ID A0A319BS61_ASPLB Unreviewed; 1087 AA.
AC A0A319BS61;
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:PYH59712.1};
GN ORFNames=BO96DRAFT_443803 {ECO:0000313|EMBL:PYH59712.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH59712.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH59712.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH59712.1,
RC ECO:0000313|Proteomes:UP000247441};
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 (DEC-2016) 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; KZ821342; PYH59712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319BS61; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000247441; 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:PYH59712.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 174..330
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 442..614
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1087 AA; 123537 MW; DAEA308C00800CC7 CRC64;
MDELFDVFED QPQAVRPADG APKRAKKDKS KKRQVNGDVK EDGAATETPT ETPEDVEFTD
APVVEEEEDE AKEDEESPAA DNNEQPDAKR PRLEKEPEPV VADSFETEQE REVAGSAGLQ
GVNDSTSVKL SHQVRHQVAI PPKYPYVPIS EHKPPETPAR VWPFTLDPFQ QVAIASIQRE
ESVLVSAHTS AGKTVVAEYA IAQCLKNNQR VIYTSPIKAL SNQKYREFAE EFGDAGLMTG
DVTINPTATC LVMTTEILRS MLYRGSEIMR EVAWVIFDEI HYMRDAIRGV VWEETIILLP
DKVRYVFLSA TIPNAMQFAE WVTKMHNQPC HVVYTDFRPT PLQHYFFPNG SEGMHLIVDE
KGVFREENFQ KAMSSIADKR GDDPSDAMAK RKGKGKDKRL NKGGTQEKSD IFKIVKMVML
KNLNPVIVFS FSKRECESCA LQMKNLAFND DSEKEMVQKV FDSAIEMLSE EDRDLPQIQN
ILPLLRRGIG VHHSGLLPIL KETIEILFQE GLIKVLFATE TFSIGLNMPA RTVVFTSVRK
FDGFSQRWVT PSEFIQMSGR AGRRGLDDRG IVIMMVGEEM DPAVAKEIVR GEQDRLNSAF
HLGYNMILNL MRVEGISPEF MLEKCFYQFQ NTAGVAELEK QLTEMEEKRA NLSIPDEGTI
REYYDLRKQL RKFGDDVQAV MSHPEHCLSY MTPGRLVQIK HKDLEFGWGI VVNWKHRKPP
KNSNEEFNDH QKHVVDVLLN IADGDSVGTK SFEDLPAGVR PPKEGEKSRM EVVPVVLSCI
QSIAHVCLRL PKDLKPNDTR NNLKNTLEEV KKRFPDGIAT LDPIENMGIK DDEFKKTLRK
IEVLESRLLS NPLHESPRLP ELYDQYSEKV NLGTKIKETK KKISDAMAIM QLEELKCRKR
VLRRFGFINE AEVVQLKARV ACEISTGDEL MLSELLFNGF FNNLTPEQVA AALSVFVFEE
KTKETPALTR EDLAKPLREI QAQARIVAKV SQESKLAVNE EEYVQGFHWE LMEVIFEWAN
GKSFADICKM TDVYEGSLIR VFRRLEECLR QMAQAAKVMG SEDLEGKFET ALTKVRRDIV
AAQSLYL
//
