RNF1_GIBFU
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 03-AUG-2022, entry version 120.
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}.
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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: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 PIRSF; PIRSF037430; RNase_U2; 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; 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
