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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//