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Protein

Extracellular guanyl-specific ribonuclease Fl2

Gene
N/A
Organism
Gibberella baccata (Fusarium lateritium)
Status
Reviewed-Annotation score: Annotation score: 2 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 sitei40 – 401By similarity
Active sitei58 – 581Proton acceptorBy similarity
Active sitei91 – 911Proton donorBy similarity

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:
Extracellular guanyl-specific ribonuclease Fl2 (EC:3.1.27.3)
Short name:
RNase Fl2
OrganismiGibberella baccata (Fusarium lateritium)
Taxonomic identifieri5523 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium lateritium species complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 105105Extracellular guanyl-specific ribonuclease Fl2PRO_0000137378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid
Disulfide bondi6 ↔ 102By similarity
Disulfide bondi24 ↔ 83By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Structurei

3D structure databases

ProteinModelPortaliP16412.
SMRiP16412. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribonuclease N1/T1 family.Curated

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.

P16412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QSATTCSSKP YSAQQVRAAA NAACQYYQSN DTAGSTTYPH TYHNYEGFDF
60 70 80 90 100
AVNGPYQEYP IRTSGVYSGG SPGADRVIIN TQCQFAGAIT HTGASGNQFV

GCSNT
Length:105
Mass (Da):11,107
Last modified:January 31, 1994 - v2
Checksum:iC467E556628076C4
GO

Cross-referencesi

3D structure databases

ProteinModelPortaliP16412.
SMRiP16412. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. "A new isoform of intracellular RNAase of Fl2 Fusarium lateritium. Characteristics and determining the primary structure."
    Shlyapnikov S.V., Bezborodova S.I., Chepurnova N.K., Dementiev A.A.
    Dokl. Akad. Nauk SSSR 306:1496-1499(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: 54228.

Entry informationi

Entry nameiRNF2_GIBBA
AccessioniPrimary (citable) accession number: P16412
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1990
Last sequence update: January 31, 1994
Last modified: September 30, 2014
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. 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.