ID B0Y5Q8_ASPFC Unreviewed; 1082 AA.
AC B0Y5Q8;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=ATP dependent RNA helicase (Dob1), putative {ECO:0000313|EMBL:EDP50093.1};
GN ORFNames=AFUB_064250 {ECO:0000313|EMBL:EDP50093.1};
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:EDP50093.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP50093.1, 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 -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; DS499598; EDP50093.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y5Q8; -.
DR EnsemblFungi; EDP50093; EDP50093; AFUB_064250.
DR VEuPathDB; FungiDB:AFUB_064250; -.
DR HOGENOM; CLU_002902_0_1_1; -.
DR PhylomeDB; B0Y5Q8; -.
DR Proteomes; UP000001699; 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:EDP50093.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 169..325
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 405..609
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 370..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 122648 MW; EDE5CB3B500A9269 CRC64;
MDELFDVFED QPQAAAKVTD VAPKRPKKDK SKKRQVNGDV KENGAATEPK EDIEIPDAPT
GELADGEQAE APATENNEQQ PDAKRPRLEK EPQPVLADEF ETAQEREVAA SAGLQAAKET
TSVKLSHQVR HQVAIPPNYP YVPISQHKPP ENPARVWPFT LDPFQQVAVA SIQREESVLV
SAHTSAGKTV VAEYAIAQSL KNNQRVIYTS PIKALSNQKY REFAAEFGDV GLMTGDVTIN
PTATCLVMTT EILRSMLYRG SEIMREVAWV IFDEIHYMRD AIRGVVWEET IILLPDKVRY
VFLSATIPNA MQFAEWIVKM HNQPCHVVYT DFRPTPLQHY FFPAGGEGIF LVVDEKGAFR
EENFQKAMGS IADKKGDDPS DAMAKRKGKG KDKRLNKGGN EGPSDIYKIV KMIMLKNLNP
VIVFSFSKRE CEACALKMST LAFNDDSEKE MVSKVFNSAI EMLSEEDRNL PQIQNILPLL
RRGIGVHHSG LLPILKETIE ILFQEGLIKV LFATETFSIG LNMPAKTVVF TSVRKFDGFS
QRWVTPSEFV QMSGRAGRRG LDDRGIVIMM VGEEMDPAVA KEIVRGEQDR LNSAFHLGYN
MILNLMRVEG ISPEFMLERC FYQFQNTAGV ADLEKQLQEF EEKRANMTIP DEGTIREYYE
LRTQLDKYAD DIQAVISYPD YSLPFMLPGR LVHIKHKDKD FGWGVVVNYK QRKPPKNSTE
EIPRDKRYVV DVLLNIAEGP SVATKTFEEL PSGVRPVKEG ENSRMEVVPV LTECIRAISH
IRMKLPKDLN PKEAKNGVKK SLAEIHKRFP DGIATLDPIE DMNIKDESFK KLLRKVEVLE
SRLLSNPLHN SPRLPELYEQ YSEKVELGTK IKETKKKISE AMSIMQLDEL KCRKRVLRRF
GFINEAEVVQ LKARVACEIS TGDELMLSEL LFNGFFNKLT PEQIAAVLSV FVFEEKSKET
PALTRDELAK PLKEIQAQAR IVAKVSQESK LAVNEEEYVN SFHWELMEVI YEWANGKSFA
DICGMTDVYE GSLIRVFRRL EECLRQMAQA SKVMGNEELE SKFEEALTKV RRDIVAAQSL
YL
//
