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Database: UniProt
Entry: Q6LW99_PHOPR
LinkDB: Q6LW99_PHOPR
Original site: Q6LW99_PHOPR 
ID   Q6LW99_PHOPR            Unreviewed;       825 AA.
AC   Q6LW99;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=HD Cas3-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=PBPRC0040 {ECO:0000313|EMBL:CAG17978.1};
OS   Photobacterium profundum (strain SS9).
OG   Plasmid pPBPR1 {ECO:0000313|EMBL:CAG17978.1,
OG   ECO:0000313|Proteomes:UP000000593}.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG17978.1, ECO:0000313|Proteomes:UP000000593};
RN   [1] {ECO:0000313|Proteomes:UP000000593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR377818; CAG17978.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6LW99; -.
DR   KEGG; ppr:PBPRC0040; -.
DR   eggNOG; COG1203; Bacteria.
DR   HOGENOM; CLU_013924_2_0_6; -.
DR   Proteomes; UP000000593; Plasmid pPBPR1.
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; 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; PTHR47963:SF9; CRISPR-ASSOCIATED ENDONUCLEASE_HELICASE CAS3; 1.
DR   PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR   Pfam; PF18019; 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; 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};
KW   Plasmid {ECO:0000313|EMBL:CAG17978.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000593}.
FT   DOMAIN          35..213
FT                   /note="HD Cas3-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51643"
FT   DOMAIN          274..454
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   825 AA;  92930 MW;  196B38025FAD5A1A CRC64;
     MSRREVAYGF SKGLFMSSAT YFKYWGKVEK DSEQADIGYH LLPYHCLDVA AVADKWLTRS
     NVLLKQISAH IGKTEQEARS IVLFFVLLHD FGKFDARFQN FVESIRIKLQ GNEYEVESEA
     YSHGSFGYLH FRKVHGNNEA MKAVAGHHGY CDVSLDPFSP EAEPDADDEL IELDKHAREE
     WVKFCLEWTG LSQIPDVGEI PMLAGLCSVS DWIGSSITNF TQEPDLDLYQ YYKQILPKAD
     AALIESGMVQ VLSGAGFEFL FNGYTPRGIQ TLIEQIPQQP GLTIVESDTG SGKTEFALAY
     ASRLIENKLA DGIVFGLPTQ ATANGLFDRI GDAAEKLFPD STVTLAHGKS RYILKDKYLS
     PDENGFLHRS NKRAFLGSMS VATVDQILMG VLSIKHQFIR SFGTRKSVLI LDEIHSFDAY
     MYGLIEQVLK GQHQAFSSVI LLSATLPNTQ KNKLLRPYGG STQSDCYPLI THTSVEGETN
     EFTLTTGTVR KQIKAEKWCS ATLLPNQQQQ QQLLNWAMKG AMVGVICNTV NDAQKLYLSL
     QEVLPKDQGP ELDIDIFHAR YTFADRAKIE KSVLNVYGKN APRKGRILIA TQVVEQSLDL
     DFDVMVSQIA PIEFLMQRMG RLWRHDRVDS ELAKRTISVN EPVFITLIPS TKASDWKTHY
     QGSGFVYRNI RSLYRTEQYL HEHQVLTFPD CYREAIEYVH AEQMFAEEPE ALESLFNEYQ
     DSNSASSYVA KMNANLESKP LSDVDPRCAL LTREGEMTVS VVLVDEHGKL LHGGDYQEQQ
     DRELSTVSIA KKHVRGIQDA DYYCVKATVG QDIDYTELGV ILPKN
//
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