE   RecName: Full=CRISPR-associated endonuclease/helicase Cas3;
DE            EC=3.1.-.-;
DE            EC=3.6.4.-;
DE   AltName: Full=CRISPR-associated ssDNA endonuclease/helicase Cas3;
GN   Name=cas3; OrderedLocusNames=TTHB187;
OS   Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579).
OG   Plasmid pTT27.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HB8 / ATCC 27634 / DSM 579;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y.,
RA   Shibata T., 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.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 6-260 IN PRESENCE AND
RP   ABSENCE OF NI(2+), FUNCTION AS A SSDNA ENDONUCLEASE, ACTIVITY
RP   REGULATION, COFACTOR, AND MUTAGENESIS OF HIS-24; HIS-69; ASP-70;
RP   LYS-73; HIS-105; HIS-137; HIS-138 AND ASP-205.
RC   STRAIN=HB8 / ATCC 27634 / DSM 579;
RX   PubMed=21775431; DOI=10.1074/jbc.m111.270017;
RA   Mulepati S., Bailey S.;
RT   "Structural and biochemical analysis of nuclease domain of clustered
RT   regularly interspaced short palindromic repeat (CRISPR)-associated
RT   protein 3 (Cas3).";
RL   J. Biol. Chem. 286:31896-31903(2011).
CC   -!- FUNCTION: CRISPR (clustered regularly interspaced short
CC       palindromic repeat), is an adaptive immune system that provides
CC       protection against mobile genetic elements (viruses, transposable
CC       elements and conjugative plasmids). CRISPR clusters contain
CC       sequences complementary to antecedent mobile elements and target
CC       invading nucleic acids. CRISPR clusters are transcribed and
CC       processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate
CC       in CRISPR interference, the third stage of CRISPR immunity. The N-
CC       terminal domain (residues 6-260) acts as a ssDNA endonuclease, has
CC       no activity on dsDNA. {ECO:0000269|PubMed:21775431}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:21775431};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:21775431};
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000269|PubMed:21775431};
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000269|PubMed:21775431};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:21775431};
CC       Note=The ssDNA endonuclease activity (residues 6-260) is
CC       stimulated by Mn(2+), Co(2+), Ni(2+), Cu(2+) and Zn(2+), but not
CC       by Mg(2+) or Ca(2+). A Ni(2+) ion is seen in crystals upon
CC       soaking. {ECO:0000269|PubMed:21775431};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA, Mg(2+) and Ca(2+).
CC       {ECO:0000269|PubMed:21775431}.
CC   -!- DOMAIN: Proteins of this family have an N-terminal nuclease domain
CC       and a C-terminal helicase/ATPase domain. In some CRISPR/Cas
CC       systems the domains are swapped, in others they are encoded
CC       separately.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-
CC       associated nuclease Cas3-HD family. {ECO:0000305}.
CC   -!- SIMILARITY: In the central section; belongs to the CRISPR-
CC       associated helicase Cas3 family. {ECO:0000305}.
DR   EMBL; AP008227; BAD71983.1; -; Genomic_DNA.
DR   RefSeq; WP_011229117.1; NC_006462.1.
DR   RefSeq; YP_145426.1; NC_006462.1.
DR   PDB; 3SK9; X-ray; 1.80 A; A=6-260.
DR   PDB; 3SKD; X-ray; 2.00 A; A=6-260.
DR   PDBsum; 3SK9; -.
DR   PDBsum; 3SKD; -.
DR   SMR; Q53VY2; -.
DR   PRIDE; Q53VY2; -.
DR   EnsemblBacteria; BAD71983; BAD71983; BAD71983.
DR   GeneID; 3167883; -.
DR   KEGG; ttj:TTHB187; -.
DR   PATRIC; fig|300852.9.peg.2138; -.
DR   HOGENOM; HOG000015796; -.
DR   KO; K07012; -.
DR   OMA; CVCWIRN; -.
DR   PhylomeDB; Q53VY2; -.
DR   BioCyc; TTHE300852:G1GKC-2167-MONOMER; -.
DR   EvolutionaryTrace; Q53VY2; -.
DR   Proteomes; UP000000532; Plasmid pTT27.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3210.30; -; 1.
DR   InterPro; IPR035011; Cas3.
DR   InterPro; IPR041372; Cas3_C.
DR   InterPro; IPR006483; CRISPR-assoc_Cas3_HD.
DR   InterPro; IPR038257; CRISPR-assoc_Cas3_HD_sf.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR006474; Helicase_Cas3_CRISPR-ass_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24031:SF596; PTHR24031:SF596; 2.
DR   Pfam; PF18395; Cas3_C; 1.
DR   Pfam; PF18019; HD_6; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01587; cas3_core; 1.
DR   TIGRFAMs; TIGR01596; cas3_HD; 1.
DR   PROSITE; PS51643; HD_CAS3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; ATP-binding; Complete proteome;
KW   Endonuclease; Helicase; Hydrolase; Metal-binding; Nuclease;
KW   Nucleotide-binding; Plasmid; Reference proteome.
FT   CHAIN         1    920       CRISPR-associated endonuclease/helicase
FT                                Cas3.
FT                                /FTId=PRO_0000417609.
FT   DOMAIN       14    207       HD Cas3-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00974}.
FT   DOMAIN      274    480       Helicase ATP-binding.
FT   NP_BIND     287    294       ATP. {ECO:0000250}.
FT   MOTIF       428    431       DEAH box.
FT   METAL        24     24       Divalent metal cation.
FT   METAL        69     69       Divalent metal cation.
FT   METAL        70     70       Divalent metal cation.
FT   METAL       205    205       Divalent metal cation.
FT   MUTAGEN      24     24       H->A: Loss of endonuclease activity.
FT                                {ECO:0000269|PubMed:21775431}.
FT   MUTAGEN      69     69       H->A: Loss of endonuclease activity.
FT                                {ECO:0000269|PubMed:21775431}.
FT   MUTAGEN      70     70       D->A: Loss of endonuclease activity.
FT                                {ECO:0000269|PubMed:21775431}.
FT   MUTAGEN      73     73       K->A: Loss of endonuclease activity.
FT                                {ECO:0000269|PubMed:21775431}.
FT   MUTAGEN     105    105       H->A: Loss of endonuclease activity.
FT                                {ECO:0000269|PubMed:21775431}.
FT   MUTAGEN     137    137       H->A: Loss of endonuclease activity.
FT                                {ECO:0000269|PubMed:21775431}.
FT   MUTAGEN     138    138       H->A: Loss of endonuclease activity.
FT                                {ECO:0000269|PubMed:21775431}.
FT   MUTAGEN     205    205       D->A: Loss of endonuclease activity.
FT                                {ECO:0000269|PubMed:21775431}.
FT   HELIX         6     11       {ECO:0000244|PDB:3SK9}.
FT   STRAND       13     16       {ECO:0000244|PDB:3SK9}.
FT   HELIX        21     38       {ECO:0000244|PDB:3SK9}.
FT   HELIX        41     51       {ECO:0000244|PDB:3SK9}.
FT   HELIX        55     66       {ECO:0000244|PDB:3SK9}.
FT   TURN         67     70       {ECO:0000244|PDB:3SK9}.
FT   HELIX        71     73       {ECO:0000244|PDB:3SK9}.
FT   HELIX        76     78       {ECO:0000244|PDB:3SK9}.
FT   HELIX       105    119       {ECO:0000244|PDB:3SK9}.
FT   HELIX       124    133       {ECO:0000244|PDB:3SK9}.
FT   TURN        136    139       {ECO:0000244|PDB:3SK9}.
FT   HELIX       144    156       {ECO:0000244|PDB:3SK9}.
FT   HELIX       160    176       {ECO:0000244|PDB:3SK9}.
FT   HELIX       191    208       {ECO:0000244|PDB:3SK9}.
FT   TURN        211    213       {ECO:0000244|PDB:3SK9}.
FT   HELIX       225    241       {ECO:0000244|PDB:3SK9}.
FT   TURN        243    245       {ECO:0000244|PDB:3SK9}.
FT   STRAND      248    252       {ECO:0000244|PDB:3SK9}.
FT   STRAND      255    259       {ECO:0000244|PDB:3SK9}.
SQ   SEQUENCE   920 AA;  102127 MW;  D0A13064DD5B8191 CRC64;
     MSVEEAALAL WAKSGNPFHP LLAHMLDTAA VALAVLRMEP PRTRALYAED WGLPEEGALA
     WAAALVGLHD LGKASPVFQA GWEEGKERVQ RAGLPFGELL DWVAHGVFTE LFLRRLLKEK
     GLPERAANDL AAALGAHHGF PANAEEKSRA RRHLRTEDPL WKEARRWLLE EVFRRLGAPL
     PPSQGNGEAR PEAVLRVMAL ASFADWVASD PSLFPYGRDP RRGDYLKEAL RLAQEALNRL
     GWPAFAKAQR REFGELFPYI PKPNALQESV PALLEGACTP VLLLVEAPMG MGKTEAALYA
     HHLLQAGLGH RGLYVALPTQ ATANGLFPRV RGFLERLGEG SRLELQLQHG TALLNPHYAG
     LLERAAPRQV GEEEEGGAVA SAWFSARKRA MLAPYGVGTL DQALLGVLRV KHHFVRLWGL
     MNRVVVLDEV HAYDVYTSGL LQALLRWLRA LGSSAVVMTA TLPPSRRRAL LEAWAGEEVE
     GQDLGPYPRV VLVGEGVKAR SLPPAREVEV ALEVLREVDV EPLAQRLKGA LPGAVGAIVN
     TVDRAQDLYR ALGEGTPLTL EELARRLGGI SGGQAWEEVR QALPERGGEV VGKVLTDGTL
     VFLLHARFPA EERALRGSVV LALFGKGGPR PPRAILVATQ VAEQSLDLDF DLLYTDLAPI
     DLLFQRSGRL HRHERPRPEE HARPRLLLGV PEDLDFGKPL YWDKVYEDYV LLATWRALSG
     RDRLRVPGDL EALLEEIYEG ENPESFPEGL RERAKKSLKA LQERRDREAN TARRLSLSEL
     DRLLAYWDEG ALVAQERLED DEEKAETQRL LTRLGDPSVA VVPLFRVGEG LFLDREGRRR
     APLKGEVSRE EAEALFRRAV RLSRFPLPQE LLKEEPPPAW RKSGLLRGLR PLEVGRVFRS
     GERAFQVELD PELGVVYLPV
//
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