ID   CS3HE_METJA             Reviewed;         614 AA.
AC   Q57828;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=CRISPR-associated helicase Cas3;
DE            EC=3.6.4.-;
GN   Name=cas3; Synonyms=cas3'; OrderedLocusNames=MJ0383;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   PROBABLE FUNCTION, AND ATP-DEPENDENCE.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=22009198; DOI=10.1038/emboj.2011.377;
RA   Beloglazova N., Petit P., Flick R., Brown G., Savchenko A., Yakunin A.F.;
RT   "Structure and activity of the Cas3 HD nuclease MJ0384, an effector enzyme
RT   of the CRISPR interference.";
RL   EMBO J. 30:4616-4627(2011).
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.
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; L77117; AAB98371.1; -; Genomic_DNA.
DR   PIR; G64347; G64347.
DR   RefSeq; WP_010869882.1; NC_000909.1.
DR   AlphaFoldDB; Q57828; -.
DR   SMR; Q57828; -.
DR   STRING; 243232.MJ_0383; -.
DR   EnsemblBacteria; AAB98371; AAB98371; MJ_0383.
DR   GeneID; 1451240; -.
DR   KEGG; mja:MJ_0383; -.
DR   eggNOG; arCOG01444; Archaea.
DR   HOGENOM; CLU_502152_0_0_2; -.
DR   OMA; IQRIGRC; -.
DR   OrthoDB; 18962at2157; -.
DR   PhylomeDB; Q57828; -.
DR   Proteomes; UP000000805; 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:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
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   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   3: Inferred from homology;
KW   Antiviral defense; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..614
FT                   /note="CRISPR-associated helicase Cas3"
FT                   /id="PRO_0000106846"
FT   DOMAIN          27..219
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          244..386
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   614 AA;  71568 MW;  016CF1A6F4EDEF1A CRC64;
     MDIINFFKQI TDHEPYDYQI RAWEKINKIM ELGGRVVIEI PTAGGKTEAA IIPYLYQFIS
     NDWKVPRLIY VLPTRSLVEK QVERIRNYIK KILEIKGYSK DKVEELAKKI VQVEYGLEET
     HAFLGFVVLT TWDTFLYGLA AHRTVGDRFT FPCGAIAQSL VVFDEIQMYQ DESLYMPRLI
     GLVVKRLVEA NVPLVFMTAT LPTELKKILG IHDEEPITVN PEDTKKPERG EVVVEFKEKL
     SDEELSNEIK KAINEGKKVL IIKNTVNSAI EVYEKVKQLG NSLLLHSRFT VEDRAEKEKD
     IDKAEIIVAT QVVEAGLDLT NVGLVITDLA PLDALIQRIG RCARRKGERG KVIVVLPNFN
     EKINEDHREK VILGFKNIPF ENAYVTLVNN KDYGRVIELT IETIEEKKGK SKIVPKKFYI
     GDLGNKTIRK LIENNKILKK KDLYFIPYST QPYDPLIMIK SFDEVESVSE YLYDIIKARE
     ALDRVYKEYY ENNIVPKDYY SAYIYFRELK LFSTPPEYEL KARPEMFAIL YPLENAEEKV
     KNKEIIEFNP KYVIRVSYNW LKNKWEKFDK KFELIKEYDE KGWICSLKKA GKLQPYKIYI
     IDDKYYSKET GIII