ID A0A074W7S7_9PEZI Unreviewed; 1278 AA.
AC A0A074W7S7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Antiviral helicase {ECO:0000313|EMBL:KEQ65977.1};
GN ORFNames=M437DRAFT_72814 {ECO:0000313|EMBL:KEQ65977.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ65977.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ65977.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ65977.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; KL584826; KEQ65977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074W7S7; -.
DR STRING; 1043003.A0A074W7S7; -.
DR HOGENOM; CLU_002902_1_4_1; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000030672; 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; -; 2.
DR Gene3D; 2.30.30.1160; -; 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:KEQ65977.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030672};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 314..470
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 601..802
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 217..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..247
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1278 AA; 142883 MW; 692ADD1AE0884474 CRC64;
MDELAPALEK LRLADAPSGG IDAILDQQRP RKRTRRSPDH IRSSLEKDFL APSTSFSTPW
LDRLQQRWDC PANYEELFEL APTQTRTIIR FTREGLEGRV TGYKEVTVPA NSATAKNSTS
ILRKPANRAD FVRGAAGFFP FAPGGLDAVE ATAAAEEQLL LGNQANSTVK QSGLDKVINF
GPEGALLELP PGFTRGLDLQ KKAPADQATA QEVETVLEEE PQDPVVANGD IDEAQPTDED
EDEGEEEELD ALLPVEFPAL AARGQLGLSS NKRSGHEWAH MVDVNRPMPN FRDLVPEMAR
EWPFEPDTFQ KEAIYHLENG DSVFVAAHTS AGKTVVAEYA IALAAKHMTK AIYTSPIKAL
SNQKFRDFRQ EFDDVGILTG DVQIRPEASC LIMTTEILRS MLYRGADIIR DVEFVIFDEV
HYVNDLERGV VWEEVIIMLP EHVTLILLSA TVPNTLEFAS WVGRTKKKNI YVISTPKRPV
PLEHYLWAGK EMYKIVNADK QFIEKGWKDA NDVLSGKDKI KAAEEKQEAA AAAARGGGSQ
RGGRAQTQRG GGQRGGAQRG GAQQRGGRGG APAPRGQGNI ARTGRGGGRT TAAQDRNIWV
HLIQHLRKED LLPACIFVFS KKRCEENADA LSNLDYCTAT EKSAIHMILE KSLARLKPED
RQLPQIRRLR ELLSRGIAVH HGGMLPIVKE CVEILFAKTL VKVLFATETF AMGLNLPTRT
VVFSGYRKHD GRQFRDLLPG EYTQMAGRAG RRGLDPVGSV IIVAPGADEA PPAGRLRQMM
LGDPTKLRSQ FRLTYNMILN LLRVEALKIE EMIKRSFSEN ATQALLPEHE QKVKLSEADL
AKIKREPCDI CDKDLEECHT AAMRYQQLTS DLHLALLSSP IGRRMLQPKR LVVYKRDGVR
TVGVLLREGV SKGISPSLSV MEVAPSKSKR QNADLLPYLP RYRRRFTPQP SAPEQMKLRL
ATVPYSELEC LTGSTLQFDV TGASSKMPEA MEQLKEQLLG ACSSWTSATW QEADYSRIKE
IGIRNILDER NKAAYDAQEN KECVLCENLE KHFAMMHDEW LIKENINQLR ALMSDQNLQL
LPDYEQRIAV LKDLGFVDEN SRVELKGKVA CEIHSADELV LTELVLENVL ADYEPEEIVA
LLSAFVFQEK TDQIPTMTPA LERGQETIIK ISEKVNHYQT LHQVILSADD SNDFVSRPRF
GLVEVIYEWA RGMSFNRITD LTDVMEGTIV RVITRLDETC REVKNAARII GDPTLFTKMQ
TCQEMIKRDI CATASLYM
//
