ID B0XNA1_ASPFC Unreviewed; 915 AA.
AC B0XNA1;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=AFUB_004230 {ECO:0000313|EMBL:EDP55726.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP55726.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP55726.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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 PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR EMBL; DS499594; EDP55726.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XNA1; -.
DR EnsemblFungi; EDP55726; EDP55726; AFUB_004230.
DR VEuPathDB; FungiDB:AFUB_004230; -.
DR HOGENOM; CLU_001832_6_1_1; -.
DR PhylomeDB; B0XNA1; -.
DR Proteomes; UP000001699; 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:0004386; F:helicase activity; 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; 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:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 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 Helicase {ECO:0000313|EMBL:EDP55726.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 198..361
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 383..558
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 102885 MW; 5C9798D1A4130336 CRC64;
MASDGMPPAK RLKSSNLPPH LRDAKRKDID NWETNRMLTS GVAQRRDFEG DFLPEDEEGT
RVHLLVHDLR PPFLDGRTIF TKQLEPISAV RDPQSDMAVF SRKGSKVVRE RRQQRERQKQ
AQEATTMAGT ALGNIMGVKE DEGDSAVAMP VEDTYRSGNK FAQHLKKDEG GQSSFSKSKT
LREQREYLPA FAVREELLRV IRDNQVIVVV GETGSGKTTQ LTQFLHEDGY SKYGIIGCTQ
PRRVAAMSVA KRVSEEMEVD LGAEVGYAIR FEDCTSKDTV IKYMTDGVLL RESLVQPDLD
KYSCIIMDEA HERALNTDVL MGLLKKVLAR RRDLKLIVTS ATMNSERFSR FFGGAPEFII
PGRTFPVDLH FSRTPCEDYV DSAVKQVLAI HVSQGPGDIL VFMTGQEDIE VTCELIDERL
KMLNDPPKLS ILPIYSQMPA EQQAKIFERA PPGVRKVIVA TNIAETSLTV DGIMFVVDSG
YSKLKVYNPR MGMDTLQITP ISQANANQRS GRAGRTGPGK AYRLYTESAY KNELYIQTIP
EIQRTSLSNT VLLLKSLGVK DLLDFDFMDP PPQETISTSL FELWSLGALD NLGDLTPLGR
AMTPFPMDPP LAKLLITASE EYGCSEEMLT IVSMLSVPSV FYRPKERQEE SDAAREKFFV
PESDHLTLLH VYTQWKSNGY SDGWCMKHFL HPKALRRAKE VREQLHDIMT VQKMRLVSCG
TDWDVIRKCI CSGFYHQAAK VKGIGEFINL RTSVSMQLHP TSALYGLGYV PEYVVYHELI
LTSKEYMSTV TAVDPHWLAE LGGVFYSVKE KGYSQRERRV TEQEFNRRME IETQMAADRE
RAAAEKLREQ ERNDPSRRKK EVEAGSVVRR PAVTGARRIG GVTASSTTRN GTNGASGGGT
VVKKPQIKRR PGRAF
//
