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Conserved domains on  [gi|1366246874|gb|PSI02992|]
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ribonuclease [Bacillus subtilis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
microbial_RNases super family cl00212
microbial_RNases. Ribonucleases (RNAses) cleave phosphodiester bonds in RNA and are essential ...
 37-143 2.48e-53

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.


The actual alignment was detected with superfamily member cd00933:

Pssm-ID: 469661 [Multi-domain]  Cd Length: 107  Bit Score: 163.83  E-value: 2.48e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366246874  37 LNSFTEVSDFVAKNGRLPVNYITKGEARKLGWDSKKGNLSKVAPGKSIGGDIYKNREKLLPEAKNRVWREADINYTTGYR 116
Cdd:cd00933     1 INTFQGVADYLQTYHRLPDNYITKSQAKELGWVAPKGNLWDVAPGKSIGGDRFSNREGRLPAAGGRTWREADINYQGGHR 80

                          90       100
                  ....*....|....*....|....*..
gi 1366246874 117 GNDRLLYSNDGLIYKTTDHYKTFVKLK 143
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 ...
 37-143 2.48e-53

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: 163.83  E-value: 2.48e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366246874  37 LNSFTEVSDFVAKNGRLPVNYITKGEARKLGWDSKKGNLSKVAPGKSIGGDIYKNREKLLPEAKNRVWREADINYTTGYR 116
Cdd:cd00933     1 INTFQGVADYLQTYHRLPDNYITKSQAKELGWVAPKGNLWDVAPGKSIGGDRFSNREGRLPAAGGRTWREADINYQGGHR 80

                          90       100
                  ....*....|....*....|....*..
gi 1366246874 117 GNDRLLYSNDGLIYKTTDHYKTFVKLK 143
Cdd:cd00933    81 GADRLLYSNDGLIYKTTDHYRTFTRIR 107
Ribonuclease pfam00545
ribonuclease; This enzyme hydrolyses RNA and oligoribonucleotides.
 59-141 6.41e-24

ribonuclease; This enzyme hydrolyses RNA and oligoribonucleotides.


Pssm-ID: 459849  Cd Length: 81  Bit Score: 88.07  E-value: 6.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366246874  59 TKGEARKLGWdskKGNLSKVAPGksiGGDIYKNREKLLPEAKNRVWREADINYT-TGYRGNDRLLYSND---GLIYKTTD 134
Cdd:pfam00545   1 TTLEAIEAGW---WPGPFPYPPD---GGDVFGNREGRLPQAPGGYYREYDVNTPgGRYRGARRIVTGDGldgGEIYYTAD 74


                  ....*..
gi 1366246874 135 HYKTFVK 141
Cdd:pfam00545  75 HYNSFVR 81
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 8-93 2.60e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 36.87  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366246874   8 KVTGKLAGTVskTNKSAKYVESsvKAKKVLNSFTEVSDFVAknGRLPvnyITKGEARKLGWDSKKGNLSKVAPGKSIGG- 86
Cdd:PTZ00314  137 KVGGKLLGIV--TSRDIDFVKD--KSTPVSEVMTPREKLVV--GNTP---ISLEEANEVLRESRKGKLPIVNDNGELVAl 207

                          90
                  ....*....|.
gi 1366246874  87 ----DIYKNRE 93
Cdd:PTZ00314  208 vsrsDLKKNRG 218
 
Name Accession Description Interval E-value
barnase cd00933
Barnase, a member of the family of homologous microbial ribonucleases, catalyses the cleavage ...
 37-143 2.48e-53

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: 163.83  E-value: 2.48e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366246874  37 LNSFTEVSDFVAKNGRLPVNYITKGEARKLGWDSKKGNLSKVAPGKSIGGDIYKNREKLLPEAKNRVWREADINYTTGYR 116
Cdd:cd00933     1 INTFQGVADYLQTYHRLPDNYITKSQAKELGWVAPKGNLWDVAPGKSIGGDRFSNREGRLPAAGGRTWREADINYQGGHR 80

                          90       100
                  ....*....|....*....|....*..
gi 1366246874 117 GNDRLLYSNDGLIYKTTDHYKTFVKLK 143
Cdd:cd00933    81 GADRLLYSNDGLIYKTTDHYRTFTRIR 107
Ribonuclease pfam00545
ribonuclease; This enzyme hydrolyses RNA and oligoribonucleotides.
 59-141 6.41e-24

ribonuclease; This enzyme hydrolyses RNA and oligoribonucleotides.


Pssm-ID: 459849  Cd Length: 81  Bit Score: 88.07  E-value: 6.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366246874  59 TKGEARKLGWdskKGNLSKVAPGksiGGDIYKNREKLLPEAKNRVWREADINYT-TGYRGNDRLLYSND---GLIYKTTD 134
Cdd:pfam00545   1 TTLEAIEAGW---WPGPFPYPPD---GGDVFGNREGRLPQAPGGYYREYDVNTPgGRYRGARRIVTGDGldgGEIYYTAD 74


                  ....*..
gi 1366246874 135 HYKTFVK 141
Cdd:pfam00545  75 HYNSFVR 81
microbial_RNases cd00389
microbial_RNases. Ribonucleases (RNAses) cleave phosphodiester bonds in RNA and are essential ...
 80-136 4.07e-17

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: 70.34  E-value: 4.07e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1366246874  80 PGKSIGGDIYKNREKLLPEAKNRVWREADINYT-TGYRGNDRLLYSNDGLIYKTTDHY 136
Cdd:cd00389    14 FGYSIYGHVFNNREGFLPFKGSGYYHEYPVNTPgGGSRGADRVVYGGDGEFYGTIDHY 71
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 8-93 2.60e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 36.87  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366246874   8 KVTGKLAGTVskTNKSAKYVESsvKAKKVLNSFTEVSDFVAknGRLPvnyITKGEARKLGWDSKKGNLSKVAPGKSIGG- 86
Cdd:PTZ00314  137 KVGGKLLGIV--TSRDIDFVKD--KSTPVSEVMTPREKLVV--GNTP---ISLEEANEVLRESRKGKLPIVNDNGELVAl 207

                          90
                  ....*....|.
gi 1366246874  87 ----DIYKNRE 93
Cdd:PTZ00314  208 vsrsDLKKNRG 218
 
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.
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