P10282 (RNF1_GIBFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Guanyl-specific ribonuclease F1 Short name=RNase F1 EC=3.1.27.3
Organism	Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium moniliforme)
Taxonomic identifier	5127 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Gibberella › Fusarium fujikuroi complex

Protein attributes

Sequence length	131 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in G-P with 2',3'-cyclic phosphate intermediates.
Sequence similarities	Belongs to the ribonuclease N1/T1 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro endoribonuclease activity Inferred from electronic annotation. Source: InterPro ribonuclease T1 activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.2 Ref.3

Chain

26 – 131

106

Guanyl-specific ribonuclease F1

PRO_0000030834

Sites

Active site

65

1

Active site

83

1

Proton acceptor

Active site

116

1

Proton donor

Amino acid modifications

Modified residue

26

1

Pyrrolidone carboxylic acid

Disulfide bond

31 ↔ 127

Ref.3

Disulfide bond

49 ↔ 108

Ref.3

Experimental info

Sequence conflict

57

1

T → S AA sequence Ref.2

Sequence conflict

57

1

T → S AA sequence Ref.3

Sequence conflict

61

1

S → T AA sequence Ref.2

Sequence conflict

61

1

S → T AA sequence Ref.3

Sequence conflict

129 – 131

3

GTN → NTG AA sequence Ref.2

Secondary structure

1

.

.

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.

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.

.

131

Helix Strand Turn

Details...

Beta strand

29 – 31

3

Beta strand

34 – 36

3

Helix

38 – 53

16

Beta strand

64 – 67

4

Beta strand

81 – 85

5

Beta strand

88 – 91

4

Beta strand

99 – 105

7

Beta strand

106 – 108

3

Beta strand

110 – 116

7

Turn

120 – 122

3

Sequences

	Sequence		Length	Mass (Da)
	P10282 [UniParc]. Last modified August 31, 2004. Version 4. Checksum: 4AD743FA7E042284	FASTA	131	13,606
	10 20 30 40 50 60 MLFFKSIASL AALVSLAVAS PIESRQSATT CGSTNYSASQ VRAAANAACQ YYQNDDTAGS 70 80 90 100 110 120 STYPHTYNNY EGFDFPVDGP YQEFPIKSGG VYTGGSPGAD RVVINTNCEY AGAITHTGAS 130 GNNFVGCSGT N

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB006460 mRNA. Translation: BAA31984.1.

PIR

JS0484.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P10282.

SMR

P10282. Positions 26-131.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.10.450.30. 1 hit.

InterPro

IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]

Pfam

PF00545. Ribonuclease. 1 hit.
[Graphical view]

SUPFAM

SSF53933. Ribonuclease/ribotoxin. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P10282.

Entry information

Entry name

RNF1_GIBFU

Accession

Primary (citable) accession number: P10282
Secondary accession number(s): O74124

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	August 31, 2004
Last modified:	April 3, 2013
This is version 90 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program