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Conserved domains on  [gi|7297954|gb|AAF53198|]
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uncharacterized protein Dmel_CG5418 [Drosophila melanogaster]

Protein Classification

nucleoside hydrolase( domain architecture ID 10119096)

nucleoside hydrolase cleaves the N-glycosidic bond in nucleosides generating ribose and the respective base; similar to Aedes aegypti salivary purine nucleosidase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nuc_hydro_CeIAG cd02649
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ...
 10-332 1.15e-111

nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring nucleoside hydrolase from Caenorhabditis elegans. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the purine-preferring nucleoside hydrolase (IAG-NH) from C. elegans and the salivary purine nucleosidase from Aedes aegypti. C. elegans IAG-NH exhibits a high affinity for the substrate analogue p-nitrophenylriboside (p-NPR).


:

Pssm-ID: 239115 [Multi-domain]  Cd Length: 306  Bit Score: 327.29  E-value: 1.15e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   10 RLVVFDCDIGTDDAWALALLLRGeqlslasgRRYKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPIVTR 89
Cdd:cd02649   1 RKLIIDTDCGGDDAWALLMALAS--------PNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   90 TWlDISRFHGTDGLNDIGgYPDVSDLQEqLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYgDDFLDKIGGIF 169
Cdd:cd02649  73 GP-TAAYFHGKDGFGDVG-FPEPKDELE-LQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLD-PSLPQKIKRLY 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  170 IMGGNIYGRGNIMKCAEFNFMMDPEAAHTTLERLKVPAVILPWEPSIDDDfnlSLDWRLDVLGSVDHPLveLLSRVERSM 249
Cdd:cd02649 149 IMGGNREGVGNTTPAAEFNFHVDPEAAHIVLNSFGCPITIVPWETTLLAF---PLDWEFEDKWANRLEK--ALFAESLNR 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  250 LVPR------DIKHWINPDAALAAAYIFPKaMIAEQLDYHATVELAGVHTRGQMVLDHLRGrrvdaiHGKKSNVRIITHL 323
Cdd:cd02649 224 REYAfaseglGGDGWVPCDALAVAAALDPS-IITRRLTYAVDVELHGELTRGQMVVDWLGT------LKKKPNARVITKI 296


                ....*....
gi 7297954  324 NREPFRTIM 332
Cdd:cd02649 297 DREKFKELL 305
 
Name Accession Description Interval E-value
nuc_hydro_CeIAG cd02649
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ...
 10-332 1.15e-111

nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring nucleoside hydrolase from Caenorhabditis elegans. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the purine-preferring nucleoside hydrolase (IAG-NH) from C. elegans and the salivary purine nucleosidase from Aedes aegypti. C. elegans IAG-NH exhibits a high affinity for the substrate analogue p-nitrophenylriboside (p-NPR).


Pssm-ID: 239115 [Multi-domain]  Cd Length: 306  Bit Score: 327.29  E-value: 1.15e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   10 RLVVFDCDIGTDDAWALALLLRGeqlslasgRRYKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPIVTR 89
Cdd:cd02649   1 RKLIIDTDCGGDDAWALLMALAS--------PNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   90 TWlDISRFHGTDGLNDIGgYPDVSDLQEqLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYgDDFLDKIGGIF 169
Cdd:cd02649  73 GP-TAAYFHGKDGFGDVG-FPEPKDELE-LQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLD-PSLPQKIKRLY 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  170 IMGGNIYGRGNIMKCAEFNFMMDPEAAHTTLERLKVPAVILPWEPSIDDDfnlSLDWRLDVLGSVDHPLveLLSRVERSM 249
Cdd:cd02649 149 IMGGNREGVGNTTPAAEFNFHVDPEAAHIVLNSFGCPITIVPWETTLLAF---PLDWEFEDKWANRLEK--ALFAESLNR 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  250 LVPR------DIKHWINPDAALAAAYIFPKaMIAEQLDYHATVELAGVHTRGQMVLDHLRGrrvdaiHGKKSNVRIITHL 323
Cdd:cd02649 224 REYAfaseglGGDGWVPCDALAVAAALDPS-IITRRLTYAVDVELHGELTRGQMVVDWLGT------LKKKPNARVITKI 296


                ....*....
gi 7297954  324 NREPFRTIM 332
Cdd:cd02649 297 DREKFKELL 305
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 10-332 2.10e-67

Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; Inosine-uridine nucleoside N-ribohydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 441560 [Multi-domain]  Cd Length: 310  Bit Score: 214.63  E-value: 2.10e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   10 RLVVFDCDIGTDDAWALALLLRGEQLslasgrryKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPIVtR 89
Cdd:COG1957   3 RKVIIDTDPGIDDALALLLALASPEI--------DLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLV-R 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   90 TWLDISRFHGTDGLndigGYPDVSDLQEQLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYgDDFLDKIGGIF 169
Cdd:COG1957  74 PLVTAEHVHGEDGL----GGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKD-PELAERIKRIV 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  170 IMGGNIYGRGNIMKCAEFNFMMDPEAAHTTLERlKVPAVILPWEPS----IDDDfnlsldwRLDVLGSVDHPLVELLSRV 245
Cdd:COG1957 149 IMGGAFFVPGNVTPVAEFNIYVDPEAAKIVFAS-GIPITMVGLDVThqalLTPE-------DLARLAALGTPLGRFLADL 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  246 ERSMLvPRDIKHWINPDA----ALAAAYifpkaMIAEQL----DYHATVELAGVHTRGQMVLDhLRGRrvdaiHGKKSNV 317
Cdd:COG1957 221 LDFYL-DFYRERYGLDGCplhdPLAVAY-----LLDPELfttrPAPVDVETDGELTRGQTVVD-WRGV-----TGRPPNA 288

                       330
                ....*....|....*
gi 7297954  318 RIITHLNREPFRTIM 332
Cdd:COG1957 289 RVALDVDAERFLDLL 303
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
12-329 3.57e-60

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 193.96  E-value: 3.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954     12 VVFDCDIGTDDAWALALLLRGEQLslasgrryKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGcanpivtrtw 91
Cdd:pfam01156   1 VIIDTDPGIDDALALLLALASPEI--------ELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG---------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954     92 ldisrfhgtdglndiggypdvsdlqeqlqqehavnamyRLVCQyPKQVDFLLCGPLTNFASCINLYgDDFLDKIGGIFIM 171
Cdd:pfam01156  63 --------------------------------------EAIRE-PGEVTLVATGPLTNLALALRLD-PELAKKIKELVIM 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    172 GGNIYGRGNIMKCAEFNFMMDPEAAHTTLERlKVPAVILPWE----PSIDDDFnlsLDWRLDVLGSVDHPLVELLSRVER 247
Cdd:pfam01156 103 GGAFGVRGNVTPAAEFNIFVDPEAAKIVFTS-GLPITMVPLDvthqALLTPED---LERLAALGTPLGRFLADLLRFYAE 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    248 SMLVPRDIKHWINPDAALAAAYIFPKamIAEQLDYHATVELAGVHTRGQMVLDHLRGrrvdaiHGKKSNVRIITHLNREP 327
Cdd:pfam01156 179 FYRERFGIDGPPLHDPLAVAVALDPE--LFTTRRLNVDVETTGGLTRGQTVVDDRGG------WGKPPNVRVATDVDVDR 250


                  ..
gi 7297954    328 FR 329
Cdd:pfam01156 251 FW 252
PRK10768 PRK10768
ribonucleoside hydrolase RihC; Provisional
 12-197 8.32e-33

ribonucleoside hydrolase RihC; Provisional


Pssm-ID: 182713 [Multi-domain]  Cd Length: 304  Bit Score: 123.87  E-value: 8.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    12 VVFDCDIGTDDAWALALLLRGEQLSLasgrryKLIaiTCVQGNTDVVNGAQNALKILRLLERrDVPVFRGCANPIVtRTW 91
Cdd:PRK10768   5 IILDTDPGIDDAVAIAAALFAPELDL------KLI--TTVAGNVSVEKTTRNALKLLHFFNS-DVPVAQGAAKPLV-RPL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    92 LDISRFHGTDGLndiGGYpDVSDLQEQLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYGDDfLDKIGGIFIM 171
Cdd:PRK10768  75 RDAASVHGESGM---EGY-DFPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEV-KPYIKRIVLM 149

                        170       180
                 ....*....|....*....|....*.
gi 7297954   172 GGNIyGRGNIMKCAEFNFMMDPEAAH 197
Cdd:PRK10768 150 GGSA-GRGNVTPNAEFNIAVDPEAAA 174
 
Name Accession Description Interval E-value
nuc_hydro_CeIAG cd02649
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ...
 10-332 1.15e-111

nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring nucleoside hydrolase from Caenorhabditis elegans. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the purine-preferring nucleoside hydrolase (IAG-NH) from C. elegans and the salivary purine nucleosidase from Aedes aegypti. C. elegans IAG-NH exhibits a high affinity for the substrate analogue p-nitrophenylriboside (p-NPR).


Pssm-ID: 239115 [Multi-domain]  Cd Length: 306  Bit Score: 327.29  E-value: 1.15e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   10 RLVVFDCDIGTDDAWALALLLRGeqlslasgRRYKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPIVTR 89
Cdd:cd02649   1 RKLIIDTDCGGDDAWALLMALAS--------PNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   90 TWlDISRFHGTDGLNDIGgYPDVSDLQEqLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYgDDFLDKIGGIF 169
Cdd:cd02649  73 GP-TAAYFHGKDGFGDVG-FPEPKDELE-LQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLD-PSLPQKIKRLY 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  170 IMGGNIYGRGNIMKCAEFNFMMDPEAAHTTLERLKVPAVILPWEPSIDDDfnlSLDWRLDVLGSVDHPLveLLSRVERSM 249
Cdd:cd02649 149 IMGGNREGVGNTTPAAEFNFHVDPEAAHIVLNSFGCPITIVPWETTLLAF---PLDWEFEDKWANRLEK--ALFAESLNR 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  250 LVPR------DIKHWINPDAALAAAYIFPKaMIAEQLDYHATVELAGVHTRGQMVLDHLRGrrvdaiHGKKSNVRIITHL 323
Cdd:cd02649 224 REYAfaseglGGDGWVPCDALAVAAALDPS-IITRRLTYAVDVELHGELTRGQMVVDWLGT------LKKKPNARVITKI 296


                ....*....
gi 7297954  324 NREPFRTIM 332
Cdd:cd02649 297 DREKFKELL 305
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 10-332 2.10e-67

Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; Inosine-uridine nucleoside N-ribohydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 441560 [Multi-domain]  Cd Length: 310  Bit Score: 214.63  E-value: 2.10e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   10 RLVVFDCDIGTDDAWALALLLRGEQLslasgrryKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPIVtR 89
Cdd:COG1957   3 RKVIIDTDPGIDDALALLLALASPEI--------DLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLV-R 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   90 TWLDISRFHGTDGLndigGYPDVSDLQEQLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYgDDFLDKIGGIF 169
Cdd:COG1957  74 PLVTAEHVHGEDGL----GGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKD-PELAERIKRIV 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  170 IMGGNIYGRGNIMKCAEFNFMMDPEAAHTTLERlKVPAVILPWEPS----IDDDfnlsldwRLDVLGSVDHPLVELLSRV 245
Cdd:COG1957 149 IMGGAFFVPGNVTPVAEFNIYVDPEAAKIVFAS-GIPITMVGLDVThqalLTPE-------DLARLAALGTPLGRFLADL 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  246 ERSMLvPRDIKHWINPDA----ALAAAYifpkaMIAEQL----DYHATVELAGVHTRGQMVLDhLRGRrvdaiHGKKSNV 317
Cdd:COG1957 221 LDFYL-DFYRERYGLDGCplhdPLAVAY-----LLDPELfttrPAPVDVETDGELTRGQTVVD-WRGV-----TGRPPNA 288

                       330
                ....*....|....*
gi 7297954  318 RIITHLNREPFRTIM 332
Cdd:COG1957 289 RVALDVDAERFLDLL 303
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
12-329 3.57e-60

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 193.96  E-value: 3.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954     12 VVFDCDIGTDDAWALALLLRGEQLslasgrryKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGcanpivtrtw 91
Cdd:pfam01156   1 VIIDTDPGIDDALALLLALASPEI--------ELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG---------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954     92 ldisrfhgtdglndiggypdvsdlqeqlqqehavnamyRLVCQyPKQVDFLLCGPLTNFASCINLYgDDFLDKIGGIFIM 171
Cdd:pfam01156  63 --------------------------------------EAIRE-PGEVTLVATGPLTNLALALRLD-PELAKKIKELVIM 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    172 GGNIYGRGNIMKCAEFNFMMDPEAAHTTLERlKVPAVILPWE----PSIDDDFnlsLDWRLDVLGSVDHPLVELLSRVER 247
Cdd:pfam01156 103 GGAFGVRGNVTPAAEFNIFVDPEAAKIVFTS-GLPITMVPLDvthqALLTPED---LERLAALGTPLGRFLADLLRFYAE 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    248 SMLVPRDIKHWINPDAALAAAYIFPKamIAEQLDYHATVELAGVHTRGQMVLDHLRGrrvdaiHGKKSNVRIITHLNREP 327
Cdd:pfam01156 179 FYRERFGIDGPPLHDPLAVAVALDPE--LFTTRRLNVDVETTGGLTRGQTVVDDRGG------WGKPPNVRVATDVDVDR 250


                  ..
gi 7297954    328 FR 329
Cdd:pfam01156 251 FW 252
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
 12-328 4.85e-44

nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, xanthosine-inosine-uridine-adenosine-preferring and, uridine-cytidine preferring nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains proteins similar to nucleoside hydrolases which hydrolyze both pyrimidine and purine ribonucleosides: the inosine-uridine preferring nucleoside hydrolase from Crithidia fasciculata, the inosine-uridine-xanthosine preferring nucleoside hydrolase RihC from Escherichia coli and the xanthosine-inosine-uridine-adenosine-preferring nucleoside hydrolase RihC from Salmonella enterica serovar Typhimurium. This group also contains proteins similar to the pyrimidine-specific uridine-cytidine preferring nucleoside hydrolases URH1 from Saccharomyces cerevisiae, E. coli RihA and E. coli RihB. E. coli RihA is equally efficient with uridine and cytidine, E. coli RihB prefers cytidine over uridine. S. cerevisiae URH1 prefers uridine over cytidine.


Pssm-ID: 239117 [Multi-domain]  Cd Length: 302  Bit Score: 153.47  E-value: 4.85e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   12 VVFDCDIGTDDAWALALLLRGEQLslasgrryKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPIVtRTW 91
Cdd:cd02651   2 IIIDCDPGHDDAVAILLALFHPEL--------DLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLV-RPL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   92 LDISRFHGTDGLNDiggyPDVSDLQEQLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYGDDfLDKIGGIFIM 171
Cdd:cd02651  73 ITASDIHGESGLDG----ADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPEL-AERIKEIVLM 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  172 GGNiYGRGNIMKCAEFNFMMDPEAAHTTLERlKVPAVILPWE--------PSIDDDFnlsldwrLDVLGSVDHPLVELLS 243
Cdd:cd02651 148 GGA-LGRGNITPAAEFNIFVDPEAAKIVFNS-GIPITMVPLDvthkalatPEVIERI-------RALGNPVGKMLAELLD 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  244 RVERSMlvprDIKHWINP---DaALAAAYIF-PKAMIAEQLDyhATVELAGVHTRGQMVLDhLRGRrvdaiHGKKSNVRI 319
Cdd:cd02651 219 FFAETY----GSAFTEGPplhD-PCAVAYLLdPELFTTKRAN--VDVETEGELTRGRTVVD-LRGV-----TGRPANAQV 285


                ....*....
gi 7297954  320 ITHLNREPF 328
Cdd:cd02651 286 AVDVDVEKF 294
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 12-300 5.40e-44

nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the inosine-uridine preferring nucleoside hydrolase from Crithidia fasciculata, the xanthosine-inosine-uridine-adenosine-preferring nucleoside hydrolase RihC from Salmonella enterica serovar Typhimurium, the purine-specific inosine-adenosine-guanosine-preferring nucleoside hydrolase from Trypanosoma vivax and, pyrimidine-specific uridine-cytidine preferring nucleoside hydrolases such as URH1 from Saccharomyces cerevisiae, RihA and RihB from Escherichia coli. Nucleoside hydrolases are of interest as a target for antiprotozoan drugs as, no nucleoside hydrolase activity or genes encoding these enzymes have been detected in humans and, parasitic protozoans lack de novo purine synthesis relying on nucleoside hydrolase to scavenge purine and/or pyrimidines from the environment.


Pssm-ID: 238257 [Multi-domain]  Cd Length: 295  Bit Score: 153.25  E-value: 5.40e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   12 VVFDCDIGTDDAWALALLLRGEQLslasgrryKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPivtrtw 91
Cdd:cd00455   1 VILDTDPGIDDAFALMYALLHPEI--------ELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRP------ 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   92 LDISRFHGTDGLNDIGGYPDVSDLQEQLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYgDDFLDKIGGIFIM 171
Cdd:cd00455  67 LTGEIPAAYPEIHGEGGLGLPIPPIIEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILD-PDIKDRVKEIVIM 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  172 GGNIYGRGNIMKCAEFNFMMDPEAAHTTLERLKvPAVILPwepsidddfnlsLDWRLDVLgsVDHPLVELLSRVERSMLV 251
Cdd:cd00455 146 GGAFLVPGNVTPVAEANFYGDPEAANIVFNSAK-NLTIVP------------LDVTNQAV--LTPPMVERIFEQGTSIGL 210

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7297954  252 P--------------RDIKHWINPDAALAAAYIFPkaMIAEQLDYHATVELAGVhTRGQMVLD 300
Cdd:cd00455 211 LikpmidyyykayqkPGIEGSPIHDPLAVAYLLNP--SMFDYSKVPVDVDTDGL-TRGQTIAD 270
nuc_hydro_CaPnhB cd02650
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ...
 12-196 1.82e-36

NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes Purine/pyrimidine nucleoside hydrolase (pnhB). Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity.


Pssm-ID: 239116 [Multi-domain]  Cd Length: 304  Bit Score: 133.94  E-value: 1.82e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   12 VVFDCDIGTDDAWALALLLRGeqlslasgRRYKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPIVTRTw 91
Cdd:cd02650   2 LILDTDPGIDDAMALAYALAH--------PDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPP- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   92 LDISRF-HGTDGLNDIGGYPDVSdlqeQLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLygD-DFLDKIGGIF 169
Cdd:cd02650  73 FRIATFvHGDNGLGDVELPAPPR----QPEDESAADFLIELANEYPGELTLVAVGPLTNLALALAR--DpDFAKLVKQVV 146

                       170       180
                ....*....|....*....|....*..
gi 7297954  170 IMGGNIYGRGNIMKCAEFNFMMDPEAA 196
Cdd:cd02650 147 VMGGAFTVPGNVTPAAEANIHGDPEAA 173
PRK10768 PRK10768
ribonucleoside hydrolase RihC; Provisional
 12-197 8.32e-33

ribonucleoside hydrolase RihC; Provisional


Pssm-ID: 182713 [Multi-domain]  Cd Length: 304  Bit Score: 123.87  E-value: 8.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    12 VVFDCDIGTDDAWALALLLRGEQLSLasgrryKLIaiTCVQGNTDVVNGAQNALKILRLLERrDVPVFRGCANPIVtRTW 91
Cdd:PRK10768   5 IILDTDPGIDDAVAIAAALFAPELDL------KLI--TTVAGNVSVEKTTRNALKLLHFFNS-DVPVAQGAAKPLV-RPL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    92 LDISRFHGTDGLndiGGYpDVSDLQEQLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYGDDfLDKIGGIFIM 171
Cdd:PRK10768  75 RDAASVHGESGM---EGY-DFPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEV-KPYIKRIVLM 149

                        170       180
                 ....*....|....*....|....*.
gi 7297954   172 GGNIyGRGNIMKCAEFNFMMDPEAAH 197
Cdd:PRK10768 150 GGSA-GRGNVTPNAEFNIAVDPEAAA 174
nuc_hydro_3 cd02653
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 12-324 7.34e-31

NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity.


Pssm-ID: 239119 [Multi-domain]  Cd Length: 320  Bit Score: 119.02  E-value: 7.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   12 VVFDCDIGTDDAWALALLLRGEQLslasgrryKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPiVTRTW 91
Cdd:cd02653   2 VIIDCDPGIDDALALLYLLASPDL--------DVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKP-LAGPL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   92 LDISRFHGTDGLndigGYPDVSDLQEQLQQEHAVNAMYRLVCQYPkQVDFLLCGPLTNFASCINLyGDDFLDKIGGIFIM 171
Cdd:cd02653  73 TTAQDTHGPDGL----GYAELPASTRTLSDESAAQAWVDLARAHP-DLIGLATGPLTNLALALRE-EPELPRLLRRLVIM 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  172 GGNIYGRGNIMKCAEFNFMMDPEAAHTTLERLK---VPAVILPwepsidddfnlsldwrLDVLGSVD-HP-LVELLSRVE 246
Cdd:cd02653 147 GGAFNSRGNTSPVAEWNYWVDPEAAKEVLAAFGghpVRPTICG----------------LDVTRAVVlTPnLLERLARAK 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  247 RSML-VPRDIK------HW---------INpDAALAAAYIFPKamIAEQLDYHATVELAGVhTRGQMVLDHLrGRRvdai 310
Cdd:cd02653 211 DSVGaFIEDALrfyfefHWayghgygavIH-DPLAAAVALNPN--LARGRPAYVDVECTGV-LTGQTVVDWA-GFW---- 281

                       330
                ....*....|....
gi 7297954  311 hGKKSNVRIITHLN 324
Cdd:cd02653 282 -GKGANAEILTKVD 294
rihA PRK10443
ribonucleoside hydrolase 1; Provisional
 10-328 1.86e-24

ribonucleoside hydrolase 1; Provisional


Pssm-ID: 182465 [Multi-domain]  Cd Length: 311  Bit Score: 101.67  E-value: 1.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    10 RLVVFDCDIGTDDAWALALLLRGEQLslasgrryKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPIVtR 89
Cdd:PRK10443   3 LPIILDCDPGHDDAIALVLALASPEL--------DVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLM-R 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    90 TWLDISRFHGTDGLNDiggyPDVSDLQEQLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYGdDFLDKIGGIF 169
Cdd:PRK10443  74 ELIIADNVHGESGLDG----PALPEPTFAPQNCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHP-ELHSKIARIV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   170 IMGGNIyGRGNIMKCAEFNFMMDPEAAHTTLERlKVPAVILPWEPS-----IDDDFNlsldwRLDVLG-SVDHPLVELLS 243
Cdd:PRK10443 149 IMGGAM-GLGNWTPAAEFNIYVDPEAAEIVFQS-GIPIVMAGLDVThkaqiMDEDIE-----RIRAIGnPVATIVAELLD 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   244 RVERSMLVPRdikhWINPDAAL----AAAYIFPKAMIAEQlDYHATVELAGVHTRGQMVLDHLrgrrvdAIHGKKSNVRI 319
Cdd:PRK10443 222 FFMEYHKDEK----WGFVGAPLhdpcTIAWLLKPELFTTV-ERWVGVETQGEYTQGMTVVDYY------QLTGNKPNATV 290


                 ....*....
gi 7297954   320 ITHLNREPF 328
Cdd:PRK10443 291 LVDVDRQGF 299
PLN02717 PLN02717
uridine nucleosidase
 10-196 5.96e-24

uridine nucleosidase


Pssm-ID: 178319 [Multi-domain]  Cd Length: 316  Bit Score: 100.07  E-value: 5.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    10 RLVVFDCDIGTDDAWALALLLRGEQLslasgrryKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPIVTR 89
Cdd:PLN02717   1 KKLIIDTDPGIDDAMAILMALRSPEV--------EVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    90 TWLDISRF-HGTDGLNDIGGYPDVSDLQEQLQQEHAVnamyRLVCQYPKQVDFLLCGPLTNFASCINLyGDDFLDKIGGI 168
Cdd:PLN02717  73 TKPRIADFvHGSDGLGNTNLPPPKGKKIEKSAAEFLV----EKVSEYPGEVTVVALGPLTNLALAIKL-DPSFAKKVGQI 147

                        170       180
                 ....*....|....*....|....*...
gi 7297954   169 FIMGGNIYGRGNIMKCAEFNFMMDPEAA 196
Cdd:PLN02717 148 VVLGGAFFVNGNVNPAAEANIFGDPEAA 175
nuc_hydro_CjNH cd02654
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ...
 12-200 4.90e-22

nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. This group contains eukaryotic and bacterial proteins similar to C. jejuni nucleoside hydrolase. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. C. jejuni nucleoside hydrolase is inactive against natural nucleosides or against common nucleoside analogues.


Pssm-ID: 239120 [Multi-domain]  Cd Length: 318  Bit Score: 94.93  E-value: 4.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   12 VVFDCDIG----TDDAWALALLLRGEQLslasgrryKLIAITCVQGNTDVVNGAQNALKILRLLERRDVPVFRGCANPIV 87
Cdd:cd02654   2 VILDNDIAmgrdTDDGLALALLLWSPEV--------ELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANTPLG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   88 T--RTWLDISRFHGTDGLNDIGGyPDVSDLQEQLQ-----QEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYgDD 160
Cdd:cd02654  74 RtnRAFHAWESLYGAYLWQGAWS-PEYSDMYTNASiirnaSIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRID-PD 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 7297954  161 FLDKIGGIFIMGGNIYGRG---NIMKCAEFNFMMDPEAAHTTL 200
Cdd:cd02654 152 FAPLAKELVIMGGYLDDIGefvNRHYASDFNLIMDPEAASIVL 194
rihB PRK09955
ribosylpyrimidine nucleosidase;
9-210 4.38e-21

ribosylpyrimidine nucleosidase;


Pssm-ID: 182166 [Multi-domain]  Cd Length: 313  Bit Score: 92.32  E-value: 4.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954     9 ERLVVFDCDIGTDDAWALALLLRGEQLSLasgrryklIAITCVQGNTDVVNGAQNALKILRLLERrDVPVFRGCANPIVt 88
Cdd:PRK09955   3 KRKIILDCDPGHDDAIAMMMAAKHPAIDL--------LGITIVAGNQTLDKTLINGLNVCQKLEI-NVPVYAGMPQPIM- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    89 RTWLDISRFHGTDGLNDiggyPDVSDLQEQLQQEHAVNAMYRLVCQYPKQVDFLLCGPLTNFASCINLYgDDFLDKIGGI 168
Cdd:PRK09955  73 RQQIVADNIHGETGLDG----PVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQ-PAILPKIREI 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 7297954   169 FIMGGnIYGRGNIMKCAEFNFMMDPEAAHTTLeRLKVPAVIL 210
Cdd:PRK09955 148 VLMGG-AYGTGNFTPSAEFNIFADPEAARVVF-TSGVPLVMM 187
nuc_hydro_1 cd02648
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ...
 12-313 2.83e-19

NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity.


Pssm-ID: 239114 [Multi-domain]  Cd Length: 367  Bit Score: 87.63  E-value: 2.83e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   12 VVFDCDIGTDDAwaLALLLrgeqlSLASGRRYKLIAITCVQGNTDVVNGAQNALKILRLLERRDV---------PVF-RG 81
Cdd:cd02648   4 IIIDTDPGVDDV--LAILL-----ALSSPEEVDVALISLTFGNTTLDHALRNVLRLFHVLERERAwratpgvryRAFsAD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   82 CANPIVT--------RTWLDISRFHGTDGLNDIG-GYPDVSDLQEQLQQEH---------AVNAMYRLVCQYPKQ-VDFL 142
Cdd:cd02648  77 AEKPIVAsgsdqpleGERLTASYFHGRDGLSGVHwLHPDFTPVETWIPEIVapltpsdkpAYDVILDILREEPDHtVTIA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  143 LCGPLTNFASCINLYGDDFLdKIGGIFIMGGNIYGRGNIMKCAEFNFMMDPEAA---------HTTLERLKVPAVILPWE 213
Cdd:cd02648 157 ALGPLTNLAAAARKDPETFA-KVGEVVVMGGAIDVPGNTSPVAEFNCFADPYAAavvideppsTAPEARRKLPLQVFPLD 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954  214 psIDDDFNLSldwrldvLGSVDHPLVELLSRVERSMLVPRDIKHW----------------INPDAA--------LAAAY 269
Cdd:cd02648 236 --ITTGHTLP-------YSSLFATYVTPRDAPERGSPLARWLEHVfistflthpraftpeeFLPDRSelfemhdpLAVWY 306

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 7297954  270 IFPKAMIAEQLDYHA---------TVELAGVHTRGQMVLDHlrgRRVDAIHGK 313
Cdd:cd02648 307 AIFADMPATGSIDGNgwkhtprdfRVETSGQWTRGMCVVDR---RGVDEVTGT 356
nuc_hydro_TvIAG cd02647
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ...
 10-202 3.69e-16

nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring nucleoside hydrolase from Trypanosoma vivax. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. Nucleoside hydrolases vary in their substrate specificity. This group contains eukaryotic and bacterial proteins similar to the purine specific inosine-adenosine-guanosine-preferring nucleoside hydrolase (IAG-NH) from T. vivax. T. vivax IAG-NH is of the order of a thousand to ten thousand fold more specific towards the naturally occurring purine nucleosides, than towards the pyrimidine nucleosides.


Pssm-ID: 239113 [Multi-domain]  Cd Length: 312  Bit Score: 78.23  E-value: 3.69e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   10 RLVVFDCDIGTDDAWALALLLRGEQLslasgrryKLIAITCVQGNTD--VVNGAQNALKILRLLERRD-VPVFRGCANPI 86
Cdd:cd02647   1 KNVIFDHDGNVDDLVALLLLLKNEKV--------DLKGIGVSGIDADcyVEPAVSVTRKLIDRLGQRDaIPVGKGGSRAV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   87 VT--RTWLDISRFHGTDGLNDIGGYPDVSDLQEQLQQEHAVNamyrLVCQYPKQVDFLLCGPLTNFASCINLYgDDFLDK 164
Cdd:cd02647  73 NPfpRSWRRDAAFSVDHLPILNERYTVETPLAEETAQLVLIE----KIKASLEPVTLLVTGPLTNLARALDSD-PDISSN 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 7297954  165 IGGIFIMGGNIYGRGNIMK-----CAEFNFMMDPEAAHTTLER 202
Cdd:cd02647 148 IEEVYIMGGGVDAPGNVFTppsngTAEFNIFWDPLAAKTVFDS 190
PTZ00313 PTZ00313
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
 12-201 2.60e-12

inosine-adenosine-guanosine-nucleoside hydrolase; Provisional


Pssm-ID: 140334 [Multi-domain]  Cd Length: 326  Bit Score: 66.81  E-value: 2.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    12 VVFDCDIGTDDAWALALLLrgeqlslASGRRYKLIAITCVQGNTDVVNGAQNALKILRLLERRD-VPVFrgcanPIVTRT 90
Cdd:PTZ00313   5 VILDHDGNHDDLVALALLL-------GNPEKVKVIGCICTDADCFVDDAFNVTGKLMCMMHAREaTPLF-----PIGKSS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954    91 WLDISRFH-----GTDGLNDIG--GYPDVSDLQEQLQQEHAV----NAMYRLVCQYPKQVDFLLCGPLTNFASCINLYGD 159
Cdd:PTZ00313  73 FKGVNPFPsewrwSAKNMDDLPclNIPEHVAIWEKLKPENEAlvgeELLADLVMSSPEKVTICVTGPLSNVAWCIEKYGE 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 7297954   160 DFLDKIGGIFIMGGNIYGRGNIM-----KCAEFNFMMDPEAAHTTLE 201
Cdd:PTZ00313 153 EFTKKVEECVIMGGAVDVGGNVFlpgtdGSAEWNIYWDPPAAKTVLM 199
nuc_hydro_2 cd02652
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 12-215 3.32e-06

NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity.


Pssm-ID: 239118 [Multi-domain]  Cd Length: 293  Bit Score: 48.27  E-value: 3.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   12 VVFDCDIGTD--DAWALALLLRGEQLSLASgrryklIAITCVQGNTDVVNGAQNalkilRLLERRDVPVfrGCANPIVTR 89
Cdd:cd02652   1 LILDTDIGGDpdDALALALAHALQKCDLLA------VTITLADASARRAIDAVN-----RFYGRGDIPI--GADYHGWPE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7297954   90 TWLDISRFhgtdGLNDIGGYPDVSDLQEQLqqeHAVNAMYRLVCQYPKQ-VDFLLCGPLTNFASCINLYGDDFL------ 162
Cdd:cd02652  68 DAKDHAKF----LLEGDRLHHDLESAEDAL---DAVKALRRLLASAEDAsVTIVSIGPLTNLAALLDADADPLTgpelvr 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 7297954  163 DKIGGIFIMGGNIYGRGNIMKCAEFNFMMDPEAAHTTLERLKVPAVILPWEPS 215
Cdd:cd02652 141 QKVKRLVVMGGAFYDPDGNVQHREYNFVTDPKAAQRVAGRAQHLGIPVRIVWS 193
 
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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