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Conserved domains on  [gi|16974822|pdb|1IQQ|A]
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Chain A, S3-RNase

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 ...
1-200 3.57e-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. 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: 176.37  E-value: 3.57e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A        1 YDYFQFTQQYQLAVCNSNRTLCKDPPDKLFTVHGLWPSNMVGPDPSKC-PIKNIRKRE-KLLEHQLEIIWPNVFDRTKNN 78
Cdd:cd01061   1 FDYLQLVLQWPDTYCSTGPCCCRPPPPDSFTIHGLWPDNCSGTYPQFCdSSSNFDSILiSDLLNELNKYWPDLTGPKNNQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A       79 LFWDKEWMKHGSCGYPTIDNENHYFETVIKMYisKKQNVSRILSKAKIEPDGKKRALLDIENAIRNGAdNKKPKLKCQKK 158
Cdd:cd01061  81 SFWEHEWNKHGTCSSTLLYNQYDYFDTALKLK--DKLDLLKILAKAGIVPSTQTYTLSDIQNAIKAAT-GVTPVIKCSKD 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
1IQQ_A      159 GTTTELVEITLCSDKSGEHFIDCPHPFepisPHYCPTNNIKY 200
Cdd:cd01061 158 PGKGELNEIWICFDKKGGEFIDCPRPP----KSTCPDDGIKF 195
 
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 ...
1-200 3.57e-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. 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: 176.37  E-value: 3.57e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A        1 YDYFQFTQQYQLAVCNSNRTLCKDPPDKLFTVHGLWPSNMVGPDPSKC-PIKNIRKRE-KLLEHQLEIIWPNVFDRTKNN 78
Cdd:cd01061   1 FDYLQLVLQWPDTYCSTGPCCCRPPPPDSFTIHGLWPDNCSGTYPQFCdSSSNFDSILiSDLLNELNKYWPDLTGPKNNQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A       79 LFWDKEWMKHGSCGYPTIDNENHYFETVIKMYisKKQNVSRILSKAKIEPDGKKRALLDIENAIRNGAdNKKPKLKCQKK 158
Cdd:cd01061  81 SFWEHEWNKHGTCSSTLLYNQYDYFDTALKLK--DKLDLLKILAKAGIVPSTQTYTLSDIQNAIKAAT-GVTPVIKCSKD 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
1IQQ_A      159 GTTTELVEITLCSDKSGEHFIDCPHPFepisPHYCPTNNIKY 200
Cdd:cd01061 158 PGKGELNEIWICFDKKGGEFIDCPRPP----KSTCPDDGIKF 195
Ribonuclease_T2 pfam00445
Ribonuclease T2 family;
1-181 8.01e-35

Ribonuclease T2 family;


Pssm-ID: 459812  Cd Length: 181  Bit Score: 121.30  E-value: 8.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A          1 YDYFQFTQQYQLAVCNSNRTLCKDPPDKLFTVHGLWPSNMVGP-DPSKCPIKNIRKREKL--LEHQLEIIWPNVFDRTKN 77
Cdd:pfam00445   1 FDFLLLTQQWPGTYCDTKPSCCGPDSGADFTIHGLWPDNDGGGgYPQFCDRSRPFDPSEIsdLLNDLNKYWPSLKSGNGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A         78 NlFWDKEWMKHGSCGYPTIDNENHYFETVIKMYisKKQNVSRILSKAKIEP-DGKKRALLDIENAIRNGADNKKPKLKCQ 156
Cdd:pfam00445  81 S-FWKHEWEKHGTCASTSLDDEHDYFNAALKLR--KKLNLLSALASAGIVPsDTKTYTLSDIKDALKKGFGGTPYIQCNR 157
                         170       180
                  ....*....|....*....|....*
1IQQ_A        157 KKGTTTELVEITLCSDKsGEHFIDC 181
Cdd:pfam00445 158 DPSGNQQLYEIRLCFDK-GLTFIDC 181
RnaI COG3719
Ribonuclease I [Translation, ribosomal structure and biogenesis];
22-199 5.18e-08

Ribonuclease I [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442933  Cd Length: 222  Bit Score: 51.12  E-value: 5.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A       22 CKDPPDKLFTVHGLWPSNMVGPdPSKCPIKNIRKREKLLEHQLEIIwPNVfdrtknNLFWdKEWMKHGSC-GYPTidneN 100
Cdd:COG3719  61 CRAGRAYGFVLHGLWPQYERGW-PSYCGTPEPALSRATRAALADVM-PSA------GLAR-HEWKKHGTCsGLSP----D 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A      101 HYFETVIKMYisKKQNVSRILSKAKIepdGKKRALLDIENAIR--NGAdnkkpklkcqkkGTT---------TELVEITL 169
Cdd:COG3719 128 DYFALARRLR--EAVNIPAVGRALNI---GKTVTAAEVEAAFDaaNPG------------LAPdaiavtcrrGRLTEVRI 190
                       170       180       190
                ....*....|....*....|....*....|
1IQQ_A      170 CSDKSGEhFIDCPHpfePISPHYCPTNNIK 199
Cdd:COG3719 191 CLSKDLK-PRPCGL---ADVRRGCRAGFIL 216
 
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 ...
1-200 3.57e-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. 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: 176.37  E-value: 3.57e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A        1 YDYFQFTQQYQLAVCNSNRTLCKDPPDKLFTVHGLWPSNMVGPDPSKC-PIKNIRKRE-KLLEHQLEIIWPNVFDRTKNN 78
Cdd:cd01061   1 FDYLQLVLQWPDTYCSTGPCCCRPPPPDSFTIHGLWPDNCSGTYPQFCdSSSNFDSILiSDLLNELNKYWPDLTGPKNNQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A       79 LFWDKEWMKHGSCGYPTIDNENHYFETVIKMYisKKQNVSRILSKAKIEPDGKKRALLDIENAIRNGAdNKKPKLKCQKK 158
Cdd:cd01061  81 SFWEHEWNKHGTCSSTLLYNQYDYFDTALKLK--DKLDLLKILAKAGIVPSTQTYTLSDIQNAIKAAT-GVTPVIKCSKD 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
1IQQ_A      159 GTTTELVEITLCSDKSGEHFIDCPHPFepisPHYCPTNNIKY 200
Cdd:cd01061 158 PGKGELNEIWICFDKKGGEFIDCPRPP----KSTCPDDGIKF 195
RNase_T2 cd00374
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
1-200 1.26e-43

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: 144.14  E-value: 1.26e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A        1 YDYFQFTQQYQLAVCNSNRTLCKD-PPDKLFTVHGLWPSNMVGPDPSKCPIKNIRK--REKLLEHQLEIIWPNVFDRTKN 77
Cdd:cd00374   1 FDYYVLVLQWPPTFCATGPCKCCGtPPPDSFTIHGLWPDNCDGTYPQFCDSSSFFDksKDSDLLDELNKYWPDLMPGKDS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A       78 NlFWDKEWMKHGSCgYPTIDNENHYFETVIKMYisKKQNVSRILSKAKIEP-DGKKRALLDIENAIRNGAdNKKPKLKCQ 156
Cdd:cd00374  81 S-FWKHEWNKHGTC-SGTLLDQDDYFRTALKLL--DKLDLLSILAKAGIKPsDGSTYTLAFIQNAIKAAT-GATPSLKCT 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
1IQQ_A      157 KKGTTTELVEITLCSDKSGEHFIDCPHPFepisPHYCPTNNIKY 200
Cdd:cd00374 156 KDPGKGLLTEIWICFDKDALKFIDCPTPG----KSTCPADGIKF 195
Ribonuclease_T2 pfam00445
Ribonuclease T2 family;
1-181 8.01e-35

Ribonuclease T2 family;


Pssm-ID: 459812  Cd Length: 181  Bit Score: 121.30  E-value: 8.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A          1 YDYFQFTQQYQLAVCNSNRTLCKDPPDKLFTVHGLWPSNMVGP-DPSKCPIKNIRKREKL--LEHQLEIIWPNVFDRTKN 77
Cdd:pfam00445   1 FDFLLLTQQWPGTYCDTKPSCCGPDSGADFTIHGLWPDNDGGGgYPQFCDRSRPFDPSEIsdLLNDLNKYWPSLKSGNGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A         78 NlFWDKEWMKHGSCGYPTIDNENHYFETVIKMYisKKQNVSRILSKAKIEP-DGKKRALLDIENAIRNGADNKKPKLKCQ 156
Cdd:pfam00445  81 S-FWKHEWEKHGTCASTSLDDEHDYFNAALKLR--KKLNLLSALASAGIVPsDTKTYTLSDIKDALKKGFGGTPYIQCNR 157
                         170       180
                  ....*....|....*....|....*
1IQQ_A        157 KKGTTTELVEITLCSDKsGEHFIDC 181
Cdd:pfam00445 158 DPSGNQQLYEIRLCFDK-GLTFIDC 181
RnaI COG3719
Ribonuclease I [Translation, ribosomal structure and biogenesis];
22-199 5.18e-08

Ribonuclease I [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442933  Cd Length: 222  Bit Score: 51.12  E-value: 5.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A       22 CKDPPDKLFTVHGLWPSNMVGPdPSKCPIKNIRKREKLLEHQLEIIwPNVfdrtknNLFWdKEWMKHGSC-GYPTidneN 100
Cdd:COG3719  61 CRAGRAYGFVLHGLWPQYERGW-PSYCGTPEPALSRATRAALADVM-PSA------GLAR-HEWKKHGTCsGLSP----D 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A      101 HYFETVIKMYisKKQNVSRILSKAKIepdGKKRALLDIENAIR--NGAdnkkpklkcqkkGTT---------TELVEITL 169
Cdd:COG3719 128 DYFALARRLR--EAVNIPAVGRALNI---GKTVTAAEVEAAFDaaNPG------------LAPdaiavtcrrGRLTEVRI 190
                       170       180       190
                ....*....|....*....|....*....|
1IQQ_A      170 CSDKSGEhFIDCPHpfePISPHYCPTNNIK 199
Cdd:COG3719 191 CLSKDLK-PRPCGL---ADVRRGCRAGFIL 216
RNase_T2_prok cd01062
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
1-109 2.94e-06

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: 45.83  E-value: 2.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IQQ_A        1 YDYFQFTQQYQLAVCNS-----NRTLCKDPPDKLFTVHGLWPSNMVGPDPSKCPIKN-IRKREKLLEhQLEIIWPnvfdr 74
Cdd:cd01062   1 FDYYVLALSWQPGFCATqgdrpECATCGTLDAYGFTLHGLWPQKPKGGWPEYCGVTSePPLSEETRS-RLLDVMP----- 74
                        90       100       110
                ....*....|....*....|....*....|....*.
1IQQ_A       75 tKNNLFWdKEWMKHGSC-GYptidNENHYFETVIKM 109
Cdd:cd01062  75 -ASGLIR-HEWRKHGTCsGL----DPDAYFAKARNL 104
 
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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