P00649 (RN_BACIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Ribonuclease EC=3.1.27.- Alternative name(s): Binase RNase Bi
Organism	Bacillus intermedius
Taxonomic identifier	1400 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	162 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)

Function	This is a purine-specific ribonuclease.
Subcellular location	Secreted.
Sequence similarities	Belongs to the ribonuclease N1/T1 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro endoribonuclease activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Propeptide

30 – 53

24

PRO_0000030824

Chain

54 – 162

109

Ribonuclease

PRO_0000030825

Sites

Active site

125

1

Proton acceptor

Active site

154

1

Proton donor

Experimental info

Sequence conflict

74 – 75

2

DN → ND AA sequence Ref.3

Sequence conflict

93

1

N → D AA sequence Ref.3

Sequence conflict

119 – 120

2

SG → GS AA sequence Ref.3

Secondary structure

1

.

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162

Helix Strand Turn

Details...

Helix

59 – 69

11

Helix

79 – 84

6

Helix

89 – 91

3

Helix

94 – 97

4

Beta strand

102 – 108

7

Beta strand

112 – 115

4

Beta strand

118 – 120

3

Beta strand

123 – 127

5

Beta strand

132 – 134

3

Beta strand

139 – 143

5

Beta strand

148 – 153

6

Beta strand

159 – 162

4

Sequences

	Sequence		Length	Mass (Da)
	P00649 [UniParc]. Last modified May 1, 1992. Version 3. Checksum: CD6740EDFBCF5295	FASTA	162	17,956
	10 20 30 40 50 60 MKKISSVFTM FALIAAILFS GFIPQQAYAE TPLTQTATNE TATIQLTSDV HTLAVINTFD 70 80 90 100 110 120 GVADYLIRYK RLPDNYITKS QASALGWVAS KGNLAEVAPG KSIGGDVFSN REGRLPSASG 130 140 150 160 RTWREADINY VSGFRNADRL VYSSDWLIYK TTDHYATFTR IR

References

[1]	"Cloning of the gene encoding RNase binase from Bacillus intermedius 7P." Schulga A.A., Nurkiyanova K.M., Zakharyev V.M., Kirpichnikov M.P., Skryabin K.G. Nucleic Acids Res. 20:2375-2375(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 7P.
[2]	"The cloning and determination of the nucleotide sequence of the RNase gene in Bacillus intermedius." Nurkiyanova K.M., Shulga A.A., Zakharyev V.M., Kirpichnikov M.P., Skryabin K.G., Baev A.A. Dokl. Akad. Nauk SSSR 309:1476-1479(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 7P.
[3]	"Primary structure of ribonuclease from Bacillus intermedius 7P." Aphanasenko G.A., Dudkin S.M., Kaminir L.B., Leshchinskaya I.B., Severin E.S. FEBS Lett. 97:77-80(1979) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 54-162. Strain: 7P.
[4]	"RNA cleavage without hydrolysis. Splitting the catalytic activities of binase with Asn101 and Thr101 mutations." Okorokov A.L., Panov K.I., Offen W.A., Mukhortov V.G., Antson A.A., Karpeisky M.Y., Wilkinson A.J., Dodson G.G. Protein Eng. 10:273-278(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) AND MUTAGENESIS OF HIS-154.
[5]	"Three-dimensional structure of binase in solution." Reibarkh M.Y.A., Nolde D.E., Vasilieva L.I., Bocharov E.V., Shulga A.A., Kirpichnikov M.P., Arseniev A.S. FEBS Lett. 431:250-254(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[6]	"The structure of substrate-free microbial ribonuclease binase and of its complexes with 3'GMP and sulfate ions." Polyakov K.M., Lebedev A.A., Okorokov A.L., Panov K.I., Schulga A.A., Pavlovsky A.G., Karpeisky M.Y., Dodson G.G. Acta Crystallogr. D 58:744-750(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 54-162.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53697 Genomic DNA. Translation: CAA37735.1.

PIR

NRBSI. A00796.
S22653.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BUJ	NMR	-	A	54-162	[»]
1GOU	X-ray	1.65	A/B	54-162	[»]
1GOV	X-ray	2.00	A/B	54-162	[»]
1GOY	X-ray	2.00	A/B	54-162	[»]
2RBI	X-ray	2.20	A/B	54-162	[»]
4HAA	X-ray	1.90	A/B/C/D	54-162	[»]

ProteinModelPortal

P00649.

SMR

P00649. Positions 54-162.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.10.450.30. 1 hit.

InterPro

IPR001887. Barnase.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]

Pfam

PF00545. Ribonuclease. 1 hit.
[Graphical view]

PIRSF

PIRSF001013. Barnase. 1 hit.

PRINTS

PR00117. BARNASE.

SUPFAM

SSF53933. Ribonuclease/ribotoxin. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P00649.

Entry information

Entry name

RN_BACIN

Accession

Primary (citable) accession number: P00649

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	May 1, 1992
Last modified:	April 3, 2013
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program