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Database: UniProt
Entry: A0A0F2SDU8_9FIRM
LinkDB: A0A0F2SDU8_9FIRM
Original site: A0A0F2SDU8_9FIRM 
ID   A0A0F2SDU8_9FIRM        Unreviewed;       815 AA.
AC   A0A0F2SDU8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=CRISPR-associated protein {ECO:0000313|EMBL:KJS49058.1};
GN   ORFNames=VR66_10625 {ECO:0000313|EMBL:KJS49058.1};
OS   Peptococcaceae bacterium BRH_c23.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS49058.1, ECO:0000313|Proteomes:UP000033503};
RN   [1] {ECO:0000313|EMBL:KJS49058.1, ECO:0000313|Proteomes:UP000033503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS49058.1};
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 (MAR-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:KJS49058.1}.
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DR   EMBL; LADV01000124; KJS49058.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2SDU8; -.
DR   PATRIC; fig|1629714.3.peg.1752; -.
DR   Proteomes; UP000033503; 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; 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.
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          15..208
FT                   /note="HD Cas3-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51643"
FT   DOMAIN          279..457
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   815 AA;  91691 MW;  03454C628A5932FC CRC64;
     MHTNSKRFIA HIRAADKHEQ YVDEHNDHVA DLAAAVAQDY GLANIAKLAG RHHDDGKNTP
     EFAAYIRAAA EGKKVVRGSV IHSTHGAMLV NELASSKLSS RLTAEMVRMA IMSHHGLRDC
     LSLDGDAVFA EAAEKVADSY ESVKKVVYRH YGENSINQEF IEACCDTRSI VASIQALQRK
     SKSLGSLQFY LAMFARLLTS LVIDADRTDT ACFEEKRALP RPKAPDERWA MWETYLAHYE
     KELEELPKGK KPSSLDPYRG EISRACAEFD GGEAGIFRLV VPCGAGKTLA ALRYALHTAR
     HYRKERIFYI APFNSILEQN AAEISRFIGD PAAVLEHHSN IMFNDDESKD KKEEEKRYQL
     LTENWAQSPV VATTAVQFLN TLFGGKTSNL RRMQALGNSV IILDEIQALP IKVLKLFNGA
     MNFLASFCKT SVVLCSATQP LLDKVDNYRI LPPKSIIADE EKYSEAFRRV QIVDCMTERG
     YSREEAADFI AGQLDEARSV LAIVNTKRGA REIFKQIRNR LGDETPYRIF HLSTNMCPAH
     RSRVLRQLRA GLEDKESGEK IICISTSLIE AGVDVSFERV VRSLSGLDNI VQAAGRCNRN
     YETACGIVSI INLRDEQTGR LGYLKEARQA TQELLYSIKT SPGRYPGGAL SKAAMKEYYA
     RYFYSLFAEM AYPLKFDPEH NLLHLLTNNP SGQRGFAEKY PQERLPELKQ AFREAGEAFS
     VIEDDGKVDV FIDYDHEAGN RLQKLKAATT LQEKRSALRQ LQPYTVQLRE NDWIQRQRLA
     LTPEDAGILV LPPGYYDGEY GVDETLDIKM ETLII
//
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