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Database: UniProt
Entry: A0A0L1IUZ0_ASPNO
LinkDB: A0A0L1IUZ0_ASPNO
Original site: A0A0L1IUZ0_ASPNO 
ID   A0A0L1IUZ0_ASPNO        Unreviewed;      1080 AA.
AC   A0A0L1IUZ0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Putative ATP dependent RNA helicase (Dob1) {ECO:0000313|EMBL:KNG83386.1};
GN   ORFNames=ANOM_007737 {ECO:0000313|EMBL:KNG83386.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG83386.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG83386.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG83386.1,
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   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010140}.
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:KNG83386.1}.
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DR   EMBL; JNOM01000272; KNG83386.1; -; Genomic_DNA.
DR   RefSeq; XP_015404309.1; XM_015552993.1.
DR   AlphaFoldDB; A0A0L1IUZ0; -.
DR   STRING; 1509407.A0A0L1IUZ0; -.
DR   GeneID; 26809541; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000037505; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR   CDD; cd18024; DEXHc_Mtr4-like; 1.
DR   CDD; cd13154; KOW_Mtr4; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 1.
DR   Gene3D; 2.40.30.300; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR048392; MTR4-like_stalk.
DR   InterPro; IPR025696; MTR4_beta-barrel.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016438; SKI2-like.
DR   InterPro; IPR012961; Ski2/MTR4_C.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21408; MTR4-like_stalk; 1.
DR   Pfam; PF13234; MTR4_beta-barrel; 1.
DR   PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KNG83386.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037505}.
FT   DOMAIN          167..323
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          406..607
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1080 AA;  121987 MW;  92615D4BD358CFD2 CRC64;
     MDELFDVFED QPQAVKPSDG APKRSKKDKS KKRQVNGDVK ESGATVEAKE PVAVADAPVE
     ETSEPEEGDA PTTDNNEQPD AKRPRLEKEP EPVVADLFET AQEREVAGSA GLQAANDSAS
     VVLSHQIRHQ VAIPPNYPYV PISEHKAPEN PARVWPFTLD PFQQVSIASI QREESVLVSA
     HTSAGKTVVA EYAIAQSLKN NQRVIYTSPI KALSNQKYRE FAAEFGDVGL MTGDVTINPT
     ATCLVMTTEI LRSMLYRGSE IMREVAWVVF DEIHYMRDAT RGVVWEETII LLPDKVRYVF
     LSATIPNAMQ FAEWIVKMHN QPCHVVYTDY RPTPLQHYFF PAGAEGIHLV VDEKGVFREE
     NFQKAMSTIA DKKGDDPADA MAKRKGKGKD KKLNKGGNKG PSDIFKIVKM IMIKNYNPVI
     VFSFSKRECE SGALQMSNLA FNDDSEKEMV SKVFNSAIEM LSEEDRNLPQ IQNILPLLRR
     GIGVHHSGLL PILKETIEIL FQEGLIKVLF ATETFSIGLN MPAKTVVFTS VRKFDGFSQR
     WVTPSEFIQM SGRAGRRGLD DRGIVIMMVG EEMDPAVAKE IVRGEQDRLN SAFHLGYNMI
     LNLMRVEGIS PEFMLERCFY QFQNTAGVAT LEKELAELEE KRANMTISDE GTIREYYDLR
     KQIRQFTDDM QAVISHPNYC LPFIQPGRLI SIKHKDVDFG WGVVVNYKQR KPPKNSTEEP
     TPYQKYVVDV LLRIADGPSV GTKTFEELPS GVRPPKEGEN SRMEVVPVVL SCVHSISHIR
     IFLPKDLRSA DSKNGVKKAL DEVQKRFPDG IAVLDPIENM NIKDDNFKKL LRKIEVLESR
     LLSNPLHNSP RLPELYEQYS DKVETGSKIK ATKKKISEAM SIMQLDELKC RKRVLRRFGF
     INEAEVVQLK ARVACEISTG DELMLSELLF NGFFNNLTPE QVASVLSVFV FEEKSKETPA
     LTRDELAKPL KEIQAQARIV AKVSQESKLA VNEEEYVQSF HWELMEVIYD WANGKSFADI
     CKMTDVYEGS LIRVFRRLEE CLRQMAQAAK VMGSEELESK FETALTKVRR DIVAAQSLYL
//
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