ID A0A2S4PX30_9PEZI Unreviewed; 1084 AA.
AC A0A2S4PX30;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=EPUL_002077 {ECO:0000313|EMBL:POS86567.1};
OS Erysiphe pulchra.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=225359 {ECO:0000313|EMBL:POS86567.1, ECO:0000313|Proteomes:UP000237438};
RN [1] {ECO:0000313|EMBL:POS86567.1, ECO:0000313|Proteomes:UP000237438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cflorida {ECO:0000313|EMBL:POS86567.1};
RA Wadl P.A., Mack B.M., Moore G., Beltz S.B.;
RT "Development of genomic resources for the powdery mildew, Erysiphe
RT pulchra.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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:POS86567.1}.
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DR EMBL; PEDP01000299; POS86567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4PX30; -.
DR STRING; 225359.A0A2S4PX30; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000237438; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd16449; RING-HC; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000237438};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 422..610
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 773..827
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 930..1074
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 854..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..879
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1084
FT /evidence="ECO:0000313|EMBL:POS86567.1"
SQ SEQUENCE 1084 AA; 123667 MW; AEC144EF0433B87F CRC64;
MTQEQILNVE EEINLQLALL ESLDDSVSDR QELEKEITER LRVLRQQYQN LRKDFNTAVP
ESSTSNITSH SFPAESIAFN SSLDTQTFDS GISDGLNQSA FVNSHVAQTP QTPQYRKRQY
SEYSDSAALS PCHVTKFQRL SLDSLDIDQG STFQRFPIYN VDELENGCAD TLIKQQKEIE
ERIKREKLDE QYARQLQAEF QDTYSFNLSA HQSSYPRSPI PEQPVTFNTS QSSGNLSREI
QQPSVFSLSR WSRGEPSTYE RNTAFIDLDD KSDIRSEISL STESDKEVEV VQSNTISTDV
NNYKDEVSFG IESSNFSTQD NLNHLNHQNS SSSSYQPNLS PMYHFKSDHG SPHVGFYLKS
IYDNLSGRFY STDMKKSEMK DECKELAKNI RLDVETRREE TPEALVHPLY EHQKIALFWL
KSKEESIIKG GILADDMGLG KTISALALII SRPSSTISRK TTLIVGPVAL IRQWEREIRV
KIKNKWRLST IIVHGSSKKY GWDDICHYDI VLTTYGTLAS EYRRLIKWNE THPGKSLDES
ILKKNFPLVG PKSRFYRIIL DEAQSIKNRN TVSAKACFYL NATYRICLTG TPMMNNIAEL
YSVVLFLRVK PYNEWSRFNR DFGILSRSYG SEIAIESAMK KLQALLKAIL FRRTKNTLID
GKPIISLPPK IEEIQHVVFD DDESAFYNAL ESKTKIQFNK YLAAGSVGRN YSNILVLLLR
LRQACCHPHL IYDFDQASPA ESQVEEDEMI RLARSLAPNV IKRLLNCDGA FECPICYDGV
ENPRIIIPCG HDTCNECLAR ISDQQALQRA SEHEVGKEVV SKCPSCRGPL ILSKVIDYIS
FKKVHILDKK EIDENDVETE SDSETQSDDG SETEDEDEGS LNSDLRNFIV SGPKNDQDEA
NKSAANRKRY MKYLKSRWQP SAKISKCMEL VRKFLDEGQK ILIFSQFVSL LDLLQVPIEE
EKWNCLRYDG SMSADLRYAA VEKFCDSTTH NLMLLSLKAG NAGLNLVAAS RVIILDPFWN
PFIEMQAVDR AYRIGQQNIV EIHRILIKNT VEDRIVELQE KKRKLVDMAL DEGAARSLGR
LDEA
//
