ID A0A061H1H1_9BASI Unreviewed; 492 AA.
AC A0A061H1H1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=RNase III domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFL1_06415 {ECO:0000313|EMBL:EPQ25959.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ25959.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ25959.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ25959.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE361648; EPQ25959.1; -; Genomic_DNA.
DR RefSeq; XP_007882148.1; XM_007883957.1.
DR AlphaFoldDB; A0A061H1H1; -.
DR GeneID; 19320492; -.
DR KEGG; pfp:PFL1_06415; -.
DR eggNOG; KOG3769; Eukaryota.
DR HOGENOM; CLU_034765_0_1_1; -.
DR OrthoDB; 1384985at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd19873; DSRM_MRPL3_like; 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; IPR044443; Ribosomal_mL44_DSRM_fung.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR11207:SF32; 54S RIBOSOMAL PROTEIN L3, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11207; RIBONUCLEASE III; 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:UP000053664};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 164..333
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 360..430
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 50846 MW; 771B147D6A24F59A CRC64;
MSSSRSVARA ARPLLQHSSS APRLRSATPS TSAIAGSSSP LASSSAASSS AASSSSSSSS
SASSSALHTS SHRAASPAAV ASTAVAGGAS SSPLDRHAPA SHLPQLARKD AALYAALRPP
PLSAVAALAA RLNLLPASLD APTRSRRIQL VYQACTHPSF QELVKKAAEQ GGLHLEVSGA
GLVRKSPEAN PLDSLQYLPQ QIASPDADAP AAADAGLANR ALSTVGNSLL GMMASEYLHL
RYPNLPTRVL KAAVAAYVGP STLADVAGEI GLGGQGILRW NRQARVPTRS APAPTKGDIA
AKSAPSRTRG LLSRDVSADA MRALVAVIFQ ELGLSAARHF ITTHFLSRNL DLASLLKFAD
PKRALSATCA KHGREAPQSR LIAESGRLSI NPIFVVGVYS GMQKVGEGSG SSIRMAEYRA
AEDALRRLFL AQTPIEDLNL PSTTLDAVYG PKDGRKPFIP SSIPVYDGAG KTYSPLPLGA
CEVLEAAGKD RQ
//
