ID M5FRM0_DACPD Unreviewed; 1400 AA.
AC M5FRM0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Ribonuclease III {ECO:0000313|EMBL:EJT97649.1};
GN ORFNames=DACRYDRAFT_119311 {ECO:0000313|EMBL:EJT97649.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT97649.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJT97649.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT97649.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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DR EMBL; JH795876; EJT97649.1; -; Genomic_DNA.
DR STRING; 1858805.M5FRM0; -.
DR HOGENOM; CLU_000907_4_2_1; -.
DR OMA; TEFNYER; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000030653; 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:0004525; F:ribonuclease III activity; IEA:InterPro.
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; 1.
DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 2.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
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; PF03368; Dicer_dimer; 1.
DR Pfam; PF00636; Ribonuclease_3; 2.
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; PS50142; RNASE_3_2; 2.
PE 4: Predicted;
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:UP000030653}.
FT DOMAIN 833..918
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1100..1256
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1400 AA; 156966 MW; AC9A1F316DE3079A CRC64;
MDREERIQDA ERSRERQRQA SRAQRDAESS LGHEDVALGV TDSNNVSSEE NLRKRKRHVA
IDDSDDSDDV EEIEFELSQE VPPLEPAPRH IYGGKTRAAS TTTTELVLPC DPSPFTEASL
GPLYNQIHAL DPDELVFKKN FKSVQLLVTE LGPYAADMIW QRYAGAQEAR RNGLVKEKRV
PASFSEVEEM RSKLVDMVRA HKFPSIVLDP QSTDCNASPR LLTLLQVLKQ MMAKEKDRFR
GIIFVYRRTT AKALADLLNR NAQVLPNVRA RPLIGSSAVL MDPNADHLTK TQATTQFRDG
TINLLVTTGI GVDLSVERCS IVIVFDSFSA HAAGQLRQSH LLKITSIFLI LIEKGKQKDI
QALSAFLPRR SKEKSEEEST PPAAEHPRST GIDSEDEDQA SILVPETGAR VSALDALQVL
TRYVSIKEKS AVSLNVDYHV MGENNRIFRC TIRFPPSAEL EDVTSESCPS KAAARRQAAY
MACEELNARG LLGALVAQAG KKLKTITKVT PPSVFDNEVG VDVERKLSKG RSRKDRSSKL
YPRKKPDVWN TCLLVHNDVL FPFIIHLDAR DAKLPGVYRT MCLLTRIRLP DLAPFELYFP
ELKKSEDQAT PPTVTARFLR SEPLHLEPEQ LIAVHRYTIR VVRSVTSRQY ICQRDKMVYY
LLPLKLGWSP RTRPTNSPSV YAIEDEIDWA DVEAGAGQLP YLPLDMEKLE EEVKDAVLQD
RQMEFTRKYE PVRVRHDLTP LSKPKDSERE QQYASILEFC RANIRNFKGI EDESQPLIEV
GKMAPPLSRL SPLCHSAPSS RNPPAKYLMP ELCVKYCLSL SSYRTSMILP SVMARVEEML
LVQECNSVVF HDRLDEVFLL PALTSPSAGA GYDYQRLELL GDSFLKYISS IFLFVTCPQD
GEGSLHIHRQ RIISNSALQF HSDRVGQLPQ YIQSRQHSPR QWCPPNFLLY HPCMASALDT
SEKFIQGMEE RIEASNDGPT AGGSPPESGV TKALESHQAN AETSPDNSTV SRSPMPYSAR
ERALMREEQH QELGDKSVAD VAEAVLGAAW LTGQREMALY VCHILGLPMT RMGSWDFLRD
HAHIFFHEEL DIGPLSQPKV EAVEAILGHK FKNPFLAATA LTHSSMSSTD FPCYERLEFI
GDAILDFVTV RLLYMRWGEL HEGWLTMLKG AIVSNAALAA FCVDLGLHHY IIHDSPHLVE
TVSSYAKEIT KAKEEDLAAA AAEDRAPGEY WVTLEPPKVL SDIVEALLGA IYVSDSFDPS
GYENVFDRLF KPFFMKRVSL NTLSQHPTSL LFALLQQRGC HRFELTKTRA ETDLLTEVQC
DFVLHGKVLA TSIHSSSAGA SRRASAMALE LIQTQPELLD KLCSCTKIRN ESEAQQPPSD
PIPVEEEEED LLAKEDLSGS
//
