ID A0A0M8MTM5_9HYPO Unreviewed; 1318 AA.
AC A0A0M8MTM5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Dicer-like protein 2 {ECO:0000313|EMBL:KOS19156.1};
GN ORFNames=ESCO_001305 {ECO:0000313|EMBL:KOS19156.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS19156.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS19156.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) 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:KOS19156.1}.
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DR EMBL; LGSR01000020; KOS19156.1; -; Genomic_DNA.
DR STRING; 150374.A0A0M8MTM5; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000053831; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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; 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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR014720; dsRBD_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 PANTHER; PTHR14950; DICER-RELATED; 1.
DR PANTHER; PTHR14950:SF37; ENDORIBONUCLEASE DICER; 1.
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; SM00490; HELICc; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
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; PS50137; DS_RBD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00517; RNASE_3_1; 2.
DR PROSITE; PS50142; RNASE_3_2; 3.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00657}.
FT DOMAIN 1..95
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 270..449
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 466..563
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 809..872
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 903..989
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1031..1215
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1246..1313
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
SQ SEQUENCE 1318 AA; 149229 MW; 90554C6370E21076 CRC64;
MKLITSQINV DTWDEHVWEV VLNGTNIIVS TYQVLLDALT HAFISMSRLS LLVFDEAHNC
IGKNPGQKVM MDHYRPSKLA RRSVPAILGL TATPSIRSNV QDLEKLETSM DARCISPTIH
RDELLKCVRR PRLKYITYVP GDLVSTSTMR SLHDVFRNMD IRQDPYILKL RANLTERNKR
ELAQAITKNN TYSQDQMRKL CSRSMELCRQ LGTWAADLYI AKVVENLLGR IDGGDDFFDK
FINEEKKYLA NTLRQVVVEP TPDVPRQAKD LSDKVRLLMQ ELLSADPSVM GIIFVQERVM
VSMLLEVLRS NEAIRERYRI GTMVGTSNNS NRKKDLYDVP GNADIKSLEE FRFERLNLLI
ATSVLEEGID VRACNLVICF DSPLTPKSFI QRRGRARMTD SQLVLFAESA PRKVSDWESL
ELEMKQLYED QEREIRRLER IEDSEGSSEM YYIVPASGAR LDFDNAKSHL DHFCSVLSKH
EYVDSRPDYI ITRVADTTPA MLSAAVLLPS FVPASLRRAE SSRPWLSEKN ATKDAAFQAY
VALHRAGLVN DHLLPLKLEE PAGIEGRAAE LTVEPQLNPW VAAAPAWMDP ADKWRYSLSC
VDGFGQPMGN FEIVLPVWLN RPRPITMFMD RNSRWELRIS EGMPLLHVDL NSIPDHTSTL
LALHFAHRWP VDHQRNHVIR VFAPNTVLSM DQIGAGALDP DSEDIKQGRY LIRDPRSNFS
PFLYQNLIPS KPLISDVKKR WDFDWDNAPS DVPYLSLSPW TKRTDFLHPM IGDASKEMPS
SKQYAAVLPL TWATVDTISV RYTQFGMLIP SLLHKLEVML VAKELAKTLL EPVEISNLDL
VLEAICAPGA GEPVCYEKLE FLGDSILKFC TSILALSQSE WPSFFSPFTG YGLDKETDSH
TDPDFPEGYL SQYRDRLVAN SRLSRANIEK GLAKFIITRS FTGHRWRPLY LDTYLPGGDF
AAEADRKIST KTLADVVEAL IGAAYLDGHL PKALKCITVF LGEDCNWSSV LRGHETLFNM
ASDKEALPAV LAPLEQLVGY AFRRKALLIE AVTHASYIAD TGNRSYERLE FLGDAVLDYI
IVTRVFESNP RMPHYEMHTL KTAMVNGDFI AFMTMEHGLR TTDSVVEADA ATGKARISSE
DSCTYLWKFM RHALLSIGLE QKETVGRHRN TRESILRVMT TGGHYPWDLL AHLQAKKFYS
DLFEALLGAV WIDSGGSIDV CRAVVARFGI LDYLDRILRD GVCCLHPKER LNRLTSSESI
TYQVDVRERS TGEREFVCAV TVGERLVVTV DDGLNREEVQ TKAAHAAVEV LMAERASR
//
