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Database: UniProt
Entry: V9FMJ9_PHYPR
LinkDB: V9FMJ9_PHYPR
Original site: V9FMJ9_PHYPR 
ID   V9FMJ9_PHYPR            Unreviewed;      1192 AA.
AC   V9FMJ9;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=F443_04527 {ECO:0000313|EMBL:ETI52301.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI52301.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI52301.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI52301.1,
RC   ECO:0000313|Proteomes:UP000018721};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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:ETI52301.1}.
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DR   EMBL; ANIZ01000825; ETI52301.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9FMJ9; -.
DR   EnsemblProtists; ETI52301; ETI52301; F443_04527.
DR   OrthoDB; 54635at2759; -.
DR   Proteomes; UP000018721; Unassembled WGS sequence.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd17920; DEXHc_RecQ; 1.
DR   CDD; cd18794; SF2_C_RecQ; 1.
DR   Gene3D; 1.10.150.80; HRDC domain; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR010997; HRDC-like_sf.
DR   InterPro; IPR002121; HRDC_dom.
DR   InterPro; IPR044876; HRDC_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR018982; RQC_domain.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF153; ATP-DEPENDENT DNA HELICASE Q-LIKE 4A; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00570; HRDC; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   Pfam; PF09382; RQC; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00341; HRDC; 1.
DR   SMART; SM00956; RQC; 1.
DR   SUPFAM; SSF47819; HRDC-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50967; HRDC; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018721}.
FT   DOMAIN          400..576
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          590..753
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          601..665
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          1007..1087
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
FT   REGION          72..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          922..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1166..1192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          211..269
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        112..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..962
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1166..1180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1192 AA;  132315 MW;  4511E52BD95A5FD2 CRC64;
     MCILYPSVVL SSSDGTADKE NCLETIQRGR DALLKFQALR ARSKASTKLK VVPTPRIALG
     TIPVINTAPI PAPIDTSRQY GDSSAGRGRN GADYAPSAAG FQPAPAASDV VDLTGTTPSS
     PSRANTGYQN NRTTISARSA VQQTSFTGMD DDTDSLFDDV DVDALVANHQ RVQQQKRRGA
     PQVPSLSKES FVSPPSTQTN GSQETASAML AEDLRQSIKQ TRENLRKVRE ECDDASLEGE
     VPEFMQKRRS ELEQELEELS RRYRECKGTT KASPQSRNVS PVQIPPRAVQ TPQSYQCGGD
     SSNKNPMCSC GMTTVEARVQ HGANANRLYY RCNTCGFHSW VDAASSSGGN SGVHQTRPRA
     IEQPCVSSDP SVNSKMQRAK RVLRDVFGHN SFRPNQERTV MEAFSGRDVF VLMPTGGGKS
     LCFQLPACID DGVTIVISPL VSLIQDQVQQ LEALDVGVAN LKGDQDYATE QRPIISELFS
     NQIRIKMLYV TPEKIASSGM LNNLFESLEK RGLLARFVID EAHCISQWGH DFRKDYLNLG
     TLRTKFPSVP IMALTATANS QTEADIVRNL KLKNPFITRS SFNRPNLTYD VRKKTSKFMA
     EIADFVRKHI DDSGIIYCLS KKDCEQTAEK LIKALGFEHT RKASQISFYH AGLEAADRAY
     RHHEWSKGKI KLICATVAFG MGINKPDVRY VIHHTIPQSV THYYQEAGRA GRDGEVANCI
     LYYSFLDLTR RRKLITKDRE NMQHRNVHLQ NLRRMTEFCE NQVECRRTSL LEYFGEHFSS
     EQCHGTCDNC KNKVLGISFE KSDVTEDCVA LAEMIKALQA NGDPATLVQI AQIFLGMVVK
     GKEWKQDQFS QLGGFGRGKG RYSRSEVERI LYHMILRQYL REVDQSNAKG FTTTFLSLGI
     NSNRLMRGER VRIVCKTKYQ SRASASDGAP EESTKTSKKK AQKKTIASKK TKKPSKTIKK
     KKASAKNVVE ELSDDYDDDV VEVAPPSATT TEYPLIPERI SSRRIPEDHA ETLAQILKDW
     RASVCDSQNV MPYHILTTGG IASIANSVPV SNAELLEIDG VGRIRVKKYG AAIIDIVKTY
     LEKNNLTPSP VQASRSSNVL DSLEVLDSGV EVVQAPAAPK SSPFFQDKTK RKTSLTSSKT
     ASHAVIDDNF DDIDWGELDA DMLNQTSSKA VTNGRKRSLD SDTTWTAKKR SN
//
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