RN_WEICA
ID RN_WEICA Reviewed; 109 AA.
AC P37203;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Ribonuclease;
DE EC=3.1.27.-;
DE AltName: Full=RNase Bco;
OS Weizmannia coagulans (Bacillus coagulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Weizmannia.
OX NCBI_TaxID=1398;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=8220218;
RA Shlyapnikov S.V., Dementiev A.A.;
RT "Amino acid sequence and catalytic properties of the Bacillus coagulans
RT extracellular ribonuclease.";
RL Dokl. Akad. Nauk 332:382-384(1993).
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 AlphaFoldDB; P37203; -.
DR SMR; P37203; -.
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..109
FT /note="Ribonuclease"
FT /id="PRO_0000137366"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 109 AA; 12182 MW; 6EC8CA58F0D29B96 CRC64;
AVINTFDGVA DYLIRYKRLP DNYITKSQAS ALGWVASKGN LAEVAPGKSI GGDVFSNREG
RLPSASGRTW READINYVSG FRNADRLVYS SDWLIYKTTD HYATFARIR