P00653 (RNMS_ASPSA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Guanyl-specific ribonuclease Ms Short name=RNase Ms EC=3.1.27.3
Organism	Aspergillus saitoi (Aspergillus phoenicis)
Taxonomic identifier	5063 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	105 AA.
Sequence status	Complete.
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
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond
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

Chain

1 – 105

105

Guanyl-specific ribonuclease Ms

PRO_0000137370

Sites

Active site

39

1

Active site

57

1

Proton acceptor

Active site

91

1

Proton donor

Amino acid modifications

Disulfide bond

3 ↔ 11

Disulfide bond

7 ↔ 102

Secondary structure

1

.

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.

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105

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Beta strand

10 – 12

3

Helix

14 – 30

17

Beta strand

37 – 41

5

Beta strand

55 – 60

6

Beta strand

74 – 80

7

Beta strand

85 – 91

7

Beta strand

94 – 97

4

Sequences

	Sequence		Length	Mass (Da)
	P00653 [UniParc]. Last modified August 1, 1991. Version 2. Checksum: 94CF56D109242EFD	FASTA	105	11,332
	10 20 30 40 50 60 ESCEYTCGST CYWSSDVSAA KAKGYSLYES GDTIDDYPHG YHDYEGFDFP VSGTYYEYPI 70 80 90 100 MSDYDVYTGG SPGADRVIFN GDDELAGVIT HTGASGDDFV ACSSS

References

[1]	"Primary structure of a minor ribonuclease from Aspergillus saitoi." Watanabe H., Ohgi K., Irie M. J. Biochem. 91:1495-1509(1982) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Three-dimensional structure of ribonuclease Ms*3'-guanylic acid complex at 2.5-A resolution." Nonaka T., Mitsui Y., Irie M., Nakamura K.T. FEBS Lett. 283:207-209(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SEQUENCE REVISION TO 52-54; 80 AND 95.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

NRASTP. A00800.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RDS	X-ray	1.80	A	1-105	[»]
1RMS	X-ray	1.90	A	1-105	[»]

ProteinModelPortal

P00653.

SMR

P00653. Positions 1-105.

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

P00653.

Entry information

Entry name

RNMS_ASPSA

Accession

Primary (citable) accession number: P00653

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 1, 1991
Last modified:	April 3, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program