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Database: UniProt
Entry: A0A177VU66_9BASI
LinkDB: A0A177VU66_9BASI
Original site: A0A177VU66_9BASI 
ID   A0A177VU66_9BASI        Unreviewed;      1624 AA.
AC   A0A177VU66;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   31-JUL-2019, entry version 13.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAJ30950.1};
GN   ORFNames=A4X06_g1782 {ECO:0000313|EMBL:OAJ30950.1};
OS   Tilletia controversa (dwarf bunt fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Tilletiales; Tilletiaceae; Tilletia.
OX   NCBI_TaxID=13291 {ECO:0000313|EMBL:OAJ30950.1, ECO:0000313|Proteomes:UP000077684};
RN   [1] {ECO:0000313|EMBL:OAJ30950.1, ECO:0000313|Proteomes:UP000077684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 236426 {ECO:0000313|EMBL:OAJ30950.1,
RC   ECO:0000313|Proteomes:UP000077684};
RA   Nguyen H.D., Samba Siva P., Cullis J., Levesque C.A., Hambleton S.;
RT   "Draft genome sequence of Tilletia caries and Tilletia controversa.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000256|PROSITE-ProRule:PRU00657}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAJ30950.1}.
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DR   EMBL; LWDE01000125; OAJ30950.1; -; Genomic_DNA.
DR   EnsemblFungi; OAJ30950; OAJ30950; A4X06_g1782.
DR   Proteomes; UP000077684; 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   Complete proteome {ECO:0000313|Proteomes:UP000077684};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077684};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      175    375       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      530    706       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   DOMAIN      727    819       Dicer dsRNA-binding fold.
FT                                {ECO:0000259|PROSITE:PS51327}.
FT   DOMAIN     1148   1288       RNase III. {ECO:0000259|PROSITE:PS50142}.
FT   DOMAIN     1338   1492       RNase III. {ECO:0000259|PROSITE:PS50142}.
FT   REGION        1    132       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     16     31       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     65     90       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    108    123       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   1624 AA;  183551 MW;  5493B3F6E91BFA46 CRC64;
     MGLLKRIFWS APSGSDQAEA GPSSERIQQD NSNTAREPDD EPMLMDTAPA KSSPAAPVRG
     ESRTSHAMAT HSSSQPQLSQ GGTPRSGPAE SQVQRREEPA PRAPVAQSDP RPSSSSSHTI
     PENLWAPSLD PRARPRLKGA KVMFVEDDQD LLKPDARKEP TKIRKLKPRK YQLALYEQAK
     SHNIIACLDT GAGKTLVAVM LLQYFNEVEL VRTSSQSVSE ARTAAFPQVE TPLRRIGLFL
     VTRVPLVDQQ AKVIVNNSNL EVTRFSGSDA HQSGTRNAWD TVRRRSDVAV ATAQVVLTAL
     MHGFLRMEDI YCIVFDEAHH AFGDEPYAGI MKFYEQYVKK PVPDQPLPRI FGMTASPLKK
     LGGDEARTSE RLESIMKAHI LTAPVIHRAE LALAVNKPIE CIVEYEPPTF FEDSILTKSI
     REKSHAAKDL LPVLERIEFH TKEHGPLFAD IIWATSVNEL KKQTATQSAL TMINTEWLLE
     KQSATENRRG QLTSNSRNAR LIDDEVRRTF ELPDTLTLTN EHVTPKILKL MKILMCFCAT
     EESREGLRGI IFVERRDTAY ALHELVRRQE NLRWLKTGYV IGHGDGGEAI GLKQGHTSQE
     AVLSRFRSGE FNLLIATSVI EEGIDVSPCN LIIRFDLFTN HVGFIQSKGR ARHKQSKFIM
     MAERGSEQHY RLIKEVADTD RALRGWLTDL PDDRIHDVRF MAEKDDPDGD LVLEVEETGA
     RLYVQQAVML LATVHASLVT VDSACHAAQY KSEQLPNCEG FRCTITLPEN WKIPDIVSDV
     RASKKAAKRL AAFRACEALH KAGKLNAFLR PSASIAKSRK RGMLPLAPTR LQEGVQVQVQ
     QLQSYRGLKL GFDEESNTWK VHATLVRLDK IPQNALNGPC RMMIVLTVDP VSATSEFRLR
     FTTTDHTFAG LPASSPLTLD SERMEAFRRY TMRLLRWVGR QPQWYCDDMP YILVPATMNA
     GNARVFDFEK HVDMEEVTRL GQWFTKKVLE SGMDVSLGQF YDRILLEKDY EIGAVAYAVT
     GVTRYKEEYG ELERQRSKRR TESGRSKATW KSGIPNVPDE ALGMNWFTVS RIERMQNWAT
     GHLEDSTGPK FYHATALPPT NVWVHAISAS VYRSGLVMPV ILDRIHQALC AQRCNEEIFQ
     GMVGTSHLIE ALTVPTAAYS FNYERLEFIG DTFLKLLATA YVFAENIESQ EGLLHNARRE
     IIMNRTLLKH CMEHKLDDFM LLQSFSSRAW VPPNFVNPSG GRATTHTISG PRGEGYLPTS
     FHTRAPVQQK TLADLAESAM GAGLMTDGLS GALHVSRCLD ITPRPVHSLK ETAELYREKT
     AEEIRRHKLD NAFDPGALAE LEGFLGYKFR LPHIALQAIS HHSINLVGMT FSYERLEFLG
     DAVLDFLAVK DIYNRHTDFD QGELTEYKDK LCMNRTLGAL AEAIGMHRFL NSAPGALQFT
     IRDANEALRL RRLEEQRKPK DARGIYWAEV KIPKSVADIV ESLIGAVALD SSYDMDVLQG
     MYDRMFKPFY NEFCRPSTEI DDAIREFEKF MYDEGCNKWR YVHDSTYQDD QKVYVTEIHA
     HNVVWIRSRY CKTRRRSQIE ACRNLRDTLH SPSTLDAFRD KCQCTPSGAR RETWGATKRK
     ERGH
//
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