ID K1WA30_TRIAC Unreviewed; 1201 AA.
AC K1WA30;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Antiviral helicase SKI2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1Q2_07129 {ECO:0000313|EMBL:EKC98533.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC98533.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC98533.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC98533.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKC98533.1}.
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DR EMBL; AMBO01000387; EKC98533.1; -; Genomic_DNA.
DR AlphaFoldDB; K1WA30; -.
DR STRING; 1220162.K1WA30; -.
DR eggNOG; KOG0947; Eukaryota.
DR HOGENOM; CLU_002902_1_4_1; -.
DR InParanoid; K1WA30; -.
DR OMA; CGSDITR; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000006757; 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; 3.
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; 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; PF17911; Ski2_N; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 3.
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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 297..443
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 585..746
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 183..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 132959 MW; B92544C91ED24E59 CRC64;
MVQATEESTL SPERFLELLQ AAAHPTESDL PSETLAESLG ISALPTGQEA IDLVKKDVLS
PPKDLAGPDL WRWQAPLPCP VPLPALPLDT RPPTHMVAPS FKGIDGTFTK WRDALAPKPP
AHPSLSSSLQ REPAAAQNFV RGKSTNAPFL PGGLEPAITY EEAEEELEEE DGWKTRAPGF
RRGVQLEGDQ NMTTKAKRKT RGGDDPSLQV SRLGDDETTE PGERALVPAA KNVDDLLPIG
RLPAPPPARK QFEKVAGKQE WAHVVDVNKE LVNFHELVPE MARQYPFELD NFQKEAVYRL
EMGDSVFVAA HTSAGKTVVA EAIYTSPIKA LSNQKFRDFK QTFDPSTVGI LTGDVQINPE
GSCLIMTTEI LRSMLYKGAD LIRDVEFVIF DEVHYVNDAE RGVVWEEVII MLPEHVNIIL
LSATVPNTKE FADWVGRTKR KNIYVISTPM RPVPLEHYLW AGKEIHKIVD SKGQFLGSGY
KSAGDALRRK QDKEREAAGL PPLTRTGGRG GAPVKARDLP TGRSAPFSRV GGGRSHTNRG
GGQGAPAPAN GGRGGGGGGR GGRGGGRPGG RGQLDQNVWT HLIAYLRKNH LLPVVNFVFS
KKRCEEYAQT LSTTDLCDSK EKSEVHVTWE RALTRLKEVV EILFARGLVK VLFATETFAM
GVNMPAKSVV FSGIRKHDGT TFRNLLPGEY TQMAGRAGRR GLDTTGTVII LNGGDELPAQ
QELQEMMLGV PNRLTSQFRL TYNMILNLLR VEALRVEEMI KRSFSENAAQ KLAPEQQKQI
EKILAKLPNV ECPTCKPDIE AYYDLSAEIV RVNTSMMNQA AWAPGKHLVP GRIVLIRDAR
FPGNVAIILR NAPSVVREGV KSDARAYHVL ILATKQQIAD ASKPELKDSE LAPRWPPVLS
PSTAQNPRYW LTAIESSSIG FVTDRLLKVD VNGILDKRQK EPALKAMNEL VKVQEDITSG
GELNEVDWAR LSKLEFQEQL RNRISLADRV SKLGCQLCKN FEEDNLELLP DYESRVEVLK
ELSFIDENST VLLKGRVACE INSAPELILT ELILDNILAD YTPEEAVALL SVFVFVEKTE
SVPEIPPRIA QGLDTIYAIA DNVENCQLRR NVVFDDFREK YKPGLVEVVY EWARGMPFSE
ITNLTDVPEG TIVRVITRLD ETCREVRDAA RVIGDAELFQ KMEEAQALIK RDIVFAASLY
L
//
