ID A0A165I1R6_9BASI Unreviewed; 405 AA.
AC A0A165I1R6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ribonuclease III {ECO:0000313|EMBL:KZT60023.1};
GN ORFNames=CALCODRAFT_159370 {ECO:0000313|EMBL:KZT60023.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT60023.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT60023.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT60023.1,
RC ECO:0000313|Proteomes:UP000076842};
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; KV423935; KZT60023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165I1R6; -.
DR STRING; 1353952.A0A165I1R6; -.
DR InParanoid; A0A165I1R6; -.
DR OrthoDB; 5475137at2759; -.
DR Proteomes; UP000076842; 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; 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 PANTHER; PTHR14950; DICER-RELATED; 1.
DR PANTHER; PTHR14950:SF37; ENDORIBONUCLEASE DICER; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF00636; Ribonuclease_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:UP000076842};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 47..171
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 294..367
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 405 AA; 44293 MW; 388E8C157E4B96E4 CRC64;
MGTGDDPRSD HGDSSSLSDS VASMSFAEKS AGETEEQAPK LPPLPEIQSR DILLEVFMHR
SVLARPSTLF QDSPNDLFRD NERLEHLGDA VVQLCATMLI RDLYPTLRVG PASKVRTRVV
SNVALAKHTA AYGLHEKLGV SHAQERQLKQ SIAVRGDLFE AYVGGVFKDS EYSLPPVYKW
LKELFTPVVR QAYEQEWADH SVSVLGDVPS PAPEGVTSSK SPGDSLAGTS QEPVMVATAL
HEARPILPLT MSTPTLAPAT AAVPISPYSA IRAPTIVSAP PSPYRFPAPK TESGQLSFLN
QCLIQRGKTI DWTFDERGGN KTTPLWAVEA WIKNDAGMDE CVGRAQAPTK KAAKNEAARQ
AIAYLKYAVR GLRFLRAPGY VGLIVHKVKI VHPFHPRRLL YINLI
//
