ID   D3HQK8_LEGLN            Unreviewed;      1091 AA.
AC   D3HQK8;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Putative DNA/RNA helicases, superfamily II, SNF2 family {ECO:0000313|EMBL:CBJ11178.1};
GN   OrderedLocusNames=LLO_0833 {ECO:0000313|EMBL:CBJ11178.1};
OS   Legionella longbeachae serogroup 1 (strain NSW150).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ11178.1, ECO:0000313|Proteomes:UP000001060};
RN   [1] {ECO:0000313|EMBL:CBJ11178.1, ECO:0000313|Proteomes:UP000001060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSW150 {ECO:0000313|EMBL:CBJ11178.1,
RC   ECO:0000313|Proteomes:UP000001060};
RX   PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA   Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA   Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA   Etienne J., Hartland E., Buchrieser C.;
RT   "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT   unique strategies to cause Legionnaires' disease.";
RL   PLoS Genet. 6:E1000851-E1000851(2010).
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DR   EMBL; FN650140; CBJ11178.1; -; Genomic_DNA.
DR   RefSeq; WP_003632525.1; NC_013861.1.
DR   AlphaFoldDB; D3HQK8; -.
DR   STRING; 661367.LLO_0833; -.
DR   KEGG; llo:LLO_0833; -.
DR   eggNOG; COG0553; Bacteria.
DR   eggNOG; COG4715; Bacteria.
DR   HOGENOM; CLU_000315_21_0_6; -.
DR   OrthoDB; 9760715at2; -.
DR   Proteomes; UP000001060; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd18012; DEXQc_arch_SWI2_SNF2; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR007527; Znf_SWIM.
DR   PANTHER; PTHR10799:SF1020; BTAF (TBP-ASSOCIATED FACTOR) HOMOLOG; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50966; ZF_SWIM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:CBJ11178.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001060};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          52..87
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          640..798
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          924..1084
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1091 AA;  124904 MW;  8F51F434145FC631 CRC64;
     MLNEALSTMP DVFEAKILLR GQEYFEKGHV LNIRFSDGLL KGRVKGSASQ IYDVHMDLKA
     WPKKSAHCTC AYQSNCKHAA ACLLALRDRE KNNSKSLPAN KLDKKLDIWL KNLRAQEAAT
     IKTQEATHHL VYLIDLKFEG HEHRVVIKLA LAKLLKRGGY GKMITFNSLS DSKKQHFIGD
     DNDLVALLLF KCGVSGWFDS LNIRNSELLE RIISTGRAFF IQNPNKAIQL GESIRGTCQW
     VLSHNGSQNL VLMHEDNAFK PLLLDNSWYF NYSEAKIGCL LTSYPIKQLS YLLEAPSIPL
     DQAELLANKM AHTCPEFPVP QVFKQREVRE VLPVPVLVLD TISEFDEESS WLYDTDEELH
     ALFTVHVVFD YAGLIITASD QCDTVVRQQE GVLIQYVRDK DFEKLKWDEV QSLLDLRVPR
     TWEYEQWGKA KKVDFIIQNI NVLADLEFLR SQSIPDLKEK GWRVECVGTL YQEVVNADEV
     EWYSDLQEST TDFFSYQLGI LVEGKQVSIV PLIADLIQRY SANSLDNLSD DQLVKLPLQD
     GRALQLEMGR IKPLIRLLLQ FGLRHFDAHQ SVSLSKYQLI LMREAELAIA ALKTRWQGAE
     TLREQIRQLT LLTNIPEIQA PLGLQVRLRD YQRYGFSWLQ FLRISHFNGI LADDMGLGKT
     VQTLAHLLYE KEQGRTQSAT LIVAPTSLVG NWLVEAKRFT PQLNVLIHHG AERHQDNFDD
     YDLVISTYGL IQRDKEKFVS YPFYYLILDE AQFIKNARTK TTQIIQQLHA THRLCLTGTP
     LENHLGELWS LFHFLMPGLL GDAKQFRLWF RTPIEKYADR ERREILIKRV QPFILRRTKN
     QVARELPPKT EMTHTIELIG AQRDLYEAIR MSMEKKVRDA IAKQGLGKSH ILLLDALLKL
     RQVCCDPRLL SLPEAAIAHG TSAKLEALMD LLNNLIGEGR RVLVFSQFTS MLQLIEEELR
     ARHYDYLKLT GQTQHRQAMV DKFQEGNTPV FLISLKAGGT GLNLTRADTV IQYDPWWNPA
     VEAQATDRAH RIGQENPVFV YKLITAGTVE EAILTMQEKK RLLGESVLSP DSTKATALSE
     NDIEQFFMPL S
//