ID   RNS3_KITAU              Reviewed;         141 AA.
AC   P30289;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Guanyl-specific ribonuclease Sa3;
DE            Short=RNase Sa3;
DE            EC=4.6.1.24;
DE   Flags: Precursor;
GN   Name=rnaSA3;
OS   Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=1894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC 12843
RC   / NCIMB 8234 / A-377;
RX   PubMed=1398084; DOI=10.1016/0378-1119(92)90082-z;
RA   Homerova D., Hollaenderova Z., Kormanec J., Sevcik J.;
RT   "Cloning and sequencing of the gene encoding a ribonuclease from
RT   Streptomyces aureofaciens CCM3239.";
RL   Gene 119:147-148(1992).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 45-141.
RX   PubMed=12228255; DOI=10.1074/jbc.m208425200;
RA   Sevcik J., Urbanikova L., Leland P.A., Raines R.T.;
RT   "X-ray structure of two crystalline forms of a streptomycete ribonuclease
RT   with cytotoxic activity.";
RL   J. Biol. Chem. 277:47325-47330(2002).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAA26809.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M82920; AAA26809.1; ALT_FRAME; Genomic_DNA.
DR   PIR; JC1287; JC1287.
DR   PDB; 1MGR; X-ray; 1.70 A; A=43-141.
DR   PDB; 1MGW; X-ray; 2.00 A; A=43-141.
DR   PDBsum; 1MGR; -.
DR   PDBsum; 1MGW; -.
DR   AlphaFoldDB; P30289; -.
DR   SMR; P30289; -.
DR   EvolutionaryTrace; P30289; -.
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   3D-structure; Disulfide bond; Endonuclease; Hydrolase; Lyase; Nuclease;
KW   Secreted; Signal.
FT   SIGNAL          1..36
FT                   /note="Or 43"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..141
FT                   /note="Guanyl-specific ribonuclease Sa3"
FT                   /id="PRO_0000030830"
FT   ACT_SITE        99
FT                   /note="Proton acceptor"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT   DISULFID        52..141
FT                   /evidence="ECO:0000250"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:1MGR"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:1MGR"
FT   HELIX           58..69
FT                   /evidence="ECO:0007829|PDB:1MGR"
FT   TURN            76..79
FT                   /evidence="ECO:0007829|PDB:1MGR"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:1MGR"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:1MGR"
FT   STRAND          124..129
FT                   /evidence="ECO:0007829|PDB:1MGR"
FT   STRAND          135..138
FT                   /evidence="ECO:0007829|PDB:1MGR"
SQ   SEQUENCE   141 AA;  14820 MW;  DB128BB3E60FDCF6 CRC64;
     MRIPPRLVAL AGAAAVAATL IAGPVAAAAP ASHAVAASSA ASASVKAVGR VCYSALPSQA
     HDTLDLIDEG GPFPYSQDGV VFQNREGLLP AHSTGYYHEY TVITPGSPTR GARRIITGQQ
     WQEDYYTADH YASFRRVDFA C