RN_BACIN
ID RN_BACIN Reviewed; 162 AA.
AC P00649;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 3.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Ribonuclease;
DE EC=3.1.27.-;
DE AltName: Full=Binase;
DE AltName: Full=RNase Bi;
DE Flags: Precursor;
OS Bacillus intermedius.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1400;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=7P;
RX PubMed=1594455; DOI=10.1093/nar/20.9.2375;
RA Schulga A.A., Nurkiyanova K.M., Zakharyev V.M., Kirpichnikov M.P.,
RA Skryabin K.G.;
RT "Cloning of the gene encoding RNase binase from Bacillus intermedius 7P.";
RL Nucleic Acids Res. 20:2375-2375(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=7P;
RX PubMed=2632211;
RA Nurkiyanova K.M., Shulga A.A., Zakharyev V.M., Kirpichnikov M.P.,
RA Skryabin K.G., Baev A.A.;
RT "The cloning and determination of the nucleotide sequence of the RNase gene
RT in Bacillus intermedius.";
RL Dokl. Akad. Nauk SSSR 309:1476-1479(1989).
RN [3]
RP PROTEIN SEQUENCE OF 54-162.
RC STRAIN=7P;
RX PubMed=761620; DOI=10.1016/0014-5793(79)80056-3;
RA Aphanasenko G.A., Dudkin S.M., Kaminir L.B., Leshchinskaya I.B.,
RA Severin E.S.;
RT "Primary structure of ribonuclease from Bacillus intermedius 7P.";
RL FEBS Lett. 97:77-80(1979).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) AND MUTAGENESIS OF HIS-154.
RX PubMed=9153077; DOI=10.1093/protein/10.3.273;
RA Okorokov A.L., Panov K.I., Offen W.A., Mukhortov V.G., Antson A.A.,
RA Karpeisky M.Y., Wilkinson A.J., Dodson G.G.;
RT "RNA cleavage without hydrolysis. Splitting the catalytic activities of
RT binase with Asn101 and Thr101 mutations.";
RL Protein Eng. 10:273-278(1997).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=9708913; DOI=10.1016/s0014-5793(98)00765-0;
RA Reibarkh M.Y.A., Nolde D.E., Vasilieva L.I., Bocharov E.V., Shulga A.A.,
RA Kirpichnikov M.P., Arseniev A.S.;
RT "Three-dimensional structure of binase in solution.";
RL FEBS Lett. 431:250-254(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 54-162.
RX PubMed=11976484; DOI=10.1107/s0907444902003207;
RA Polyakov K.M., Lebedev A.A., Okorokov A.L., Panov K.I., Schulga A.A.,
RA Pavlovsky A.G., Karpeisky M.Y., Dodson G.G.;
RT "The structure of substrate-free microbial ribonuclease binase and of its
RT complexes with 3'GMP and sulfate ions.";
RL Acta Crystallogr. D 58:744-750(2002).
CC -!- FUNCTION: This is a purine-specific ribonuclease.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the ribonuclease N1/T1 family. {ECO:0000305}.
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DR EMBL; X53697; CAA37735.1; -; Genomic_DNA.
DR PIR; A00796; NRBSI.
DR PIR; S22653; S22653.
DR PDB; 1BUJ; NMR; -; A=54-162.
DR PDB; 1GOU; X-ray; 1.65 A; A/B=54-162.
DR PDB; 1GOV; X-ray; 2.00 A; A/B=54-162.
DR PDB; 1GOY; X-ray; 2.00 A; A/B=54-162.
DR PDB; 2RBI; X-ray; 2.20 A; A/B=54-162.
DR PDB; 4HAA; X-ray; 1.90 A; A/B/C/D=54-162.
DR PDBsum; 1BUJ; -.
DR PDBsum; 1GOU; -.
DR PDBsum; 1GOV; -.
DR PDBsum; 1GOY; -.
DR PDBsum; 2RBI; -.
DR PDBsum; 4HAA; -.
DR AlphaFoldDB; P00649; -.
DR SMR; P00649; -.
DR BRENDA; 4.6.1.24; 664.
DR EvolutionaryTrace; P00649; -.
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 3D-structure; Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..53
FT /evidence="ECO:0000269|PubMed:761620"
FT /id="PRO_0000030824"
FT CHAIN 54..162
FT /note="Ribonuclease"
FT /id="PRO_0000030825"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT ACT_SITE 154
FT /note="Proton donor"
FT CONFLICT 74..75
FT /note="DN -> ND (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..120
FT /note="SG -> GS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:1GOU"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:1GOU"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1GOU"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1GOU"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1GOU"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1BUJ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1BUJ"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:1GOU"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1GOU"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1GOU"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1GOU"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1GOU"
SQ SEQUENCE 162 AA; 17956 MW; CD6740EDFBCF5295 CRC64;
MKKISSVFTM FALIAAILFS GFIPQQAYAE TPLTQTATNE TATIQLTSDV HTLAVINTFD
GVADYLIRYK RLPDNYITKS QASALGWVAS KGNLAEVAPG KSIGGDVFSN REGRLPSASG
RTWREADINY VSGFRNADRL VYSSDWLIYK TTDHYATFTR IR
