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Database: UniProt
Entry: K0NE71_DESTT
LinkDB: K0NE71_DESTT
Original site: K0NE71_DESTT 
ID   K0NE71_DESTT            Unreviewed;       719 AA.
AC   K0NE71;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=CRISPR-associated helicase, Cas3 family {ECO:0000313|EMBL:CCK79125.1};
GN   OrderedLocusNames=TOL2_C09600 {ECO:0000313|EMBL:CCK79125.1};
OS   Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacula.
OX   NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK79125.1, ECO:0000313|Proteomes:UP000007347};
RN   [1] {ECO:0000313|EMBL:CCK79125.1, ECO:0000313|Proteomes:UP000007347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX   PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA   Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA   Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT   "Complete genome, catabolic sub-proteomes and key-metabolites of
RT   Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT   sulfate-reducing bacterium.";
RL   Environ. Microbiol. 15:1334-55(2013).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated
CC       nuclease Cas3-HD family. {ECO:0000256|ARBA:ARBA00006847}.
CC   -!- SIMILARITY: In the central section; belongs to the CRISPR-associated
CC       helicase Cas3 family. {ECO:0000256|ARBA:ARBA00009046}.
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DR   EMBL; FO203503; CCK79125.1; -; Genomic_DNA.
DR   RefSeq; WP_014956475.1; NC_018645.1.
DR   AlphaFoldDB; K0NE71; -.
DR   STRING; 651182.TOL2_C09600; -.
DR   KEGG; dto:TOL2_C09600; -.
DR   PATRIC; fig|651182.5.peg.1152; -.
DR   HOGENOM; CLU_009347_1_1_7; -.
DR   OrthoDB; 9810236at2; -.
DR   Proteomes; UP000007347; 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:0046872; F:metal ion binding; 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   CDD; cd09641; Cas3''_I; 1.
DR   Gene3D; 1.10.3210.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR006674; HD_domain.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR006474; Helicase_Cas3_CRISPR-ass_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01587; cas3_core; 1.
DR   NCBIfam; TIGR01596; cas3_HD; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   PANTHER; PTHR47959:SF16; CRISPR-ASSOCIATED NUCLEASE_HELICASE CAS3-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51643; HD_CAS3; 1.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007347}.
FT   DOMAIN          11..192
FT                   /note="HD Cas3-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51643"
SQ   SEQUENCE   719 AA;  81685 MW;  2D5A55B3F994F46A CRC64;
     MDVCDHIKAK GAPEFTTLYA HLCQVKSAIK VFAGYLNFDV ETAKLGAVFH DIGKASPIFQ
     ERLVSKYKTG QSTFRHEIAS CFFLSLVEKT YHPQLIEMII AHHKSIENDK GLKGILDLEE
     NEDDIFEFHI EHWDVWKLDA LKILAGFGIN SRDIGYDEAK ENYFKVLEYC ENTIMNNGYS
     EWRGLLMSAD HFASALSSAA PDYLPHTFKK PILEFYNRTS QLYPLSLKKA SSNRPHTMVV
     ACTGAGKTDY LFRRCRGRVF YTLPFQASIN AMFKRVKTDL IKLNPNLDIR VLHSSSKISS
     GAESHEDMLL QRLVGSSVKV LTPYQLASII FATRGFESMI EDLKGCDVIL DEIHTYDNVS
     KSIVLKIVEV LNHIGCRIHI GTATMSSSLY NEIIDLLGRD FVSEISLDSI ELEKFDRHIL
     HKIGSWDDAH AVIKEAIKKN NKILLVCNRV DSAQEMFEIV KEAFSDIPLL LIHSRFKRGD
     RRDKEASLLG LDSQGNTTFE FNTSSNACIV VSTQVVEVSL DISFDLMITE TAPIDSLIQR
     FGRINRKRTP ATIGTYKPVY VIAPPEDEKA ARPYELEILR KSYAVLDHDQ VLHESDYQEK
     INCVYPDLSY TSIENHTAYK GNGRWNVPML THRDRSILLE LLEVDSVNCI VDSDCQAYEQ
     AGFEDQMMLE IPVRYYAVKN YFQLNFGSNP FVIPDSGYSR ETGLDLAKAN DRKADLNFL
//
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