ID W2JX95_PHYPR Unreviewed; 1625 AA.
AC W2JX95;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 13-SEP-2023, entry version 45.
DE RecName: Full=ATPase family AAA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=L916_00468 {ECO:0000313|EMBL:ETL50263.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL50263.1, ECO:0000313|Proteomes:UP000053864};
RN [1] {ECO:0000313|EMBL:ETL50263.1, ECO:0000313|Proteomes:UP000053864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL50263.1,
RC ECO:0000313|Proteomes:UP000053864};
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 CJ05E6.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914}.
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DR EMBL; KI670424; ETL50263.1; -; Genomic_DNA.
DR EnsemblProtists; ETL50263; ETL50263; L916_00468.
DR VEuPathDB; FungiDB:PPTG_00404; -.
DR Proteomes; UP000053864; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR045199; ATAD2-like.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23069; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23069:SF0; TAT-BINDING HOMOLOG 7; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 792..843
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1096..1166
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..374
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1532
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1625 AA; 184240 MW; 873E384D1F378613 CRC64;
MEDDESEDVD TDELEESKEE DEEEETTKRA SRRLQTELDI TSPPPSTGHE EVSSASPESS
TRYSLRTRPK PKRIDESIYN DVFPTAHSTY AESTPESQVP SKKRRRRRNR SRRSKRQKRR
VEQEEDEEDD DEEEEQDEET QYEDGMSMRE INRKIKAQER QEREQQRRER STRYSLRSRE
SLTMSDASVV SPPQTESRGR TTRRSQVAEN HVEEEEQEED ADNESQSEND AISDDGQDED
DAEEPASSTR YHLRQRRQVA TDETSIATRS RTKTRVAPMF EPEDTSRRYS LRDRSKTHRA
DAEEDTAASP ETSAYAEYQK RQATRASRRS STTGSGSNRR LFLPDMDSSP PPRRRRSRGR
NKYSRGRRNR HRRSLSSSSS GSSSSSDMYM DDDDSDGGMR TTSPWRSSKS SRKSGSSRAD
ITPVEVDRSI TWDSVGGLKS HIEALKEMVM LPLLYPEFYS KYSVSPPSGV LFYGPPGTGK
TLLARALANS CSFYGEGEQP SGSIQATSPA QKKKKQRPRR HVTFYMRKGA DCLSKWVGEA
ERQLRLLFEE AKRNQPSIIF FDEIDGLAPV RSAKQDQIHA SIVSTLLALM DGMDSRGRVV
VIGATNRLDA IDPALRRPGR FDRELGFKLP SVDERKSMLA IHSKHWKPPL SNRFLTELAE
QTVGYCGADI KALCAEAALC SLRRVYPQVY ASQDKLLINL DKVVVARGDF VKAAKKITPA
SHRAISSFAS PLPRAVKGLL QTQLMQVLRD VARHFPLFPL DKAAIDDAVT TNSEEDEEEE
EDDVDIYAVT SHDDCDVCHG NEGELLCCDA CPGAFHRACL SEMATSTEED TGGLWFCLDC
RTSSSAAMQR AIQRGKKKRV HSIASLHLPR HSGFPRVLIA GKAGMGQQYI GPALLHSLEG
LTHFSLDYPS LVADSNSHFP EEALIQRLSE AQKCLPCVIY LPHVELWWKN TNESMHLTLK
MMLMDLQVRA NLPILFLACT APSCDEKTLP EDLLALFKED PSVSLTSVVM EMDAPSEEAR
LTHFDQVFSS FATPPAVQKK KRSKHEKLAV LPLAPLPPAP SKMELSPEEQ KKRRERDFHF
LRELRIFLSQ VLHYCYSQRL YTPFYVPVDP VAVPNYYLIV KRPMDLSTMR DKLNDEEYTC
FEQFMDDIQL IVRNANVFNP KRSRTRHIAH AAGTMKDNIL SYAHRFRIRQ GYDLFAKCRE
VTKRLRAHPT MYGEYGQRFL KTGRNTRKNS VRAAEKPGVR TSARLRGVKA PEISLDAAIS
RATESTNVIS NGVKEERTEV QCGNKSKEEV PKLQSAQQWF DEEEEEKKSD EEASTDDKSD
DKTNEDTGEE MEEEVYEEGD RIFVSSRTHP GINREGGAAV VQSRNKDGTY NVKYILGGSE
KSVSCKYVRR LTDDAVMESV KTQRSVANDA DGVASVRLIQ DEEKMDETDY FDELLWPLLK
EEGWTRDDNF DIIEASGKES GLAVQRVVFT PGKTRDGETV MLNSVVEALK YINEDPELSL
KLFGNRYAER MMTEEALGEE ASSDEETVEM EEASAAENNV AVAEGNNDEP MPEAEEEVQE
TPEFIYDEAR MTAVLTKLVE KTANWSVDKL RDELLMLNKL AYPFRNSFDR TELMTLIEAH
VATLL
//
