NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|62738927]
View 

Chain C, NONSECRETORY RIBONUCLEASE

Protein Classification

RNase_A_canonical domain-containing protein( domain architecture ID 10638767)

RNase_A_canonical domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RNAse_Pc smart00092
Pancreatic ribonuclease;
5-135 9.82e-51

Pancreatic ribonuclease;


:

Pssm-ID: 128403  Cd Length: 123  Bit Score: 157.07  E-value: 9.82e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62738927      5 QFTWAQWFETQHINMT-----SQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPsnKTRKNCHHSGSQV 79
Cdd:smart00092   1 KETRAQKFLRQHIDSTpssssSNYCNQMMKRRNMTQGRCKPVNTFVHESLADVKAVCSQKNVTCK--NGQTNCYQSNSRF 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 62738927     80 PLIHCNLTTPSpqNISNCRYAQTPANMFYIVACDNRdqrrdppqyPVVPVHLDRII 135
Cdd:smart00092  79 HITDCRLTGSS--KYPNCRYKTTQANKHIIVACEGN---------PYVPVHFDASV 123
 
Name Accession Description Interval E-value
RNAse_Pc smart00092
Pancreatic ribonuclease;
5-135 9.82e-51

Pancreatic ribonuclease;


Pssm-ID: 128403  Cd Length: 123  Bit Score: 157.07  E-value: 9.82e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62738927      5 QFTWAQWFETQHINMT-----SQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPsnKTRKNCHHSGSQV 79
Cdd:smart00092   1 KETRAQKFLRQHIDSTpssssSNYCNQMMKRRNMTQGRCKPVNTFVHESLADVKAVCSQKNVTCK--NGQTNCYQSNSRF 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 62738927     80 PLIHCNLTTPSpqNISNCRYAQTPANMFYIVACDNRdqrrdppqyPVVPVHLDRII 135
Cdd:smart00092  79 HITDCRLTGSS--KYPNCRYKTTQANKHIIVACEGN---------PYVPVHFDASV 123
RnaseA pfam00074
Pancreatic ribonuclease; Ribonucleases. Members include pancreatic RNAase A and angiogenins. ...
 7-132 9.35e-43

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: 137.00  E-value: 9.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62738927     7 TWAQWFETQHINMTSQQ-----CTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPSNktRKNCHHSGSQVPL 81
Cdd:pfam00074   1 TRAQWFLRQHIDPPPSPlsdryCNTMMKRRNMTTPRCKPVNTFLHESFEDIQAVCGNPNVTCKNG--RKNCHRSSSPVSI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 62738927    82 IHCNLTTPSpqNISNCRYAQTPANMFYIVACDnrdqrRDPPqYPVVPVHLD 132
Cdd:pfam00074  79 TDCRLTGGS--KYPNCRYRTTLSNRYIVVACE-----GDPP-YPGVPVHLD 121
RNase_A_canonical cd06265
Canonical RNase A family includes all vertebrate homologues to the bovine pancreatic ...
 9-133 1.11e-35

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: 118.99  E-value: 1.11e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62738927   9 AQWFETQHINMT---SQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCpsNKTRKNCHHSGSQVPLIHCN 85
Cdd:cd06265   3 YQKFLRQHVDPPrtgIRYCNVMMRRRNMTKGRCKPVNTFIHESFADVRAVCTNPNVTC--KNGRNNCHKSNSPFPVTDCN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 62738927  86 LTTPSpqNISNCRYAQTPANMFYIVACDNRdqrrdppqypvVPVHLDR 133
Cdd:cd06265  81 LTGGS--RYPNCRYRGTPSTRKIVVACENG-----------VPVHLDG 115
 
Name Accession Description Interval E-value
RNAse_Pc smart00092
Pancreatic ribonuclease;
5-135 9.82e-51

Pancreatic ribonuclease;


Pssm-ID: 128403  Cd Length: 123  Bit Score: 157.07  E-value: 9.82e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62738927      5 QFTWAQWFETQHINMT-----SQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPsnKTRKNCHHSGSQV 79
Cdd:smart00092   1 KETRAQKFLRQHIDSTpssssSNYCNQMMKRRNMTQGRCKPVNTFVHESLADVKAVCSQKNVTCK--NGQTNCYQSNSRF 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 62738927     80 PLIHCNLTTPSpqNISNCRYAQTPANMFYIVACDNRdqrrdppqyPVVPVHLDRII 135
Cdd:smart00092  79 HITDCRLTGSS--KYPNCRYKTTQANKHIIVACEGN---------PYVPVHFDASV 123
RnaseA pfam00074
Pancreatic ribonuclease; Ribonucleases. Members include pancreatic RNAase A and angiogenins. ...
 7-132 9.35e-43

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: 137.00  E-value: 9.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62738927     7 TWAQWFETQHINMTSQQ-----CTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPSNktRKNCHHSGSQVPL 81
Cdd:pfam00074   1 TRAQWFLRQHIDPPPSPlsdryCNTMMKRRNMTTPRCKPVNTFLHESFEDIQAVCGNPNVTCKNG--RKNCHRSSSPVSI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 62738927    82 IHCNLTTPSpqNISNCRYAQTPANMFYIVACDnrdqrRDPPqYPVVPVHLD 132
Cdd:pfam00074  79 TDCRLTGGS--KYPNCRYRTTLSNRYIVVACE-----GDPP-YPGVPVHLD 121
RNase_A_canonical cd06265
Canonical RNase A family includes all vertebrate homologues to the bovine pancreatic ...
 9-133 1.11e-35

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: 118.99  E-value: 1.11e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62738927   9 AQWFETQHINMT---SQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCpsNKTRKNCHHSGSQVPLIHCN 85
Cdd:cd06265   3 YQKFLRQHVDPPrtgIRYCNVMMRRRNMTKGRCKPVNTFIHESFADVRAVCTNPNVTC--KNGRNNCHKSNSPFPVTDCN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 62738927  86 LTTPSpqNISNCRYAQTPANMFYIVACDNRdqrrdppqypvVPVHLDR 133
Cdd:cd06265  81 LTGGS--RYPNCRYRGTPSTRKIVVACENG-----------VPVHLDG 115
RNase_A cd00163
RNase A family, or Pancreatic RNases family; includes vertebrate RNase homologs to the bovine ...
 9-132 5.36e-24

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: 89.36  E-value: 5.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62738927   9 AQWFETQHINMTSQQ-----CTNAMQVINNYQR-RCKNQNTFLLTTFANVVNVCGNPNMTCpsNKTRKNCHHSGSQVPLI 82
Cdd:cd00163   3 ARTFRRQHIDYPKSNgdpryCNSMMRRKKVTENgSCKKQHTFIHESLEEVQAVCNNPSVFC--KNGGENCHRSKRPLDLT 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 62738927  83 HCNLTTPSPqnISNCRYAQTPANMFYIVACDNRdqrrdppqyPVVPVHLD 132
Cdd:cd00163  81 VCKLTGGSR--IPNCRYNTTYTEKFILVTCDDK---------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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH