ID A0A6A6UPD5_9PEZI Unreviewed; 1290 AA.
AC A0A6A6UPD5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 10-JUN-2026, entry version 22.
DE SubName: Full=Antiviral helicase {ECO:0000313|EMBL:KAF2672754.1};
GN ORFNames=BT63DRAFT_396477 {ECO:0000313|EMBL:KAF2672754.1};
OS Microthyrium microscopicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Microthyriales; Microthyriaceae;
OC Microthyrium.
OX NCBI_TaxID=703497 {ECO:0000313|EMBL:KAF2672754.1, ECO:0000313|Proteomes:UP000799302};
RN [1] {ECO:0000313|EMBL:KAF2672754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 115976 {ECO:0000313|EMBL:KAF2672754.1};
RA Haridas S., Albert R., Binder M., Bloem J., LaButti K., Salamov A.,
RA Andreopoulos B., Baker S., Barry K., Bills G., Bluhm B., Cannon C.,
RA Castanera R., Culley D., Daum C., Ezra D., Gonzalez J., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B., Goodwin S., Spatafora J., Crous P.,
RA Grigoriev I.;
RT "101 Dothideomycetes genomes: a test case for predicting lifestyles and
RT emergence of pathogens.";
RL Stud. Mycol. 0:0-0(2020).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; MU004231; KAF2672754.1; -; Genomic_DNA.
DR OrthoDB; 64767at2759; -.
DR Proteomes; UP000799302; Unassembled WGS sequence.
DR GO; GO:0055087; C:Ski complex; IEA:TreeGrafter.
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:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IEA:TreeGrafter.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR FunFam; 3.40.50.300:FF:000354; ATP-dependent RNA helicase SKI2; 1.
DR FunFam; 3.40.50.300:FF:000987; DEAD/DEAH box RNA helicase; 1.
DR FunFam; 1.10.3380.30:FF:000001; Ski2 ATP-dependent RNA helicase; 1.
DR Gene3D; 1.10.3380.30; -; 2.
DR Gene3D; 2.30.30.1160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR025696; Beta-barrel_MTR4.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR050699; RNA-DNA_Helicase.
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:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL-RELATED; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KAF2672754.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000799302};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 324..480
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 614..815
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 201..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..574
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..596
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1290 AA; 145575 MW; 13EAAC8DAC13FE37 CRC64;
MESLASALEK FQLAANSITD DAYIDDILDE SRPRKRVRKT KEQLKKELED EFLTPSPSFS
THWLNQLQER WKTPINHAEL FRIAPTQTRT VIRFNREGLE GKVTGYNEIT VPASSATAKN
STSILRKPAN RAEFVRGAAG FFPFTPGGLD GVEAIAAIED QALLLEENVK AKKTGGLDRV
INFAAEGGLL EIAPGLPRGI REQKISEEEK KDAKEVEKAL DEEPEPTPSN ANGNQNTLEA
LLAADDEDED EDQSGDEDID ALLPIEFPAL APRGDLSMHQ DRKSRREWAH MVDVNRDITN
FKELVPDMAR DWPFELDTFQ KEAVYHLESG DSVFVAAHTS AGKTVVAEYA IALAAKHMTK
AIYTSPIKAL SNQKFRDFRN EFDDVGILTG DVQIRPEASC LIMTTEILRS MLYRGADIIR
DVEFVIFDEV HYVNDLERGV VWEEVIIMLP EHVTLILLSA TVPNTYEFAS WVGRTKKKDI
YVISTLKRPI PLEHYLWAGK EMHKIVNSEK QFLELGWKAA NDVIQGKDKV KAPAFNEEQP
ASRGGNLRGS GRGTNHRGQP NRGGPQRGGG GRGGSSQQSR GRGLPSHTGR GNIARTGRGG
GRTTAAQDRN VWVNLVQHLR KAELLPACIF VFSKKRCEEN AAALSNMDYC TAAEKSAIHM
TIEKSVARLK PEDRQLPQIL KLRELLGRGF AVHHGGMLPI LKEVVEILFA KSLVKVLFAT
ETFAMGLNLP TRTVVFSGYR KHDGRSFRDL LPGEYTQMAG RAGRRGLDTV GTVIIVAPGA
DEAPPVQRLR QMMLGDPTKL RSQFRLTYNM ILNLLRVEAL KIEEMIKRSF SEDATQALLP
EHEKQVNISQ ANLAKIKREP CDICDVDLEK FHQACMNYER INSELHVKLL GHPFARRVFE
PKRLVVFKHE GIRKVGMLIQ EGFNRGQEPT LPIIEFSSRS KRDRSDALPF IAKVSEYFEP
LPKKFKDISF RICVVPAKDI ERVTQAKINV ESPLKFLNAK VNTQKLAEDE ILPLCQNWKF
RDWNEFSWSK IKAMELREVI AAREKEVEVA LSCSCLKCPN FLKHFTAEHD EWLIKETIAE
LQQLMSDQNL RLLPDYEQRI EVLKELGFID EHSRVELKGK VACEIHTADE LVLTELILEN
VLADYEPEEI VALLSAFVFQ EKTDSVPTLT SNLEKGRDKI IEISERVNSV QTKWQVIQSA
DDSNDFVSQP RFGMVEVVYE WARGMSFNRI TDLTDVMEGT IVRVISRLDE TCREAKNAAR
IIGDPALYQK MTTCQELIKR DVCAVASLYM
//
