ID   RNPC_PENCH              Reviewed;         102 AA.
AC   P09647;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Guanyl-specific ribonuclease Pc;
DE            Short=RNase Pc;
DE            EC=4.6.1.24;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=152A;
RX   PubMed=3080339; DOI=10.1016/0014-5793(86)80208-3;
RA   Shlyapnikov S.V., Bezborodova S.I., Kulikov V.A., Yakovlev G.I.;
RT   "Express analysis of protein amino acid sequences. Primary structure of
RT   Penicillium chrysogenum 152A guanyl-specific ribonuclease.";
RL   FEBS Lett. 196:29-33(1986).
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}.
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DR   PIR; A23620; A23620.
DR   AlphaFoldDB; P09647; -.
DR   SMR; P09647; -.
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   Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW   Nuclease.
FT   CHAIN           1..102
FT                   /note="Guanyl-specific ribonuclease Pc"
FT                   /id="PRO_0000137373"
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:0000250"
FT   DISULFID        6..101
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   102 AA;  10745 MW;  49D8947B267D5506 CRC64;
     ACAATCGSVC YTSSAISAAQ EAGYDLYSAN DDVSNYPHEY RNYEGFDFPV SGTYYEFPIL
     RSGAVYSGNS PGADRVVFNG NDQLAGVITH TGASGNNFVA CD
//