CS3HE_THETK
ID CS3HE_THETK Reviewed; 566 AA.
AC G4RJZ3;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=CRISPR-associated helicase Cas3;
DE EC=3.6.4.-;
GN Name=cas3; Synonyms=cas3'; OrderedLocusNames=TTX_1253;
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
RN [2]
RP SUBUNIT, INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX PubMed=22408157; DOI=10.1128/jb.00206-12;
RA Plagens A., Tjaden B., Hagemann A., Randau L., Hensel R.;
RT "Characterization of the CRISPR/Cas subtype I-A system of the
RT hyperthermophilic crenarchaeon Thermoproteus tenax.";
RL J. Bacteriol. 194:2491-2500(2012).
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). Cas3
CC plus Cascade participate in CRISPR interference, the third stage of
CC CRISPR immunity. Probably unwinds dsDNA templates, thus providing
CC substrates for CRISPR-associated endonuclease Cas3-HD. Unwinding is
CC strongly increased in the presence of ATP, implying the helicase uses
CC ATP to unwind substrate (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Can form a Cascade complex with Csa5, Cas7, Cas5a, Cas3' and
CC Cas8a2. {ECO:0000269|PubMed:22408157}.
CC -!- INDUCTION: Repressed by 5 J/m2 ultraviolet light and 50 mM NaCl,
CC slightly induced by 20 J/m2 ultraviolet light, 100 and 150 mM Nacl.
CC Member of the csa5-cas7-cas5a-cas3-cas3'-cas8a2 operon.
CC {ECO:0000269|PubMed:22408157}.
CC -!- DOMAIN: Proteins of this family have an N-terminal nuclease domain and
CC a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the
CC domains are swapped, in others they are encoded separately.
CC -!- SIMILARITY: Belongs to the CRISPR-associated helicase Cas3 family.
CC {ECO:0000305}.
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DR EMBL; FN869859; CCC81888.1; -; Genomic_DNA.
DR RefSeq; WP_014127143.1; NC_016070.1.
DR AlphaFoldDB; G4RJZ3; -.
DR SMR; G4RJZ3; -.
DR STRING; 768679.TTX_1253; -.
DR EnsemblBacteria; CCC81888; CCC81888; TTX_1253.
DR GeneID; 11262133; -.
DR KEGG; ttn:TTX_1253; -.
DR PATRIC; fig|768679.9.peg.1266; -.
DR eggNOG; arCOG01444; Archaea.
DR HOGENOM; CLU_491460_0_0_2; -.
DR OMA; MLIHGRM; -.
DR OrthoDB; 18962at2157; -.
DR Proteomes; UP000002654; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR035011; Cas3.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR006474; Helicase_Cas3_CRISPR-ass_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24031:SF539; PTHR24031:SF539; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01587; cas3_core; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..566
FT /note="CRISPR-associated helicase Cas3"
FT /id="PRO_0000422229"
FT DOMAIN 41..234
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 250..400
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 179..182
FT /note="DEAH box"
FT BINDING 54..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 566 AA; 63347 MW; 01EA94B46AEE805F CRC64;
MVGRRLDTLV RELSLAWCRS KGEPSCAVRE DLLAEQAKAA EVIERSDGVI LLKAPTGFGK
TEIWTAPFFA QWLRGEWFAP RMYVVEPMHA LLRQMKRRME VYAQAVQGLG LPRLNVAEDH
GEVAKPLFLY GGHIVLTTVD SLAYGYLARR VQRWREEGVE RGRYSMPAGL LASAYIVLDE
AHLIQDEAYL GPRVLGKIVC DLASAGAKVV ISTATVPETF LKHIPCLGGR LTLGSGTVRR
NVKVERRKGV LKAEEIECGK PTIVIVNTIE RARRIYKQVR CGKKAVVHSL MRREDKERQL
SKVLADGKVA EDAVLIGTQA LEVGLDFSNL RALYTETAPV DALIQRIGRV GRDGDKAEAY
IYEAEGDAPY PQTLMRATRE ALEKELLGGA ALTSWEDAQR AVDKVYNEKA VEELMTRGLA
WYGQALGYLQ ELSLFSYPPR GEVRIRPSNY ITLVIADVKQ DGDKGRYITE DDVERGAMKM
SYTSRDDPRI NALLQKVSTA YTVRGVATAK DETRYYLSEL RRSWDGVEVV VVDRRDVEEL
YDEAGLDVAQ LSGGGQKRKG RGRRRR
