Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00651 (RNT1_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanyl-specific ribonuclease T1

Short name=RNase T1
EC=3.1.27.3
Gene names
Name:rntA
ORF Names:AO090011000118
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length130 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Subunit structure

Monomer.

Sequence similarities

Belongs to the ribonuclease N1/T1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.3
Chain27 – 130104Guanyl-specific ribonuclease T1
PRO_0000030833

Sites

Active site661 Ref.5 Ref.6 Ref.7
Active site841Proton acceptor Ref.5 Ref.6 Ref.7
Active site1181Proton donor Ref.5 Ref.6

Amino acid modifications

Disulfide bond28 ↔ 36 Ref.3
Disulfide bond32 ↔ 129 Ref.3

Secondary structure

....................... 130
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00651 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 3F49EF41E85E230A

FASTA13013,960
        10         20         30         40         50         60 
MMYSKLLTLT TLLLPTALAL PSLVERACDY TCGSNCYSSS DVSTAQAAGY QLHEDGETVG 

        70         80         90        100        110        120 
SNSYPHKYNN YEGFDFSVSS PYYEWPILSS GDVYSGGSPG ADRVVFNENN QLAGVITHTG 

       130 
ASGNNFVECT 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of the ribonuclease T1 gene (rntA) from Aspergillus oryzae and its expression in Saccharomyces cerevisiae and Aspergillus oryzae."
Fujii T., Yamaoka H., Gomi K., Kitamoto K., Kumagai C.
Biosci. Biotechnol. Biochem. 59:1869-1874(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: ATCC 42149 / RIB 40.
[2]"Genome sequencing and analysis of Aspergillus oryzae."
Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. expand/collapse author list , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 42149 / RIB 40.
[3]"The structure and function of ribonuclease T1. XVII. Isolation and amino acid sequences of papain and subtilisin peptides from ribonuclease T1 -- the complete covalent structure of ribonuclease T1."
Takahashi K.
J. Biochem. 70:945-960(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-130.
[4]"A revision and confirmation of the amino acid sequence of ribonuclease T1."
Takahashi K.
J. Biochem. 98:815-817(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 97-99.
[5]"The identification of a glutamic acid residue as part of the active site of ribonuclease T-1."
Takahashi K., Stein W.H., Moore S.
J. Biol. Chem. 242:4682-4690(1967) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[6]"The structure and function of ribonuclease T1. XII. Further studies on rose bengal-catalyzed photooxidation of ribonuclease T1 --identification of a critical histidine residue."
Takahashi K.
J. Biochem. 69:331-338(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[7]"Three-dimensional structure of the ribonuclease T1 2'-GMP complex at 1.9-A resolution."
Arni R., Heinemann U., Tokuoka R., Saenger W.
J. Biol. Chem. 263:15358-15368(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[8]"Three-dimensional structure of ribonuclease T1 complexed with guanylyl-2',5'-guanosine at 1.8-A resolution."
Koepke J., Maslowska M., Heinemann U., Saenger W.
J. Mol. Biol. 206:475-488(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[9]"Three-dimensional structure of a mutant ribonuclease T1 (Y45W) complexed with non-cognizable ribonucleotide, 2'AMP, and its comparison with a specific complex with 2'GMP."
Hakoshima T., Itoh T., Tomita K., Goda K., Nishikawa S., Morioka H., Uesugi S., Ohtsuka E., Ikehara M.
J. Mol. Biol. 223:1013-1028(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT TRP-71.
[10]"Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography."
Zegers I., Loris R., Dehollander G., Fattah Haikal A., Poortmans F., Steyaert J., Wyns L.
Nat. Struct. Biol. 5:280-283(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[11]"Three-dimensional structure of ribonuclease T1 complexed with an isosteric phosphonate substrate analogue of GpU: alternate substrate binding modes and catalysis."
Arni R.K., Watanabe L., Ward R.J., Kreitman R.J., Kumar K., Walz F.G. Jr.
Biochemistry 38:2452-2461(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[12]"Dissection of the structural and functional role of a conserved hydration site in RNase T1."
Langhorst U., Loris R., Denisov V.P., Doumen J., Roose P., Maes D., Halle B., Steyaert J.
Protein Sci. 8:722-730(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[13]"A nucleophile activation dyad in ribonucleases. A combined X-ray crystallographic/ab initio quantum chemical study."
Mignon P., Steyaert J., Loris R., Geerlings P., Loverix S.
J. Biol. Chem. 277:36770-36774(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
[14]"Two-dimensional 1H-NMR investigation of ribonuclease T1. Resonance assignments, secondary and low-resolution tertiary structures of ribonuclease T1."
Hoffmann E., Rueterjans H.
Eur. J. Biochem. 177:539-560(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D28341 Genomic DNA. Translation: BAA05707.1.
D49428 mRNA. Translation: BAA08407.1.
AP007171 Genomic DNA. Translation: BAE64671.1.
PIRNRAST1. JC4325.
RefSeqXP_001825804.1. XM_001825752.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B2MX-ray2.00A/B27-130[»]
1BIRX-ray1.80A/B27-130[»]
1BU4X-ray1.90A27-130[»]
1BVIX-ray1.90A/B/C/D27-130[»]
1CH0X-ray2.30A/B/C27-130[»]
1DETX-ray1.80A27-130[»]
1FYSX-ray2.00A27-130[»]
1FZUX-ray1.80A27-130[»]
1G02X-ray1.86A27-130[»]
1GSPX-ray2.20A27-130[»]
1HYFX-ray1.70A27-130[»]
1HZ1X-ray1.80A27-130[»]
1I0VX-ray1.23A27-130[»]
1I0XX-ray1.65A/B/C/D27-130[»]
1I2EX-ray1.80A27-130[»]
1I2FX-ray1.95A27-130[»]
1I2GX-ray1.85A27-130[»]
1I3FX-ray2.35A27-130[»]
1I3IX-ray1.76A27-130[»]
1IYYNMR-A27-130[»]
1LOVX-ray1.55A27-130[»]
1LOWX-ray1.90A27-130[»]
1LOYX-ray1.55A27-130[»]
1LRAX-ray1.90A27-130[»]
1Q9EX-ray1.70A/B/C27-130[»]
1RGAX-ray1.70A27-130[»]
1RGCX-ray2.00A/B27-130[»]
1RGKX-ray1.87A27-130[»]
1RGLX-ray2.00A27-130[»]
1RHLX-ray1.95A27-130[»]
1RLSX-ray1.90A27-130[»]
1RN1X-ray1.84A/B/C27-130[»]
1RN4X-ray1.80A27-130[»]
1RNTX-ray1.90A27-130[»]
1TRPX-ray2.40A/B27-130[»]
1TRQX-ray2.30A/B27-130[»]
1TTOX-ray2.10A/B/C27-130[»]
1YGWNMR-A27-130[»]
2AADX-ray2.00A/B27-130[»]
2AAEX-ray1.80A27-130[»]
2BIRX-ray2.30A27-130[»]
2BU4X-ray1.95A27-130[»]
2GSPX-ray1.80A27-130[»]
2HOHX-ray1.90A/B/C/D27-130[»]
2RNTX-ray1.80A27-130[»]
3BIRX-ray1.80A27-130[»]
3BU4X-ray1.77A27-130[»]
3GSPX-ray1.90A27-130[»]
3HOHX-ray1.95A/B/C/D27-130[»]
3RNTX-ray1.80A27-130[»]
3SYUX-ray1.95A27-130[»]
3URPX-ray3.19A27-130[»]
4BIRX-ray1.70A27-130[»]
4BU4X-ray1.80A27-130[»]
4GSPX-ray1.65A27-130[»]
4HOHX-ray2.05A/B/C/D27-130[»]
4RNTX-ray2.20A27-130[»]
5BIRX-ray2.00A/B27-130[»]
5BU4X-ray1.77A27-130[»]
5GSPX-ray1.80A27-130[»]
5HOHX-ray2.00A/B/C/D27-130[»]
5RNTX-ray3.20A27-130[»]
6GSPX-ray2.20A27-130[»]
6RNTX-ray1.80A27-130[»]
7GSPX-ray2.00A/B27-130[»]
7RNTX-ray1.90A27-130[»]
8RNTX-ray1.80A27-130[»]
9RNTX-ray1.50A27-130[»]
ProteinModelPortalP00651.
SMRP00651. Positions 27-130.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00004829.

Chemistry

BindingDBP00651.
ChEMBLCHEMBL1075043.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00004916; CADAORAP00004829; CADAORAG00004916.
GeneID5997907.
KEGGaor:AOR_1_212054.

Phylogenomic databases

HOGENOMHOG000217295.
OMAYQEFPIR.
OrthoDBEOG7XSTSF.

Enzyme and pathway databases

SABIO-RKP00651.

Family and domain databases

Gene3D3.10.450.30. 1 hit.
InterProIPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamPF00545. Ribonuclease. 1 hit.
[Graphical view]
SUPFAMSSF53933. SSF53933. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00651.
PROP00651.

Entry information

Entry nameRNT1_ASPOR
AccessionPrimary (citable) accession number: P00651
Secondary accession number(s): Q2U194
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references