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P00651

- RNT1_ASPOR

UniProt

P00651 - RNT1_ASPOR

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Protein
Guanyl-specific ribonuclease T1
Gene
rntA, AO090011000118
Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 4 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 sitei66 – 6613 Publications
Active sitei84 – 841Proton acceptor3 Publications
Active sitei118 – 1181Proton donor2 Publications

GO - Molecular functioni

  1. RNA binding Source: InterPro
  2. endoribonuclease activity Source: InterPro
  3. ribonuclease T1 activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

SABIO-RKP00651.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanyl-specific ribonuclease T1 (EC:3.1.27.3)
Short name:
RNase T1
Gene namesi
Name:rntA
ORF Names:AO090011000118
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 7

Subcellular locationi

GO - Cellular componenti

  1. cell septum Source: ASPGD
  2. hyphal tip Source: ASPGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 Publication
Add
BLAST
Chaini27 – 130104Guanyl-specific ribonuclease T1
PRO_0000030833Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 361 Publication
Disulfide bondi32 ↔ 1291 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi5062.CADAORAP00004829.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 324
Beta strandi35 – 373
Helixi39 – 5517
Turni60 – 634
Beta strandi64 – 685
Beta strandi82 – 865
Beta strandi91 – 933
Beta strandi101 – 1077
Beta strandi108 – 1103
Beta strandi112 – 1187
Beta strandi121 – 1244
Beta strandi126 – 1283

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP00651.
SMRiP00651. Positions 27-130.

Miscellaneous databases

EvolutionaryTraceiP00651.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000217295.
OMAiYQEFPIR.
OrthoDBiEOG7XSTSF.

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.

P00651-1 [UniParc]FASTAAdd to Basket

« Hide

MMYSKLLTLT TLLLPTALAL PSLVERACDY TCGSNCYSSS DVSTAQAAGY    50
QLHEDGETVG SNSYPHKYNN YEGFDFSVSS PYYEWPILSS GDVYSGGSPG 100
ADRVVFNENN QLAGVITHTG ASGNNFVECT 130
Length:130
Mass (Da):13,960
Last modified:November 1, 1995 - v2
Checksum:i3F49EF41E85E230A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D28341 Genomic DNA. Translation: BAA05707.1.
D49428 mRNA. Translation: BAA08407.1.
AP007171 Genomic DNA. Translation: BAE64671.1.
PIRiJC4325. NRAST1.
RefSeqiXP_001825804.1. XM_001825752.2.

Genome annotation databases

EnsemblFungiiCADAORAT00004916; CADAORAP00004829; CADAORAG00004916.
GeneIDi5997907.
KEGGiaor:AOR_1_212054.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D28341 Genomic DNA. Translation: BAA05707.1 .
D49428 mRNA. Translation: BAA08407.1 .
AP007171 Genomic DNA. Translation: BAE64671.1 .
PIRi JC4325. NRAST1.
RefSeqi XP_001825804.1. XM_001825752.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B2M X-ray 2.00 A/B 27-130 [» ]
1BIR X-ray 1.80 A/B 27-130 [» ]
1BU4 X-ray 1.90 A 27-130 [» ]
1BVI X-ray 1.90 A/B/C/D 27-130 [» ]
1CH0 X-ray 2.30 A/B/C 27-130 [» ]
1DET X-ray 1.80 A 27-130 [» ]
1FYS X-ray 2.00 A 27-130 [» ]
1FZU X-ray 1.80 A 27-130 [» ]
1G02 X-ray 1.86 A 27-130 [» ]
1GSP X-ray 2.20 A 27-130 [» ]
1HYF X-ray 1.70 A 27-130 [» ]
1HZ1 X-ray 1.80 A 27-130 [» ]
1I0V X-ray 1.23 A 27-130 [» ]
1I0X X-ray 1.65 A/B/C/D 27-130 [» ]
1I2E X-ray 1.80 A 27-130 [» ]
1I2F X-ray 1.95 A 27-130 [» ]
1I2G X-ray 1.85 A 27-130 [» ]
1I3F X-ray 2.35 A 27-130 [» ]
1I3I X-ray 1.76 A 27-130 [» ]
1IYY NMR - A 27-130 [» ]
1LOV X-ray 1.55 A 27-130 [» ]
1LOW X-ray 1.90 A 27-130 [» ]
1LOY X-ray 1.55 A 27-130 [» ]
1LRA X-ray 1.90 A 27-130 [» ]
1Q9E X-ray 1.70 A/B/C 27-130 [» ]
1RGA X-ray 1.70 A 27-130 [» ]
1RGC X-ray 2.00 A/B 27-130 [» ]
1RGK X-ray 1.87 A 27-130 [» ]
1RGL X-ray 2.00 A 27-130 [» ]
1RHL X-ray 1.95 A 27-130 [» ]
1RLS X-ray 1.90 A 27-130 [» ]
1RN1 X-ray 1.84 A/B/C 27-130 [» ]
1RN4 X-ray 1.80 A 27-130 [» ]
1RNT X-ray 1.90 A 27-130 [» ]
1TRP X-ray 2.40 A/B 27-130 [» ]
1TRQ X-ray 2.30 A/B 27-130 [» ]
1TTO X-ray 2.10 A/B/C 27-130 [» ]
1YGW NMR - A 27-130 [» ]
2AAD X-ray 2.00 A/B 27-130 [» ]
2AAE X-ray 1.80 A 27-130 [» ]
2BIR X-ray 2.30 A 27-130 [» ]
2BU4 X-ray 1.95 A 27-130 [» ]
2GSP X-ray 1.80 A 27-130 [» ]
2HOH X-ray 1.90 A/B/C/D 27-130 [» ]
2RNT X-ray 1.80 A 27-130 [» ]
3BIR X-ray 1.80 A 27-130 [» ]
3BU4 X-ray 1.77 A 27-130 [» ]
3GSP X-ray 1.90 A 27-130 [» ]
3HOH X-ray 1.95 A/B/C/D 27-130 [» ]
3RNT X-ray 1.80 A 27-130 [» ]
3SYU X-ray 1.95 A 27-130 [» ]
3URP X-ray 3.19 A 27-130 [» ]
4BIR X-ray 1.70 A 27-130 [» ]
4BU4 X-ray 1.80 A 27-130 [» ]
4GSP X-ray 1.65 A 27-130 [» ]
4HOH X-ray 2.05 A/B/C/D 27-130 [» ]
4RNT X-ray 2.20 A 27-130 [» ]
5BIR X-ray 2.00 A/B 27-130 [» ]
5BU4 X-ray 1.77 A 27-130 [» ]
5GSP X-ray 1.80 A 27-130 [» ]
5HOH X-ray 2.00 A/B/C/D 27-130 [» ]
5RNT X-ray 3.20 A 27-130 [» ]
6GSP X-ray 2.20 A 27-130 [» ]
6RNT X-ray 1.80 A 27-130 [» ]
7GSP X-ray 2.00 A/B 27-130 [» ]
7RNT X-ray 1.90 A 27-130 [» ]
8RNT X-ray 1.80 A 27-130 [» ]
9RNT X-ray 1.50 A 27-130 [» ]
ProteinModelPortali P00651.
SMRi P00651. Positions 27-130.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5062.CADAORAP00004829.

Chemistry

BindingDBi P00651.
ChEMBLi CHEMBL1075043.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAORAT00004916 ; CADAORAP00004829 ; CADAORAG00004916 .
GeneIDi 5997907.
KEGGi aor:AOR_1_212054.

Phylogenomic databases

HOGENOMi HOG000217295.
OMAi YQEFPIR.
OrthoDBi EOG7XSTSF.

Enzyme and pathway databases

SABIO-RK P00651.

Miscellaneous databases

EvolutionaryTracei P00651.
PROi P00651.

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

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiRNT1_ASPOR
AccessioniPrimary (citable) accession number: P00651
Secondary accession number(s): Q2U194
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 118 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

3D-structure, Complete proteome, 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

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