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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

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/U2.
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/U2.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
SUPFAMiSSF53933. SSF53933. 1 hit.
ProtoNetiSearch...

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: December 9, 2015
This is version 101 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

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 one 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.