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Database: UniProt
Entry: A0A1B8GIG6_9PEZI
LinkDB: A0A1B8GIG6_9PEZI
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ID   A0A1B8GIG6_9PEZI        Unreviewed;      1661 AA.
AC   A0A1B8GIG6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Dicer-like protein 1 {ECO:0000256|ARBA:ARBA00020797};
GN   Name=DCL1 {ECO:0000313|EMBL:OBT95631.1};
GN   ORFNames=VE01_05942 {ECO:0000313|EMBL:OBT95631.1};
OS   Pseudogymnoascus verrucosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=342668 {ECO:0000313|EMBL:OBT95631.1, ECO:0000313|Proteomes:UP000091956};
RN   [1] {ECO:0000313|EMBL:OBT95631.1, ECO:0000313|Proteomes:UP000091956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBT95631.1,
RC   ECO:0000313|Proteomes:UP000091956};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000091956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX   PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT   white-nose syndrome of bats.";
RL   Nat. Commun. 9:35-35(2018).
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}.
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DR   EMBL; KV460234; OBT95631.1; -; Genomic_DNA.
DR   RefSeq; XP_018129364.1; XM_018275400.1.
DR   STRING; 342668.A0A1B8GIG6; -.
DR   GeneID; 28839328; -.
DR   OrthoDB; 342391at2759; -.
DR   Proteomes; UP000091956; 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   CDD; cd18802; SF2_C_dicer; 1.
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; IPR014720; dsRBD_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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000091956};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00657}.
FT   DOMAIN          208..390
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          531..700
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          733..823
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000259|PROSITE:PS51327"
FT   DOMAIN          1167..1278
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          1325..1492
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          1523..1595
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1661 AA;  186720 MW;  79FAC3978B17B15A CRC64;
     MCHTVGTAAP LHGQSGVDGA PTEGNMDLDI EISQVTTLKS PTTPKPPTTP AHQADSPPSI
     VSLPSAFNMQ VPEVMVPALA TRSTDAVIED LRRRGLHPGA PTVDKEPLTV YVEEVSRTQK
     EDIAIEDEDA GDESESDDES PAHPSENQEL SYEKSVRESY IRSRVFQAAK DSTAPETKGD
     DKQSVKWLIK DSGSQEIISS PREYQIELFE KAKTQNTIAV LDTGSGKTLI AALLLRHVID
     EELERRASGG DKRIAFFLVD SVALVFQQYA VLKCNLNHKM EQFCGDMGCD LWSKELWEKH
     FNENMVIVCT AEVLFQCLHH SFITIKQINL LIFDEAHHAK RNHAYARIIK DFYASEPDQS
     LLPRIFGMTA SPVDARTNIK KGAAELEALL HSQIATASDA SLLQYTNKKT REEVAYYDPL
     PPPTESQLFK RAHQLVGGIK ECSKPLEYAV TASSDLGSWV ADRVLLISFT GEDVKRLGAQ
     IESNFHKQAQ IDPIPLSNLE DRKEKLRSAQ QIIMEHVFAS PQLSRSQLSS KVLGLASKLR
     ERFERTTFDK CIVFVKQRYT AKLLADLFAS PQIGTPHLRV GSLTGTRNRS GADLESSFRN
     QVITLRRFRQ GEINCLFATS VAEEGLDIPD CNLVIRFDLY STVIQYIQSR GRARQDNSVY
     FHFIERGNKV QDALAREVRR NENILKEFCQ ALPEDRLLSG NNYNMDYFLA KERNIMRTYT
     EPSTGAKLTY RMSLSVLANF VASLPHSSES TPHPEYMMTA MGAKYVCEVI LPENSPVHGA
     IGRPANTKQV AKCSAAFEAC LSLRKGKHLD EYLLSTFKDR GPAMRNAQLA ITSKANTDYD
     MRTKPSMWAA GETPSELFLT ILSLKDPVQL DRPSQPLGLL TRGPLPPLPL FQLYFGGGKH
     TAAVSTAVGS LAVSSETLEL INTFTLRIFK DIFSKEYESD PAQMPYFIVP ISDTDTTCRA
     RLPVDLISWD ILRIVSDNQW LTWDKSTPES FFEDKYIIDP FDGSRKIWAR KVTHAYKPLD
     PVPPNTAARS ARKNNLNILE YSCSLFKVAR SKRTFSETQP VIEGDVIPFR RNFLDDHDDP
     ANSGPTKCYV VPEPLTISAL PTLIVAMAYT FPAIIHRIES YLIAVEACSM LHLPISADLA
     LECMTKDSRN TDEHGDEQVE FQRGMGNNYE RLEFLGDCFL KMATSISLYT LHPDSNEFDF
     HVKRMLMICN KNLMDVALQL KLYEFIRSQA FNRRAWYPEG LVLKKGKAAQ APKKHKLGDK
     TIADVSEALI GAALLTPSNG HAMDHAVRAV TELVCSTDHA IEKWEDYFKG YTKPKYQITA
     STASQRNLAE QIEITHDYHF HYPRLLRSAF IHPSYPFVYE RIPNYQRLEF LGDSLLDMAC
     VNFLFHRFPT KDPQWLTEHK MAMVSNQFLG AVCVALGFHT QLLQFNPIIQ SSITEYVCEI
     TEAREQAEQD AIRDGKLPSD CARDYWLHAK LPPKCLPDII EAYIGAIFVD SSFNYEEVER
     FFDLHIKWYF EDITLYDTFA NKHPVTFLHK FLQQNMGCAK YRITASSMPD DSSGTPPKIL
     ATVMIHSQIL VGVERDSARY AKIAVAQKAL EILKAGTLTQ FRQTYRCDCK EKGLDVEDCN
     MEDAAQESME DHVGIKTLDV ESALGADIGV EGSRNGSISS A
//
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