ID A2RAP7_ASPNC Unreviewed; 914 AA.
AC A2RAP7;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=An18g03910 {ECO:0000313|EMBL:CAK97428.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK97428.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK97428.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270404; CAK97428.1; -; Genomic_DNA.
DR RefSeq; XP_001398849.1; XM_001398812.1.
DR AlphaFoldDB; A2RAP7; -.
DR EnsemblFungi; CAK97428; CAK97428; An18g03910.
DR GeneID; 4989955; -.
DR KEGG; ang:An18g03910; -.
DR VEuPathDB; FungiDB:An18g03910; -.
DR HOGENOM; CLU_001832_6_1_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000006706; Chromosome 8L.
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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
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..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 102592 MW; F65B95ED14B855E6 CRC64;
MASNDQPPAK RLKSSNLPPQ LRDAKRKDID NWETNRMLTS GVAQRRDFDG DFMPEDEEGT
RVHLLVHDLR PPFLDGRTIF TKQLEPISAV RDPQSDMAVF SRKGSKVVRE RRQQRERQKQ
AQEATTMAGT ALGNLMGVKE DEGDSAVAMP VEDAYKSGNK FAQHLKKDEG GQSSFSKSKT
LREQREFLPA FAVREDLLRV IRDNQVVVVV GETGSGKTTQ LTQFLHEDGY SKFGMIGCTQ
PRRVAAMSVA KRVSEEMEVD LGDEVGYAIR FEDCTGPKTV IKYMTDGVLL RESLVQQDLD
KYSCIIMDEA HERALNTDVL MGLLKKVLAR RRDLKLIVTS ATMNAERFSR FYGGAPEFII
PGRTFPVDVH FSRTPCEDYV DSAVKQVLAI HVSQGPGDIL VFMTGQEDIE ATCELVDERL
KLLNDPPKLS ILPIYSQMPA EQQAKIFERA EPGVRKVIVA TNIAETSLTV DGIMFVVDSG
YSKLKVYNPK MGMDTLQITP ISQANANQRS GRAGRTGPGK AYRLYTEVAY KNELYLQTIP
EIQRTSLSNT VLLLKSLGVK DLLDFDFMDP PPQETITTSL FELWSLGALD NLGDLTPLGR
RMTPFPMDPP LAKLIITAAE TYGCSEEMLT IVSMLSVPSV FYRPRERQEE SDAAREKFFV
PESDHLTLLH VYTQWKANGY SDGWCTRHFL HAKALRRARE VRDQLHDIMT VQKMPLVSCG
TDWDEIRKCI CSGFYHQAAR VKGIGEFLNL RTSVSMQLHP TSALYGLGYV PEYVVYHELI
LTSKEYMSTV TAVDPHWLAE LGGVFYSVKE KGYSQRERRI TEQEFNRRVE IETQMAADRE
RAAAEKQREA ERNDPSRRRK EIEVGSVVRR PVATARRVGG VTASSSGGGA RNGGSGGGSV
VKKPQIKRKP GRAF
//
