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
//