ID A0A0G4IN50_PLABS Unreviewed; 870 AA.
AC A0A0G4IN50;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=PBRA_005239 {ECO:0000313|EMBL:CEO96630.1};
OS Plasmodiophora brassicae (Clubroot disease agent).
OC Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC Plasmodiophoridae; Plasmodiophora.
OX NCBI_TaxID=37360 {ECO:0000313|EMBL:CEO96630.1, ECO:0000313|Proteomes:UP000039324};
RN [1] {ECO:0000313|EMBL:CEO96630.1, ECO:0000313|Proteomes:UP000039324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:CEO96630.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) 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};
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|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CDSF01000068; CEO96630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4IN50; -.
DR STRING; 37360.A0A0G4IN50; -.
DR EnsemblProtists; CEO96630; CEO96630; PBRA_005239.
DR OMA; DYPDATT; -.
DR OrthoDB; 5480246at2759; -.
DR Proteomes; UP000039324; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR027417; P-loop_NTPase.
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 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|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000039324}.
FT DOMAIN 37..341
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 342..616
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 870 AA; 96018 MW; CEC59DF20B4D3A70 CRC64;
METFRSRPDA SKWAVTPSKA SAPAASPPRI PRSLLVNLNP EQLRAVKYDG ASPLIIVAGA
GSGKTATLTM RIADLISTRH VSPEQILAVT FTRKAGDEMR ARLHSSGLGA LAGRVRACNF
HQLCLSILKE HFRDAGFAQT PQVLSRDTQR RIVREAILHW KTAHKSDRLN VGVTVSDDDM
SDASNEGDRD KASPGVSTRD INYFCDFIGK AKARRQKPNE FVDDHANIYA HYLQSLKSGG
QLDFQDFVPL TIRLLKCRPN ILHSLRQRWL HIIVDEYQDV SDDQFELIQL LVGSSGHLTV
CGDDDQSIYA FRFGTSQSFN LLKSSYPKHE LVMLTETYRS SPEIVQLASK VINHNKNRTS
KAIVTTKPSS SPVMFRICGD FGAEVRDVVS QIRRLVDVNH MQLSDIAILC RTRSPLVFFA
RALQEALIPF EAARDEKETS GREAKQSKQV LDMIAYCHLI CDPPVRQEEI DAAFLRVVNV
PKRQIGKSTV DMIVNKQKQQ KDMSLLKVAS RLISSSDLPA RARKSLSDFL SLIRVLKSQC
RSKPNVETIK KIDAGTGYSA KTKMKGDLIG LIEVAQRADH AKATLAEMCE MCKASPMTPA
TSRNAVTLST IHQAKGKEWT CVFVVQFNEG VIPVEFRITD QSHVASPKQA SQEELLHQSH
EHIEEERRIC YVGLTRAKTH LFLSATKMDA KGSNSVPSRF VQEFPEQLVA PWPGAANVQC
TTPKAPPHSE SSRAPSSAEG QRALASGASK PTFTGFQTAA SLRGQQGLQP AASAPSQPFR
PPTLLPSGSA FPTSGGTFQA GVRTLSQRMP MATPSARPMS SYQRLQETSN LPQQVPTAGP
TGQSERRPND VKRPAPVIRS FVPPSKRHFI
//
