RNSA_KITAU
ID RNSA_KITAU Reviewed; 96 AA.
AC P05798;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Guanyl-specific ribonuclease Sa;
DE Short=RNase Sa;
DE EC=4.6.1.24;
GN Name=rnaSA;
OS Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Kitasatospora.
OX NCBI_TaxID=1894;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3098582; DOI=10.1016/0014-5793(86)81138-3;
RA Shlyapnikov S.V., Both V., Kulikov V.A., Dementiev A.A., Sevcik J.,
RA Zelinka J.;
RT "Amino acid sequence determination of guanyl-specific ribonuclease Sa from
RT Streptomyces aureofaciens.";
RL FEBS Lett. 209:335-339(1986).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=3118883;
RA Shlyapnikov S.V., Both V., Kulikov V.A., Dementiev A.A., Zelinka J.;
RT "Extracellular guanyl-specific ribonuclease Sa from the actinomycete
RT Streptomyces aureofaciens. Primary structure and homology with
RT ribonucleases from bacteria and fungi.";
RL Bioorg. Khim. 13:760-772(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=1654932; DOI=10.1107/s0108768190009569;
RA Sevcik J., Dodson E.J., Dodson G.G.;
RT "Determination and restrained least-squares refinement of the structures of
RT ribonuclease Sa and its complex with 3'-guanylic acid at 1.8-A
RT resolution.";
RL Acta Crystallogr. B 47:240-253(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8396032; DOI=10.1111/j.1432-1033.1993.tb18145.x;
RA Sevcik J., Zegers I., Wyns L., Dauter Z., Wilson K.S.;
RT "Complex of ribonuclease Sa with a cyclic nucleotide and a proposed model
RT for the reaction intermediate.";
RL Eur. J. Biochem. 216:301-305(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=15299531; DOI=10.1107/s0907444992007261;
RA Sevcik J., Hill C.P., Dauter Z., Wilson K.S.;
RT "Complex of ribonuclease from Streptomyces aureofaciens with 2'-GMP at 1.7-
RT A resolution.";
RL Acta Crystallogr. D 49:257-271(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), AND SEQUENCE REVISION TO 72.
RX PubMed=15299705; DOI=10.1107/s0907444995007669;
RA Sevcik J., Dauter Z., Lamzin V.S., Wilson K.S.;
RT "Ribonuclease from Streptomyces aureofaciens at atomic resolution.";
RL Acta Crystallogr. D 52:327-344(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF COMPLEX WITH BARSTAR.
RX PubMed=9757110; DOI=10.1107/s0907444998004429;
RA Sevcik J., Urbanikova L., Dauter Z., Wilson K.S.;
RT "Recognition of RNase Sa by the inhibitor barstar: structure of the complex
RT at 1.7 A resolution.";
RL Acta Crystallogr. D 54:954-963(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) AND MUTAGENESIS OF ASN-39.
RX PubMed=9819211; DOI=10.1021/bi9815243;
RA Hebert E.J., Giletto A., Sevcik J., Urbanikova L., Wilson K.S., Dauter Z.,
RA Pace C.N.;
RT "Contribution of a conserved asparagine to the conformational stability of
RT ribonucleases Sa, Ba, and T1.";
RL Biochemistry 37:16192-16200(1998).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=11455593; DOI=10.1002/prot.1085;
RA Laurents D., Perez-Canadillas J.M., Santoro J., Rico M., Schell D.,
RA Pace C.N., Bruix M.;
RT "Solution structure and dynamics of ribonuclease Sa.";
RL Proteins 44:200-211(2001).
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}.
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DR PIR; A25655; NRSM.
DR PDB; 1AY7; X-ray; 1.70 A; A=1-96.
DR PDB; 1BOX; X-ray; 1.60 A; A=1-96.
DR PDB; 1C54; NMR; -; A=1-96.
DR PDB; 1GMP; X-ray; 1.70 A; A/B=1-96.
DR PDB; 1GMQ; X-ray; 1.80 A; A/B=1-96.
DR PDB; 1GMR; X-ray; 1.77 A; A/B=1-96.
DR PDB; 1I70; X-ray; 1.70 A; A/B=1-96.
DR PDB; 1I8V; X-ray; 1.25 A; A/B=1-96.
DR PDB; 1LNI; X-ray; 1.00 A; A/B=1-96.
DR PDB; 1RGE; X-ray; 1.15 A; A/B=1-96.
DR PDB; 1RGF; X-ray; 1.20 A; A/B=1-96.
DR PDB; 1RGG; X-ray; 1.20 A; A/B=1-96.
DR PDB; 1RGH; X-ray; 1.20 A; A/B=1-96.
DR PDB; 1RSN; X-ray; 2.00 A; A/B=1-96.
DR PDB; 1SAR; X-ray; 1.80 A; A/B=1-96.
DR PDB; 1T2H; X-ray; 1.00 A; A/B=1-96.
DR PDB; 1T2I; X-ray; 1.10 A; A=1-96.
DR PDB; 1UCI; X-ray; 1.80 A; A/B=1-96.
DR PDB; 1UCJ; X-ray; 1.81 A; A/B=1-96.
DR PDB; 1UCK; X-ray; 1.80 A; A/B=1-96.
DR PDB; 1UCL; X-ray; 1.82 A; A/B=1-96.
DR PDB; 1YNV; X-ray; 1.20 A; X=1-96.
DR PDB; 1ZGX; X-ray; 1.13 A; A=1-63, B=64-96.
DR PDB; 2SAR; X-ray; 1.80 A; A/B=1-96.
DR PDB; 3A5E; X-ray; 1.60 A; A=1-96.
DR PDB; 4GHO; X-ray; 1.10 A; A/B=1-96.
DR PDB; 4J5G; X-ray; 1.31 A; A/B=1-94.
DR PDB; 4J5K; X-ray; 1.23 A; A/B=1-96.
DR PDBsum; 1AY7; -.
DR PDBsum; 1BOX; -.
DR PDBsum; 1C54; -.
DR PDBsum; 1GMP; -.
DR PDBsum; 1GMQ; -.
DR PDBsum; 1GMR; -.
DR PDBsum; 1I70; -.
DR PDBsum; 1I8V; -.
DR PDBsum; 1LNI; -.
DR PDBsum; 1RGE; -.
DR PDBsum; 1RGF; -.
DR PDBsum; 1RGG; -.
DR PDBsum; 1RGH; -.
DR PDBsum; 1RSN; -.
DR PDBsum; 1SAR; -.
DR PDBsum; 1T2H; -.
DR PDBsum; 1T2I; -.
DR PDBsum; 1UCI; -.
DR PDBsum; 1UCJ; -.
DR PDBsum; 1UCK; -.
DR PDBsum; 1UCL; -.
DR PDBsum; 1YNV; -.
DR PDBsum; 1ZGX; -.
DR PDBsum; 2SAR; -.
DR PDBsum; 3A5E; -.
DR PDBsum; 4GHO; -.
DR PDBsum; 4J5G; -.
DR PDBsum; 4J5K; -.
DR AlphaFoldDB; P05798; -.
DR SMR; P05798; -.
DR IntAct; P05798; 1.
DR STRING; 1894.JOER01000031_gene352; -.
DR DrugBank; DB03178; Guanosine-2',3'-cyclophosphorothioate.
DR DrugBank; DB01937; Guanosine-2'-monophosphate.
DR eggNOG; COG4290; Bacteria.
DR BRENDA; 4.6.1.24; 5978.
DR EvolutionaryTrace; P05798; -.
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; Direct protein sequencing; Disulfide bond; Endonuclease;
KW Hydrolase; Lyase; Nuclease; Secreted.
FT CHAIN 1..96
FT /note="Guanyl-specific ribonuclease Sa"
FT /id="PRO_0000137367"
FT ACT_SITE 54
FT /note="Proton acceptor"
FT ACT_SITE 85
FT /note="Proton donor"
FT DISULFID 7..96
FT MUTAGEN 39
FT /note="N->A,D,S: Decreases protein stability."
FT CONFLICT 72
FT /note="T -> C (in Ref. 1; AA sequence and 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1LNI"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1LNI"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:1LNI"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:1LNI"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1SAR"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1BOX"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1C54"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:1LNI"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1C54"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1LNI"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1LNI"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1LNI"
SQ SEQUENCE 96 AA; 10576 MW; FA4DB2FD0BA8A7E4 CRC64;
DVSGTVCLSA LPPEATDTLN LIASDGPFPY SQDGVVFQNR ESVLPTQSYG YYHEYTVITP
GARTRGTRRI ITGEATQEDY YTGDHYATFS LIDQTC
