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Database: UniProt
Entry: A0A101WHZ9_9FIRM
LinkDB: A0A101WHZ9_9FIRM
Original site: A0A101WHZ9_9FIRM 
ID   A0A101WHZ9_9FIRM        Unreviewed;       804 AA.
AC   A0A101WHZ9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=CRISPR-associated protein Cas3 {ECO:0000313|EMBL:KUO72928.1};
GN   ORFNames=APF81_10695 {ECO:0000313|EMBL:KUO72928.1};
OS   Desulfosporosinus sp. BRH_c37.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO72928.1, ECO:0000313|Proteomes:UP000053148};
RN   [1] {ECO:0000313|EMBL:KUO72928.1, ECO:0000313|Proteomes:UP000053148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO72928.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUO72928.1}.
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DR   EMBL; LOEW01000228; KUO72928.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101WHZ9; -.
DR   Proteomes; UP000053148; Unassembled WGS sequence.
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   CDD; cd17930; DEXHc_cas3; 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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR006474; Helicase_Cas3_CRISPR-ass_core.
DR   InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01587; cas3_core; 1.
DR   NCBIfam; TIGR01596; cas3_HD; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 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.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS50177; NTF2_DOMAIN; 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}.
FT   DOMAIN          9..206
FT                   /note="HD Cas3-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51643"
FT   DOMAIN          260..446
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          639..787
FT                   /note="NTF2"
FT                   /evidence="ECO:0000259|PROSITE:PS50177"
SQ   SEQUENCE   804 AA;  91531 MW;  97DF6612987C0D2F CRC64;
     MLCAHINPLT LMEQSVKKHL NNVCILSREY GSKISLGATG ELIGILHDLG KGTRKFDSYI
     RYCSKHPNDK SLKGSINHST AGAKYIYDAF YNSTDQYQKF TAQIISLAIC SHHGGLIDCL
     DLGGMDKFTD RMNPDKDILY DEALNYFNEK CLELSQIKDL FNKATEEIKS MFIKINKIDG
     SGKFGRFAAG VLEKYLFSCV IDADRYDTYI FMEGKERKPN IDKSALWNEL SDVLETKLES
     YPKETKIELL RDEVSLACKN FAENSPGIYQ LSVPTGGGKT LSSLRYALEH AKKFDKDRIF
     YIIPFTTIID QNAKEIKDIL GHEDMILEHH SNLILDYSQD NDEELEDYKL LTERWDSPII
     LTTMVQFLNT LFSGGTQDAR RIHNLANSVI IFDEIQAIPI KCINIFNSAI NFLAYICNAT
     VILCTATQPL LEKTEMPLKL SERPNIISDI HEKFKQFKRV NLVPKILVGG YSAISLKDFV
     LDKMDQVKSV LVILNTKNSA KEVFNELRVA NKELPKEKQY TIFHLSTSMC PSHRMSVLQK
     MREKLGQERV ICISTQLIEA GVNISFGCVV RSLAGLDNIA QAAGRCNRHG EKECSDVYIV
     NVEGENVSKL VDIKIAQECT SRVLRDFEEN RNLFDNDLLS QKTMERYYKY YFHERRNQMN
     YTMSKPNSDR SLYDILSGNN EAANEFNSRN GYQSKLMLKQ AFKTAGNEFQ AIDENTTGII
     VPYKEGKELI TLINGACSLS ELKQYLKRAQ QFSVNLFETD KRKLEYMGGF IGLKNNSILV
     LKDEFYNDDV GVTFDKAPMG FCNA
//
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