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Conserved domains on  [gi|2500573|sp|Q38717|]
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RecName: Full=Ribonuclease S-4; AltName: Full=S4-RNase; AltName: Full=Stylar glycoprotein 4; 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 ...
34-211 1.15e-65

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: 201.79  E-value: 1.15e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573   34 DYLKLVLQWPKSFCLINsRKCQRNPLPSNFTIHGLWPDNYTRQAPQSC-TTNNFQRFTDTDIEQRMEESWPDLKQQSiag 112
Cdd:cd01061   2 DYLQLVLQWPDTYCSTG-PCCCRPPPPDSFTIHGLWPDNCSGTYPQFCdSSSNFDSILISDLLNELNKYWPDLTGPK--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573  113 LSYNFWQDQWRKHGSCCFPPHESEI-YFLKALELKDRLDVLTILENNNFNPGTpQPFSVLRVFNTISRAIGKTPILKCA- 190
Cdd:cd01061  78 NNQSFWEHEWNKHGTCSSTLLYNQYdYFDTALKLKDKLDLLKILAKAGIVPST-QTYTLSDIQNAIKAATGVTPVIKCSk 156
                       170       180
                ....*....|....*....|....
gi 2500573  191 ---QSYLKEVVICVDNNGASVVHC 211
Cdd:cd01061 157 dpgKGELNEIWICFDKKGGEFIDC 180
 
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 ...
34-211 1.15e-65

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: 201.79  E-value: 1.15e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573   34 DYLKLVLQWPKSFCLINsRKCQRNPLPSNFTIHGLWPDNYTRQAPQSC-TTNNFQRFTDTDIEQRMEESWPDLKQQSiag 112
Cdd:cd01061   2 DYLQLVLQWPDTYCSTG-PCCCRPPPPDSFTIHGLWPDNCSGTYPQFCdSSSNFDSILISDLLNELNKYWPDLTGPK--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573  113 LSYNFWQDQWRKHGSCCFPPHESEI-YFLKALELKDRLDVLTILENNNFNPGTpQPFSVLRVFNTISRAIGKTPILKCA- 190
Cdd:cd01061  78 NNQSFWEHEWNKHGTCSSTLLYNQYdYFDTALKLKDKLDLLKILAKAGIVPST-QTYTLSDIQNAIKAATGVTPVIKCSk 156
                       170       180
                ....*....|....*....|....
gi 2500573  191 ---QSYLKEVVICVDNNGASVVHC 211
Cdd:cd01061 157 dpgKGELNEIWICFDKKGGEFIDC 180
Ribonuclease_T2 pfam00445
Ribonuclease T2 family;
34-202 6.68e-41

Ribonuclease T2 family;


Pssm-ID: 459812  Cd Length: 181  Bit Score: 137.87  E-value: 6.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573     34 DYLKLVLQWPKSFCLiNSRKCQRNPLPSNFTIHGLWPDNY-TRQAPQSCTTNN-FQRFTDTDIEQRMEESWPDLKQQSia 111
Cdd:pfam00445   2 DFLLLTQQWPGTYCD-TKPSCCGPDSGADFTIHGLWPDNDgGGGYPQFCDRSRpFDPSEISDLLNDLNKYWPSLKSGN-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573    112 glSYNFWQDQWRKHGSCCFPPHESEI-YFLKALELKDRLDVLTILENNNFNPGTPQPFSVLRVFNTISRAIGKTPILKC- 189
Cdd:pfam00445  79 --GESFWKHEWEKHGTCASTSLDDEHdYFNAALKLRKKLNLLSALASAGIVPSDTKTYTLSDIKDALKKGFGGTPYIQCn 156
                         170
                  ....*....|....*..
gi 2500573    190 ----AQSYLKEVVICVD 202
Cdd:pfam00445 157 rdpsGNQQLYEIRLCFD 173
RnaI COG3719
Ribonuclease I [Translation, ribosomal structure and biogenesis];
34-200 1.07e-11

Ribonuclease I [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442933  Cd Length: 222  Bit Score: 62.30  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573   34 DYLKLVLQWPKSFC-----LINSRKCQRNPlPSNFTIHGLWPdNYTRQAPQSCTTNnfQRFTDTDIEQRMEESWPDlkqq 108
Cdd:COG3719  36 DYYVLALSWSPGFCategdARGKPQCRAGR-AYGFVLHGLWP-QYERGWPSYCGTP--EPALSRATRAALADVMPS---- 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573  109 siAGLsynFWQdQWRKHGSCC-FPPHEseiYFLKALELKDRLDVLTILENNNfNPGTPQPFSVLRVFNTISRAIGKTPI- 186
Cdd:COG3719 108 --AGL---ARH-EWKKHGTCSgLSPDD---YFALARRLREAVNIPAVGRALN-IGKTVTAAEVEAAFDAANPGLAPDAIa 177
                       170
                ....*....|....
gi 2500573  187 LKCAQSYLKEVVIC 200
Cdd:COG3719 178 VTCRRGRLTEVRIC 191
 
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 ...
34-211 1.15e-65

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: 201.79  E-value: 1.15e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573   34 DYLKLVLQWPKSFCLINsRKCQRNPLPSNFTIHGLWPDNYTRQAPQSC-TTNNFQRFTDTDIEQRMEESWPDLKQQSiag 112
Cdd:cd01061   2 DYLQLVLQWPDTYCSTG-PCCCRPPPPDSFTIHGLWPDNCSGTYPQFCdSSSNFDSILISDLLNELNKYWPDLTGPK--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573  113 LSYNFWQDQWRKHGSCCFPPHESEI-YFLKALELKDRLDVLTILENNNFNPGTpQPFSVLRVFNTISRAIGKTPILKCA- 190
Cdd:cd01061  78 NNQSFWEHEWNKHGTCSSTLLYNQYdYFDTALKLKDKLDLLKILAKAGIVPST-QTYTLSDIQNAIKAATGVTPVIKCSk 156
                       170       180
                ....*....|....*....|....
gi 2500573  191 ---QSYLKEVVICVDNNGASVVHC 211
Cdd:cd01061 157 dpgKGELNEIWICFDKKGGEFIDC 180
RNase_T2 cd00374
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
34-211 4.53e-60

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: 187.28  E-value: 4.53e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573   34 DYLKLVLQWPKSFCLINSRKCQRNPLPSNFTIHGLWPDNYTRQAPQSC-TTNNFQRFTDTDIEQRMEESWPDLKQQSiag 112
Cdd:cd00374   2 DYYVLVLQWPPTFCATGPCKCCGTPPPDSFTIHGLWPDNCDGTYPQFCdSSSFFDKSKDSDLLDELNKYWPDLMPGK--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573  113 lSYNFWQDQWRKHGSCCFPPHESEIYFLKALELKDRLDVLTILENNNFNPGTPQPFSVLRVFNTISRAIGKTPILKCA-- 190
Cdd:cd00374  79 -DSSFWKHEWNKHGTCSGTLLDQDDYFRTALKLLDKLDLLSILAKAGIKPSDGSTYTLAFIQNAIKAATGATPSLKCTkd 157
                       170       180
                ....*....|....*....|...
gi 2500573  191 --QSYLKEVVICVDNNGASVVHC 211
Cdd:cd00374 158 pgKGLLTEIWICFDKDALKFIDC 180
Ribonuclease_T2 pfam00445
Ribonuclease T2 family;
34-202 6.68e-41

Ribonuclease T2 family;


Pssm-ID: 459812  Cd Length: 181  Bit Score: 137.87  E-value: 6.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573     34 DYLKLVLQWPKSFCLiNSRKCQRNPLPSNFTIHGLWPDNY-TRQAPQSCTTNN-FQRFTDTDIEQRMEESWPDLKQQSia 111
Cdd:pfam00445   2 DFLLLTQQWPGTYCD-TKPSCCGPDSGADFTIHGLWPDNDgGGGYPQFCDRSRpFDPSEISDLLNDLNKYWPSLKSGN-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573    112 glSYNFWQDQWRKHGSCCFPPHESEI-YFLKALELKDRLDVLTILENNNFNPGTPQPFSVLRVFNTISRAIGKTPILKC- 189
Cdd:pfam00445  79 --GESFWKHEWEKHGTCASTSLDDEHdYFNAALKLRKKLNLLSALASAGIVPSDTKTYTLSDIKDALKKGFGGTPYIQCn 156
                         170
                  ....*....|....*..
gi 2500573    190 ----AQSYLKEVVICVD 202
Cdd:pfam00445 157 rdpsGNQQLYEIRLCFD 173
RNase_T2_prok cd01062
Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism ...
34-202 5.34e-13

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: 65.09  E-value: 5.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573   34 DYLKLVLQWPKSFCLINSRKCQRNPLPS----NFTIHGLWPDNYTRQAPQSCttnnfQRFTDTDIE----QRMEESWPDl 105
Cdd:cd01062   2 DYYVLALSWQPGFCATQGDRPECATCGTldayGFTLHGLWPQKPKGGWPEYC-----GVTSEPPLSeetrSRLLDVMPA- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573  106 kqqsiaglSYNFWQdQWRKHGSCCFPPHESeiYFLKALELKDRLDVLTilENNNFNPGTPQPFSVLRV-----FNTISRA 180
Cdd:cd01062  76 --------SGLIRH-EWRKHGTCSGLDPDA--YFAKARNLREALKIPP--ELRLLAGNIGVTASEIRQafikaNPGLPPD 142
                       170       180
                ....*....|....*....|..
gi 2500573  181 IGKtpiLKCAQSYLKEVVICVD 202
Cdd:cd01062 143 AVS---VSCQGGLLTEVRICLD 161
RnaI COG3719
Ribonuclease I [Translation, ribosomal structure and biogenesis];
34-200 1.07e-11

Ribonuclease I [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442933  Cd Length: 222  Bit Score: 62.30  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573   34 DYLKLVLQWPKSFC-----LINSRKCQRNPlPSNFTIHGLWPdNYTRQAPQSCTTNnfQRFTDTDIEQRMEESWPDlkqq 108
Cdd:COG3719  36 DYYVLALSWSPGFCategdARGKPQCRAGR-AYGFVLHGLWP-QYERGWPSYCGTP--EPALSRATRAALADVMPS---- 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500573  109 siAGLsynFWQdQWRKHGSCC-FPPHEseiYFLKALELKDRLDVLTILENNNfNPGTPQPFSVLRVFNTISRAIGKTPI- 186
Cdd:COG3719 108 --AGL---ARH-EWKKHGTCSgLSPDD---YFALARRLREAVNIPAVGRALN-IGKTVTAAEVEAAFDAANPGLAPDAIa 177
                       170
                ....*....|....
gi 2500573  187 LKCAQSYLKEVVIC 200
Cdd:COG3719 178 VTCRRGRLTEVRIC 191
 
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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