ID D3HRC8_LEGLN Unreviewed; 1084 AA.
AC D3HRC8;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN OrderedLocusNames=LLO_1100 {ECO:0000313|EMBL:CBJ11455.1};
OS Legionella longbeachae serogroup 1 (strain NSW150).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ11455.1, ECO:0000313|Proteomes:UP000001060};
RN [1] {ECO:0000313|EMBL:CBJ11455.1, ECO:0000313|Proteomes:UP000001060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ11455.1,
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
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DR EMBL; FN650140; CBJ11455.1; -; Genomic_DNA.
DR RefSeq; WP_003632216.1; NC_013861.1.
DR AlphaFoldDB; D3HRC8; -.
DR STRING; 661367.LLO_1100; -.
DR KEGG; llo:LLO_1100; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_009270_0_0_6; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000001060; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000001060}.
FT DOMAIN 1..485
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 497..758
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 22..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1084 AA; 124743 MW; 16916AB80A70372A CRC64;
MLVDSTQRSQ ATDPSLSYIV QAPAGSGKTE ILTQRYLRLL STVKAPEQIV ALTFTRKAAS
EMRERILLAL QQAANHQPAN SPHQQMTLDF ADKALHSDAH YQWNLLQQPG RLRVITIDSL
CQSINQAIPL LEKQIAYAQI TDKTSSHYLN AGRHCIQYAM ATPQYQEAIK TLLLHVDNRQ
DRLLDLFSEL LSQRDQWIGP LFQARNQAKA TFEHALKIIE QHELNRFKKS LPQHIAKELT
VNARQLALIE NNPGSPRYLL RDWHDFEHAD QETVKALSKL LLTKDAGFRK SFDHHVGLLA
SSCSPDEYKR IKNASKELLN ELSEYPDFLE ALIQVSNLPD PQYDPEQWQV LQALFLLLPL
LVGHLHVLFS EKNEVDFTTI SQQALSALGD ADNPTDLALY LDNTLHHILV DEFQDTSITQ
FELLTKLVHG WQEGDGKTLF IVGDPMQSIY RFRQAEVGLF FRAKEQGIGS VKLHPLELSC
NFRSTQTIVD WVNKHFAHIF PAQIDIESGS VPFHPSVNVI KDKENSTIYA IKFKTREQEA
QKLIEAVQHE LQAYPQKNIA ILVRSRTQLS AIIRLLRQHQ IPYQGTDITL LTHLSHLRDV
WSLTQALLTP ANRLSWLAVL RSPYCGLSLS DIHAIARFNT KKSIYFALLN LNQIQGISEE
GIIRARFLIH VMHQALTQRY ETQLSSWVIH TLKKLHIENI LNESQLNDLE QYWTLLDRYE
QDGRLPDMKE FLMELNKLYS QQTNSSRLHV MTIHKSKGLE FDTVILPGLG AQANHGDKPM
LRWLNLPTQN HGNLLLMSPI QAAHQEHCAL YDYLTQLDEI KSRYETQRLL YVAVTRAKSR
LYLMDYSEKS SKSSFRSLLK QQEFIEVDPA YPAEEGTLSF PKLLRLPLNF YLTPKPDVFF
NNKTSTTSLT TSIPRLIGII THRLLHWICN NHPETIAEVP WGLPRYELRK LGFDEKMQLD
ALQTIQNQIT KLFEDPTGSW IIAKHHQELN EYELLVKQKN IPITRIIDRT FEDQGKCWVI
DFKTGKEDEA SLLKHQQQLN EYGSYLSSRS QLPIYCGIYY LASNHWISWQ YGSISIPVVY
DETP
//
