ID A0A3M6VP27_9STRA Unreviewed; 1147 AA.
AC A0A3M6VP27;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RMX67306.1};
GN ORFNames=DD238_003205 {ECO:0000313|EMBL:RMX67306.1};
OS Peronospora effusa.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Peronospora.
OX NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX67306.1, ECO:0000313|Proteomes:UP000282087};
RN [1] {ECO:0000313|EMBL:RMX67306.1, ECO:0000313|Proteomes:UP000282087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R14 {ECO:0000313|EMBL:RMX67306.1,
RC ECO:0000313|Proteomes:UP000282087};
RA Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA Reyes Chin-Wo S., Mou B., Michelmore R.;
RT "Comparative genomics of downy mildews reveals potential adaptations to
RT biotrophy.";
RL Submitted (JUN-2018) 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:RMX67306.1}.
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DR EMBL; QLLG01000170; RMX67306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M6VP27; -.
DR STRING; 542832.A0A3M6VP27; -.
DR VEuPathDB; FungiDB:DD237_000311; -.
DR Proteomes; UP000282087; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
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:0031491; F:nucleosome binding; IEA:InterPro.
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; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF879; CHROMATIN-REMODELING COMPLEX ATPASE CHAIN ISWI; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 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.
DR PROSITE; PS51293; SANT; 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:UP000282087}.
FT DOMAIN 223..387
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 517..668
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 907..962
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1147 AA; 130516 MW; D746A467A5CBF71D CRC64;
MTESSSISSA SSSPSSGSAS ASPSVSGASI SSPSTLNFVL KENESKEDVV ASMDEEDSED
EDNGTGKDEE TMDRSSALND DIKKPLLSSD EREKLRKEEE MVLQDQRDRQ SKSLDLVKQN
LALDAEWEKK SAREKKMAFL MAQSDVFTSF LMGGSSAMGK EMSRSKKAAK EAGSKRGKGN
KQADAQALQD MDDARYTRVT QQPSSIKFGT MKPYQLEGLN WMIRLHDSGV NGILADEMGL
GKTLQSISLL AYLREARGIE GPHIIIVPKS TVGNWMRELK RWCPSIKAFK FMGSKDERAV
QRTTVVKQNF DALVLSYEVA IIEKAILQKI KWKYLLIDEA HRVKNENSKL SRVVREFKVE
HRLLITGTPL QNNLHELWAL LNFLLPDIFS DAEDFDAWFN VDEEEGQENV IKKLHTILRP
FLLRRLKADV EHSLPPKIET KLYVGLSEMQ REWYMRVLHR DATHLNAIGG SDRVRLLNIL
MQLRKVCNHP YLFEGAEPGP PYQEGPHLWE NCGKMTLLHK LLPKLQAQGS RLLIFCQMTS
MMDILEDYMR YFGHDYCRLD GSTKGEDRDN MMEDFNAPGS TKFCFLLSTR AGGLGINLAT
ADIVILFDSD WNPQVDLQAM DRAHRIGQTK IVRVFRFISD GTVEEKIVER AERKLYLDAA
IIQQGRLAQQ NRKLSKDELM TMVRFGADEI FNARGSMITD DDIDAILARG EERTESMKGK
IAADMQHSLA NFSLAGDNGN ASVSSLYEFE GEVFSKDTNN GDILPSTFIA LPQRERKSNY
NEDEYYRQQA GLSKPKKAKK SGSDAAKVPV VHDYQFFQQE RMVALLTKKT NVENRRKELT
RLIKEAKADE ARAKARKAKP AEGEESAENS AEEEEVDDSR SAALEKELNE TEMDATDAKE
LEELEKEGFG DWTRRDLKQF ITSCERYGRA DKARVCEEVS LVLGKNPAQV ERYFETFWSR
FTELKDHAKH IEKIERGEKR LERNEVVKQA LARKCSRYSH PLRDMRLHYP AGYKSRGYIL
DEDVFLVVMM NKYGPLEHWG EIRDEIRKAW QFRFDWFFKS RTIGELQKRG EVLTRMIERE
NDELKSRTSK DEDDLAKKAK RSSSSSSKSK SKSSSSRSKT SSSSSSKKRS SSSKPSSSSS
AKRQRSS
//
