ID   RNPB_PENBR              Reviewed;         102 AA.
AC   P07446;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Guanyl-specific ribonuclease Pb1;
DE            Short=RNase Pb1;
DE            EC=4.6.1.24;
OS   Penicillium brevicompactum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5074;
RN   [1]
RP   PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX   PubMed=3922722;
RA   Shlyapnikov S.V., Yakovlev G.I., Kulikov V.A.;
RT   "Analysis of the guanyl-specific ribonuclease structures in fungi:
RT   determination of the amino acid sequence and prediction of the secondary
RT   ribonuclease structure in Penicillium brevicompactum.";
RL   Dokl. Akad. Nauk SSSR 281:226-229(1985).
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   -!- 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; A23350; NRPLTB.
DR   AlphaFoldDB; P07446; -.
DR   SMR; P07446; -.
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   Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW   Nuclease.
FT   CHAIN           1..102
FT                   /note="Guanyl-specific ribonuclease Pb1"
FT                   /id="PRO_0000137372"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        56
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        90
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        2..10
FT                   /evidence="ECO:0000269|PubMed:3922722"
FT   DISULFID        6..101
FT                   /evidence="ECO:0000269|PubMed:3922722"
SQ   SEQUENCE   102 AA;  10803 MW;  1D8AA5602C93DEEE CRC64;
     ACAATCGTVC YTSSAISSAQ AAGYNLYSTN DDVSNYPHEY HNYEGFDFPV SGTYYEFPIL
     KSGKVYTGSS PGADRVIFND DDELAGVITH TGASGNNFVA CT