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 02-SEP-2026, entry version 134. 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; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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=1-96. DR PDB; 4J5K; X-ray; 1.23 A; A/B=1-96. DR AlphaFoldDB; P05798; -. DR MDposit; P05798; -. DR SMR; P05798; -. DR IntAct; P05798; 1. 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:0046589; F:ribonuclease T1 activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR CDD; cd00607; RNase_Sa; 1. DR Gene3D; 3.10.450.30; Microbial ribonucleases; 1. DR InterPro; IPR000026; N1-like. DR InterPro; IPR016191; Ribonuclease/ribotoxin. DR Pfam; PF00545; Ribonuclease; 1. DR SUPFAM; SSF53933; Microbial ribonucleases; 1. 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; -. 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 //