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Protein

Guanyl-specific ribonuclease T1

Gene

rntA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei661 Publication1
Active sitei84Proton acceptor1 Publication1
Active sitei118Proton donor1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

BRENDAi3.1.27.3. 522.
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
Proteomesi
  • UP000006564 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

  • cell septum Source: ASPGD
  • hyphal tip Source: ASPGD
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075043.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000003083327 – 130Guanyl-specific ribonuclease T1Add BLAST104

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 361 Publication
Disulfide bondi32 ↔ 1291 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Chemistry databases

BindingDBiP00651.

Structurei

Secondary structure

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 32Combined sources4
Beta strandi35 – 37Combined sources3
Helixi39 – 55Combined sources17
Turni60 – 63Combined sources4
Beta strandi64 – 68Combined sources5
Beta strandi82 – 86Combined sources5
Beta strandi91 – 93Combined sources3
Beta strandi101 – 107Combined sources7
Beta strandi108 – 110Combined sources3
Beta strandi112 – 118Combined sources7
Beta strandi121 – 124Combined sources4
Beta strandi126 – 128Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4ODKX-ray1.40B/C59-73[»]
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00651.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribonuclease N1/T1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000217295.
OMAiYQEFPIR.
OrthoDBiEOG092C58FH.

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR000026. Gua-sp_ribonuclease_N1/T1/U2.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFiPIRSF037430. RNase_U2. 1 hit.
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

        10         20         30         40         50
MMYSKLLTLT TLLLPTALAL PSLVERACDY TCGSNCYSSS DVSTAQAAGY
60 70 80 90 100
QLHEDGETVG SNSYPHKYNN YEGFDFSVSS PYYEWPILSS GDVYSGGSPG
110 120 130
ADRVVFNENN QLAGVITHTG ASGNNFVECT
Length:130
Mass (Da):13,960
Last modified:November 1, 1995 - v2
Checksum:i3F49EF41E85E230A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsemblFungiiBAE64671; BAE64671; AO090011000118.
GeneIDi5997907.
KEGGiaor:AOR_1_212054.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4ODKX-ray1.40B/C59-73[»]
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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP00651.
ChEMBLiCHEMBL1075043.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAE64671; BAE64671; AO090011000118.
GeneIDi5997907.
KEGGiaor:AOR_1_212054.

Phylogenomic databases

HOGENOMiHOG000217295.
OMAiYQEFPIR.
OrthoDBiEOG092C58FH.

Enzyme and pathway databases

BRENDAi3.1.27.3. 522.
SABIO-RKP00651.

Miscellaneous databases

EvolutionaryTraceiP00651.
PROiP00651.

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR000026. Gua-sp_ribonuclease_N1/T1/U2.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFiPIRSF037430. RNase_U2. 1 hit.
SUPFAMiSSF53933. SSF53933. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 132 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.