ID V9FA95_PHYPR Unreviewed; 1119 AA.
AC V9FA95;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETI47693.1};
GN ORFNames=F443_08140 {ECO:0000313|EMBL:ETI47693.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI47693.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI47693.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI47693.1,
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 -!- 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:ETI47693.1}.
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DR EMBL; ANIZ01001409; ETI47693.1; -; Genomic_DNA.
DR AlphaFoldDB; V9FA95; -.
DR EnsemblProtists; ETI47693; ETI47693; F443_08140.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_0_1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000018721; 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:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000018721}.
FT DOMAIN 197..361
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 491..642
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 127575 MW; 37F9908805A6299B CRC64;
MAESSPSSSP SSSASPSPKS KDEVESVQDD ASMDGGDSVE DNDTADDEDM DDTPEDTKKT
LLSKEEREAL RREEETVLQE QRDRQSKSLD LVKQSLTQDA EWAGKSAREK KMAFLMAQSD
VFTSFLMGGS SALGKEMSRT KAAKEAGSKR GKGSKQADAQ ALQDMDDARY TRITQQPSII
KFGTMKPYQL EGLNWMIRLH DSGVNGILAD EMGLGKTLQS ISLLAYLREA RGIEGPHIII
VPKSTVGNWM RELKRWCPSI KAFKFMGSKD ERAVQKETVV KQDFDALVLS YEVAIIEKAT
LQKIKWRYLL IDEAHRVKNE NSKLSRVVRE FKVEHRLLIT GTPLQNNLHE LWALLNFLLP
DVFSDSEDFD AWFNVDEQEG QENVIKKLHT ILRPFLLRRL KADVEHSLPP KIETKLYVGL
SEMQREWYMR VLHRDATHLN AIGGSDRVRL LNILMQLRKV CNHPYLFEGA EPGPPYQEGP
HLWENCGKMT LLHKLLPKLR AQGSRVLIFC QMTSMMDILE DYMRYFGHDY CRLDGSTKGE
DRDNMMEEFN APGSSKFCFL LSTRAGGLGI NLATADIVIL FDSDWNPQVD LQAMDRAHRI
GQTKIVRVFR FITDGTVEEK IVERAERKLY LDAAIIQQGR LAQQNRKLSK DELMTMVRFG
ADEIFNARGS MITDDDIDAI LARGEERTEA MKGKIAADMQ HNLANFSLSG DNGNASVSSL
YEFEGEVFSK DTNNGDILPS TFIALPQRER KSNYNEDEYY RQQAGLSKPK KPKKSGSDAA
KVPVVHDYQF FQHERMVALL TKKTQVENRR KELTRLIKEA KADEARVKAR KAKGEDSAEN
SAEEGEGDDA RSAALEKELN ETEMDAADAK ELEELEKEGF GDWTRRDLKQ FINSCERYGR
ADKTRVCEEV SLVLGKDPVQ VERYYDTFWS RYTELKDHAK YIEKIERGEK RLERNEVVKQ
ALARKCSRYS HPLRDMRLHY PAGYKSKGYI LEEDVFLVVM MNKYGPLEHW GEIRDEIRKA
WQFRFDWFFK SRTIGELQKR GELLTRMIER ENDELKSKSS KDEDDLAKKA KKSSSSSSSK
SKSKSSSSSS RSKTSSSSSS KKRSSSSKSS SSSKKQRSS
//