1QMT,1RRA,11BG,1RNF,1B1I


Conserved Protein Domain Family
RNase_A

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cd00163: RNase_A 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 119386
View PSSM: cd00163
Aligned: 17 rows
Threshold Bit Score: 109.001
Threshold Setting Gi: 7245973
Created: 1-Nov-2000
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
catalytic sitedimerization
Conserved site includes 7 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic site [active site]
Evidence:
  • Structure:11BG_A, Bovine seminal RNase A binds uridylyl-2'-5'-phospho-guanosine and sulfate
    View structure with Cn3D
  • Comment:catalytic site of RNase A consists of pyrimidine binding ( B1) and catalytic ( P1) subsites.
  • Structure:11BG_A, Bovine seminal RNAse A binds uridylyl-2'-5'-phospho-guanosine and sulfate at P1 subsite.
    View structure with Cn3D
  • Comment:P1 subsites accommodate the phosphate where phosphodiester bond cleavage occurs.
  • Structure:11BG_A, Bovine seminal RNAse A binds uridylyl-2'-5'-phospho-guanosine and sulfate at B1 subsite
    View structure with Cn3D
  • Comment:B1 subsites accommodate the nucleotide bases on the 3' sides of the scissile bond.
  • Citation:PMID 7492594
  • Citation:PMID 9918722
  • Citation:PMID 8120892

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                 #                                   #   #                           #  
1QMT_A         7 TRAQWFAIQHISln-----------ppRCTIAMRAINnyr--wrCKNQNTFLRTtFANVVNVCGnqsircphnrtlnNCH 73  human
11BG_A         3 SAAAKFERQHMDsgnsp-----ssssnYCNLMMCCRKmtq--gkCKPVNTFVHEsLADVKAVCSqkkvtc--kngqtNCY 73  Bos taurus
Q7YRG8        60 TKEKVKRRILVNpgmpl------gdsgYCNYQIMRKNvyy-kysCVTEHYFLLMqYDELQKTCYnrfvpc--kngirKCN 130 white-fronted c...
NP_001019993  22 AVMSTLEHLHVDypqndv----pvparYCNHMIIQRVirepdhtCKKEHVFIHErPRKINGICIspkkvacqnlsaiFCF 97  human
NP_001007112  88 VGGNKMLRAQAFsqsypnylrsdlmdrECNTLMAKKMkpy-nhtCISQYIFIHEePDEIKAVCKsppvac--elkggKCH 164 pig
NP_001012993 105 SNKDYLRLDQTDr--------------ECNDMMAHKMkep-sqsCIAQYAFIHEdLNTVKAVCNspviac--elkggKCH 167 human
Q9D5A9        92 RAEPRFQSKQDYlkfd-------lsvrDCNTMMAHKIkep-nqsCINQYTFIHEdPNTVKAVCNgslvdc--dlqggKCY 161 house mouse
XP_001515593  34 SKARTFRLMHIDfprsef---apgfrgYCNGLMAYVRaqreswqCPEKHFVLHApAATVRAICAhtdsfc--edfgeFCT 108 platypus
NP_001012264  27 IGSRNFYTLSIDyprvny---pkgfrgYCNGLMSYMRgkmqnsdCPKIHYVIHApWKAIQKFCKysdsfc--enyneYCT 101 human
XP_539677    103 SNKAYLRSDLLAr--------------ECNTLMAPKVkgh-nrtCISQYTFIHEdLDTVQAVCNspvvac--qlkggKCH 165 dog
Feature 1                 #                                               ## 
1QMT_A        74 RSrfRVPLLHCDLinpgaqnisNCRYADRp--GRRFYVVACDnrdprdsprypvvPVHLD 131 human
11BG_A        74 QSksTMRITDCREtgss--kypNCAYKTTq--VEKHIIVACGgkp--------svPVHFD 121 Bos taurus
Q7YRG8       131 MSkkLVEGVYCNLtkas--nipLCQYNSFy--RRGYVLITCTwqnemqklipypiNDLVE 186 white-fronted capuchin
NP_001019993  98 QSetKFKMTVCQLiegt--rypACRYHYSp--TEGFVLVTCDdl----------rPDSFL 143 human
NP_001007112 165 KSarPFDLTFCKLskpg-qvtpHCNYVTFl--LEKHILISCNd-----------mKVQVM 210 pig
NP_001012993 168 KSsrPFDLTLCELsqpd-qvtpNCNYLTSv--IKKHIIITCNd-----------mKRQLP 213 human
Q9D5A9       162 KSprPFDLTLCKLakpg-qvtpNCHYLTYi--TEKSIFMTCNd------------KRQLE 206 house mouse
XP_001515593 109 RShkPLPVTTCARtpgl--ppsVCRYNATvhvQSHRVWLLCSskf-------egfPMDVI 159 platypus
NP_001012264 102 LTqdSLPITVCSLshqq--pptSCYYNSTl--TNQKLYLLCSrky-------eadPIGIA 150 human
XP_539677    166 RSsrPFDLTFCRLskpg-qvtpHCHYVTFi--FEKYIIISCNd-----------mKVQVV 211 dog

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