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Database: UniProt
Entry: A0A084RU96_STACH
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ID   A0A084RU96_STACH        Unreviewed;      1412 AA.
AC   A0A084RU96;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   31-JUL-2019, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFA79781.1};
GN   ORFNames=S40288_00682 {ECO:0000313|EMBL:KFA79781.1};
OS   Stachybotrys chartarum IBT 40288.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Stachybotryaceae;
OC   Stachybotrys.
OX   NCBI_TaxID=1283842 {ECO:0000313|EMBL:KFA79781.1, ECO:0000313|Proteomes:UP000028540};
RN   [1] {ECO:0000313|EMBL:KFA79781.1, ECO:0000313|Proteomes:UP000028540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40288 {ECO:0000313|EMBL:KFA79781.1,
RC   ECO:0000313|Proteomes:UP000028540};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene
RT   clusters in the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000256|PROSITE-ProRule:PRU00657}.
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DR   EMBL; KL657348; KFA79781.1; -; Genomic_DNA.
DR   EnsemblFungi; KFA79781; KFA79781; S40288_00682.
DR   Proteomes; UP000028540; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 1.10.1520.10; -; 2.
DR   Gene3D; 3.30.160.380; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF03368; Dicer_dimer; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00636; Ribonuclease_3; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00535; RIBOc; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF69065; SSF69065; 2.
DR   PROSITE; PS51327; DICER_DSRBF; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00517; RNASE_3_1; 1.
DR   PROSITE; PS50142; RNASE_3_2; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028540};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028540};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00657}.
FT   DOMAIN       59    236       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      400    563       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   DOMAIN      588    685       Dicer dsRNA-binding fold.
FT                                {ECO:0000259|PROSITE:PS51327}.
FT   DOMAIN      941   1084       RNase III. {ECO:0000259|PROSITE:PS50142}.
FT   DOMAIN     1124   1303       RNase III. {ECO:0000259|PROSITE:PS50142}.
FT   REGION        1     20       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      536    563       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS      1     19       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   1412 AA;  158935 MW;  E6077A23211AC6BF CRC64;
     MVDSDLGSGT SSPAPPTPHA QVNETIRHVV DGNVTAPTPA PDTSDGTSRL NPRAYQQEMF
     DHSLQRNTIV AMDTGSGKTQ VAILRIAAEL DKASTDKIIW FLAPTVSLCQ QQFNVIRLQI
     PAVSIKIVTG EDNADTWSEN IWATLLDGVR IVVTTHQILL DALSHAAIKM SNLSLIIFDE
     AHCCRGKHPG GKIMTDFYHR QKGLGAPVPA VLGLTASPFV KSRLVDLEIL ESTLDSKCIT
     PTLHREELVR HVSRPQIVTV VYPTPKDIVY TPSMASLRDV VNDYDLYKDP YVIDLMTDQT
     EKNIRKLERV FKRRDSFTEK QLRGLYCRSI SLCQQLGPWA ADRFLSRTTT YFLNRLGSMD
     DFHDWIGAEK LYLAKLLQAM PQQSSPVPQA KDVSHKVELL VKELVSVAEK VTGIIFVQER
     AAVTMLHELL ETCEPVSKKF RIGTLVGTSN MPGKRKEIYE FQGSSDPKTL EKFRAGEINL
     LIATSVLEEG IDVPACNMVI CFDEPSTPKS FIQRRGRARM KDSRLVLFLQ DSCDTLDKWQ
     ILEEQLKAQY EDEERQLRQL ELLDDSDYIG GAFFEVPSTG ARLDLDNAKQ HLEHFCSVLS
     RAEYVDHRPD YIIHAIETGT VPTLRATILL PSFVPPELRR IEGLSEWRSE KKATKDAAFQ
     AYLALYKAGL ISEYLLPFSA SCEVPVIEGR AAEVGGDSLM SPWPQVAQLW RSSRDRWLYT
     LSYHGANGEK IGDYGLLLPT KLPRIRTLPM YVQHEEVHSV QCNSVKQLTH EEAARMPDHT
     ATLLALNFCH KWDVEPGEQV VRLFALDADI DIGQIGSGTH EDINDAVKAG TYLIRNHEGA
     SYFYGGMIDS KPPFERVKTR FFGYENAPVD APYLVLKKYS RRTDFLHTFN SAPTQEASSK
     KSYSCVLPLE LARVDAIEVR HAYFGRLIPP IMHELEVMLV TQELAETLLK PVGLSNLELI
     RTAISSGSAR EPQNYEKLEF FGDSFLKYCA VVNVFAKYPK WNEYYLSSAK DRLVSNSRLQ
     RAAVEKGLVK FILTRPFTGQ DWRPIYIDEA CEQGGLPSHK RKLSTKTIAD VVEALIGASY
     QDGGIGKALK CISVFIDDGD WQDIGVLQAH LFNQAVLSQL PPVLAPLEDL IGYSFRKKAL
     LVEAMTHASY IANKDTMSLE RLEFLGDAVL DYIIVNKLVQ VHPPLAQDRM HLIKAALTNK
     DFLAFITLES GVQKRETIVM PTLDVKEEQS RLSLWQFMRH MDHDMGLDQL ATQERYNRVR
     GDITGAMESG ADYPWTLLCK LHARKFFSDV FEALLGALWI DSGSLEVCES VATRFGILPY
     MERILRDKVN VRHPKEQMGI SAGSMKVTYD VIGERWTQGD QSVVYSCRLL VGDKVVADVQ
     DGVSREEITT RAAEEAVRFM KTEAWLQTRD EQ
//
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