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Database: UniProt
Entry: A0A316V1V5_9BASI
LinkDB: A0A316V1V5_9BASI
Original site: A0A316V1V5_9BASI 
ID   A0A316V1V5_9BASI        Unreviewed;      1284 AA.
AC   A0A316V1V5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Putative SKI2-antiviral protein and putative helicase {ECO:0000313|EMBL:PWN30163.1};
GN   ORFNames=BDZ90DRAFT_229191 {ECO:0000313|EMBL:PWN30163.1};
OS   Jaminaea rosea.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Jaminaea.
OX   NCBI_TaxID=1569628 {ECO:0000313|EMBL:PWN30163.1, ECO:0000313|Proteomes:UP000245884};
RN   [1] {ECO:0000313|EMBL:PWN30163.1, ECO:0000313|Proteomes:UP000245884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 5214 {ECO:0000313|EMBL:PWN30163.1,
RC   ECO:0000313|Proteomes:UP000245884};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010140}.
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DR   EMBL; KZ819662; PWN30163.1; -; Genomic_DNA.
DR   STRING; 1569628.A0A316V1V5; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000245884; 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; 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:PWN30163.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245884};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          341..499
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          619..814
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1284 AA;  142984 MW;  9C1522745360CEA7 CRC64;
     MDRDELSSIL ESIRSAPSSS KAPDGGIEAL REALSHAGLA KQDAAAKSAY SREELVEQLK
     DKLLTPQASL QGEELVKRQV HWHRKPDFSS LLPAQPLPQT TSLRFIRTGL GSNVIGTKEV
     VTHQPPSTSQ AARKARLEAQ KVNASQRKGM SFVRGRSGGA MFMPGGLDDD DLLIESIQGE
     RVDQEQGIER DVEEVEEAIK GWGRGMRTKA PGLSRGFKAA TDEDEDEEEV ETGAEMDIAK
     SLVPAPVYQP SLKASLRVGG SAADAPQQRN SQLDEELDEL LPTEKPPTHS SRRAAKVDLE
     EKTEWAHVLD ASKRLANFND LVPDMAHKFP FTLDPFQQEA VYHLEQGDDV FVAAHTSAGK
     TVVAEYAVAL AQRHMTRCIY TSPIKALSNQ KFRDFKQTFG AENVGILTGD VQINSEAPCL
     IMTTEILRSM LYRGADLIRD VEFVIFDEVH YVNDQERGVV WEEVIILLPR HISIILLSAT
     VPNTKEFADW VGRTKKKDIY VISTSKRPVP LEHFLYANKD LFKIVGADGK FAERGIKDAG
     DALKRKQDKE REAAGVAQPT RQGARGGAAG GANSNSRGGR GSFGPQRGGA RGGRGGGASS
     VARTIGGDTK NLWVHLTGML KKKDLLPVVV FVFSKRRCEE YASSLPNTDF CSAKDKSEVH
     VVIERSIMRL KGPDRTLPQI QRMRELLARG IAVHHGGLLP IVKEIVELLF QRGLVKVLFA
     TETFAMGVNM PARSVVFSGI RKHDGHGFRD LLAGEYTQMS GRAGRRGLDA TGVVIINSAD
     QLPETTTLHK MLLGQPTKLQ SQFRLTYNMI LNLLRVETLK VEEMIKRSFS ENASQRLLPD
     QQKKAAEARK KLDRLPQVSP PERADELSQY YDAAWAAFMS NHSVLDLALE QQQGSRIFAP
     GRVVLLRDAH FDHNPAVIVK QVSSREFLVL GAVTQQRKEG RLDVPDKAVP PIWPPQMKRD
     AGDELVYDLR EVPLTSFAFI SAHVLKIEQS MIMAHRKSAM NRTVDLMREP IAELRVELRE
     VDWTKMRRLD FQEALKSRDE RGAIAVAHLV DTTLPDFDKQ YRLTHARKQL EKEVARIEHS
     MSNQNLELLP DYEQRVGVLK TLRFIDPLTE SVLLKGRVAC EINSADELVL TELILDNVFA
     GYEAEEIVAL LSVFVFKERT DGAEEEEFPP RLSEGLATIL GTAERVSQVQ AEHQLNYDDY
     AVSLKTGLVN VVYQWARGRS FGEIMEMTEV AEGTIVRVMT RLDQTCLEVR DAARVVGDQG
     LREKMEEAQQ MITRDILAAP SLYI
//
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