RNA1_ASPPL
ID RNA1_ASPPL Reviewed; 104 AA.
AC Q7M515;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Guanyl-specific ribonuclease Ap1;
DE Short=ApI;
DE Short=RNase Ap1;
DE EC=4.6.1.24;
OS Aspergillus pallidus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=29839;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3139002;
RA Shlyapnikov S.V., Bezborodova S.I., Dementiev A.A., Kulikov V.A.;
RT "Amino acid sequence of ribonuclease Ap1 from Aspergillus pallidus.";
RL Bioorg. Khim. 14:589-595(1988).
RN [2]
RP PROTEIN SEQUENCE, AND CRYSTALLIZATION.
RX PubMed=3140903;
RA Bezborodova S.I., Ermekbaeva L.A., Shlyapnikov S.V., Polyakov K.M.,
RA Bezborodov A.M.;
RT "Ribonuclease Ap1 of Aspergillus pallidus: purification, determination of
RT primary structure and crystallization.";
RL Biokhimiia 53:965-973(1988).
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 -!- SUBCELLULAR LOCATION: Secreted.
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; JN0429; JN0429.
DR AlphaFoldDB; Q7M515; -.
DR SMR; Q7M515; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Secreted.
FT CHAIN 1..104
FT /note="Guanyl-specific ribonuclease Ap1"
FT /id="PRO_0000137371"
FT ACT_SITE 40
FT /evidence="ECO:0000250"
FT ACT_SITE 58
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 92
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT DISULFID 2..10
FT /evidence="ECO:0000250"
FT DISULFID 6..103
FT /evidence="ECO:0000250"
SQ SEQUENCE 104 AA; 11043 MW; 1C106140955A4AE6 CRC64;
DCDYTCGSHC YSASAVSDAQ SAGYQLYSAG QSVGRSRYPH QYRNYEGFNF PVSGNYYEWP
ILSSGSTYNG GSPGADRVVF NNNDELAGLI THTGASGNGF VACG
