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Database: UniProt
Entry: F8PH45_SERL3
LinkDB: F8PH45_SERL3
Original site: F8PH45_SERL3 
ID   F8PH45_SERL3            Unreviewed;       322 AA.
AC   F8PH45;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=DRBM domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SERLA73DRAFT_174019 {ECO:0000313|EMBL:EGO04941.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
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DR   EMBL; GL945474; EGO04941.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8PH45; -.
DR   STRING; 936435.F8PH45; -.
DR   eggNOG; ENOG502SNSJ; Eukaryota.
DR   HOGENOM; CLU_056047_1_0_1; -.
DR   InParanoid; F8PH45; -.
DR   OMA; YAMGWAP; -.
DR   OrthoDB; 1704304at2759; -.
DR   Proteomes; UP000008063; 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   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:UP000008063};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00266}.
FT   DOMAIN          79..170
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          251..318
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
SQ   SEQUENCE   322 AA;  35260 MW;  2F12BA9AB58554E4 CRC64;
     MLTPRLRNHV FDSSIMPSTS TPDFDSGKAS VDTINVALKR SRSPTQMGDI PELPKLQGES
     ILEVFTHRSL RIACKASYHD SETLAVLGEE VLHMMTTQLL LFKKPRLKVE EITNKRHMLL
     QDEMIDNWTN LYRLRNQVRC DPSSLSSLNS VQEGRLLFNA YLGAVFAQGG IKPVQEWIGG
     LFRLSSDLFR DSSTAEPGPS GLSSQPAKKL KVDDEHYSVL PPSSAPPPIP SPPPFTAFLS
     NPLTPAQPNL AFLPLFNQAA HQRGVTISYP ATFSGPAHAG TWAITCVVNG IKKGHGCGPS
     KQLAKEEAAK EAYFAMGWAP RG
//
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