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Database: UniProt
Entry: A0A135SX86_9PEZI
LinkDB: A0A135SX86_9PEZI
Original site: A0A135SX86_9PEZI 
ID   A0A135SX86_9PEZI        Unreviewed;      1611 AA.
AC   A0A135SX86;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Dicer-like protein 1 {ECO:0000256|ARBA:ARBA00020797};
GN   ORFNames=CNYM01_03121 {ECO:0000313|EMBL:KXH40529.1};
OS   Colletotrichum nymphaeae SA-01.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH40529.1, ECO:0000313|Proteomes:UP000070054};
RN   [1] {ECO:0000313|EMBL:KXH40529.1, ECO:0000313|Proteomes:UP000070054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-01 {ECO:0000313|EMBL:KXH40529.1,
RC   ECO:0000313|Proteomes:UP000070054};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXH40529.1}.
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DR   EMBL; JEMN01001314; KXH40529.1; -; Genomic_DNA.
DR   Proteomes; UP000070054; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd18034; DEXHc_dicer; 1.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 3.30.160.380; Dicer dimerisation domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.1520.10; Ribonuclease III domain; 2.
DR   InterPro; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR006935; Helicase/UvrB_N.
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   PANTHER; PTHR14950:SF62; DICER-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR14950; DICER-RELATED; 1.
DR   Pfam; PF03368; Dicer_dimer; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF69065; RNase III domain-like; 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   Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW   Antiviral protein {ECO:0000256|ARBA:ARBA00022721};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00657}.
FT   DOMAIN          168..350
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          484..666
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          683..773
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000259|PROSITE:PS51327"
FT   DOMAIN          1124..1235
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          1286..1471
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   REGION          17..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1611 AA;  182493 MW;  9AB98137757F7DE8 CRC64;
     METSKRQRIG DWPLIDGLGK LCLTPLPSKP STPVERSHEQ PSTTGLGTIC PAIEISTNLP
     SPSYSTATSS RHGPIVNTDD VEEQDQADED EEDDYRRWSV NPERPRKISE KKRQDHAKFQ
     SWIESNQAKV LEAASKTKAP AQGSVAYLVK ESENRRIIQT PREYQIELFE RAKQKNIIAV
     LDTGTGKTLI AALLLRHILE KEVEDRALGK PKRTAFFLVD KVSLVFQQHA VLECNLEHSV
     ARYCGDMVDE MWSSEFWAKQ FEENMVVVCT AAILQKCLMH SYIRMDQINL LIFDEAHHTK
     KNHPYARIIK DFYIKEPEKD KRPKILGMTA SPVDAQTNMK VATAQLECLL HSEIATVSEE
     SLALNPNQRK ITEREIHYTP LVRSFESELV QKIQALVRRN QLFDKELQWT TTAMAELGPW
     VADRFWKLYL TDNTIARLAN RTDINYSGFD GNGKHTAAVQ KLRDIVQSHN FKPPTLSLDD
     VSSKVLRLWD ELKVRFSQPT DYRCIVFVEM RLTAVMLAEL FKQDGMDLPH LKPAALVGSQ
     ASAGLGNMSF KEQLLTITKF RRGEVNCIFS TQVAEEGIDI PACNVVMRFD LYKSVIQYIQ
     SKGRARQHDS EYLSFVEIGN GRHTRAVAQA TYDQSVLRRF CSALPEDKKI MGMDINASVM
     QAELHYQTYT IKETGAKLTW MSSLEVLANF ASSLRQSSDE VSMPEYVVTN QGQSFIAEVH
     LPPKSPILSI TGMPHKRKQA ARCSAAFELC KELIKKKYID LNLQPIFTKK LPAMRNARLA
     ISANKRAEYK MRTKPELWSR VGAFDHLYVT VLALASPDAV GKESKPLLLL TREKLPDLPP
     IPLFFGNDQQ SDAFAVCLPR PINISSADSE LLKSFTLRVF KDVFSKEYEA AIFDMPYFLA
     PTTQSHSADH QHADAATLVD WDHLQATNDR EYLDWDDSTS DEFFTDKLVI DPYAGSRKLR
     LRGVRKDLKP MDPVPEGVPD PGHRPWRDSA VEKNIKEYSV SLWMKSRLKR TWRDTQPVVE
     AEVISLRRNL LDDFVEATNE ESKVCYVILE PLRVSTLPME TVVMAFTFPA IIHRMDQVMV
     ALDLCKLLKL DIRPDLALEA VTKDSDNSDE HDAEKINFQG GMGNNYERLE FIGDTCLKMA
     TTIALFTNNP DNNEFQYHVE RMLLISNRNL LNKAIDRNLQ EYVRSKSFNR RSWYPQGLRL
     IRGKEGTVDA NHALADKSIA DVCEALIGAA HLTFSDSNNF DMAIRAVSAM VNDKNHRMTS
     WADYYAGYKP PSWQTEPASA MYRDVVRQVK NKVGYDFKSP ALLRSAFKHP SCPHNVCSLP
     NYQRLEFLGD ALLDMVCVDF LYHKFPSADP EWLTRHKSTM VSNRFLACLC VKLDLHKHIL
     TAQASLLSQT QEFVAALRFA EESAREEALR EAVQNGALAD GKQGKEALVT KATGNATTAT
     PVSYWQHVED APKYLSDMME AYIGAVFVDS GYDYGQVRAF FEAHVRPFFT DMSLYSDYAL
     NHPVTNVSHM LRNDFGCDGW RLMTNEVVPP IEAGAGVITE TQVLCGIMIH GQVYFHATAA
     SGRYAKVAVA KMAITKFTDM DREAFRKEFA CDCQDVEGEC GTQQVDPRLA A
//
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