NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1065209]
View 

Chain A, BARNASE

Protein Classification

ribonuclease( domain architecture ID 10097120)

ribonuclease hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates

CATH:  3.10.450.30
EC:  3.1.27.-
Gene Ontology:  GO:0004521|GO:0003723

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
barnase cd00933
Barnase, a member of the family of homologous microbial ribonucleases, catalyses the cleavage ...
 4-110 1.27e-70

Barnase, a member of the family of homologous microbial ribonucleases, catalyses the cleavage of single-stranded RNA via a two-step mechanism thought to be similar to that of pancreatic ribonuclease. The mechanism involves a transesterification to give a 2', 3'-cyclic phosphate intermediate, followed by hydrolysis to yield a 3' nucleotide. The active site residues His and Glu act as general acid-base groups during catalysis, while the Arg and Lys residues are important in binding the reactive phosphate, the latter probably binding the phosphate in the transition state. Barstar, a small 89 residue intracellular protein is a natural inhibitor of Barnase.


:

Pssm-ID: 238471 [Multi-domain]  Cd Length: 107  Bit Score: 205.82  E-value: 1.27e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065209    4 INTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNREGKLPGKSGRTWREADANYTSGFR 83
Cdd:cd00933   1 INTFQGVADYLQTYHRLPDNYITKSQAKELGWVAPKGNLWDVAPGKSIGGDRFSNREGRLPAAGGRTWREADINYQGGHR 80

                        90       100
                ....*....|....*....|....*..
gi 1065209   84 NSDRILYSSDWLIYKTTDHYQTFTKIR 110
Cdd:cd00933  81 GADRLLYSNDGLIYKTTDHYRTFTRIR 107
 
Name Accession Description Interval E-value
barnase cd00933
Barnase, a member of the family of homologous microbial ribonucleases, catalyses the cleavage ...
 4-110 1.27e-70

Barnase, a member of the family of homologous microbial ribonucleases, catalyses the cleavage of single-stranded RNA via a two-step mechanism thought to be similar to that of pancreatic ribonuclease. The mechanism involves a transesterification to give a 2', 3'-cyclic phosphate intermediate, followed by hydrolysis to yield a 3' nucleotide. The active site residues His and Glu act as general acid-base groups during catalysis, while the Arg and Lys residues are important in binding the reactive phosphate, the latter probably binding the phosphate in the transition state. Barstar, a small 89 residue intracellular protein is a natural inhibitor of Barnase.


Pssm-ID: 238471 [Multi-domain]  Cd Length: 107  Bit Score: 205.82  E-value: 1.27e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065209    4 INTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNREGKLPGKSGRTWREADANYTSGFR 83
Cdd:cd00933   1 INTFQGVADYLQTYHRLPDNYITKSQAKELGWVAPKGNLWDVAPGKSIGGDRFSNREGRLPAAGGRTWREADINYQGGHR 80

                        90       100
                ....*....|....*....|....*..
gi 1065209   84 NSDRILYSSDWLIYKTTDHYQTFTKIR 110
Cdd:cd00933  81 GADRLLYSNDGLIYKTTDHYRTFTRIR 107
Ribonuclease pfam00545
ribonuclease; This enzyme hydrolyses RNA and oligoribonucleotides.
 26-108 1.46e-24

ribonuclease; This enzyme hydrolyses RNA and oligoribonucleotides.


Pssm-ID: 459849  Cd Length: 81  Bit Score: 88.46  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065209     26 TKSEAQALGWvasKGNLADVAPGksiGGDIFSNREGKLPGKSGRTWREADANYT-SGFRNSDRILYSSDWL---IYKTTD 101
Cdd:pfam00545   1 TTLEAIEAGW---WPGPFPYPPD---GGDVFGNREGRLPQAPGGYYREYDVNTPgGRYRGARRIVTGDGLDggeIYYTAD 74


                  ....*..
gi 1065209    102 HYQTFTK 108
Cdd:pfam00545  75 HYNSFVR 81
 
Name Accession Description Interval E-value
barnase cd00933
Barnase, a member of the family of homologous microbial ribonucleases, catalyses the cleavage ...
 4-110 1.27e-70

Barnase, a member of the family of homologous microbial ribonucleases, catalyses the cleavage of single-stranded RNA via a two-step mechanism thought to be similar to that of pancreatic ribonuclease. The mechanism involves a transesterification to give a 2', 3'-cyclic phosphate intermediate, followed by hydrolysis to yield a 3' nucleotide. The active site residues His and Glu act as general acid-base groups during catalysis, while the Arg and Lys residues are important in binding the reactive phosphate, the latter probably binding the phosphate in the transition state. Barstar, a small 89 residue intracellular protein is a natural inhibitor of Barnase.


Pssm-ID: 238471 [Multi-domain]  Cd Length: 107  Bit Score: 205.82  E-value: 1.27e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065209    4 INTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNREGKLPGKSGRTWREADANYTSGFR 83
Cdd:cd00933   1 INTFQGVADYLQTYHRLPDNYITKSQAKELGWVAPKGNLWDVAPGKSIGGDRFSNREGRLPAAGGRTWREADINYQGGHR 80

                        90       100
                ....*....|....*....|....*..
gi 1065209   84 NSDRILYSSDWLIYKTTDHYQTFTKIR 110
Cdd:cd00933  81 GADRLLYSNDGLIYKTTDHYRTFTRIR 107
Ribonuclease pfam00545
ribonuclease; This enzyme hydrolyses RNA and oligoribonucleotides.
 26-108 1.46e-24

ribonuclease; This enzyme hydrolyses RNA and oligoribonucleotides.


Pssm-ID: 459849  Cd Length: 81  Bit Score: 88.46  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1065209     26 TKSEAQALGWvasKGNLADVAPGksiGGDIFSNREGKLPGKSGRTWREADANYT-SGFRNSDRILYSSDWL---IYKTTD 101
Cdd:pfam00545   1 TTLEAIEAGW---WPGPFPYPPD---GGDVFGNREGRLPQAPGGYYREYDVNTPgGRYRGARRIVTGDGLDggeIYYTAD 74


                  ....*..
gi 1065209    102 HYQTFTK 108
Cdd:pfam00545  75 HYNSFVR 81
microbial_RNases cd00389
microbial_RNases. Ribonucleases (RNAses) cleave phosphodiester bonds in RNA and are essential ...
 37-103 4.62e-20

microbial_RNases. Ribonucleases (RNAses) cleave phosphodiester bonds in RNA and are essential for both non-specific RNA degradation and for numerous forms of RNA processing. The alignment contains fungal RNases (U2, T1, F1, Th, Pb, N1, and Ms) and bacterial RNases (barnase, binase, RNase Sa) , the majority of which are guanyl specific and fungal ribotoxins.


Pssm-ID: 238228  Cd Length: 71  Bit Score: 76.89  E-value: 4.62e-20
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1065209   37 ASKGNLADVAPGKSIGGDIFSNREGKLPGKSGRTWREADANYTS-GFRNSDRILYSSDWLIYKTTDHY 103
Cdd:cd00389   4 ALNLIASGGPFGYSIYGHVFNNREGFLPFKGSGYYHEYPVNTPGgGSRGADRVVYGGDGEFYGTIDHY 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH