ID Q5WVC9_LEGPL Unreviewed; 652 AA.
AC Q5WVC9;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0000259|PROSITE:PS51193};
GN OrderedLocusNames=lpl1886 {ECO:0000313|EMBL:CAH16125.1};
OS Legionella pneumophila (strain Lens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245 {ECO:0000313|EMBL:CAH16125.1, ECO:0000313|Proteomes:UP000002517};
RN [1] {ECO:0000313|EMBL:CAH16125.1, ECO:0000313|Proteomes:UP000002517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens {ECO:0000313|EMBL:CAH16125.1,
RC ECO:0000313|Proteomes:UP000002517};
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC {ECO:0000256|ARBA:ARBA00038058}.
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DR EMBL; CR628337; CAH16125.1; -; Genomic_DNA.
DR RefSeq; WP_011215884.1; NC_006369.1.
DR AlphaFoldDB; Q5WVC9; -.
DR KEGG; lpf:lpl1886; -.
DR LegioList; lpl1886; -.
DR HOGENOM; CLU_012117_2_0_6; -.
DR Proteomes; UP000002517; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 20..288
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
SQ SEQUENCE 652 AA; 73079 MW; C946C84727BC2D9E CRC64;
MEEITTFAET CRRTLSEKGR LSTAIPGFVA RAPQADLAVA IANAIVQRSI LVAEAGTGTG
KTFAYLLPCL LSGKKALIST ATKTLQDQLF QKDLPTLIRA LGLSVRIQNL KGRSNYICQY
RVEKHAEEGQ FQSPQCAHEI LHVRDKLSQM QEGVRSELPE INEDSSVWHY VTSTTDNCLG
AECPNHETCF LVKARKRAMD ADIVVINHHL FFADSQLKKE GFSELLPGVD VVVFDEAHQL
ADIASNFNGE RLGTRQFKDL VADMLNEWPI LDLANQPLKS ISHKADKLVD QLLNALPTRE
ERISWDLVKR NKEFMEAWDT WLSLKDELVQ CLESEDATDI PGLKRCKERL LDLETILLSF
TEENNNKIRW LERFKHTLVF HATPYDVAES FSQLLKHQSC AYIFTSATLT MASAFDSFCK
PLGLDKVQTL LLSSPFDYQQ QALLYLPRGI PDPKDAHYYD ALLEKALPVI EACGGRCFFL
FTSHKAVKLV AQMMSNTLKY PLLIQGDEAK PILLSRFRQL GNAVLLGTST FWEGVDVKGE
ALSCVIIDKL PFANPVDPVI RGRMSYLKKK GLSGFDELSL PNAVIALKQG VGRLIRDITD
KGILMIADPR LTGREYGRTI LASLPGLPKT RDEEKVLHFI KELALNDETV SD
//
