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Protein

Guanyl-specific ribonuclease F1

Gene
N/A
Organism
Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium fujikuroi)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in G-P with 2',3'-cyclic phosphate intermediates.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651
Active sitei83 – 831Proton acceptor
Active sitei116 – 1161Proton donor

GO - Molecular functioni

  1. endoribonuclease activity Source: InterPro
  2. ribonuclease T1 activity Source: UniProtKB-EC
  3. RNA binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Names & Taxonomyi

Protein namesi
Recommended name:
Guanyl-specific ribonuclease F1 (EC:3.1.27.3)
Short name:
RNase F1
OrganismiGibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium fujikuroi)
Taxonomic identifieri5127 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium fujikuroi species complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25252 PublicationsAdd
BLAST
Chaini26 – 131106Guanyl-specific ribonuclease F1PRO_0000030834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Pyrrolidone carboxylic acid
Disulfide bondi31 ↔ 1271 Publication
Disulfide bondi49 ↔ 1081 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1
131
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 313Combined sources
Beta strandi34 – 363Combined sources
Helixi38 – 5316Combined sources
Beta strandi64 – 674Combined sources
Beta strandi81 – 855Combined sources
Beta strandi88 – 914Combined sources
Beta strandi99 – 1057Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi110 – 1167Combined sources
Turni120 – 1223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FUSX-ray1.30A27-131[»]
1FUTX-ray2.00A27-131[»]
1RCKNMR-A27-131[»]
1RCLNMR-A27-131[»]
ProteinModelPortaliP10282.
SMRiP10282. Positions 26-131.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10282.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribonuclease N1/T1 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
SUPFAMiSSF53933. SSF53933. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10282-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLFFKSIASL AALVSLAVAS PIESRQSATT CGSTNYSASQ VRAAANAACQ
60 70 80 90 100
YYQNDDTAGS STYPHTYNNY EGFDFPVDGP YQEFPIKSGG VYTGGSPGAD
110 120 130
RVVINTNCEY AGAITHTGAS GNNFVGCSGT N
Length:131
Mass (Da):13,606
Last modified:August 31, 2004 - v4
Checksum:i4AD743FA7E042284
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571T → S AA sequence (PubMed:6433932)Curated
Sequence conflicti57 – 571T → S AA sequence (PubMed:3103481)Curated
Sequence conflicti61 – 611S → T AA sequence (PubMed:6433932)Curated
Sequence conflicti61 – 611S → T AA sequence (PubMed:3103481)Curated
Sequence conflicti129 – 1313GTN → NTG AA sequence (PubMed:6433932)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006460 mRNA. Translation: BAA31984.1.
PIRiJS0484.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006460 mRNA. Translation: BAA31984.1.
PIRiJS0484.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FUSX-ray1.30A27-131[»]
1FUTX-ray2.00A27-131[»]
1RCKNMR-A27-131[»]
1RCLNMR-A27-131[»]
ProteinModelPortaliP10282.
SMRiP10282. Positions 26-131.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP10282.

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
SUPFAMiSSF53933. SSF53933. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of cDNA encoding ribonuclease F1 from Fusarium moniliforme."
    Yoshida H., Iizuka M., Norioka N., Norioka S., Sakiyama F.
    Biochem. Mol. Biol. Int. 45:555-560(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The primary structure of ribonuclease F1 from Fusarium moniliforme."
    Hirabayashi J., Yoshida H.
    Biochem. Int. 7:255-262(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-131.
  3. "Peptide fractionation by high-performance liquid chromatography on an Asahipak GS-320 column: application to determination of the disulfide pairings in ribonuclease F1."
    Yoshida H., Naijo S.
    Anal. Biochem. 159:273-279(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-131, DISULFIDE BONDS.
  4. "Crystal structures of ribonuclease F1 of Fusarium moniliforme in its free form and in complex with 2'GMP."
    Vassylyev D.G., Katayanagi K., Ishikawa K., Tsujimoto-Hirano M., Danno M., Paehler A., Matsumoto O., Matsushima M., Yoshida H., Morikawa K.
    J. Mol. Biol. 230:979-996(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 26-131.
  5. "The three-dimensional structure of guanine-specific ribonuclease F1 in solution determined by NMR spectroscopy and distance geometry."
    Nakai T., Yoshikawa W., Nakamura H., Yoshida H.
    Eur. J. Biochem. 208:41-51(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 26-131.

Entry informationi

Entry nameiRNF1_GIBFU
AccessioniPrimary (citable) accession number: P10282
Secondary accession number(s): O74124
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: August 31, 2004
Last modified: November 26, 2014
This is version 98 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.