ID A0A420HTZ8_9PEZI Unreviewed; 967 AA.
AC A0A420HTZ8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=OnM2_046060 {ECO:0000313|EMBL:RKF60914.1};
OS Erysiphe neolycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF60914.1, ECO:0000313|Proteomes:UP000286134};
RN [1] {ECO:0000313|EMBL:RKF60914.1, ECO:0000313|Proteomes:UP000286134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG2 {ECO:0000313|EMBL:RKF60914.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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 -!- 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:RKF60914.1}.
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DR EMBL; MCFK01004658; RKF60914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420HTZ8; -.
DR STRING; 212602.A0A420HTZ8; -.
DR Proteomes; UP000286134; 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 CDD; cd18807; SF1_C_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:UP000286134}.
FT DOMAIN 8..282
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 283..590
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 916..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 967 AA; 108944 MW; 4AB8832065BD94DA CRC64;
MDGNILNSLN KSQKAAVTSD PHGQLSILAG PGSGKTHTLV ARIAWLLSNG TLPWNILVTT
FTVKTAREMK ERIEKLVGAS KSSKLILGTF HSIARRYLTQ YGHLIGLKNN FDIADSVDSL
AIIKRIVKKY ELNADPKVVR NRISGIKARG GNRDQKWMKK LPLSIESQEF DLCYREYEEA
LHRSDLFDYD DLLLNCVKLI REHPICVSNI EAVLIDEFQD TNTVQFDLMR LFAACKQQVT
IVGDPDQSIY SFRAAELQNY QRFQHQYPKS TTITLEENYR SSGAIISTAL NVIKQDSGRI
SKSLVPTNNI GTRPVIRKLL DAHKEAEWIS LEIQRVIGMT GGLLDLSDFS ILLRSAALSR
LIENSLRKTG LAYRMVGGVR FYDRVEVRIL LDYLRAVNQP NNDDALSNIL NVPPRRIGDT
TIRKLIEEAS NQKITLWSLI LMIAKEKKHT NMKLTQQVIQ GLSCLCDIIE TSRTKIFNLD
NPLSLSDLLK HILDQTNYEE WLHVYHNDIL KLRWSNVEEL VTQVMEFQEN IADGYEDESL
PLIAGVPQKG SINVLAKFLA NVALSSGIEN NDGEVQTPQI TISTIHAAKG LEWPVVFIPA
VYQGSIPHLR SDDSKEERRL LYVAMTRAKV LLYLSYPLKS SRGEKTALSE FISLRSLAPA
IIPVGPVIRS EVVHSISQIL RRPNPTAEGI ASSSSLLPSK FDNLFPADAE NNRNDTEMQS
YNMSAKRDVD MAYQDQKRRC IEPKELNFHL KESNSTFISD KHDSDHMNCS FKSSFISASS
HLENLSNSMD KLQDKKSQGT KELKRKDRLH FSPNSRLSTT KLRQSNLKVY FGKSNLEMDD
TSTGIRLCGT RDNLELNVQP PLTESSIQKL SEPLPLVKLG NEGYYHKSVS LVDLTHVSCE
TQNLSTENRK SVFNVPDKSS MTATGLTREN PVKSRKTLGV KRSMAGWSSR KEFVPPSLSK
ENHSSQT
//
