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Database: UniProt
Entry: A0A316UHS7_9BASI
LinkDB: A0A316UHS7_9BASI
Original site: A0A316UHS7_9BASI 
ID   A0A316UHS7_9BASI        Unreviewed;      1276 AA.
AC   A0A316UHS7;
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:PWN23483.1};
GN   ORFNames=BCV69DRAFT_264609 {ECO:0000313|EMBL:PWN23483.1};
OS   Pseudomicrostroma glucosiphilum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Pseudomicrostroma.
OX   NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN23483.1, ECO:0000313|Proteomes:UP000245942};
RN   [1] {ECO:0000313|EMBL:PWN23483.1, ECO:0000313|Proteomes:UP000245942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN23483.1,
RC   ECO:0000313|Proteomes:UP000245942};
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; KZ819321; PWN23483.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316UHS7; -.
DR   STRING; 1684307.A0A316UHS7; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000245942; 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:PWN23483.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245942};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          326..484
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          608..804
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          192..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1276 AA;  142331 MW;  13D0958B2C02E114 CRC64;
     MASSSSSSKP HHDRLARLQA QLKELRLAPS SELVGSRYSR NEIKEMLQKR FTATHNRIEQ
     PGLDELQVHW RRTPDLKSLL PSDPLPQTTS LRFIRAGLDG HIIGSQEVVT HQPASSSAVA
     RKTQLELRKL AATQRKGMSF VRGRSGGTMF MPGGLDDDDL ALEPEGEVDG VEAEVKQVEA
     AIKDWGRGLR TIPPGFERGF RAPGQGEEDE EDEADLMDDD ASKGLVAAPV YQPSLKQPAS
     LKVSGAPEPP SSNEATNELD ELLPTDKPHT GAEASSSRSK GRQDIEKREW AHVVDSSKRL
     ANFDQLIPHP AHKFPFTLDP FQQEAVYHLE QGDSVFVAAH TSAGKTVVAE YAIALAQKHM
     TRCIYTSPIK ALSNQKYRDF KTTFGAENVG ILTGDVQINP EAPCLIMTTE ILRSMLYRGA
     DLIRDVEFVI FDEVHYVNDQ ERGVVWEEVI ILCPQHISLI LLSATVPNTR EFADWVGRTK
     KKDIYVISTS KRPVPLEHFL YANRDIFKVV DASSRFLESG IKEAGDALKR KQDKEREAAG
     IAQPVRQGAR GGSAGGSNAR GGRGGGGVQR GGLVARGGTP AQRGRGGAAS MARTMGGDTK
     NLYVHLTGLL KKKDLLPVVI FVFSKRRCEE YASSIPNTDL CTAKEKSEVH IVIERSLMRL
     KGSDRQLPQI QRMRELLGRG VAVHHGGLLP IVKEIVELLF QRGLVKVLFA TETFAMGVNM
     PARSVVFSGI RKHDGHSFRE LLAGEYTQMS GRAGRRGLDK TGVVIINAAE ELPETAILHK
     MLLGQPTKLQ SQFRLTYNMI LNLLRVETLK VEEMIKRSFS ENASQRLLPD QQKKVEERKK
     KLERLPRVQP PEREEELRRY HDAARAVGVA FHGVLELALE QQQGSKIFAP GRVVLLRDAH
     FNNNPAVLVK QVASRIFLVL AAVSPRRKKG EYDLEDDSQV APRWPPVMST EGEEELVYDL
     REVPLQSLSL VTKHTLKIDQ SMIMAHRISA MNKTVEAMQG TIVELRAAGE RAASSQEVEW
     SKLRRLDFQE SLKSRDDRAR TVAPIEEGEN FAKEYRITHA RKGLEREIAR IEHSMSNQNL
     ELLPDYEQRV EVLKTLRFID PLTESVLLKG RVACEINSAD ELVLTELILD NVFATYTPAE
     IVALLSVFVF QEKSDSEPVL TERLQEGLAT ILSTSERVSQ VQAEHQLNYN DYSTSLKIGL
     VEVVHRWAEG TSFEEITQLT DVAEGTIVRV MTRLDQTCLE VRDAARVIGD GQLKEKMEEA
     QVMIRRDILA APSLYF
//
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