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Database: UniProt
Entry: A0A3S0Q3R4_9BURK
LinkDB: A0A3S0Q3R4_9BURK
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ID   A0A3S0Q3R4_9BURK        Unreviewed;       695 AA.
AC   A0A3S0Q3R4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=ATP-dependent DNA helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920};
DE            EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01920};
DE   AltName: Full=DNA 3'-5' helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920};
GN   Name=rep {ECO:0000256|HAMAP-Rule:MF_01920};
GN   ORFNames=EKL30_06995 {ECO:0000313|EMBL:RTZ45866.1};
OS   Candidimonas sp. SYP-B2681.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Candidimonas.
OX   NCBI_TaxID=2497686 {ECO:0000313|EMBL:RTZ45866.1, ECO:0000313|Proteomes:UP000288599};
RN   [1] {ECO:0000313|EMBL:RTZ45866.1, ECO:0000313|Proteomes:UP000288599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SYP-B2681 {ECO:0000313|EMBL:RTZ45866.1,
RC   ECO:0000313|Proteomes:UP000288599};
RA   Zhang M.-Y., Zhang Y.-X.;
RT   "Candidimonas lamiisoli sp. nov., a novel bacterium can accelerate seed
RT   germination.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase
CC       involved in DNA replication; it can initiate unwinding at a nick in the
CC       DNA. It binds to the single-stranded DNA and acts in a progressive
CC       fashion along the DNA in the 3' to 5' direction. {ECO:0000256|HAMAP-
CC       Rule:MF_01920}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_01920};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01920};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01920}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|HAMAP-Rule:MF_01920}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RTZ45866.1}.
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DR   EMBL; RYDV01000002; RTZ45866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S0Q3R4; -.
DR   OrthoDB; 5905204at2; -.
DR   Proteomes; UP000288599; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01920; Helicase_Rep; 1.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR005752; Helicase_Rep.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF64; ATP-DEPENDENT DNA HELICASE REP; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01920};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_01920}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01920};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01920};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01920};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01920};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01920}; Reference proteome {ECO:0000313|Proteomes:UP000288599}.
FT   DOMAIN          1..272
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          273..580
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         17..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT   BINDING         270
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01920"
SQ   SEQUENCE   695 AA;  78225 MW;  B536D66370B8DC77 CRC64;
     MQRQAVLYLD GPCLVLAGAG SGKTRVITQK IAYLLRECGY SAKQVVALTF TNKAAREMND
     RVKLLVDPKL AKGLTVSTFH SLGLRFLREE ATHAGLKPQF SILDSNDALG IIQELLATTD
     KARLRAVQQN ISLWKNALMD PDAADRSASS PSEVEAAKIY RSYSATLVAY QSVDFDDLIR
     LPALLMENNA EVRQRWQARV HYLLVDEYQD TNVCQYRLVQ WLTGDRAMLT AVGDDDQAIY
     AWRGATVENL AKLTTDYPSL KIIKLEQNYR SVQRILSAAN QVISKNPNLF GKKLWSDLGM
     GEPIQVTPMD SEEAEAESIA VRVSAARFER QAEWRDFAVL YRSNHQARAL EQALRNLRIP
     YTISGGQSFF EKPEIRDILA YLRLIANDND DPAFIRAVTT PRRGIGQATL QSLGQFAAER
     QLSLFEAIFE IGTTERLAAK QLEPLQVFGA FIQRIQMRAG RKEAVLRVMP GSGNLFAGDE
     TPHDIGADGA RDDSAGTIMD DLLNVIQYER FLYDTLEERP AQTRWNNVME LVSWLKRKAS
     EDDLTLVQLV QHVALVTMLE RSEDEDPDAV KLSTLHASKG LEYPHVYLAG VEEGLLPHLG
     RDEDDADPAT AAEAMALRIQ EERRLMYVGI TRAQRSLHLT WCKKRRRARE DVVRECSRFI
     EEMGLADVKM EEDPATRALT PKDRLGMLRA LLNKS
//
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