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Database: UniProt
Entry: A0A329T516_9STRA
LinkDB: A0A329T516_9STRA
Original site: A0A329T516_9STRA 
ID   A0A329T516_9STRA        Unreviewed;       622 AA.
AC   A0A329T516;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   08-NOV-2023, entry version 20.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN   ORFNames=PC110_g550 {ECO:0000313|EMBL:RAW43226.1};
OS   Phytophthora cactorum.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW43226.1, ECO:0000313|Proteomes:UP000251314};
RN   [1] {ECO:0000313|EMBL:RAW43226.1, ECO:0000313|Proteomes:UP000251314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10300 {ECO:0000313|EMBL:RAW43226.1,
RC   ECO:0000313|Proteomes:UP000251314};
RA   Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT   "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL   Submitted (JAN-2018) 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=3.6.4.12;
CC         Evidence={ECO:0000256|RuleBase:RU364117};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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:RAW43226.1}.
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DR   EMBL; MJFZ01000006; RAW43226.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A329T516; -.
DR   STRING; 29920.A0A329T516; -.
DR   Proteomes; UP000251314; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   CDD; cd18794; SF2_C_RecQ; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF72; ATP-DEPENDENT DNA HELICASE Q1; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364117};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000251314}.
FT   DOMAIN          96..275
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          303..449
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          599..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..49
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        605..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  70041 MW;  FA12DA31C0A74DA5 CRC64;
     MVDAEAELAQ VEQELQEVEE DLNVFLLRQS ELLERKRELQ EQLECEQIED DAAAAKNTEK
     AAPDWKAQFQ WTEQIHTLLT DTFHLPGFRS VQEEVINATL SKQDVFVVMR SGGGKSLCYQ
     LPALFDGNAG FTVVISPLIS LIQDQVMLFN DIAGEGSACK LSGEQSRGEA SAIYKSLLAS
     DSSLKILLIT PEKLIKSKLL MSRLEKAYQT ERLKRFVIDE AHCCSQWGHD FRSDYSKLGI
     LKRQFPKVPI LALTATATPR LAKDVKAILE IQNCVSFRTS FLRNNLHYEV MEKPAKDATA
     MDSLVRLVKS FSSSDTGIVY CLTRKETEQV TQHLCHANVR AACYHAYVEN KEETYIAWIR
     NKLQVVVATI AFGLGINKPD VRFVIHFTLS KSIEGYYQES GRAGRDGKPA RCVLMYKPSD
     VLRVCNIVQA EVGGMLSMRS MIKYCEELSQ CRQSSMAAYF GEAFESTTIC GGVCDNCKRD
     INTEDTIDLS EHSKALISIT EDAKKLERRL TLKQLIDEFT SRKFAQEWTD LNPTIASISR
     SVCDTLVINL LLSNVLQPEI SYTAYNTICY LVPGPRAQHL KRDRFQIQLP RCLMDATKGS
     DGATATKSLK KRKRSPEIIE ID
//
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