ID   RNI_AERHY               Reviewed;         215 AA.
AC   Q07465;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Ribonuclease {ECO:0000305};
DE            EC=3.1.27.- {ECO:0000269|PubMed:7685334};
DE   Flags: Precursor;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=Ah1133;
RX   PubMed=7685334; DOI=10.1128/jb.175.12.3710-3722.1993;
RA   Favre D., Ngai P.K., Timmis K.N.;
RT   "Relatedness of a periplasmic, broad-specificity RNase from Aeromonas
RT   hydrophila to RNase I of Escherichia coli and to a family of eukaryotic
RT   RNases.";
RL   J. Bacteriol. 175:3710-3722(1993).
CC   -!- FUNCTION: One of the few RNases that cleave the phosphodiester bond
CC       between any two nucleotide. Shows a preference for adenylic acid.
CC       {ECO:0000269|PubMed:7685334}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.4 mM for ApA (periplasmic form) {ECO:0000269|PubMed:7685334};
CC         KM=0.08 mM for ApA (cytoplasmic form) {ECO:0000269|PubMed:7685334};
CC         KM=0.8 mM for GpA (periplasmic form) {ECO:0000269|PubMed:7685334};
CC         KM=0.2 mM for GpA (cytoplasmic form) {ECO:0000269|PubMed:7685334};
CC         KM=1 mM for CpA (periplasmic form) {ECO:0000269|PubMed:7685334};
CC         KM=0.2 mM for CpA (cytoplasmic form) {ECO:0000269|PubMed:7685334};
CC         KM=1 mM for UpA (periplasmic form) {ECO:0000269|PubMed:7685334};
CC         KM=0.3 mM for UpA (cytoplasmic form) {ECO:0000269|PubMed:7685334};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:7685334}. Cytoplasm
CC       {ECO:0000269|PubMed:7685334}. Note=An RNase I-like form (periplasmic)
CC       and RNase I*-like form (cytoplasmic) appear to be isoforms apparently
CC       encoded by the same gene. The cytoplasmic form is less active towards
CC       natural polymer RNA. {ECO:0000269|PubMed:7685334}.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR   EMBL; X67054; CAA47438.1; -; Genomic_DNA.
DR   PIR; A47118; A47118.
DR   AlphaFoldDB; Q07465; -.
DR   SMR; Q07465; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   Gene3D; 3.90.730.10; -; 1.
DR   InterPro; IPR001568; RNase_T2-like.
DR   InterPro; IPR036430; RNase_T2-like_sf.
DR   InterPro; IPR018188; RNase_T2_His_AS_1.
DR   InterPro; IPR033130; RNase_T2_His_AS_2.
DR   PANTHER; PTHR11240; PTHR11240; 1.
DR   Pfam; PF00445; Ribonuclease_T2; 1.
DR   SUPFAM; SSF55895; SSF55895; 1.
DR   PROSITE; PS00530; RNASE_T2_1; 1.
DR   PROSITE; PS00531; RNASE_T2_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endonuclease; Hydrolase; Nuclease; Periplasm; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..215
FT                   /note="Ribonuclease"
FT                   /id="PRO_0000030962"
FT   REGION          144..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        62
FT                   /evidence="ECO:0000250|UniProtKB:P08056"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000250|UniProtKB:P08056"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000250|UniProtKB:P08056"
SQ   SEQUENCE   215 AA;  24410 MW;  4442BCE5B0F67203 CRC64;
     MKKIVVLLGM LLAPWFSSAV QAKGEAGEFD YYAMALSWSP EHCAIKPADR DQCSRQLGFV
     LHGLWPQYQR GYPSSCTRER LDPAMEQEFA GLYPSRFLYR HEWEKHGTCS GLSQHDFHQL
     ASDLRQKRED PGRLSVSCRA AAQKPLPAQG GSGQCQRLAG PGQHHGGLRR RWRFLREVYI
     CLNKEGTDAV TCSDEMQKRE LPSCGQPDFL LRTVR