ID A0A0S7DWF0_9EURO Unreviewed; 1293 AA.
AC A0A0S7DWF0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GIM38448.1};
GN ORFNames=ALT_000832 {ECO:0000313|EMBL:GIM38448.1}, CNMCM8060_001203
GN {ECO:0000313|EMBL:KAF4180510.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM38448.1};
RN [1] {ECO:0000313|EMBL:GIM38448.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM38448.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
RN [2] {ECO:0000313|EMBL:KAF4180510.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4180510.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF4180510.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4180510.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) 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:GIM38448.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BCLY01000008; GIM38448.1; -; Genomic_DNA.
DR EMBL; JAAAPS010000012; KAF4180510.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DWF0; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_4135; -.
DR Proteomes; UP000713487; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 1.20.1500.20; -; 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 InterPro; IPR040801; Ski2_N.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF8; HELICASE SKI2W; 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 Pfam; PF17911; Ski2_N; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 332..488
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 646..817
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 539..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1293 AA; 144654 MW; D00D8BD844492968 CRC64;
MAETVASILA GLNLNSENLS GSAFDAQLVE EEKGTYRHRG PRQRPRQSAS DLKAELEREF
LTPSPRFSSE WLNRLQKRWD VPVDYTDLYE IAPTQTRTIV RFTREGLEGR VTGYHEVTVP
AAAANAKNST SLLRRPAGRA DFVRGAAGFF PFAPGGLDGV EAIAEMESEA QAAERSRTGG
KQSGLDRIIN FGAEGGLLEI APGFSRGLQF EAAKTKETAE GDEEVEHALQ QEESDLHVER
DEDAVSDVEG GVKIGEDDEL SGEEDIDSLL PVEFPALEPR APLLGGVKQR QGGKEWAHVV
DVNKHIPNFH ELVPDMAREW PFELDTFQKE AVYHLENGDS VFVAAHTSAG KTVVAEYAIA
LASKHMTKAI YTSPIKALSN QKFRDFRTEF DDVGILTGDV QINPEASCLI MTTEILRSML
YRGADLIRDV EFVIFDEVHY VNDLERGVVW EEVIIMLPEH VTLILLSATV PNTYEFASWV
GRTKKKDIYV ISTAKRPVPL EHYLWAGKDK YKIVDSNKRF LETGWKEADN IISGRDKIKA
QKAAEAQAQS QAQRGGQQGR GRGQPAGRGA PRGNAQRGGA PRGRGQPANR GTGNIARTGR
GGGRTTAAQD KTIWVQLVGH LRKENLLPGC IFVFSKKRCE ENADSLSNQD FCNASEKSLI
HMFIEKSLTR LKPEDRTLPQ ILRLRELLSR GIAVHHGGLL PIMKEIVEIL FAKSLVKILF
ATETFAMGLN LPTRTVVFSG FRKHDGRGFR DLLPGEYTQM AGRAGRRGLD TVGYVIIVSA
GRDEAPPAGA LRKMILGDPT KLRSQFRLTY NMILNLLRVE ALKIEEMIKR SFSENATQAL
LPEHEKQVQL SEASLAKIKR EPCDICDIDL VACHDAAIEY EKLTSELHVG LLASPVGKRL
FMPKRLVVYR KDGFRTAGII VREGVGGGAS PSIQVLEIGK LSHRRHPSDI LPFLPRFRHL
LHPLPTRGAD MTLKVCKIPL SDLECVTNTM VKVGGPTWYL NIKKEAIKFA DKELSKLCAS
WTSPVWDEMD WARIKELQVR DILEKRQAQA AITQSCRCLQ CPSFLKHFEM QHDEWQVKEN
ISQLKQLMSD QNLQLLPDYE QRIQVLRDLG FIDEQSRVQL KGKVACEIHS ADELVLTELI
LENVLAEYEP EEIVALLSAF VFQEKTENVP TLTPRLEKGK EAIIRIAEKV NDLQIQYQVI
QSSEDSNDFA SQPRFGLAEV VYEWAKGMSF NRITDLTDVM EGTIVRTITR LDETCREVRN
AAKLVGDPTL YTKMQQAQEL IKRDVIFAAS LYM
//
