ID   RN_NIACI                Reviewed;         110 AA.
AC   P35078; Q45109;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Ribonuclease;
DE            EC=3.1.27.-;
DE   AltName: Full=RNase Bci;
OS   Niallia circulans (Bacillus circulans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=1397;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=BCF 247;
RX   PubMed=8224254; DOI=10.1016/0014-5793(93)81721-b;
RA   Dementiev A.A., Moiseyev G.P., Shlyapnikov S.V.;
RT   "Primary structure and catalytic properties of extracellular ribonuclease
RT   of Bacillus circulans.";
RL   FEBS Lett. 334:247-249(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8183279;
RA   Fedorova N.D., Schulga A.A., Peredelchuk M.Y.U., Kozharinova L.V.,
RA   Golyshin P.N., Ryabchenko N.F., Kirpichnikov M.P.;
RT   "Cloning of the gene for extracellular Bacillus circulans RNAase.";
RL   Mol. Biol. (Mosk.) 28:468-471(1994).
CC   -!- FUNCTION: Hydrolyzes phosphodiester bonds in RNA, poly- and
CC       oligoribonucleotides resulting in 3'-nucleoside monophosphates via
CC       2',3'-cyclophosphate intermediates.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the ribonuclease N1/T1 family. {ECO:0000305}.
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DR   EMBL; Z29626; CAA82734.1; -; Genomic_DNA.
DR   PIR; S38944; S38944.
DR   AlphaFoldDB; P35078; -.
DR   BMRB; P35078; -.
DR   SMR; P35078; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   CDD; cd00933; barnase; 1.
DR   InterPro; IPR001887; Barnase.
DR   InterPro; IPR000026; Gua-sp_ribonuclease_N1/T1/U2.
DR   InterPro; IPR016191; Ribonuclease/ribotoxin.
DR   Pfam; PF00545; Ribonuclease; 1.
DR   PIRSF; PIRSF001013; Barnase; 1.
DR   PRINTS; PR00117; BARNASE.
DR   SUPFAM; SSF53933; SSF53933; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endonuclease; Hydrolase; Nuclease; Secreted.
FT   CHAIN           1..110
FT                   /note="Ribonuclease"
FT                   /id="PRO_0000137365"
FT   ACT_SITE        73
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        102
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        101
FT                   /note="D -> H (in Ref. 2; CAA82734)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   110 AA;  12382 MW;  110FF12553730250 CRC64;
     AQVINTFDGV ADYLLTYHKL PDNYITKSEA QALGWVASKG NLADVAPGKS IGGDIFSNRE
     GKLPAKSGRT WREADINYTS GFRNSDRILY SSDWLIYKTT DHYKTFTKIR