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Conserved domains on  [gi|21311883|ref|NP_080887|]
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ribonuclease T2-B precursor [Mus musculus]

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;
39-217 5.98e-73

Ribonuclease T2 family;


:

Pssm-ID: 459812  Cd Length: 181  Bit Score: 220.69  E-value: 5.98e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883    39 WKKLILTQHWPPTVCKEVNSCQ--DSLDYWTIHGLWPDRAED------CNQSWHFNLDEIKDLLRDMKIYWPDVIHrsSN 110
Cdd:pfam00445   1 FDFLLLTQQWPGTYCDTKPSCCgpDSGADFTIHGLWPDNDGGggypqfCDRSRPFDPSEISDLLNDLNKYWPSLKS--GN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883   111 RSQFWKHEWVKHGTCAAQVdaLNSEKKYFGKSLDLYKQIDLNSVLQKFGIKPSIN-YYQLADFKDALTRIYGVVPKIQCL 189
Cdd:pfam00445  79 GESFWKHEWEKHGTCASTS--LDDEHDYFNAALKLRKKLNLLSALASAGIVPSDTkTYTLSDIKDALKKGFGGTPYIQCN 156
                         170       180
                  ....*....|....*....|....*...
gi 21311883   190 MPEQGEsvQTVGQIELCFTKeDLHLRNC 217
Cdd:pfam00445 157 RDPSGN--QQLYEIRLCFDK-GLTFIDC 181
 
Name Accession Description Interval E-value
Ribonuclease_T2 pfam00445
Ribonuclease T2 family;
39-217 5.98e-73

Ribonuclease T2 family;


Pssm-ID: 459812  Cd Length: 181  Bit Score: 220.69  E-value: 5.98e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883    39 WKKLILTQHWPPTVCKEVNSCQ--DSLDYWTIHGLWPDRAED------CNQSWHFNLDEIKDLLRDMKIYWPDVIHrsSN 110
Cdd:pfam00445   1 FDFLLLTQQWPGTYCDTKPSCCgpDSGADFTIHGLWPDNDGGggypqfCDRSRPFDPSEISDLLNDLNKYWPSLKS--GN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883   111 RSQFWKHEWVKHGTCAAQVdaLNSEKKYFGKSLDLYKQIDLNSVLQKFGIKPSIN-YYQLADFKDALTRIYGVVPKIQCL 189
Cdd:pfam00445  79 GESFWKHEWEKHGTCASTS--LDDEHDYFNAALKLRKKLNLLSALASAGIVPSDTkTYTLSDIKDALKKGFGGTPYIQCN 156
                         170       180
                  ....*....|....*....|....*...
gi 21311883   190 MPEQGEsvQTVGQIELCFTKeDLHLRNC 217
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 ...
39-221 3.25e-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: 209.11  E-value: 3.25e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883  39 WKKLILTQHWPPTVCKEVNSCQ--DSLDYWTIHGLWPDRA-----EDCNQSWHFNLDEIKDLLRDMKIYWPDVIHRSSNr 111
Cdd:cd01061   1 FDYLQLVLQWPDTYCSTGPCCCrpPPPDSFTIHGLWPDNCsgtypQFCDSSSNFDSILISDLLNELNKYWPDLTGPKNN- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883 112 SQFWKHEWVKHGTCAAqvDALNSEKKYFGKSLDLYKQIDLNSVLQKFGIKPSINYYQLADFKDALTRIYGVVPKIQCLmp 191
Cdd:cd01061  80 QSFWEHEWNKHGTCSS--TLLYNQYDYFDTALKLKDKLDLLKILAKAGIVPSTQTYTLSDIQNAIKAATGVTPVIKCS-- 155
                       170       180       190
                ....*....|....*....|....*....|
gi 21311883 192 eQGESVQTVGQIELCFTKEDLHLRNCTEPG 221
Cdd:cd01061 156 -KDPGKGELNEIWICFDKKGGEFIDCPRPP 184
RnaI COG3719
Ribonuclease I [Translation, ribosomal structure and biogenesis];
64-217 8.71e-07

Ribonuclease I [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442933  Cd Length: 222  Bit Score: 48.43  E-value: 8.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883  64 DYWTIHGLWP----DRAEDCNQSwHFNLDEikDLLRDMKIYWPDV-IHRssnrsqfwkHEWVKHGTCAAQvdalnSEKKY 138
Cdd:COG3719  67 YGFVLHGLWPqyerGWPSYCGTP-EPALSR--ATRAALADVMPSAgLAR---------HEWKKHGTCSGL-----SPDDY 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883 139 FGKSLDLYKQIDLNSVLQKfgikpsINYYQ---LADFKDALTRIYGVVP----KIQClmpEQGEsvqtVGQIELCFTKeD 211
Cdd:COG3719 130 FALARRLREAVNIPAVGRA------LNIGKtvtAAEVEAAFDAANPGLApdaiAVTC---RRGR----LTEVRICLSK-D 195

                ....*.
gi 21311883 212 LHLRNC 217
Cdd:COG3719 196 LKPRPC 201
 
Name Accession Description Interval E-value
Ribonuclease_T2 pfam00445
Ribonuclease T2 family;
39-217 5.98e-73

Ribonuclease T2 family;


Pssm-ID: 459812  Cd Length: 181  Bit Score: 220.69  E-value: 5.98e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883    39 WKKLILTQHWPPTVCKEVNSCQ--DSLDYWTIHGLWPDRAED------CNQSWHFNLDEIKDLLRDMKIYWPDVIHrsSN 110
Cdd:pfam00445   1 FDFLLLTQQWPGTYCDTKPSCCgpDSGADFTIHGLWPDNDGGggypqfCDRSRPFDPSEISDLLNDLNKYWPSLKS--GN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883   111 RSQFWKHEWVKHGTCAAQVdaLNSEKKYFGKSLDLYKQIDLNSVLQKFGIKPSIN-YYQLADFKDALTRIYGVVPKIQCL 189
Cdd:pfam00445  79 GESFWKHEWEKHGTCASTS--LDDEHDYFNAALKLRKKLNLLSALASAGIVPSDTkTYTLSDIKDALKKGFGGTPYIQCN 156
                         170       180
                  ....*....|....*....|....*...
gi 21311883   190 MPEQGEsvQTVGQIELCFTKeDLHLRNC 217
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 ...
39-221 3.25e-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: 209.11  E-value: 3.25e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883  39 WKKLILTQHWPPTVCKEVNSCQ--DSLDYWTIHGLWPDRA-----EDCNQSWHFNLDEIKDLLRDMKIYWPDVIHRSSNr 111
Cdd:cd01061   1 FDYLQLVLQWPDTYCSTGPCCCrpPPPDSFTIHGLWPDNCsgtypQFCDSSSNFDSILISDLLNELNKYWPDLTGPKNN- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883 112 SQFWKHEWVKHGTCAAqvDALNSEKKYFGKSLDLYKQIDLNSVLQKFGIKPSINYYQLADFKDALTRIYGVVPKIQCLmp 191
Cdd:cd01061  80 QSFWEHEWNKHGTCSS--TLLYNQYDYFDTALKLKDKLDLLKILAKAGIVPSTQTYTLSDIQNAIKAATGVTPVIKCS-- 155
                       170       180       190
                ....*....|....*....|....*....|
gi 21311883 192 eQGESVQTVGQIELCFTKEDLHLRNCTEPG 221
Cdd:cd01061 156 -KDPGKGELNEIWICFDKKGGEFIDCPRPP 184
RNase_T2 cd00374
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
39-221 9.87e-57

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: 179.96  E-value: 9.87e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883  39 WKKLILTQHWPPTVCKEVNSCQ---DSLDYWTIHGLWPD-----RAEDCNQSWHFNLDEIKDLLRDMKIYWPDVIHrsSN 110
Cdd:cd00374   1 FDYYVLVLQWPPTFCATGPCKCcgtPPPDSFTIHGLWPDncdgtYPQFCDSSSFFDKSKDSDLLDELNKYWPDLMP--GK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883 111 RSQFWKHEWVKHGTCAAQvdaLNSEKKYFGKSLDLYKQIDLNSVLQKFGIKPSI-NYYQLADFKDALTRIYGVVPKIQCl 189
Cdd:cd00374  79 DSSFWKHEWNKHGTCSGT---LLDQDDYFRTALKLLDKLDLLSILAKAGIKPSDgSTYTLAFIQNAIKAATGATPSLKC- 154
                       170       180       190
                ....*....|....*....|....*....|..
gi 21311883 190 mpEQGESVQTVGQIELCFTKEDLHLRNCTEPG 221
Cdd:cd00374 155 --TKDPGKGLLTEIWICFDKDALKFIDCPTPG 184
RNase_T2_prok cd01062
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
48-217 3.00e-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: 3.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883  48 WPPTVC-------KEVNSCQDSLDYWTIHGLWP-----DRAEDCNQSWHFNLDEIkdLLRDMKIYWPDvihrssnrSQFW 115
Cdd:cd01062  10 WQPGFCatqgdrpECATCGTLDAYGFTLHGLWPqkpkgGWPEYCGVTSEPPLSEE--TRSRLLDVMPA--------SGLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883 116 KHEWVKHGTCAAQvdalnSEKKYFGKSLDLYKQIDLNSVLQKFgikPSINYYQLADFKDALTRIYGVVP----KIQCLMP 191
Cdd:cd01062  80 RHEWRKHGTCSGL-----DPDAYFAKARNLREALKIPPELRLL---AGNIGVTASEIRQAFIKANPGLPpdavSVSCQGG 151
                       170       180
                ....*....|....*....|....*.
gi 21311883 192 EQGEsvqtvgqIELCFTKEDLhLRNC 217
Cdd:cd01062 152 LLTE-------VRICLDKDLK-FAAC 169
RnaI COG3719
Ribonuclease I [Translation, ribosomal structure and biogenesis];
64-217 8.71e-07

Ribonuclease I [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442933  Cd Length: 222  Bit Score: 48.43  E-value: 8.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883  64 DYWTIHGLWP----DRAEDCNQSwHFNLDEikDLLRDMKIYWPDV-IHRssnrsqfwkHEWVKHGTCAAQvdalnSEKKY 138
Cdd:COG3719  67 YGFVLHGLWPqyerGWPSYCGTP-EPALSR--ATRAALADVMPSAgLAR---------HEWKKHGTCSGL-----SPDDY 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311883 139 FGKSLDLYKQIDLNSVLQKfgikpsINYYQ---LADFKDALTRIYGVVP----KIQClmpEQGEsvqtVGQIELCFTKeD 211
Cdd:COG3719 130 FALARRLREAVNIPAVGRA------LNIGKtvtAAEVEAAFDAANPGLApdaiAVTC---RRGR----LTEVRICLSK-D 195

                ....*.
gi 21311883 212 LHLRNC 217
Cdd:COG3719 196 LKPRPC 201
 
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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