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Database: UniProt
Entry: A0A1B8B416_FUSPO
LinkDB: A0A1B8B416_FUSPO
Original site: A0A1B8B416_FUSPO 
ID   A0A1B8B416_FUSPO        Unreviewed;       781 AA.
AC   A0A1B8B416;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=FPOA_01399 {ECO:0000313|EMBL:OBS27457.1};
OS   Fusarium poae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS27457.1, ECO:0000313|Proteomes:UP000091967};
RN   [1] {ECO:0000313|EMBL:OBS27457.1, ECO:0000313|Proteomes:UP000091967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2516 {ECO:0000313|EMBL:OBS27457.1,
RC   ECO:0000313|Proteomes:UP000091967};
RA   Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA   Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT   "Living apart together: crosstalk between the core and supernumerary
RT   genomes in a fungal plant pathogen.";
RL   Submitted (JUN-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   -!- 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:OBS27457.1}.
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DR   EMBL; LYXU01000001; OBS27457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8B416; -.
DR   STRING; 36050.A0A1B8B416; -.
DR   OMA; KVKVWRH; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000091967; 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; cd17917; DEXHc_RHA-like; 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:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 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   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:UP000091967}.
FT   DOMAIN          122..311
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          338..520
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          33..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   781 AA;  86864 MW;  67FE177280175B75 CRC64;
     MATDNNSGPP AKKRKTKSKD LNALTVGGKV ISLEGYLTAP PKPKEVDAKA SETTDSETPT
     TITATTVPEK KKDNTQQRPA KNHKDYQIKD RYNEKARSRE DPKLLKTRKQ LPIWQYREDI
     QQALRNNSDV LVLVGETGSG KSTQVPQFLY QEPWCRRQKI KLAGSDEEIS VGGTVAITQP
     RRVAATTLAH RVAQEAGTPL GKGRPDGLVG YSVRFDHQVP KGSRIKFLTE GMLLQELLRD
     PNLKNYSAIV VDEIHERSLD VDLLVGFLKQ ILSSDLSGRG GIPLKVVIMS ATADVEGIQE
     FFKDVRPKTQ DENLLQVLKI KGRQYPVTVH HEPRPVADLQ DALLKTIYKI HLQEQLPGDI
     LAFLTGQEEI EAAQKLIEEY AATLASNIPK IKVFPLYGQL SMDAQREAFL PVKASFTRKI
     VLATNIAETS VTVPGVRYVV DCGKAKVKQY RARLGMESLL AKPISKSSAV QRTGRAGREG
     PGKCFRLYPE TAFKTLQDSD LPEILRNDVL GAVLTMKARG IQDVLTFPLM DPPETEAIEK
     ALIHLHFLGA LNDDGTITKT GETMARFPIS APLGAVLLAA ANPEFDCVVE AIDIISCITS
     GEDIFLSIQS EEAQEEVETF RKELQRREGD IITYLTTIQQ YTAENADRVV WCKQRKINMR
     NMRQALNIRR QLRGMCLKEK LLDEAPPADP QPFIPISPER AEQVLKCFMR GFALKTAMLA
     PDSSYVTVQG KHVVAIHPAS VLHGQKKEAI MFLEHVYTNK NYAKKVSAIQ AVWIAEALEG
     K
//
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