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   03-AUG-2022, entry version 71.
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; 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}.
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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:PLEOSDRAFT_1088612; -.
DR   BRENDA; 4.6.1.24; 4912.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
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   InterPro; IPR000026; Gua-sp_ribonuclease_N1/T1/U2.
DR   InterPro; IPR016191; Ribonuclease/ribotoxin.
DR   Pfam; PF00545; Ribonuclease; 1.
DR   SUPFAM; SSF53933; SSF53933; 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"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:3WHO"
SQ   SEQUENCE   101 AA;  10789 MW;  FF30477497990D00 CRC64;
     QTGVRSCNCA GRSFTGTDVT NAIRSARAGG SGNYPHVYNN FEGFSFSCTP TFFEFPVFRG
     SVYSGGSPGA DRVIYDQSGR FCACLTHTGA PSTNGFVECR F