ID A0A8E2F0A0_9PEZI Unreviewed; 1289 AA.
AC A0A8E2F0A0;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE SubName: Full=Antiviral helicase {ECO:0000313|EMBL:OCL07781.1};
GN ORFNames=AOQ84DRAFT_319442 {ECO:0000313|EMBL:OCL07781.1};
OS Glonium stellatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Gloniales; Gloniaceae; Glonium.
OX NCBI_TaxID=574774 {ECO:0000313|EMBL:OCL07781.1, ECO:0000313|Proteomes:UP000250140};
RN [1] {ECO:0000313|EMBL:OCL07781.1, ECO:0000313|Proteomes:UP000250140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 207.34 {ECO:0000313|EMBL:OCL07781.1,
RC ECO:0000313|Proteomes:UP000250140};
RX PubMed=27601008; DOI=10.1038/ncomms12662;
RG DOE Joint Genome Institute;
RA Peter M., Kohler A., Ohm R.A., Kuo A., Krutzmann J., Morin E., Arend M.,
RA Barry K.W., Binder M., Choi C., Clum A., Copeland A., Grisel N.,
RA Haridas S., Kipfer T., LaButti K., Lindquist E., Lipzen A., Maire R.,
RA Meier B., Mihaltcheva S., Molinier V., Murat C., Poggeler S., Quandt C.A.,
RA Sperisen C., Tritt A., Tisserant E., Crous P.W., Henrissat B., Nehls U.,
RA Egli S., Spatafora J.W., Grigoriev I.V., Martin F.M.;
RT "Ectomycorrhizal ecology is imprinted in the genome of the dominant
RT symbiotic fungus Cenococcum geophilum.";
RL Nat. Commun. 7:12662-12662(2016).
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; KV749787; OCL07781.1; -; Genomic_DNA.
DR OrthoDB; 64767at2759; -.
DR Proteomes; UP000250140; 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; -; 1.
DR Gene3D; 1.20.1500.20; -; 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:OCL07781.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000250140};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 328..484
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 193..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..590
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1289 AA; 144854 MW; BBCBE715C12A2083 CRC64;
MNGLTDALAK VHLAAQSLGT EDPNWIDSIL DQQRPRKRSR QTKEELKQEL EKEFLCPSTS
FNTKWLNELQ QRWEAPTNYS ELFEIAPTQT RTIIRFTREG LEGRVTGYKE ITVPASSATA
KNSTSLLRKP ANRANFVRGA AGFFPFAPGG LDGVEAIAAL EDEAISRQEH ERAKKQSGLD
RVINFGAEGG LLEMPPGFPR GLKSQKKPPE DNKTAEEVEE VLGEEPEPSL DTDISGKSDA
DDVLDADGIS NLNAESEAEG DEDIDSLLPV EFPALAPRGQ LGMASKRGGK EWAHMVDVNR
EIPNFRELVP DMAREWPFEL DTFQKEAVYH LENGDSVFVA AHTSAGKTVV AEYAISLAAK
HMTKAIYTSP IKALSNQKFR DFRATFDDVG ILTGDVQIRP EASCLIMTTE ILRSMLYRGA
DLIRDVEFVI FDEVHYVNDL ERGVVWEEVI IMLPEHVTLI LLSATVPNTY EFASWVGRTK
KKDIYVISTP KRPVPLEHYL WANKAMHKIV TADKKFIESG WKDANDALSG KDKVKPVSVA
EEPADARGGG AQRRGNRGQN QRGGPQRGGS QQRGGSQQRG RGQPVQRGRG NIARTGRGVG
RTTAAQDRNI WVHLIQHLRN KELLPACIFV FSKKRCEENA EALSNLDYCT AAEKSAIHMI
IEKSIARLKP EDRVLPQIRR LRELLGRGIA VHHGGMLPIV KEVVEILFAR TLVKVLFATE
TFAMGLNLPT RTVVFSGFRK HDGRAFRDLL PGEYTQMAGR AGRRGLDPVG SVIIVTPGAE
EAPPVARLRQ MILGDPTKLR SQFRLTYNMI LNLLRVEALK IEEMIKRSFS ENATQALLPE
HEKKVKLSEA DLENIKREPC DICDIDLKEC HQACMNVQRL TAELHLAVLA TPVGRRIFSP
KRLLVYKKGG IRSAGMLLRE GISKGVEPTV QVLEISTNPH CQPSDLLPYL PGFSEFFAPL
PRKESDMVLK TVFIPLSDVE CVTRTLLKVP QSLESLMKRS DALELARDQL IPVCKSWTYK
DWDEQDWERI RDLSFRNILD SRKREADIAQ HRACIKCPKF PQHFAMQHKE WLIRENIAQL
RQLMSDQNLQ LLPDYEQRIS VLKDLGFIDE NSRVELKGKV ACEIHSADEL VLTELILENV
LADYEPEEIV ALLSAFVFQE KTDVTPTLTT NLERGIAKII EISEKVNHIQ TVHQVILSAD
DSNDFVSRPR FGMVEVVYEW ARGMSFNRIT DLTDVMEGTI VRVITRLDET CREAKNAARI
IGDPTLFSKM QTAQDLIKRD ICSCASLYL
//
