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Conserved domains on  [gi|157819033|ref|NP_001099680|]
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ribonuclease T2 precursor [Rattus norvegicus]

Protein Classification

T2 family ribonuclease( domain architecture ID 10452025)

T2 family ribonuclease catalyzes a two-stage endonucleolytic cleavage of RNA to form 3'-nucleotides; similar to Danio rerio ribonuclease T2 that has ribonuclease activity, with higher activity at acidic pH

CATH:  3.90.730.10
EC:  4.6.1.19
Gene Ontology:  GO:0003723|GO:0033897
PubMed:  12109772
SCOP:  4001977

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Ribonuclease_T2 pfam00445
Ribonuclease T2 family;
37-215 1.91e-72

Ribonuclease T2 family;


:

Pssm-ID: 459812  Cd Length: 181  Bit Score: 219.14  E-value: 1.91e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033   37 WKKLILTQHWPPTVCKEVNRCR--DSLDYWTIHGLWPDRAED------CNHSWHFNLNEIKDLLRDMKIYWPDVIHPSSN 108
Cdd:pfam00445   1 FDFLLLTQQWPGTYCDTKPSCCgpDSGADFTIHGLWPDNDGGggypqfCDRSRPFDPSEISDLLNDLNKYWPSLKSGNGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033  109 rsQFWKHEWDKHGTCAAQVdaLNSERKYFGKSLDLYKQIDLNSVLQKFEIKPSIN-YYQLADFKDALTRIYGVVPKIQCL 187
Cdd:pfam00445  81 --SFWKHEWEKHGTCASTS--LDDEHDYFNAALKLRKKLNLLSALASAGIVPSDTkTYTLSDIKDALKKGFGGTPYIQCN 156
                         170       180
                  ....*....|....*....|....*...
gi 157819033  188 MPEQGEnvQTIGQIELCFTKeDFHLRNC 215
Cdd:pfam00445 157 RDPSGN--QQLYEIRLCFDK-GLTFIDC 181
 
Name Accession Description Interval E-value
Ribonuclease_T2 pfam00445
Ribonuclease T2 family;
37-215 1.91e-72

Ribonuclease T2 family;


Pssm-ID: 459812  Cd Length: 181  Bit Score: 219.14  E-value: 1.91e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033   37 WKKLILTQHWPPTVCKEVNRCR--DSLDYWTIHGLWPDRAED------CNHSWHFNLNEIKDLLRDMKIYWPDVIHPSSN 108
Cdd:pfam00445   1 FDFLLLTQQWPGTYCDTKPSCCgpDSGADFTIHGLWPDNDGGggypqfCDRSRPFDPSEISDLLNDLNKYWPSLKSGNGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033  109 rsQFWKHEWDKHGTCAAQVdaLNSERKYFGKSLDLYKQIDLNSVLQKFEIKPSIN-YYQLADFKDALTRIYGVVPKIQCL 187
Cdd:pfam00445  81 --SFWKHEWEKHGTCASTS--LDDEHDYFNAALKLRKKLNLLSALASAGIVPSDTkTYTLSDIKDALKKGFGGTPYIQCN 156
                         170       180
                  ....*....|....*....|....*...
gi 157819033  188 MPEQGEnvQTIGQIELCFTKeDFHLRNC 215
Cdd:pfam00445 157 RDPSGN--QQLYEIRLCFDK-GLTFIDC 181
RNase_T2_euk cd01061
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
37-219 8.60e-68

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: 207.96  E-value: 8.60e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033  37 WKKLILTQHWPPTVCKEVNRC--RDSLDYWTIHGLWPDRA-----EDCNHSWHFNLNEIKDLLRDMKIYWPDVIHPSSNr 109
Cdd:cd01061    1 FDYLQLVLQWPDTYCSTGPCCcrPPPPDSFTIHGLWPDNCsgtypQFCDSSSNFDSILISDLLNELNKYWPDLTGPKNN- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033 110 SQFWKHEWDKHGTCAAqvDALNSERKYFGKSLDLYKQIDLNSVLQKFEIKPSINYYQLADFKDALTRIYGVVPKIQCLmp 189
Cdd:cd01061   80 QSFWEHEWNKHGTCSS--TLLYNQYDYFDTALKLKDKLDLLKILAKAGIVPSTQTYTLSDIQNAIKAATGVTPVIKCS-- 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 157819033 190 eQGENVQTIGQIELCFTKEDFHLRNCTEPE 219
Cdd:cd01061  156 -KDPGKGELNEIWICFDKKGGEFIDCPRPP 184
RnaI COG3719
Ribonuclease I [Translation, ribosomal structure and biogenesis];
46-218 5.06e-08

Ribonuclease I [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442933  Cd Length: 222  Bit Score: 51.90  E-value: 5.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033  46 WPPTVC----KEVNR--CRDSLDY-WTIHGLWP----DRAEDCNHSwHFNL-NEIKDLLRDmkiywpdvIHPSsnrSQFW 113
Cdd:COG3719   44 WSPGFCategDARGKpqCRAGRAYgFVLHGLWPqyerGWPSYCGTP-EPALsRATRAALAD--------VMPS---AGLA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033 114 KHEWDKHGTCAAQvdalnSERKYFGKSLDLYKQIDLNSVLQKFEIKPSINyyqLADFKDALTRIYGVVP----KIQClmp 189
Cdd:COG3719  112 RHEWKKHGTCSGL-----SPDDYFALARRLREAVNIPAVGRALNIGKTVT---AAEVEAAFDAANPGLApdaiAVTC--- 180
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 157819033 190 EQGEnvqtIGQIELCFTKE--------DFHLRNCTEP 218
Cdd:COG3719  181 RRGR----LTEVRICLSKDlkprpcglADVRRGCRAG 213
 
Name Accession Description Interval E-value
Ribonuclease_T2 pfam00445
Ribonuclease T2 family;
37-215 1.91e-72

Ribonuclease T2 family;


Pssm-ID: 459812  Cd Length: 181  Bit Score: 219.14  E-value: 1.91e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033   37 WKKLILTQHWPPTVCKEVNRCR--DSLDYWTIHGLWPDRAED------CNHSWHFNLNEIKDLLRDMKIYWPDVIHPSSN 108
Cdd:pfam00445   1 FDFLLLTQQWPGTYCDTKPSCCgpDSGADFTIHGLWPDNDGGggypqfCDRSRPFDPSEISDLLNDLNKYWPSLKSGNGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033  109 rsQFWKHEWDKHGTCAAQVdaLNSERKYFGKSLDLYKQIDLNSVLQKFEIKPSIN-YYQLADFKDALTRIYGVVPKIQCL 187
Cdd:pfam00445  81 --SFWKHEWEKHGTCASTS--LDDEHDYFNAALKLRKKLNLLSALASAGIVPSDTkTYTLSDIKDALKKGFGGTPYIQCN 156
                         170       180
                  ....*....|....*....|....*...
gi 157819033  188 MPEQGEnvQTIGQIELCFTKeDFHLRNC 215
Cdd:pfam00445 157 RDPSGN--QQLYEIRLCFDK-GLTFIDC 181
RNase_T2_euk cd01061
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
37-219 8.60e-68

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: 207.96  E-value: 8.60e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033  37 WKKLILTQHWPPTVCKEVNRC--RDSLDYWTIHGLWPDRA-----EDCNHSWHFNLNEIKDLLRDMKIYWPDVIHPSSNr 109
Cdd:cd01061    1 FDYLQLVLQWPDTYCSTGPCCcrPPPPDSFTIHGLWPDNCsgtypQFCDSSSNFDSILISDLLNELNKYWPDLTGPKNN- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033 110 SQFWKHEWDKHGTCAAqvDALNSERKYFGKSLDLYKQIDLNSVLQKFEIKPSINYYQLADFKDALTRIYGVVPKIQCLmp 189
Cdd:cd01061   80 QSFWEHEWNKHGTCSS--TLLYNQYDYFDTALKLKDKLDLLKILAKAGIVPSTQTYTLSDIQNAIKAATGVTPVIKCS-- 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 157819033 190 eQGENVQTIGQIELCFTKEDFHLRNCTEPE 219
Cdd:cd01061  156 -KDPGKGELNEIWICFDKKGGEFIDCPRPP 184
RNase_T2 cd00374
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
37-219 1.14e-56

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: 179.57  E-value: 1.14e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033  37 WKKLILTQHWPPTVC---KEVNRCRDSLDYWTIHGLWPD-----RAEDCNHSWHFNLNEIKDLLRDMKIYWPDVIHPSSn 108
Cdd:cd00374    1 FDYYVLVLQWPPTFCatgPCKCCGTPPPDSFTIHGLWPDncdgtYPQFCDSSSFFDKSKDSDLLDELNKYWPDLMPGKD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033 109 rSQFWKHEWDKHGTCAAQvdaLNSERKYFGKSLDLYKQIDLNSVLQKFEIKPSI-NYYQLADFKDALTRIYGVVPKIQCl 187
Cdd:cd00374   80 -SSFWKHEWNKHGTCSGT---LLDQDDYFRTALKLLDKLDLLSILAKAGIKPSDgSTYTLAFIQNAIKAATGATPSLKC- 154
                        170       180       190
                 ....*....|....*....|....*....|..
gi 157819033 188 mpEQGENVQTIGQIELCFTKEDFHLRNCTEPE 219
Cdd:cd00374  155 --TKDPGKGLLTEIWICFDKDALKFIDCPTPG 184
RNase_T2_prok cd01062
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
46-230 2.74e-09

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: 55.08  E-value: 2.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033  46 WPPTVC-------KEVNRCRDSLDYWTIHGLWP-----DRAEDCNHSWHFNLNEIkdLLRDMKIYWPDvihpssnrSQFW 113
Cdd:cd01062   10 WQPGFCatqgdrpECATCGTLDAYGFTLHGLWPqkpkgGWPEYCGVTSEPPLSEE--TRSRLLDVMPA--------SGLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033 114 KHEWDKHGTCAAQvdalnSERKYFGKSLDLYKQIDLNSVLQKFEikpSINYYQLADFKDALTRIYGVVPkiqclmpeqGE 193
Cdd:cd01062   80 RHEWRKHGTCSGL-----DPDAYFAKARNLREALKIPPELRLLA---GNIGVTASEIRQAFIKANPGLP---------PD 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157819033 194 NVQTIGQ------IELCFTKeDFHLRNCTEPEEQPSSGQEARL 230
Cdd:cd01062  143 AVSVSCQggllteVRICLDK-DLKFAACPTADRDNCPAGTVDI 184
RnaI COG3719
Ribonuclease I [Translation, ribosomal structure and biogenesis];
46-218 5.06e-08

Ribonuclease I [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442933  Cd Length: 222  Bit Score: 51.90  E-value: 5.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033  46 WPPTVC----KEVNR--CRDSLDY-WTIHGLWP----DRAEDCNHSwHFNL-NEIKDLLRDmkiywpdvIHPSsnrSQFW 113
Cdd:COG3719   44 WSPGFCategDARGKpqCRAGRAYgFVLHGLWPqyerGWPSYCGTP-EPALsRATRAALAD--------VMPS---AGLA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819033 114 KHEWDKHGTCAAQvdalnSERKYFGKSLDLYKQIDLNSVLQKFEIKPSINyyqLADFKDALTRIYGVVP----KIQClmp 189
Cdd:COG3719  112 RHEWKKHGTCSGL-----SPDDYFALARRLREAVNIPAVGRALNIGKTVT---AAEVEAAFDAANPGLApdaiAVTC--- 180
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 157819033 190 EQGEnvqtIGQIELCFTKE--------DFHLRNCTEP 218
Cdd:COG3719  181 RRGR----LTEVRICLSKDlkprpcglADVRRGCRAG 213
 
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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