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Conserved domains on  [gi|20139363|sp|O00584|]
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RecName: Full=Ribonuclease T2; AltName: Full=Ribonuclease 6; Flags: Precursor

Protein Classification

T2 family ribonuclease( domain architecture ID 10099427)

T2 family ribonuclease catalyzes a two-stage endonucleolytic cleavage of RNA to form 3'-nucleotides; similar to Homo sapiens ribonuclease T2, which cleaves preferentially single-stranded RNA molecules between purine and uridine residues, which critically contributes to the supply of catabolic uridine and the generation of purine-2',3'-cyclophosphate-terminated oligoribonucleotides

CATH:  3.90.730.10
EC:  4.6.1.19
Gene Ontology:  GO:0003723|GO:0033897
PubMed:  12109772

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RNase_T2_euk cd01061
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
34-227 1.65e-74

Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen. Generally, RNases have two distinct binding sites: the primary site (B1 site) and the subsite (B2 site), for nucleotides located at the 5'- and 3'- terminal ends of the sessil bond, respectively. This CD includes the eukaryotic RNase T2 family members.


:

Pssm-ID: 238512 [Multi-domain]  Cd Length: 195  Bit Score: 224.90  E-value: 1.65e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363  34 WKKLIMVQHWPETVCEKIQNDCR-DPPDYWTIHGLWPDKSEG-----CNRSWPFNLEEIKDLLPEMRAYWPDVIHSFPNr 107
Cdd:cd01061   1 FDYLQLVLQWPDTYCSTGPCCCRpPPPDSFTIHGLWPDNCSGtypqfCDSSSNFDSILISDLLNELNKYWPDLTGPKNN- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363 108 SRFWKHEWEKHGTCAAqvDALNSQKKYFGRSLELYRELDLNSVLLKLGIKPSINYYQVADFKDALARVYGVIPKIQClpp 187
Cdd:cd01061  80 QSFWEHEWNKHGTCSS--TLLYNQYDYFDTALKLKDKLDLLKILAKAGIVPSTQTYTLSDIQNAIKAATGVTPVIKC--- 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20139363 188 SQDEEVQTIGQIELCLTKQDQQLQNCTEPGEQPSPKQEVW 227
Cdd:cd01061 155 SKDPGKGELNEIWICFDKKGGEFIDCPRPPKSTCPDDGIK 194
 
Name Accession Description Interval E-value
RNase_T2_euk cd01061
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
34-227 1.65e-74

Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen. Generally, RNases have two distinct binding sites: the primary site (B1 site) and the subsite (B2 site), for nucleotides located at the 5'- and 3'- terminal ends of the sessil bond, respectively. This CD includes the eukaryotic RNase T2 family members.


Pssm-ID: 238512 [Multi-domain]  Cd Length: 195  Bit Score: 224.90  E-value: 1.65e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363  34 WKKLIMVQHWPETVCEKIQNDCR-DPPDYWTIHGLWPDKSEG-----CNRSWPFNLEEIKDLLPEMRAYWPDVIHSFPNr 107
Cdd:cd01061   1 FDYLQLVLQWPDTYCSTGPCCCRpPPPDSFTIHGLWPDNCSGtypqfCDSSSNFDSILISDLLNELNKYWPDLTGPKNN- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363 108 SRFWKHEWEKHGTCAAqvDALNSQKKYFGRSLELYRELDLNSVLLKLGIKPSINYYQVADFKDALARVYGVIPKIQClpp 187
Cdd:cd01061  80 QSFWEHEWNKHGTCSS--TLLYNQYDYFDTALKLKDKLDLLKILAKAGIVPSTQTYTLSDIQNAIKAATGVTPVIKC--- 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20139363 188 SQDEEVQTIGQIELCLTKQDQQLQNCTEPGEQPSPKQEVW 227
Cdd:cd01061 155 SKDPGKGELNEIWICFDKKGGEFIDCPRPPKSTCPDDGIK 194
Ribonuclease_T2 pfam00445
Ribonuclease T2 family;
34-213 4.76e-71

Ribonuclease T2 family;


Pssm-ID: 459812  Cd Length: 181  Bit Score: 215.68  E-value: 4.76e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363    34 WKKLIMVQHWPETVCEKIQNDCR-DPPDYWTIHGLWPDKSEG------CNRSWPFNLEEIKDLLPEMRAYWPDVIHSfpN 106
Cdd:pfam00445   1 FDFLLLTQQWPGTYCDTKPSCCGpDSGADFTIHGLWPDNDGGggypqfCDRSRPFDPSEISDLLNDLNKYWPSLKSG--N 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363   107 RSRFWKHEWEKHGTCAAQVdaLNSQKKYFGRSLELYRELDLNSVLLKLGIKPSIN-YYQVADFKDALARVYGVIPKIQCL 185
Cdd:pfam00445  79 GESFWKHEWEKHGTCASTS--LDDEHDYFNAALKLRKKLNLLSALASAGIVPSDTkTYTLSDIKDALKKGFGGTPYIQCN 156
                         170       180
                  ....*....|....*....|....*...
gi 20139363   186 PPSQDEevQTIGQIELCLTKqDQQLQNC 213
Cdd:pfam00445 157 RDPSGN--QQLYEIRLCFDK-GLTFIDC 181
RnaI COG3719
Ribonuclease I [Translation, ribosomal structure and biogenesis];
55-205 4.48e-12

Ribonuclease I [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442933  Cd Length: 222  Bit Score: 63.45  E-value: 4.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363  55 CRDPPDY-WTIHGLWPdkseGCNRSWPFN--LEEIkDLLPEMRAYWPDVihsFPNRSRFWkHEWEKHGTCAAQvdalnSQ 131
Cdd:COG3719  61 CRAGRAYgFVLHGLWP----QYERGWPSYcgTPEP-ALSRATRAALADV---MPSAGLAR-HEWKKHGTCSGL-----SP 126
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20139363 132 KKYFGRSLELYRELDLNSVLLKLGIKPSINyyqVADFKDALARVYGVIP----KIQClppSQDEevqtIGQIELCLTK 205
Cdd:COG3719 127 DDYFALARRLREAVNIPAVGRALNIGKTVT---AAEVEAAFDAANPGLApdaiAVTC---RRGR----LTEVRICLSK 194
 
Name Accession Description Interval E-value
RNase_T2_euk cd01061
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
34-227 1.65e-74

Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen. Generally, RNases have two distinct binding sites: the primary site (B1 site) and the subsite (B2 site), for nucleotides located at the 5'- and 3'- terminal ends of the sessil bond, respectively. This CD includes the eukaryotic RNase T2 family members.


Pssm-ID: 238512 [Multi-domain]  Cd Length: 195  Bit Score: 224.90  E-value: 1.65e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363  34 WKKLIMVQHWPETVCEKIQNDCR-DPPDYWTIHGLWPDKSEG-----CNRSWPFNLEEIKDLLPEMRAYWPDVIHSFPNr 107
Cdd:cd01061   1 FDYLQLVLQWPDTYCSTGPCCCRpPPPDSFTIHGLWPDNCSGtypqfCDSSSNFDSILISDLLNELNKYWPDLTGPKNN- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363 108 SRFWKHEWEKHGTCAAqvDALNSQKKYFGRSLELYRELDLNSVLLKLGIKPSINYYQVADFKDALARVYGVIPKIQClpp 187
Cdd:cd01061  80 QSFWEHEWNKHGTCSS--TLLYNQYDYFDTALKLKDKLDLLKILAKAGIVPSTQTYTLSDIQNAIKAATGVTPVIKC--- 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20139363 188 SQDEEVQTIGQIELCLTKQDQQLQNCTEPGEQPSPKQEVW 227
Cdd:cd01061 155 SKDPGKGELNEIWICFDKKGGEFIDCPRPPKSTCPDDGIK 194
Ribonuclease_T2 pfam00445
Ribonuclease T2 family;
34-213 4.76e-71

Ribonuclease T2 family;


Pssm-ID: 459812  Cd Length: 181  Bit Score: 215.68  E-value: 4.76e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363    34 WKKLIMVQHWPETVCEKIQNDCR-DPPDYWTIHGLWPDKSEG------CNRSWPFNLEEIKDLLPEMRAYWPDVIHSfpN 106
Cdd:pfam00445   1 FDFLLLTQQWPGTYCDTKPSCCGpDSGADFTIHGLWPDNDGGggypqfCDRSRPFDPSEISDLLNDLNKYWPSLKSG--N 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363   107 RSRFWKHEWEKHGTCAAQVdaLNSQKKYFGRSLELYRELDLNSVLLKLGIKPSIN-YYQVADFKDALARVYGVIPKIQCL 185
Cdd:pfam00445  79 GESFWKHEWEKHGTCASTS--LDDEHDYFNAALKLRKKLNLLSALASAGIVPSDTkTYTLSDIKDALKKGFGGTPYIQCN 156
                         170       180
                  ....*....|....*....|....*...
gi 20139363   186 PPSQDEevQTIGQIELCLTKqDQQLQNC 213
Cdd:pfam00445 157 RDPSGN--QQLYEIRLCFDK-GLTFIDC 181
RNase_T2 cd00374
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
34-228 8.62e-64

Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen.


Pssm-ID: 238220  Cd Length: 195  Bit Score: 197.68  E-value: 8.62e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363  34 WKKLIMVQHWPETVCEKIQNDC--RDPPDYWTIHGLWPDKSEG-----CNRSWPFNLEEIKDLLPEMRAYWPDVIHsfPN 106
Cdd:cd00374   1 FDYYVLVLQWPPTFCATGPCKCcgTPPPDSFTIHGLWPDNCDGtypqfCDSSSFFDKSKDSDLLDELNKYWPDLMP--GK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363 107 RSRFWKHEWEKHGTCAAQvdaLNSQKKYFGRSLELYRELDLNSVLLKLGIKPSI-NYYQVADFKDALARVYGVIPKIQCl 185
Cdd:cd00374  79 DSSFWKHEWNKHGTCSGT---LLDQDDYFRTALKLLDKLDLLSILAKAGIKPSDgSTYTLAFIQNAIKAATGATPSLKC- 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20139363 186 ppSQDEEVQTIGQIELCLTKQDQQLQNCTEPGEQPSPKQEVWL 228
Cdd:cd00374 155 --TKDPGKGLLTEIWICFDKDALKFIDCPTPGKSTCPADGIKF 195
RNase_T2_prok cd01062
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
48-228 1.99e-12

Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen. Generally, RNases have two distinct binding sites: the primary site (B1 site) and the subsite (B2 site), for nucleotides located at the 5'- and 3'- terminal ends of the sessil bond, respectively. This CD includes the prokaryotic RNase T2 family members.


Pssm-ID: 238513  Cd Length: 184  Bit Score: 63.93  E-value: 1.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363  48 CEKIQNDCRDPPDYWTIHGLWPDK-----SEGCNRSWPFNL--EEIKDLLPEMRAywPDVIhsfpnrsrfwKHEWEKHGT 120
Cdd:cd01062  21 RPECATCGTLDAYGFTLHGLWPQKpkggwPEYCGVTSEPPLseETRSRLLDVMPA--SGLI----------RHEWRKHGT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363 121 CAAQvdalnSQKKYFGRSLELYRELDLnSVLLKLGIKPsiNYYQVADFKDALARVYGVIP----KIQCLPPSqdeevqtI 196
Cdd:cd01062  89 CSGL-----DPDAYFAKARNLREALKI-PPELRLLAGN--IGVTASEIRQAFIKANPGLPpdavSVSCQGGL-------L 153
                       170       180       190
                ....*....|....*....|....*....|..
gi 20139363 197 GQIELCLTKqDQQLQNCTEPGEQPSPKQEVWL 228
Cdd:cd01062 154 TEVRICLDK-DLKFAACPTADRDNCPAGTVDI 184
RnaI COG3719
Ribonuclease I [Translation, ribosomal structure and biogenesis];
55-205 4.48e-12

Ribonuclease I [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442933  Cd Length: 222  Bit Score: 63.45  E-value: 4.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139363  55 CRDPPDY-WTIHGLWPdkseGCNRSWPFN--LEEIkDLLPEMRAYWPDVihsFPNRSRFWkHEWEKHGTCAAQvdalnSQ 131
Cdd:COG3719  61 CRAGRAYgFVLHGLWP----QYERGWPSYcgTPEP-ALSRATRAALADV---MPSAGLAR-HEWKKHGTCSGL-----SP 126
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20139363 132 KKYFGRSLELYRELDLNSVLLKLGIKPSINyyqVADFKDALARVYGVIP----KIQClppSQDEevqtIGQIELCLTK 205
Cdd:COG3719 127 DDYFALARRLREAVNIPAVGRALNIGKTVT---AAEVEAAFDAANPGLApdaiAVTC---RRGR----LTEVRICLSK 194
 
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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