ID A0A1A5ZYG7_9TREE Unreviewed; 1290 AA.
AC A0A1A5ZYG7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Antiviral helicase SKI2 {ECO:0000313|EMBL:OBR82849.1};
GN ORFNames=I303_06406 {ECO:0000313|EMBL:OBR82849.1};
OS Kwoniella dejecticola CBS 10117.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296121 {ECO:0000313|EMBL:OBR82849.1, ECO:0000313|Proteomes:UP000078595};
RN [1] {ECO:0000313|EMBL:OBR82849.1, ECO:0000313|Proteomes:UP000078595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10117 {ECO:0000313|EMBL:OBR82849.1,
RC ECO:0000313|Proteomes:UP000078595};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus dejecticola CBS10117.";
RL Submitted (JUL-2013) 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; KI894034; OBR82849.1; -; Genomic_DNA.
DR RefSeq; XP_018260691.1; XM_018409688.1.
DR STRING; 1296121.A0A1A5ZYG7; -.
DR GeneID; 28970105; -.
DR VEuPathDB; FungiDB:I303_06406; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000078595; 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; 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:OBR82849.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000078595};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 315..473
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 612..811
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 113..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1290 AA; 143301 MW; 9E6E744B6B2B92EC CRC64;
MSNEQDELLA HEAFLELLDT AVNPTSSSSL SSDELASALG IDKPLNKEDA LNLLEKEVLA
PVHDLSGPEL WRWQVQPPVE LPIPPLTLRP LHQTHTVTPS YRGMDGTFTH WREGLAPKPP
AHPALSSSTT RAPGSLQNFV RGKGSYAPFL PGGLEAAATP QEDENEEAEE QEEEEGWKTR
APGLRRGIQL EGADEFLAEM LGQASIAPKA KRRRREGEFE SQLTISRLGD DEAEEIEETS
TNGHAGPSTK NVDDLLPIGR LPAPPPPRRQ FKAAVHKEWA HVVDVNQTLS NFKELVPEMA
REYPFELDNF QKEAVYRLEM GDSVFVAAHT SAGKTVVAEY AIALAAKHMT KAVYTSPIKA
LSNQKFRDFK TTFEPSTVGI LTGDVQINAE GSCLIMTTEI LRSMLYKGAD LIRDVEFVIF
DEVHYVNDAE RGVVWEEVII MLPEHVNIIL LSATVPNTKE FADWVGRTKK KDIYVISTPM
RPVPLEHFLW AGKDIHKIVD SKSRFLGDGY KAAQEATRRK QDKEREANGL PPVQRTGGRG
GAPTKARDLP TGKNAPFTKT GAGRTHANRA GGNGAPAPAV SRGGGGGGGG GRGRGGFGGR
ASHQLDQNIW THLINYLKKN KLLPVVNFVF SKKRCEEYAQ TLGAMDLNSA KEKSEVHLTW
ERALTRLKGI DKTLPQILRM RDLLSRGIGV HHGGLLPLVK EVVELLFSRG LVKVLFATET
FAMGVNMPAK CVVFSGIRKH DGTSFRNLLP GEYTQMAGRA GRRGLDTTGT VILLSGEELP
TVTELNEMML GIPNRLSSQF RLTFNMILNL LRVEALKVEE MIKRSFSENA TQKMAPEQQR
QIAHAEKQLA RLPDVECSTC KNDIDAFYQN SSEIVRVNQS IFKQASYAQN AGKIFVPGRV
VILRNGHLPG NLAILLRSAT SLITDGVKSD AKAWRMLVLV TPGQRSRKED VKEIDVPPRY
PPILPKGSFP NPQWEIATYD TTSLSFVVNR ILKIDHSGII DKSSKDARDK ALHDLTILHE
ELSSLPDLPE VDWSRIRAVE FVDAIRQRAI LDDRLAKLTC QTCPDFHDHY AILHERKIVE
QSLTSLKLAL SDQNLELLPD YESRVQALKS LSFIDENSTV LLKGRVACEI NSAPELILTE
LILENILNDY EPEEVVALLS IFVFVEKSDS QPVIPDKIAQ GLEVIYKIAD SVERAQDKCS
VQYDQFDEKY KVGLVEVVYE WARGMPFNQI TELTDVPEGT IVRVITRLDE TCREVRDAAR
VIGDADLFQK MEAAQALIKR DIVFAASLYL
//
