ID A0A319CX60_9EURO Unreviewed; 1290 AA.
AC A0A319CX60;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Antiviral helicase {ECO:0000313|EMBL:PYH89654.1};
GN ORFNames=BO71DRAFT_389226 {ECO:0000313|EMBL:PYH89654.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH89654.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH89654.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH89654.1,
RC ECO:0000313|Proteomes:UP000247810};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; KZ826019; PYH89654.1; -; Genomic_DNA.
DR STRING; 1448320.A0A319CX60; -.
DR Proteomes; UP000247810; 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, ECO:0000313|EMBL:PYH89654.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000247810};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 329..485
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 613..814
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 231..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1290 AA; 144184 MW; 5A02884D72153E08 CRC64;
MTESLTSALA ELTLHSQSVN GSAFDARLAD EENGVYRDCK PRQKARQNAA DLEAELERNF
LTPSSEFSPE WLNRLQRKWD VPTDYTDLFE VAGTQTRTIV RFDRDGLEGR VTGYHEVTVP
ATSANAKNST SLLRRPAGRA DFVRGAAGFF PFAPGGLEGV EAIAEMESET QTAEPRTGGK
QSGLDRIINF GAEGGLLEVA PGLSRGLKFE EAKTKEAAEG DEEVEHALQQ EESDLHVEQD
ETASDAGGVK IDEDAELSDE EDIDSLLPVE FPALEPHAPL LAGVQQRKTG REWAHVVDVN
KDIPNFRELV PDMAREWPFE LDTFQKEAVY HLECGDSVFV AAHTSAGKTV VAEYAISLAA
KHMTKAIYTS PIKALSNQKF RDFRTEFDDV GILTGDVQIN PEASCLIMTT EILRSMLYRG
ADLIRDVEFV IFDEVHYVND LERGVVWEEV IIMLPEHVTL ILLSATVPNT YEFASWVGRT
KKKDIYVIST AKRPVPLEHY LWGGKGKYKI VDSNKRFLES GWKEADEIIS GRDKIKAQKA
AEAQAQSQAS RGAPQGRGRG QAGGRGAPRG NAQRGGAPRG RGQPANRGTG NIARTGRGGG
RTTAAQDKTV WVQLVQHLRK ENLLPGCIFV FSKKRCEQNA DSLSNQDFTT ASEKSLTHMF
IEKSLTRLKP EDRTLPQILR LRDLLSRGIA VHHGGLLPIM KEIVEILFAK SLVKVLFATE
TFAMGLNLPT RTVVFSGFRK HDGKSFRDLL PGEYTQMAGR AGRRGLDTVG YVIIVNPGRD
EAPPAGALRR MILGDPTKLR SQFRLTYNMI LNLLRVEALK IEEMIKRSFS ENATQALLPE
HEKQVQLSEA SLAKIKREPC DICDIDLATC HDAAIEYEKL TSELHVGLLS SPVGKRLFVP
KRLIVYRKEG YRTAGIIVRE GVVGGQAPCI QVLEIGKLGS RRHPSDILPF LPGFKHLLQS
LPTRSADMAL KSYKVPLLDL ECVTSTVVKL GGPIWYLNIK KEAIKFADKE LSKHCASWTT
PVWEEMDWAR IKELQVRDIL EKRQKQAAIA QSCKCLQCPS FLKHFEMQHD EWQVKENISQ
LKQLMSDQNL ALLPDYEQRI QVLKELGFVD EQSRVQLKGK VACEIHSADE LVLTELVLEN
VLAEYEPEEI VSLLSAFVFQ EKTENVPTLT PRLEKGKEAI VRISERVNDF QIQHQVIQTS
EDSNDFASQP RFGLAEVVYE WAKGMSFNRI TDLTDVMEGT IVRTITRLDE TCREVKNAAK
LVGDPNLYTK MQEAQELIKR DVIFAASLYM
//
