ID F0RQW7_DEIPM Unreviewed; 963 AA.
AC F0RQW7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=CRISPR-associated helicase Cas3 {ECO:0000313|EMBL:ADY27676.1};
GN OrderedLocusNames=Deipr_2561 {ECO:0000313|EMBL:ADY27676.1};
OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC
OS 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP).
OG Plasmid pDEIPR03 {ECO:0000313|EMBL:ADY27676.1,
OG ECO:0000313|Proteomes:UP000007718}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY27676.1, ECO:0000313|Proteomes:UP000007718};
RN [1] {ECO:0000313|Proteomes:UP000007718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RC PLASMID=Plasmid pDEIPR03 {ECO:0000313|Proteomes:UP000007718};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete sequence of plasmid3 of Deinococcus proteolyticus DSM
RT 20540.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADY27676.1, ECO:0000313|Proteomes:UP000007718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RC PLASMID=Plasmid pDEIPR03 {ECO:0000313|Proteomes:UP000007718};
RX PubMed=22768367; DOI=10.4056/sigs.2756060;
RA Copeland A., Zeytun A., Yassawong M., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA Mavromatis K., Liolios K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA Rohde M., Sikorski J., Pukall R., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the orange-red pigmented, radioresistant
RT Deinococcus proteolyticus type strain (MRP(T)).";
RL Stand. Genomic Sci. 6:240-250(2012).
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; CP002539; ADY27676.1; -; Genomic_DNA.
DR RefSeq; WP_013623183.1; NC_015170.1.
DR AlphaFoldDB; F0RQW7; -.
DR KEGG; dpt:Deipr_2561; -.
DR eggNOG; COG1203; Bacteria.
DR HOGENOM; CLU_013924_1_0_0; -.
DR OrthoDB; 9810236at2; -.
DR Proteomes; UP000007718; Plasmid pDEIPR03.
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: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; IPR041372; Cas3_C.
DR InterPro; IPR006483; CRISPR-assoc_Cas3_HD.
DR InterPro; IPR038257; CRISPR-assoc_Cas3_HD_sf.
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 PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF16; CRISPR-ASSOCIATED NUCLEASE_HELICASE CAS3-RELATED; 1.
DR Pfam; PF18395; Cas3_C; 1.
DR Pfam; PF18019; Cas3_HD; 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.
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 Plasmid {ECO:0000313|EMBL:ADY27676.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007718}.
FT DOMAIN 22..216
FT /note="HD Cas3-type"
FT /evidence="ECO:0000259|PROSITE:PS51643"
SQ SEQUENCE 963 AA; 106124 MW; 7F1AB6F8326A875E CRC64;
MTTLAPLTRI TASLWAKSPK PTGEVKLGVL EHLLNVAACA AEILELEPPH VKAQMAADLG
LELEQGLNWV LALVALHDLG KASPAFQMKW AEGMKAVDGW LSVSRLLREP YTFHGVVSEF
CLPDFLVGQL QWSSRLAEHV SDAVGCHHGF RVENLALQDV SPAQIGDDRW RKVRFELCRL
VTVAVGADYS VVPPVKEFSA AAFMRLAGLT SFADWLGSSF PLPTQTDFSA YEDPAAYFAE
ARAQAKKLLT DPKTGIHWPQ FAPLHPALPH LEDVFSYLAN GEFRPRPLQT ALAEALAQVD
GSTLVLAEAP MGEGKTEAAL YAYLQLQHAA QHRGLYVALP TQATGSAMFE RLVEFLRAQG
SQRPVSIQLA HGGTLLNDEY QERVENTRLF YRTNTDAEGE QSVEAVRAEE WFTSRKRALL
DEFGVGTVDQ ALLGVLGVSH QFVRLWGLGN RVVVLDEVHA YDTYTSELIA ALVAWLRALG
SSVVIMSATL PDESRRKLLG AWGAREIPAA VNYPRWTVAT QTGEVTAGTI PDTDAEGNRS
RPTQQIALHS LPASAEAVAA QAVELTLNGG CTAIIVNTVQ RAQAVQSEVL RLLAERGVAA
QTCTGAVAKG AEWVGVLLYH ARYPADERQY RERAVLKYLG KEGQRPERFI LIATQVAEQS
LDFDADVMIS DLAPLDLLLQ RAGRLHRHQR PPASRHVHVH PALYIAGLGE WPAAALKAEA
WGRVYAPALL YRTWRILQGR QTLTLPTELD DLVQQVYGAA LATADLTDEQ AQTIQAAEEK
LLAERAGQAS KGRFAHIGLP TEFWQTRLTH VLEEPDTESV NDDALADEDE FPRTRLGDES
VRIVPVQQAN GKWVVCPPPK AMQPKNEPWQ EVVTHHQTLD KGDMHTAKRI FRRSLSISRW
EVVRAAKEGR LWTHGLGGDK RGWAAHPLLR DAVPLDLTAG YKDLGRLRLR LDPELGLVYE
KLS
//
