ID G4ZCN9_PHYSP Unreviewed; 887 AA.
AC G4ZCN9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=ATP-dependent helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHYSODRAFT_560281 {ECO:0000313|EMBL:EGZ17771.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ17771.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ17771.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ17771.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
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DR EMBL; JH159154; EGZ17771.1; -; Genomic_DNA.
DR RefSeq; XP_009526829.1; XM_009528534.1.
DR AlphaFoldDB; G4ZCN9; -.
DR STRING; 1094619.G4ZCN9; -.
DR EnsemblProtists; EGZ17771; EGZ17771; PHYSODRAFT_560281.
DR GeneID; 20663475; -.
DR KEGG; psoj:PHYSODRAFT_560281; -.
DR InParanoid; G4ZCN9; -.
DR OMA; TMSRCLH; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd17919; DEXHc_Snf; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT DOMAIN 316..489
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 700..862
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 109..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 99508 MW; 50A3E6FC05FE66BF CRC64;
MALGVKESVS GRLFRLSADG AEERVCGGKG AVYLSGPKVV LRCCGKTSIV ATRATKQSIL
RQGDVLLLGL RDAFYANGTL TKYEVVDTDA APPKLALHVL PTRVPSITMS SAASSATKAS
KEEEEEEMAP ASRRRGKRTR AIVESDDEAD ASSKIQDLTV DSDVSSPREE DDIFEKELET
STSAAKDWMA AFGRKESSSS SRRFTYEHGN DDDDSDEDEH YSRSHDEVGQ LLEECEEIAR
KLRRSVQKWS GNSTKSAPSS PSTSPADATD EEESAHMSIA SIDGGDRRVV TQADIPDICE
TLELKPYQVV GVNWLLLLHE NKVSGVLADE MGLGKTVQTI SFLLLLKSLE KSDKTAVGPH
LVVVPASVLN NWTRELSWIA PKMRVVTYHG SKDHRRDLEE TLDSDDFDVL LTTYAYFERD
TCQEERAFLR SFQFGYMILD EGHSIKNSNT SRFKRITALR ARTRLVLSGT PIQNKLNELL
TMLSFLMPRM FDHGSDELLS FFDGNEQKKC EKVRKILAPF ILRREKKYVL SQLVPKTVHV
ELIKVGDEQR KAYTGLLESV VKRRDAQAAM KAAAKERKKN KGKEHKADRR LRELMGSYAT
PPGGEPSAMS IFTQLRKAAN HPVLLRRHFV SDEVLETMSR CLHRAEAFGN QCSMSRVRQE
LESYSDFELH DLCVQYEAID ELRKLQLSMD TLLASAKFDY LRKLLPKLQG EGHRVLIFSQ
WTKLLDLMEV LMSHMDYRYL RLDGSTDVQE RQGLIDTYNE DKGIFVFLLS TRAGGLGINL
TAADTVILHD LDFNPTSDEQ ACDRCHRIGQ TKPVSIYKLV SENTVDHDIY KLGESKTELN
HKILDKLNAH GDGAKKKGKK SDAVTVEMLL ASVISDYKSA QVEVEEE
//
