ID A0A2P8A2W4_9PEZI Unreviewed; 1089 AA.
AC A0A2P8A2W4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PSK54812.1};
GN ORFNames=B9Z65_3901 {ECO:0000313|EMBL:PSK54812.1};
OS Elsinoe australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK54812.1, ECO:0000313|Proteomes:UP000243723};
RN [1] {ECO:0000313|EMBL:PSK54812.1, ECO:0000313|Proteomes:UP000243723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:PSK54812.1,
RC ECO:0000313|Proteomes:UP000243723};
RA Cheng Q.;
RT "Draft genome sequence of Elsinoe australis.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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:PSK54812.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NHZQ01000072; PSK54812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8A2W4; -.
DR STRING; 40998.A0A2P8A2W4; -.
DR Proteomes; UP000243723; 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; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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 InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45626:SF14; ATP-DEPENDENT DNA HELICASE (EUROFUNG); 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000243723}.
FT DOMAIN 323..513
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 861..1022
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..740
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1089
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1089 AA; 119861 MW; 01B5BE9E9E261815 CRC64;
MANERPQVQA TASLTPSNAN SQNQPPTASG AGVQKPPHAP VSSAGQHAEF GKTSPLRNPL
KQHSNIFNPN PRRPEHHRPN GPQNFYRPGQ KPLSNAQMFP QPDMAVKSQS QSYGPSSREG
FYLPGQKRQN VPTAGPTPAL SADFFEISKP TNAPSRPIQA APKPMFSSLG PNTTFVPFKP
AMPKGQGSPI VIDDDDDGFN PDAALRDDRF GAVDPYMYVD PSKAGEDIKA LLEGAFDDDE
ERPKTRLRNR ARKATPDKPK TQTLADKLAN LDVKDEKSEK TDEKDVEDDD EEDGTVEGMA
VKLLPHQVDG VSWMLDKEVG ERKKNGVLPK GGILADDMGL GKTIQSVTLI LTNPRPAVDA
KAPEGTKRKM PGKEVGKGTL VIAPLALIKQ WESEIKTRVS SSHALKVLVH HGSNRTKSHL
ELKKYDVVIT TYQIIASEHA GSSDQDEGVK VGCFGVHWYR IILDEAHSIK NRRAKSTQAC
CALKSWYRWC LTGTPMQNNL DELQSLIHFL RIKPYNDLTH WKQQITGPMK NGKGQFAIKR
VQYFLKAFMK RRTKDILKQE GALNFGGKKD VEGKKSQGMQ IVKRDIESVI CELDDYERDF
YDKLAQRAND RLQDMMGGEK TDYIGALVLL LRLRQACNHP QLIKSAMQSD KDALATAGIG
GSQSPRKAST ATSEVDDLAD LLGGLDVKTK SCDVCQAKLD SELVQKGAVR CADCEADLSV
ERVQHSHKKS HKHKSKKESK PDTKRRQPRK VILDSSDEDE DEGEGDWLVS PSQQKSNLGR
AGGTDDEDAE GGGRTLDSID SETGSEESDD NMIVRKSAHR STARQSSSTA STNSTNSTDS
DSDSSPSSPT TFSSTSYPST KIRRLLKILK SETPTHKVIV FSQFTTMLDL IQPHLQISRI
PFVRYDGSLP NPVREAALHS LRNDASVRVL LCSLKCGSLG LNLTAASRVV IVEPFWNPFV
EEQAIDRVHR LNQTVDVKVY KLTVKESVEE RILELQAKKR ELANAAIEGG KAVGKLSMRD
LLGLFGGDFD RVGTAGGQEK AQGLLHGVAP SGREERGTVA VQGRGEDPRR QMQRGGKGRR
EEDPVYGRR
//
