Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P10282

- RNF1_GIBFU

UniProt

P10282 - RNF1_GIBFU

Protein

Guanyl-specific ribonuclease F1

Gene
N/A
Organism
Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium fujikuroi)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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

    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 – 313
    Beta strandi34 – 363
    Helixi38 – 5316
    Beta strandi64 – 674
    Beta strandi81 – 855
    Beta strandi88 – 914
    Beta strandi99 – 1057
    Beta strandi106 – 1083
    Beta strandi110 – 1167
    Turni120 – 1223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MLFFKSIASL AALVSLAVAS PIESRQSATT CGSTNYSASQ VRAAANAACQ    50
    YYQNDDTAGS STYPHTYNNY EGFDFPVDGP YQEFPIKSGG VYTGGSPGAD 100
    RVVINTNCEY AGAITHTGAS GNNFVGCSGT N 131
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006460 mRNA. Translation: BAA31984.1.
    PIRiJS0484.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006460 mRNA. Translation: BAA31984.1 .
    PIRi JS0484.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FUS X-ray 1.30 A 27-131 [» ]
    1FUT X-ray 2.00 A 27-131 [» ]
    1RCK NMR - A 27-131 [» ]
    1RCL NMR - A 27-131 [» ]
    ProteinModelPortali P10282.
    SMRi P10282. Positions 26-131.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P10282.

    Family and domain databases

    Gene3Di 3.10.450.30. 1 hit.
    InterProi IPR000026. Gua-sp_ribonuclease_N1/T1.
    IPR016191. Ribonuclease/ribotoxin.
    [Graphical view ]
    Pfami PF00545. Ribonuclease. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53933. SSF53933. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 97 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