ID   A0A1I6LYB0_9EURY        Unreviewed;       917 AA.
AC   A0A1I6LYB0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=ATP dependent helicase, Lhr family {ECO:0000313|EMBL:SFS08378.1};
GN   ORFNames=SAMN05216559_3415 {ECO:0000313|EMBL:SFS08378.1};
OS   Halomicrobium zhouii.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halomicrobium.
OX   NCBI_TaxID=767519 {ECO:0000313|EMBL:SFS08378.1, ECO:0000313|Proteomes:UP000199062};
RN   [1] {ECO:0000313|EMBL:SFS08378.1, ECO:0000313|Proteomes:UP000199062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10457 {ECO:0000313|EMBL:SFS08378.1,
RC   ECO:0000313|Proteomes:UP000199062};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOZK01000003; SFS08378.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6LYB0; -.
DR   STRING; 767519.SAMN05216559_3415; -.
DR   OrthoDB; 372104at2157; -.
DR   Proteomes; UP000199062; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd17922; DEXHc_LHR-like; 1.
DR   CDD; cd18796; SF2_C_LHR; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013701; DEAD/DEAH_assoc.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR017170; Lhr-like_ATP-dep_RNA_helic_prd.
DR   InterPro; IPR045628; Lhr_WH_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47962; ATP-DEPENDENT HELICASE LHR-RELATED-RELATED; 1.
DR   PANTHER; PTHR47962:SF6; LARGE HELICASE-RELATED PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08494; DEAD_assoc; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF19306; Lhr_WH; 1.
DR   PIRSF; PIRSF037307; Lhr-like_helic_prd; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Helicase {ECO:0000313|EMBL:SFS08378.1};
KW   Hydrolase {ECO:0000313|EMBL:SFS08378.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199062}.
FT   DOMAIN          61..254
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          296..442
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   917 AA;  103265 MW;  CDB25A4DD97ADDF8 CRC64;
     MGGRERLAAV EPTFDPSDVA IDDADVLELL EPVVQEWWTE RFGEFVPDNG GFFTPPQKEA
     IPLIHERENA LIAAPTGSGK TLASFTGIIN ELFCKAREEE LENSVYCLYV SPLKSLANDI
     HRNLEVPLDG ITEKLDGRGE DVEIRHAIRH GDTSDAERSK MLETTPHILN TTPETLAILL
     NSPKFREKLR TVEYVVVDEI HSLAENKRGT HLSVSLERLE EMAHGSPTRI GCSATVEPLS
     TMAEYLVGQE EPGEGTRDYE IVDARFAREF DVELTCPTDD LIDTPRDVVQ GRFYGQLHDL
     IQRHTNTLVF TNTRSGAERV LHNLREKYDG YDEENSGCHH GSLSKDRRQE IEEQLKEGSL
     DVVTTSTSLE LGIDMPHIDL VVQVGSPKSV AALLQRIGRA GHQLGQTVTG RVVALDRDEL
     IECAVMLKKA HEGFVDRVFV PENAQDVAAQ HVYGMAINDV RREEDVKATL QRAYPYRNYD
     EHDWEQLMRY LTADYAGMED KNVYAKVWRD DNDAPDGEFH YDQFPVGEPL IGKRGRLARV
     IYMTNIGTIP DSFTCDVYTR GSDDWVGQLD EEYLDTLEKG DVFVLGGDHF QYSYRRGSKV
     YVDRTSARPT VPSWFSERLP LSYDLGQEIL QFQREFLDKL GEGGPPAIRH WLREYPLDEN
     SVRAITRMLS EQVAYAGSNS LSTDDRLVVE EALDHDEYER HYYVHSGYGR RLNDGFSRLL
     AYRVAQATSA NVKVAVADNG FTLSMPLNRK VDVEGLLTDI EPDDVRTDLR RALQGTDLLQ
     RYFRINATRS LMILKRYKGY EKSAAEQQVS SEMLLSFAED LEAFAVIEET YREILEDKLN
     VAGIEEVTGA IQDGDLSVET VRVDSPSPRA FGLATLAATD VVLAEDESAV LQEFHRRVLD
     EIDGDGSTGQ SPPVESE
//