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P00651

- RNT1_ASPOR

UniProt

P00651 - RNT1_ASPOR

Protein

Guanyl-specific ribonuclease T1

Gene

rntA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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 – 6611 Publication
    Active sitei84 – 841Proton acceptor1 Publication
    Active sitei118 – 1181Proton donor

    GO - Molecular functioni

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

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26261 PublicationAdd
    BLAST
    Chaini27 – 130104Guanyl-specific ribonuclease T1PRO_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

    1
    130
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00651.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribonuclease N1/T1 family.Curated

    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

    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: October 1, 2014
    This is version 119 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, Reference proteome

    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