ID   A0A249LGZ5_9ACTN        Unreviewed;      1065 AA.
AC   A0A249LGZ5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=PHILAsVB114_06165 {ECO:0000313|EMBL:ASY28186.1};
OS   Candidatus Planktophila limnetica.
OC   Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC   Candidatus Nanopelagicaceae; Planktophila.
OX   NCBI_TaxID=573600 {ECO:0000313|EMBL:ASY28186.1, ECO:0000313|Proteomes:UP000217221};
RN   [1] {ECO:0000313|EMBL:ASY28186.1, ECO:0000313|Proteomes:UP000217221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS-VB-114 {ECO:0000313|EMBL:ASY28186.1};
RA   Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT   "High microdiversification within the ubiquitous acI lineage of
RT   Actinobacteria.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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; CP016782; ASY28186.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A249LGZ5; -.
DR   KEGG; plim:PHILAsVB114_06165; -.
DR   OrthoDB; 4812256at2; -.
DR   Proteomes; UP000217221; 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   CDD; cd17932; DEXQc_UvrD; 1.
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; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF55; DNA HELICASE; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF12705; PDDEXK_1; 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:UP000217221}.
FT   DOMAIN          19..343
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          344..664
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          795..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1065 AA;  116910 MW;  BF651DCD3D9A988B CRC64;
     MISPLEIAAA LRSVDSKVSD PTPEQIAIIS APLEPAVVIA GAGSGKTETM SARVLWLVAN
     KIVRPDEILG LTFTRKAAGE LSIRVRKRLR QLKEAGLLDK DLALDTAITT YHSYAGRILS
     EHAIRLGIDA TSDPLGDAAL WQIASDVVRN WPDENFTNES AVSTVIDDVI GLAKLVLEHQ
     VSFESIRAED EKTLAEMQRI GGTSNEEVRK VVRIAQQRIA ILPMVEEFLK RRRDDGQLSF
     DDQMSIAADI AERFPEACEL ERAKYKVVLL DEYQDTSQSQ VRMLSALFGQ GHPVMAVGDP
     CQAIYTWRGA SAGTIGTFAK YFPKSAGHSG AELFNLSITF RNDKKILEIA NSISDQIRST
     SSVRVDPLRP RDSAGDGEIA YGVFETLDGE AQGIAEYFHK HWFAPERIAI EEDKRTSFAV
     LVRKRSQISM IESALRARSI PVEVIGVGGL IYVAEVADVL SLMKVVTDPE AGTALMRHLT
     GPRLALGAKD IAALGAYSRK RAKLGHEDSH SFIAKIAAGN PDSAEADDLF IGSLIDALDE
     IEQCDKESRA LFSEVGFTRL SRFATDLRRL RSRAGGSIID LITEIENYLN LDLEVSLRDG
     TRNGRRHLER FLDEASKFSR SGGSISAFIE WLDVTSKKEG GLKSGAPEVR SDVVQLLTIH
     TAKGAEWDFV AIPGLAEGTF PSTYTNDPDN WITNERQIPF ALRGDGDELP VFSLAQCTKD
     SEAGKVITAY AKSCAAIKKQ EEIRLGYVAV TRARTHLLCT TSWWREGSRS VDPSELFAHV
     TEVADKRGGE LLSEASAPED GVRNPIEVNP DSAYWPRDPL GDRREAFDAG VALVKKSQAH
     ALTLSGDETL DSWVHDAQAL IAEVKNRASS SIEVALPSRI STSTLVALHE DPAALALAIR
     RPIPRSQDPY SRRGTQFHAW VEKQFGAMTL FDDSYLDYFD PIEEDGKLED LKKSWLASEY
     AQRKPAAIEV PFESVIAGVL VRGRIDAVYE TPDGFEVVDW KTGSKQFGAS AAIQLAMYRL
     AWARLKSIDV SQVSAAFHYV PTSVTDKRAD LLDEAALVGL IQSLQ
//