ID A0A317W378_9EURO Unreviewed; 1205 AA.
AC A0A317W378;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=BO94DRAFT_496606 {ECO:0000313|EMBL:PWY80963.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY80963.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY80963.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY80963.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
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:PWY80963.1}.
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DR EMBL; MSFK01000021; PWY80963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317W378; -.
DR STRING; 1450535.A0A317W378; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000246702; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17982; DEXHc_DHX37; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PWY80963.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000246702}.
FT DOMAIN 373..550
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 573..818
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..271
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1205 AA; 134151 MW; 93DE17962B9DA6AB CRC64;
MPKFVPRQRK QKHRQREATN VPVDTNVAEL APVSKSEKDA KRQQLKEELR AQHAQVSSKK
QKRLDKYIEN KLKKEENLEL LKKLAQSKVD TSALQSSREL GKRKRQDERV PVSTAEDHDS
RLDSDLSDDD SDDSLPPSKA IASGSRQDAP AQKPAEDPAT GSGLKRPLQL GPDGFPVLKK
RKQAPKKPEI TITMPEVPWE GFGSGDEDQS GEDDEDSEKT SEDGSSDAES GSDEEDEEDE
EDEDCSEDEE DEDEDEEEEE EEEEEEEEEE EENHKVGKPR QSAFKTWARQ QINDAVGFKP
ATVPVVSEPM PFILEPKKPV RNTVYEEEPL PLELQVTKGD PNRKAFSVQV NRSEEIQNSR
LGLPVVGEEQ KIMEAIYNNS AIVIWGATGS GKTTQLPQFL FEAGYGNPDS PSPGIIGVTQ
PRRVAAVSMA KRVGDELGEF SEQVSYQIRF ESTASSKTAI KFMTDGILIR EIAEDFSLSK
YSVIVIDEAH ERSVNTDILI GMVSRIVDLR KAMREEDPSV KPLKLVVMSA TLRISDFTQN
PNLFRQGPPP LVQAEGRQYP VTVHFSRRTN RDYVEEAFRK VSRGHRKLPP GAMLVFLTGQ
NEIRQLSKRL KQAFKPTQRG EATQAKVQIT ANDAPLEAED LEIGGADLSI AGNQEDDGSD
YEITGLDEAE EDEDEFDLDE EAMSSSTRVH VLPLYSQLPT KEQLRVFEPP PEGSRLIVLA
TNVAETSLTI PGIKYVFDCG RAKEKQYDLA TGVQKFQIEW ISKASANQRA GRAGRTGPGH
CYRLYSSAIY ENEFAEYTDP EILRTPIEGV VLQMKSMGLH NVINFPFPTP PSRQGLAKAE
KLLKNLGALT AEGKITPIGN RLSTYPLSPR FGKMLYVGHQ HGCMPYIIAL VSALAVGDLF
VPQNQIDPVP AKDGDEAKGV YTNADRLEDT AREQRHKDYA RAHRLFSKHD DTSDALKYLS
AICAYGYASD GDSFCEQMFL RAKAFKEATQ LRRQLTDIVR SNNPGLVQAY QARLPEPSEK
QVKAIKQIVT AGFIDNVALR ADLAPVPPEM HRTPKRAIDV PYFTLMQSRE GPGMELDDKA
VYVHPSSIIA QLSAKEMPQY IVYSHLQQSS PSVVSADQTP KIRMFPLAAP SGLQLSALAH
GTPLIEYGKP IGKTDLIEGI PQRRSCWVIP SLVGEAGGSR WPLPAKKVIQ RKDAKEGWVI
EKFTS
//
