ID A0A0L1J4T4_ASPNO Unreviewed; 1211 AA.
AC A0A0L1J4T4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=ANOM_005648 {ECO:0000313|EMBL:KNG86690.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG86690.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG86690.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG86690.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KNG86690.1}.
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DR EMBL; JNOM01000106; KNG86690.1; -; Genomic_DNA.
DR RefSeq; XP_015407613.1; XM_015550905.1.
DR AlphaFoldDB; A0A0L1J4T4; -.
DR STRING; 1509407.A0A0L1J4T4; -.
DR GeneID; 26807452; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd17971; DEXHc_DHX8; 1.
DR CDD; cd21691; GH2-like_DHX8; 1.
DR CDD; cd05684; S1_DHX8_helicase; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR044762; DHX8/Prp22_DEXHc.
DR InterPro; IPR049588; DHX8_GH2-like.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049621; S1_DHX8_helicase.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 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 Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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.
DR PROSITE; PS50126; S1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:KNG86690.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505}.
FT DOMAIN 242..313
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 557..720
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 738..918
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 133..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 136196 MW; 45965CE2F0AF74DC CRC64;
MDDLQSLELF SLVSRITSEL QNHLGINDKT LAEFVIDQHL KCGSFSKFKE SLDEMGAEFP
QSLMESIDRL VLTMHPKYKT KKTDGADKAE GNDDMDLLDA LEKKGARIQR KNADEGDAKA
DAMDDTFAML EGLAGKAREE KGRTTGEDRS SRKRSRSPGY EDYDRGRRRK DKYRSRSRSY
SPPHRKRDDD VDEFGRTRSK YSSRDEYRDG HSERRRRRDD RGQDDHFRKP PPIELDDAPI
LYKVYDGRVT GVKDFGAFVN LLGVKGKVDG LVHVSAMQEG ARVNHPSDLV SRGQPVKVKV
ISIQGSRIGL SMKEVDQVTG LDLIPQRRLA SGANMERLDG TSANERYGNL SSEVPVIEDS
DGRPMKNRKR LTSPERWEIR QLIASGVVSA ADYPDLDEEY HATLTGEGTF EEEEDIDIEV
RDEEPPFLAG QTKMSLELSP IRVVKAPDGS MNRAAMAGTN LAKERRDLRQ QEAQDKAAEQ
AAEVDLNAQW QDPMAAPEDR KFAADLRTAQ QPKADDAVPE WKRVTMGKNQ SLGKRTSMSI
KQQRESLPVF KFRKQLLDAV RDNQLLIVVG DTGSGKTTQL TQYLAEAGYG NNGMIGCTQP
RRVAAMSVAK RVAEEVGCKL GAEVGYTIRF EDCTSPETRI KYMTDGMLQR EVLLDPDLKK
YSVIMLDEAH ERTIATDVLF GLLKKTIKRR PDLRLIVTSA TLDAEKFSEY FNGCPIFSIP
GRTFPVEIMY SKEPESDYLD AALITVMQIH LTEPSGDILV FLTGQEEIDT SCEILYERMK
ALGPSVPELV ILPVYSALPS EMQSRIFEPA PPGGRKVIIA TNIAETSITI DNIYYVIDPG
FVKQNAYDPK LGMDSLVVTP ISQAQAKQRA GRAGRTGPGK CFRLYTEAAY QSEMLPTTIP
EIQRQNLSHT ILMLKAMGIN DLLHFDFMDP PPTNTMLTAL EELYALSALD DEGLLTRLGR
KMADFPMEPA LAKVLIASVD MGCSEEILSI VAMLSIQSVF YRPKEKQQQA DQKKAKFHDP
QGDHLTLLNV YNGWKNSKFN NAWCFENFIQ ARQIRRAQDV RQQLLGIMDR YHHRIVSCGR
NTTKVRQALC TGFFRNAARK DPQEGYKTLV EGTPVYMHPS SALFGKPAEH VIYHTLVLTT
KEYMHCTTAI EPKWLVEAAP TFFKVAPTDR LSKRKKAERI QPLHNRFAGE DDWRLSAQRR
QGRGGGGGTW G
//
