ID A0A165C8Z2_9APHY Unreviewed; 340 AA.
AC A0A165C8Z2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Ribonuclease III {ECO:0000313|EMBL:KZT02407.1};
GN ORFNames=LAESUDRAFT_406694 {ECO:0000313|EMBL:KZT02407.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT02407.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT02407.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT02407.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV427652; KZT02407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165C8Z2; -.
DR STRING; 1314785.A0A165C8Z2; -.
DR InParanoid; A0A165C8Z2; -.
DR OrthoDB; 1704304at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
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; cd10845; DSRM_RNAse_III_family; 1.
DR CDD; cd00593; RIBOc; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF14622; Ribonucleas_3_3; 1.
DR SMART; SM00358; DSRM; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 70..186
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 246..326
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 340 AA; 37219 MW; 6CA1FA01E8E7D257 CRC64;
MVKAQVKGLS MQSETHQWLA PSQEGTWPSS AGSADSSIAR TGSQAPNLKR PRPSSTNMDA
PPPAPKLRGD IILEVFTHKS LRFPGAPTNE ESEYGDNERL SVLGEKVLET AVTFTLFNKK
PMIKAQEIES QRMEVLSDAN YNNWVINYKL REKVRCSPDA VATLTNPKET NLLFCSYVGA
VYVQNGMETV QNWIGQLIDP EYEPPVPAAD GEPYTYKRVK TEPMSSPTPP PTMHQPPPPM
APPPPLPINP LAPAQPQAAF LPLFNQTANQ RRLAVEYPAQ FSGPAHAGRW TVQCVVNGIP
KGEGSGASKQ LAKEEAARQA YYSMGWAPRE CPATPTSDVQ
//
