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
//