ID RNF1_GIBFU Reviewed; 131 AA. AC P10282; O74124; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 4. DT 27-MAR-2024, entry version 125. DE RecName: Full=Guanyl-specific ribonuclease F1; DE Short=RNase F1; DE EC=4.6.1.24; DE Flags: Precursor; OS Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium OS fujikuroi). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium; OC Fusarium fujikuroi species complex. OX NCBI_TaxID=5127; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9679656; DOI=10.1080/15216549800202942; RA Yoshida H., Iizuka M., Norioka N., Norioka S., Sakiyama F.; RT "Cloning and sequencing of cDNA encoding ribonuclease F1 from Fusarium RT moniliforme."; RL Biochem. Mol. Biol. Int. 45:555-560(1998). RN [2] RP PROTEIN SEQUENCE OF 26-131, AND PYROGLUTAMATE FORMATION AT GLN-26. RX PubMed=6433932; RA Hirabayashi J., Yoshida H.; RT "The primary structure of ribonuclease F1 from Fusarium moniliforme."; RL Biochem. Int. 7:255-262(1983). RN [3] RP PROTEIN SEQUENCE OF 26-131, AND DISULFIDE BONDS. RX PubMed=3103481; DOI=10.1016/0003-2697(86)90343-x; RA Yoshida H., Naijo S.; RT "Peptide fractionation by high-performance liquid chromatography on an RT Asahipak GS-320 column: application to determination of the disulfide RT pairings in ribonuclease F1."; RL Anal. Biochem. 159:273-279(1986). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 26-131. RX PubMed=8386773; DOI=10.1006/jmbi.1993.1214; RA Vassylyev D.G., Katayanagi K., Ishikawa K., Tsujimoto-Hirano M., Danno M., RA Paehler A., Matsumoto O., Matsushima M., Yoshida H., Morikawa K.; RT "Crystal structures of ribonuclease F1 of Fusarium moniliforme in its free RT form and in complex with 2'GMP."; RL J. Mol. Biol. 230:979-996(1993). RN [5] RP STRUCTURE BY NMR OF 26-131. RX PubMed=1511688; DOI=10.1111/j.1432-1033.1992.tb17157.x; RA Nakai T., Yoshikawa W., Nakamura H., Yoshida H.; RT "The three-dimensional structure of guanine-specific ribonuclease F1 in RT solution determined by NMR spectroscopy and distance geometry."; RL Eur. J. Biochem. 208:41-51(1992). 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 -!- 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 EMBL; AB006460; BAA31984.1; -; mRNA. DR PIR; JS0484; JS0484. DR PDB; 1FUS; X-ray; 1.30 A; A=27-131. DR PDB; 1FUT; X-ray; 2.00 A; A=27-131. DR PDB; 1RCK; NMR; -; A=27-131. DR PDB; 1RCL; NMR; -; A=27-131. DR PDBsum; 1FUS; -. DR PDBsum; 1FUT; -. DR PDBsum; 1RCK; -. DR PDBsum; 1RCL; -. DR AlphaFoldDB; P10282; -. DR SMR; P10282; -. DR EvolutionaryTrace; P10282; -. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. 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 CDD; cd00606; fungal_RNase; 1. DR Gene3D; 3.10.450.30; Microbial ribonucleases; 1. DR InterPro; IPR016191; Ribonuclease/ribotoxin. DR InterPro; IPR048269; RNase_U2. DR PANTHER; PTHR42104; EXTRACELLULAR GUANYL-SPECIFIC RIBONUCLEASE RNTA (AFU_ORTHOLOGUE AFUA_4G03230); 1. DR PANTHER; PTHR42104:SF1; EXTRACELLULAR GUANYL-SPECIFIC RIBONUCLEASE RNTA (AFU_ORTHOLOGUE AFUA_4G03230); 1. DR PIRSF; PIRSF037430; RNase_U2; 1. DR SUPFAM; SSF53933; Microbial ribonucleases; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease; KW Hydrolase; Lyase; Nuclease; Pyrrolidone carboxylic acid; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000269|PubMed:3103481, FT ECO:0000269|PubMed:6433932" FT CHAIN 26..131 FT /note="Guanyl-specific ribonuclease F1" FT /id="PRO_0000030834" FT ACT_SITE 65 FT ACT_SITE 83 FT /note="Proton acceptor" FT ACT_SITE 116 FT /note="Proton donor" FT MOD_RES 26 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:6433932" FT DISULFID 31..127 FT /evidence="ECO:0000269|PubMed:3103481" FT DISULFID 49..108 FT /evidence="ECO:0000269|PubMed:3103481" FT CONFLICT 57 FT /note="T -> S (in Ref. 2; AA sequence and 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 61 FT /note="S -> T (in Ref. 2; AA sequence and 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 129..131 FT /note="GTN -> NTG (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:1FUS" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:1FUS" FT HELIX 38..53 FT /evidence="ECO:0007829|PDB:1FUS" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:1FUS" FT STRAND 81..85 FT /evidence="ECO:0007829|PDB:1FUS" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:1RCL" FT STRAND 99..105 FT /evidence="ECO:0007829|PDB:1FUS" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:1RCL" FT STRAND 110..116 FT /evidence="ECO:0007829|PDB:1FUS" FT TURN 120..122 FT /evidence="ECO:0007829|PDB:1RCK" SQ SEQUENCE 131 AA; 13606 MW; 4AD743FA7E042284 CRC64; MLFFKSIASL AALVSLAVAS PIESRQSATT CGSTNYSASQ VRAAANAACQ YYQNDDTAGS STYPHTYNNY EGFDFPVDGP YQEFPIKSGG VYTGGSPGAD RVVINTNCEY AGAITHTGAS GNNFVGCSGT N //