P00651 (RNT1_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanyl-specific ribonuclease T1
Short name=RNase T1
EC=3.1.27.3

Gene names

Name:	rntA
ORF Names:	AO090011000118

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus oryzae

Protein attributes

Sequence length	130 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Subunit structure	Monomer.
Sequence similarities	Belongs to the ribonuclease N1/T1 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond
Technical term	3D-structure Complete proteome 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

Signal peptide

1 – 26

26

Ref.3

Chain

27 – 130

104

Guanyl-specific ribonuclease T1

PRO_0000030833

Sites

Active site

66

1

Ref.5 Ref.6 Ref.7

Active site

84

1

Proton acceptor Ref.5 Ref.6 Ref.7

Active site

118

1

Proton donor Ref.5 Ref.6

Amino acid modifications

Disulfide bond

28 ↔ 36

Ref.3

Disulfide bond

32 ↔ 129

Ref.3

Secondary structure

1

.

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130

Helix Strand Turn

Details...

Beta strand

29 – 32

4

Beta strand

35 – 37

3

Helix

39 – 55

17

Turn

60 – 63

4

Beta strand

64 – 68

5

Beta strand

82 – 86

5

Beta strand

91 – 93

3

Beta strand

101 – 107

7

Beta strand

108 – 110

3

Beta strand

112 – 118

7

Beta strand

121 – 124

4

Beta strand

126 – 128

3

Sequences

	Sequence		Length	Mass (Da)
	P00651 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 3F49EF41E85E230A	FASTA	130	13,960
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D28341 Genomic DNA. Translation: BAA05707.1.
D49428 mRNA. Translation: BAA08407.1.
AP007171 Genomic DNA. Translation: BAE64671.1.

PIR

NRAST1. JC4325.

RefSeq

XP_001825804.1. XM_001825752.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	27-125	[»]
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	27-125	[»]
1RGC	X-ray	2.00	A/B	27-125	[»]
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	27-125	[»]
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	27-125	[»]
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	27-125	[»]
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	27-125	[»]
6GSP	X-ray	2.20	A	27-130	[»]
6RNT	X-ray	1.80	A	27-125	[»]
7GSP	X-ray	2.00	A/B	27-130	[»]
7RNT	X-ray	1.90	A	27-130	[»]
8RNT	X-ray	1.80	A	27-125	[»]
9RNT	X-ray	1.50	A	27-125	[»]

ProteinModelPortal

P00651.

SMR

P00651. Positions 27-130.

ModBase

Search...

Protein-protein interaction databases

STRING

5062.CADAORAP00004829.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

CADAORAT00004916; CADAORAP00004829; CADAORAG00004916.

GeneID

5997907.

KEGG

aor:AOR_1_212054.

Phylogenomic databases

HOGENOM

HOG000217295.

OrthoDB

EOG4GBBGV.

Enzyme and pathway databases

SABIO-RK

P00651.

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

BindingDB

P00651.

ChEMBL

CHEMBL1075043.

EvolutionaryTrace

P00651.

Entry information

Entry name

RNT1_ASPOR

Accession

Primary (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:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program