ID A0A194S806_RHOGW Unreviewed; 1451 AA.
AC A0A194S806;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Dicer-like protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=RHOBADRAFT_51848 {ECO:0000313|EMBL:KPV76863.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV76863.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV76863.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV76863.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
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; KQ474075; KPV76863.1; -; Genomic_DNA.
DR RefSeq; XP_018272912.1; XM_018416046.1.
DR STRING; 578459.A0A194S806; -.
DR GeneID; 28976494; -.
DR OMA; YTCANES; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000053890; 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: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; 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; 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; PS50137; DS_RBD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50142; RNASE_3_2; 2.
PE 3: Inferred from homology;
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:UP000053890};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00657}.
FT DOMAIN 13..200
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 313..486
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 509..602
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 895..1036
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1096..1245
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1273..1354
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 1376..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1431
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1451 AA; 159329 MW; 2F802A296650FC53 CRC64;
MASLVPRLFQ EAVTEQALRS NVLVRADTGS GKTLIAVLAL RQLAAAPLPA RRTPPDDDPK
RLIVFLTPTT TLVDQQARVI EAQTSLRVQS LVGSQGVDYW QREKWQQLLI HEADVVVLTP
QIWLDVLRNA YFDLRDVQLV IFDEAHHAQK SHPYALIMRD HYHPLKARGE PVPRILGLTA
SPIWNVKNPQ QAIRNLEATL DVRILEVAKA HRPEMAAASP RATELLVEHD PPVPQELSTP
ARHLSPEQLS IISSADKRTL DRLNKAQALF GSAGVDVFLY QLLEEHVGLS SLGAPLKPPV
EPSSTALSPK MSALVSVLLE FKLEPTFHAI IFVQARHHAS VLAELLRRVT SLQGFVRPAA
LVGHGGRGGP GEQGGATAKE IGMAVKEQNE TVAAFKTSEI NLLVATRVAE EGLDVPSCHL
VIRFDALTTI TGYVQSRGRA RAANARYVVL AEKGSPDADK YRSYVKQERE LLDMYAERPD
EPDDSHEPDL DGLATYTTQS GALLTHASAV PLVAQYCQLL RTDIFTTLQN PEYVVEGFGT
AWRSTLHVPR TPALLSNVFE SLVMPSKKAA KQNASFQAAI ALHKAGALDD HLLPVRESRG
KDAKDADGRS IETQNMPGHL DVHLVHPFGD ARVSESAFVH VVEVVRSSET TRLALVCGAP
LHPVDVVKLY GRAGSAMSMR VVAVREHRWA NALERSNLLD QLENLNRICA RIVLNRRVDN
ERFYALWAPV AASGELDWSA VAAAFSPFDG SSTRRGDLVV APSRRANVRI GSFDCVRDDV
DTGSPTAQVE VDPPRRKRKV IEKYSHYPSF VQVCYDHSMP TNGPEPIIQL VPADFRPHNA
LVPPSRRVPT LYKDLASTRN YPESMILTTT LPASFFLDFS LVPSLNHLLL GRSSASALID
RFSLPPLDLA LVEEALTAPS SACGWDYQRL EHVGDSPLKL FTTIHLYLEN PLVDEGRLSR
RRDNSVDNRF LRLRSLECGL AEHILSHTLR TSTFVPEESV NATVSDDGLT MTNKLSRRLL
CDTAEAALGA ALLDGNVSST ADANMPTIKL AVDAFDKALK TGDRLGLCFG GPTPWPDRPS
ARKLLDVAPQ RAGPAFRQLE AALGYEVKTQ GQLLVQALTH RSWVGQGSSY EREEFLGDAL
LDTWATTRLV ERFPHAPPRI LTFLRALLVS NGVISALAVR MLSLHKMVLH SSPALEAAMR
DAAVKAEAFE WKEVADGELT FMWSPPKVLG DVFEALVAVV FLDSNMELAP VFAVLDKLYG
DIMPSLRFEG VRDPYSTLLQ FKDAQACSQL SIKVIRIEPS TSIVPTLPRG GAVAPSRFLA
TVTSHEQVVA KQESEAKAVA RQMACRTALK VLEREGACGC REAARRDKEE RAAAAAAAAA
AEGAGEGEAA EERELGEDEE EEERQEDVPE LEAEPEKDDE LEEEEERELI GDEATSADAA
DPEPLLRVRE Y
//
