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Conserved domains on  [gi|3913570|sp|O35290|]
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RecName: Full=Eosinophil cationic-type ribonuclease 3; AltName: Full=MR-3; Flags: Precursor

Protein Classification

RNase_A_canonical domain-containing protein( domain architecture ID 10638767)

RNase_A_canonical domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNAse_Pc smart00092
Pancreatic ribonuclease;
29-156 1.82e-43

Pancreatic ribonuclease;


:

Pssm-ID: 128403  Cd Length: 123  Bit Score: 139.74  E-value: 1.82e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913570      29 TPSRWFAIQHINNN----TNLRCNVEMLRINRFRRTCKGLNTFLHTSFANAVGVCGNPSGLCSdNISRNCHNSSSRVHIT 104
Cdd:smart00092   3 TRAQKFLRQHIDSTpsssSSNYCNQMMKRRNMTQGRCKPVNTFVHESLADVKAVCSQKNVTCK-NGQTNCYQSNSRFHIT 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 3913570     105 VCNITSrrRIPYTQCRYQPRRSVEYYTVACNPRtsldspmyPVVPVHLDGTF 156
Cdd:smart00092  82 DCRLTG--SSKYPNCRYKTTQANKHIIVACEGN--------PYVPVHFDASV 123
 
Name Accession Description Interval E-value
RNAse_Pc smart00092
Pancreatic ribonuclease;
29-156 1.82e-43

Pancreatic ribonuclease;


Pssm-ID: 128403  Cd Length: 123  Bit Score: 139.74  E-value: 1.82e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913570      29 TPSRWFAIQHINNN----TNLRCNVEMLRINRFRRTCKGLNTFLHTSFANAVGVCGNPSGLCSdNISRNCHNSSSRVHIT 104
Cdd:smart00092   3 TRAQKFLRQHIDSTpsssSSNYCNQMMKRRNMTQGRCKPVNTFVHESLADVKAVCSQKNVTCK-NGQTNCYQSNSRFHIT 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 3913570     105 VCNITSrrRIPYTQCRYQPRRSVEYYTVACNPRtsldspmyPVVPVHLDGTF 156
Cdd:smart00092  82 DCRLTG--SSKYPNCRYKTTQANKHIIVACEGN--------PYVPVHFDASV 123
RnaseA pfam00074
Pancreatic ribonuclease; Ribonucleases. Members include pancreatic RNAase A and angiogenins. ...
 29-153 1.13e-39

Pancreatic ribonuclease; Ribonucleases. Members include pancreatic RNAase A and angiogenins. Structure is an alpha+beta fold -- long curved beta sheet and three helices.


Pssm-ID: 459661  Cd Length: 121  Bit Score: 130.07  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913570     29 TPSRWFAIQHINNNTNLR----CNVEMLRINRFRRTCKGLNTFLHTSFANAVGVCGNPSGLCSDNiSRNCHNSSSRVHIT 104
Cdd:pfam00074   1 TRAQWFLRQHIDPPPSPLsdryCNTMMKRRNMTTPRCKPVNTFLHESFEDIQAVCGNPNVTCKNG-RKNCHRSSSPVSIT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 3913570    105 VCNITSRRRipYTQCRYQPRRSVEYYTVACNPrtsldSPMYPVVPVHLD 153
Cdd:pfam00074  80 DCRLTGGSK--YPNCRYRTTLSNRYIVVACEG-----DPPYPGVPVHLD 121
RNase_A_canonical cd06265
Canonical RNase A family includes all vertebrate homologues to the bovine pancreatic ...
 29-154 5.70e-32

Canonical RNase A family includes all vertebrate homologues to the bovine pancreatic ribonuclease A (RNase A) that contain the catalytic site, necessary for RNase activity. In the human genome 8 RNases , refered to as "canonical" RNases, have been identified, pancreatic RNase (RNase 1), Eosinophil Derived Neurotoxin (SEDN/RNASE 2), Eosinophil Cationic Protein (ECP/RNase 3), RNase 4, Angiogenin (RNase 5), RNase 6 or k6, the skin derived RNase (RNase 7) and RNase 8. The eight human genes are all located in a cluster on chromosome 14. Canonical RNase A enzymes have special biological activities; for example, some stimulate the development of vascular endothelial cells, dendritic cells, and neurons, are cytotoxic/anti-tumoral and/or anti-pathogenic. RNase A is involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. The catalytic mechanism is a transphosphorylation of P-O 5' bonds on the 3' side of pyrimidines and subsequent hydrolysis to generate 3' phosphate groups. The canonical RNase A family proteins have a conserved catalytic triad (two histidines and one lysine). They also share 6 to 8 cysteines that form three to four disulfide bonds. Two disulfide bonds that are close to the N and C termini contribute most significantly to conformational stability. Angiogenin or RNAse 5 has been implicated in tumor-associated angiogenesis. Comparative analysis in mammals and birds indicates that the whole family may have originated from a RNase 5-like gene. This hypothesis is supported by the fact that only RNase 5-like RNases have been reported outside the mammalian class. The RNase 5 group would therefore be the most ancient form of this family, and all other members would have arisen during mammalian evolution.


Pssm-ID: 119387  Cd Length: 115  Bit Score: 110.13  E-value: 5.70e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913570   29 TPSRWFAIQHINNNTNL--RCNVEMLRINRFRRTCKGLNTFLHTSFANAVGVCGNPSGLCSdNISRNCHNSSSRVHITVC 106
Cdd:cd06265   1 TRYQKFLRQHVDPPRTGirYCNVMMRRRNMTKGRCKPVNTFIHESFADVRAVCTNPNVTCK-NGRNNCHKSNSPFPVTDC 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 3913570  107 NITSRRRIPytQCRYQPRRSVEYYTVACNPRtsldspmypvVPVHLDG 154
Cdd:cd06265  80 NLTGGSRYP--NCRYRGTPSTRKIVVACENG----------VPVHLDG 115
 
Name Accession Description Interval E-value
RNAse_Pc smart00092
Pancreatic ribonuclease;
29-156 1.82e-43

Pancreatic ribonuclease;


Pssm-ID: 128403  Cd Length: 123  Bit Score: 139.74  E-value: 1.82e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913570      29 TPSRWFAIQHINNN----TNLRCNVEMLRINRFRRTCKGLNTFLHTSFANAVGVCGNPSGLCSdNISRNCHNSSSRVHIT 104
Cdd:smart00092   3 TRAQKFLRQHIDSTpsssSSNYCNQMMKRRNMTQGRCKPVNTFVHESLADVKAVCSQKNVTCK-NGQTNCYQSNSRFHIT 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 3913570     105 VCNITSrrRIPYTQCRYQPRRSVEYYTVACNPRtsldspmyPVVPVHLDGTF 156
Cdd:smart00092  82 DCRLTG--SSKYPNCRYKTTQANKHIIVACEGN--------PYVPVHFDASV 123
RnaseA pfam00074
Pancreatic ribonuclease; Ribonucleases. Members include pancreatic RNAase A and angiogenins. ...
 29-153 1.13e-39

Pancreatic ribonuclease; Ribonucleases. Members include pancreatic RNAase A and angiogenins. Structure is an alpha+beta fold -- long curved beta sheet and three helices.


Pssm-ID: 459661  Cd Length: 121  Bit Score: 130.07  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913570     29 TPSRWFAIQHINNNTNLR----CNVEMLRINRFRRTCKGLNTFLHTSFANAVGVCGNPSGLCSDNiSRNCHNSSSRVHIT 104
Cdd:pfam00074   1 TRAQWFLRQHIDPPPSPLsdryCNTMMKRRNMTTPRCKPVNTFLHESFEDIQAVCGNPNVTCKNG-RKNCHRSSSPVSIT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 3913570    105 VCNITSRRRipYTQCRYQPRRSVEYYTVACNPrtsldSPMYPVVPVHLD 153
Cdd:pfam00074  80 DCRLTGGSK--YPNCRYRTTLSNRYIVVACEG-----DPPYPGVPVHLD 121
RNase_A_canonical cd06265
Canonical RNase A family includes all vertebrate homologues to the bovine pancreatic ...
 29-154 5.70e-32

Canonical RNase A family includes all vertebrate homologues to the bovine pancreatic ribonuclease A (RNase A) that contain the catalytic site, necessary for RNase activity. In the human genome 8 RNases , refered to as "canonical" RNases, have been identified, pancreatic RNase (RNase 1), Eosinophil Derived Neurotoxin (SEDN/RNASE 2), Eosinophil Cationic Protein (ECP/RNase 3), RNase 4, Angiogenin (RNase 5), RNase 6 or k6, the skin derived RNase (RNase 7) and RNase 8. The eight human genes are all located in a cluster on chromosome 14. Canonical RNase A enzymes have special biological activities; for example, some stimulate the development of vascular endothelial cells, dendritic cells, and neurons, are cytotoxic/anti-tumoral and/or anti-pathogenic. RNase A is involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. The catalytic mechanism is a transphosphorylation of P-O 5' bonds on the 3' side of pyrimidines and subsequent hydrolysis to generate 3' phosphate groups. The canonical RNase A family proteins have a conserved catalytic triad (two histidines and one lysine). They also share 6 to 8 cysteines that form three to four disulfide bonds. Two disulfide bonds that are close to the N and C termini contribute most significantly to conformational stability. Angiogenin or RNAse 5 has been implicated in tumor-associated angiogenesis. Comparative analysis in mammals and birds indicates that the whole family may have originated from a RNase 5-like gene. This hypothesis is supported by the fact that only RNase 5-like RNases have been reported outside the mammalian class. The RNase 5 group would therefore be the most ancient form of this family, and all other members would have arisen during mammalian evolution.


Pssm-ID: 119387  Cd Length: 115  Bit Score: 110.13  E-value: 5.70e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913570   29 TPSRWFAIQHINNNTNL--RCNVEMLRINRFRRTCKGLNTFLHTSFANAVGVCGNPSGLCSdNISRNCHNSSSRVHITVC 106
Cdd:cd06265   1 TRYQKFLRQHVDPPRTGirYCNVMMRRRNMTKGRCKPVNTFIHESFADVRAVCTNPNVTCK-NGRNNCHKSNSPFPVTDC 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 3913570  107 NITSRRRIPytQCRYQPRRSVEYYTVACNPRtsldspmypvVPVHLDG 154
Cdd:cd06265  80 NLTGGSRYP--NCRYRGTPSTRKIVVACENG----------VPVHLDG 115
RNase_A cd00163
RNase A family, or Pancreatic RNases family; includes vertebrate RNase homologs to the bovine ...
 31-153 8.33e-18

RNase A family, or Pancreatic RNases family; includes vertebrate RNase homologs to the bovine pancreatic ribonuclease A (RNase A). Many of these enzymes have special biological activities; for example, some stimulate the development of vascular endothelial cells, dendritic cells, and neurons, are cytotoxic/anti-tumoral and/or anti-pathogenic. RNase A is involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. The catalytic mechanism is a transphosphorylation of P-O 5' bonds on the 3' side of pyrimidines and subsequent hydrolysis to generate 3' phosphate groups. The RNase A family proteins have a conserved catalytic triad (two histidines and one lysine); recently some family members lacking the catalytic residues have been identified. They also share three or four disulfide bonds. The most conserved disulfide bonds are close to the N and C termini and contribute most significantly to the conformational stability. 8 RNase A homologs had initially been identified in the human genome, pancreatic RNase (RNase 1), Eosinophil Derived Neurotoxin (EDN/RNASE 2), Eosinophil Cationic Protein (ECP/RNase 3), RNase 4, Angiogenin (RNase 5), RNase 6 or k6, the skin derived RNase (RNase 7) and RNase 8. These eight human genes are all located in a cluster on chromosome 14. Recent genomic analysis has extended the family to 13 sequences. However only the first eight identified human RNases, which are refered to as "canonical" RNases, contain the catalytic residues required for RNase A activity. The new genes corresponding to RNases 9-13 are also located in the same chromosome cluster and seem to be related to male-reproductive functions. RNases 9-13 have the characteristic disulfide bridge pattern but are unlikely to share RNase activity. The RNase A family most likely started off in vertebrates as a host-defense protein, and comparative analysis in mammals and birds indicates that the family may have originated from a RNase 5-like gene. This hypothesis is supported by the fact that only RNase 5-like RNases have been reported outside the mammalian class. The RNase 5 group would therefore be the most ancient form of this family, and all other members would have arisen during mammalian evolution.


Pssm-ID: 119386  Cd Length: 119  Bit Score: 73.95  E-value: 8.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913570   31 SRWFAIQHINNNTNLR----CNVEMLRIN-RFRRTCKGLNTFLHTSFANAVGVCGNPSGLCsDNISRNCHNSSSRVHITV 105
Cdd:cd00163   3 ARTFRRQHIDYPKSNGdpryCNSMMRRKKvTENGSCKKQHTFIHESLEEVQAVCNNPSVFC-KNGGENCHRSKRPLDLTV 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 3913570  106 CNITSRRRIPytQCRYQPRRSVEYYTVACNPRtsldspmyPVVPVHLD 153
Cdd:cd00163  82 CKLTGGSRIP--NCRYNTTYTEKFILVTCDDK--------PIVPVHLD 119
 
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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