CAS3_METJA
ID CAS3_METJA Reviewed; 728 AA.
AC Q57821;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Putative CRISPR-associated nuclease/helicase Cas3;
DE EC=3.1.-.-;
DE EC=3.6.4.-;
GN Name=cas3; OrderedLocusNames=MJ0376;
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).
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 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated
CC nuclease Cas3-HD family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the CRISPR-associated
CC helicase Cas3 family. {ECO:0000305}.
CC -!- CAUTION: This protein is about 60 residues too short at the N-terminus
CC compared to its close orthologs. {ECO:0000305}.
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DR EMBL; L77117; AAB98365.1; -; Genomic_DNA.
DR PIR; H64346; H64346.
DR RefSeq; WP_010869875.1; NC_000909.1.
DR AlphaFoldDB; Q57821; -.
DR SMR; Q57821; -.
DR STRING; 243232.MJ_0376; -.
DR PRIDE; Q57821; -.
DR EnsemblBacteria; AAB98365; AAB98365; MJ_0376.
DR GeneID; 1451233; -.
DR KEGG; mja:MJ_0376; -.
DR eggNOG; arCOG01445; Archaea.
DR HOGENOM; CLU_009347_1_1_2; -.
DR InParanoid; Q57821; -.
DR OMA; WLNIVYD; -.
DR OrthoDB; 1317at2157; -.
DR PhylomeDB; Q57821; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease 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; 1.10.3210.30; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR035011; Cas3.
DR InterPro; IPR006483; CRISPR-assoc_Cas3_HD.
DR InterPro; IPR038257; CRISPR-assoc_Cas3_HD_sf.
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; PTHR47959:SF5; PTHR47959:SF5; 1.
DR Pfam; PF00270; DEAD; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01587; cas3_core; 1.
DR PROSITE; PS51643; HD_CAS3; 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; Magnesium;
KW Metal-binding; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..728
FT /note="Putative CRISPR-associated nuclease/helicase Cas3"
FT /id="PRO_0000106839"
FT DOMAIN 1..163
FT /note="HD Cas3-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00974"
FT DOMAIN 213..404
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 434..592
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 352..355
FT /note="DEAH box"
FT BINDING 3
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 728 AA; 86467 MW; 8BC3DBCA30226B40 CRC64;
MHDIGKITEG FQNNIKKGKR SNKHPHPLYA LPIIKNIEFD YLFDIPIEVF AILSHHTQLY
NNLYADYQQY KKGTFLIEEI KEFIKNSKEA YESLGFSKFF EFEDLKIEDI PKDAKPLELH
RLRRKYWIEA NNYIKSLSFD DKIKIKSIFS FMFSILQLCD DFASLNFSEY AKDREGIFDD
VLENPEIYVP TLNIDNPISF ILKDYEPYKF QKELYNSKNK FVMLFAPCGR GKTEGALLWA
LNALKNFKRN KIILAMPTQV TSNAMYDRLV KIFGEENVGL FHGKSFIKLR DSKEIEDEDD
LEEIRDENFK GNVFFKPITI TTIDHVIYSF VHGFSQADFA LGNIQNSVII FDEVHYYEKY
TLEHLLTLFD ILRRMDIPHL LMSGTLPNFL MNNLEGYELV VDEEGLNYKP FKLKCSENHL
IWKEDDEWKV NENIINEIIE NYKKGLSQAI ILNTVERARE FYKAVRDKVP AILYHSQFAY
KDRVKKEDEI FTLEEMRKSQ NKPYVIVATQ VIEISLDMSV DVMYSELSPP DALGQRAGRL
HRKGKDWREN GKEYKLKIFL PYKHLPYSKE LIEKTINHIK FYEKPLDYRD IKDFVDNVYK
DYNLSIPSDL KLFFDEAILF GRHWTDISTI DEEGRFFKVR DDKFMKIEVV PQVYFDELGE
NSLRAEYMAK IPAYLILNEM KNEEGLIHFY PYEKRVGRKT RRYLICSFKY TYEIGFDYKE
EEEFEDIL
