ID RNPO_PLEOS Reviewed; 101 AA. AC P81762; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Guanyl-specific ribonuclease Po1; DE Short=RNase Po1; DE EC=4.6.1.24; OS Pleurotus ostreatus (Oyster mushroom) (White-rot fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus. OX NCBI_TaxID=5322; RN [1] RP PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, AND CHARACTERIZATION. RX PubMed=7798182; DOI=10.1093/oxfordjournals.jbchem.a124498; RA Nomura H., Inokuchi N., Kobayashi H., Koyama T., Iwama M., Ohgi K., RA Irie M.; RT "Purification and primary structure of a new guanylic acid specific RT ribonuclease from Pleurotus ostreatus."; RL J. Biochem. 116:26-33(1994). CC -!- CATALYTIC ACTIVITY: CC Reaction=[RNA] containing guanosine + H2O = an [RNA fragment]-3'- CC guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA CC fragment].; EC=4.6.1.24; CC -!- ACTIVITY REGULATION: Inhibited by divalent cations. Inhibition CC decreases in the order zinc, lead, cadmium, nickel, mercury. CC -!- SIMILARITY: Belongs to the ribonuclease N1/T1 family. {ECO:0000305}. 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 PIR; JX0333; JX0333. DR PDB; 3WHO; X-ray; 1.85 A; A/B/C=1-101. DR PDB; 3WR2; X-ray; 1.75 A; A/B/C/D/E/F=1-101. DR PDBsum; 3WHO; -. DR PDBsum; 3WR2; -. DR AlphaFoldDB; P81762; -. DR SMR; P81762; -. DR VEuPathDB; FungiDB:PC9H_003443; -. DR VEuPathDB; FungiDB:PLEOSDRAFT_1088612; -. DR BRENDA; 4.6.1.24; 4912. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046589; F:ribonuclease T1 activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR CDD; cd00606; fungal_RNase; 1. DR Gene3D; 3.10.450.30; Microbial ribonucleases; 1. DR InterPro; IPR016191; Ribonuclease/ribotoxin. DR PANTHER; PTHR42104; EXTRACELLULAR GUANYL-SPECIFIC RIBONUCLEASE RNTA (AFU_ORTHOLOGUE AFUA_4G03230); 1. DR PANTHER; PTHR42104:SF1; EXTRACELLULAR GUANYL-SPECIFIC RIBONUCLEASE RNTA (AFU_ORTHOLOGUE AFUA_4G03230); 1. DR SUPFAM; SSF53933; Microbial ribonucleases; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease; KW Hydrolase; Lyase; Nuclease; Pyrrolidone carboxylic acid. FT CHAIN 1..101 FT /note="Guanyl-specific ribonuclease Po1" FT /id="PRO_0000137374" FT ACT_SITE 36 FT /evidence="ECO:0000250" FT ACT_SITE 54 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 87 FT /note="Proton donor" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:7798182" FT DISULFID 7..84 FT /evidence="ECO:0000255" FT DISULFID 9..99 FT /evidence="ECO:0000250" FT DISULFID 48..82 FT /evidence="ECO:0000250" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:3WR2" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:3WR2" FT HELIX 16..27 FT /evidence="ECO:0007829|PDB:3WR2" FT STRAND 34..38 FT /evidence="ECO:0007829|PDB:3WR2" FT STRAND 50..56 FT /evidence="ECO:0007829|PDB:3WR2" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:3WR2" FT STRAND 70..76 FT /evidence="ECO:0007829|PDB:3WR2" FT STRAND 80..87 FT /evidence="ECO:0007829|PDB:3WR2" SQ SEQUENCE 101 AA; 10789 MW; FF30477497990D00 CRC64; QTGVRSCNCA GRSFTGTDVT NAIRSARAGG SGNYPHVYNN FEGFSFSCTP TFFEFPVFRG SVYSGGSPGA DRVIYDQSGR FCACLTHTGA PSTNGFVECR F //