ID V2YGU9_MONRO Unreviewed; 256 AA.
AC V2YGU9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Ribonuclease iii {ECO:0000313|EMBL:ESK90929.1};
GN ORFNames=Moror_16430 {ECO:0000313|EMBL:ESK90929.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK90929.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK90929.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK90929.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK90929.1}.
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DR EMBL; AWSO01000395; ESK90929.1; -; Genomic_DNA.
DR RefSeq; XP_007849772.1; XM_007851581.1.
DR AlphaFoldDB; V2YGU9; -.
DR STRING; 1381753.V2YGU9; -.
DR KEGG; mrr:Moror_16430; -.
DR HOGENOM; CLU_056047_1_0_1; -.
DR OrthoDB; 1694368at2759; -.
DR Proteomes; UP000017559; 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 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 SMART; SM00358; DSRM; 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:UP000017559};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 13..127
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 186..253
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 148..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 256 AA; 28769 MW; 5A533D757D2BB936 CRC64;
MSAGPILPPL PSIDNEDLTL ALFTHDSVLR QHNPEIGDVR RFQIIGRQVM EFIVTDHYFT
SRPTLTHDAL QGEKNRALDM DSYKYWFEQY RLRNKFVATP GTTPFQDDEE IRDYFHRIIG
AIYYCNGIEV TKAWIIALID PNHQPLEPPS YATSPAQSTA FLPPQPSSPP PPTPSSASTS
GLLPLPMLSL VNQLATQLRM DIRYDGESTG PPHQPTWTVK CMIQNIERGR GIGRSQKAAK
EEAARQAWVN MGWGPG
//
