NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|510996702|ref|WP_016264561|]
View 

nucleoside hydrolase [Latilactobacillus sakei]

Protein Classification

nucleoside hydrolase( domain architecture ID 10119099)

nucleoside hydrolase similar to Saccharomyces cerevisiae uridine nucleosidase and Leishmania major inosine-uridine preferring nucleoside hydrolase, which catalyzes the hydrolysis of purine and pyrimidine nucleosides into ribose and the associated base, with preference for inosine and uridine as substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
 4-307 7.05e-157

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: 440.06  E-value: 7.05e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   4 KIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIKVAADIHG 83
Cdd:cd02651    1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLITASDIHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  84 ESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPAkTITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEANASAV 163
Cdd:cd02651   81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPE-PITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 164 AEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQnFDAPPVHDPC 243
Cdd:cd02651  160 AEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAETYGSAF-TEGPPLHDPC 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996702 244 AVAYVIDPTVMTTKKVPVDIELNGTLTRGMTVADFSYPIPEDCQTSVAVKLDHAKFWGLVEDAL 307
Cdd:cd02651  239 AVAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
 
Name Accession Description Interval E-value
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
 4-307 7.05e-157

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: 440.06  E-value: 7.05e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   4 KIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIKVAADIHG 83
Cdd:cd02651    1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLITASDIHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  84 ESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPAkTITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEANASAV 163
Cdd:cd02651   81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPE-PITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 164 AEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQnFDAPPVHDPC 243
Cdd:cd02651  160 AEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAETYGSAF-TEGPPLHDPC 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996702 244 AVAYVIDPTVMTTKKVPVDIELNGTLTRGMTVADFSYPIPEDCQTSVAVKLDHAKFWGLVEDAL 307
Cdd:cd02651  239 AVAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 1-309 3.95e-150

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: 423.41  E-value: 3.95e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   1 MTKKIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIKVAAD 80
Cdd:COG1957    1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTAEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  81 IHGESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPaKTITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEA-N 159
Cdd:COG1957   81 VHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAP-GEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPgN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 160 ASAVAEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQNFDAPPV 239
Cdd:COG1957  160 VTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCPL 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 240 HDPCAVAYVIDPTVMTTKKVPVDIELNGTLTRGMTVADFSYPIPEDCQTSVAVKLDHAKFWGLVEDALRT 309
Cdd:COG1957  240 HDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLAR 309
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
5-300 3.82e-103

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 302.21  E-value: 3.82e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702    5 IILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGcsrplieeikvaadihge 84
Cdd:pfam01156   1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG------------------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   85 sgldgvvlpkptvelekihavdliiDLIMSHPakTITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEA-NASAV 163
Cdd:pfam01156  63 -------------------------EAIREPG--EVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRgNVTPA 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  164 AEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQNFDAPPVHDPC 243
Cdd:pfam01156 116 AEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDPL 195

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 510996702  244 AVAYVIDPTVMTTKKVPVDIELNGTLTRGMTVADFSYPIPEDCQTSVAVKLDHAKFW 300
Cdd:pfam01156 196 AVAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFW 252
rihA PRK10443
ribonucleoside hydrolase 1; Provisional
 1-308 9.91e-99

ribonucleoside hydrolase 1; Provisional


Pssm-ID: 182465 [Multi-domain]  Cd Length: 311  Bit Score: 293.11  E-value: 9.91e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   1 MTKKIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIKVAAD 80
Cdd:PRK10443   1 MALPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  81 IHGESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPAKtITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEANA 160
Cdd:PRK10443  81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEP-VTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMGLGNW 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 161 SAVAEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQ-NFDAPPV 239
Cdd:PRK10443 160 TPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFMEYHKDEKwGFVGAPL 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510996702 240 HDPCAVAYVIDPTVMTTKKVPVDIELNGTLTRGMTVADFSYPIPEDCQTSVAVKLDHAKFWGLVEDALR 308
Cdd:PRK10443 240 HDPCTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQLTGNKPNATVLVDVDRQGFVDLLAERLK 308
 
Name Accession Description Interval E-value
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
 4-307 7.05e-157

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: 440.06  E-value: 7.05e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   4 KIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIKVAADIHG 83
Cdd:cd02651    1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLITASDIHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  84 ESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPAkTITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEANASAV 163
Cdd:cd02651   81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPE-PITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 164 AEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQnFDAPPVHDPC 243
Cdd:cd02651  160 AEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAETYGSAF-TEGPPLHDPC 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996702 244 AVAYVIDPTVMTTKKVPVDIELNGTLTRGMTVADFSYPIPEDCQTSVAVKLDHAKFWGLVEDAL 307
Cdd:cd02651  239 AVAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 1-309 3.95e-150

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: 423.41  E-value: 3.95e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   1 MTKKIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIKVAAD 80
Cdd:COG1957    1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTAEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  81 IHGESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPaKTITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEA-N 159
Cdd:COG1957   81 VHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAP-GEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPgN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 160 ASAVAEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQNFDAPPV 239
Cdd:COG1957  160 VTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCPL 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 240 HDPCAVAYVIDPTVMTTKKVPVDIELNGTLTRGMTVADFSYPIPEDCQTSVAVKLDHAKFWGLVEDALRT 309
Cdd:COG1957  240 HDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLAR 309
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 5-303 3.07e-103

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: 303.87  E-value: 3.07e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   5 IILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIKVAADIHGE 84
Cdd:cd00455    1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  85 SGLDGVVlPKPTVELEKIHAVDLIIDLIMSHPaKTITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGY-HEANASAV 163
Cdd:cd00455   81 EGGLGLP-IPPIIEADDPEAVQLLIDLIRKYP-DEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFlVPGNVTPV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 164 AEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQNfDAPPVHDPC 243
Cdd:cd00455  159 AEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGLLIKPMIDYYYKAYQKPGI-EGSPIHDPL 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 244 AVAYVIDPTVMTTKKVPVDIELNGtLTRGMTVADFsYPIPEDCQTSVAVKLDHAKFWGLV 303
Cdd:cd00455  238 AVAYLLNPSMFDYSKVPVDVDTDG-LTRGQTIADF-RENPGNGVTRVAVNLDYPDFIELI 295
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
5-300 3.82e-103

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 302.21  E-value: 3.82e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702    5 IILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGcsrplieeikvaadihge 84
Cdd:pfam01156   1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG------------------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   85 sgldgvvlpkptvelekihavdliiDLIMSHPakTITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEA-NASAV 163
Cdd:pfam01156  63 -------------------------EAIREPG--EVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRgNVTPA 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  164 AEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQNFDAPPVHDPC 243
Cdd:pfam01156 116 AEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDPL 195

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 510996702  244 AVAYVIDPTVMTTKKVPVDIELNGTLTRGMTVADFSYPIPEDCQTSVAVKLDHAKFW 300
Cdd:pfam01156 196 AVAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFW 252
rihA PRK10443
ribonucleoside hydrolase 1; Provisional
 1-308 9.91e-99

ribonucleoside hydrolase 1; Provisional


Pssm-ID: 182465 [Multi-domain]  Cd Length: 311  Bit Score: 293.11  E-value: 9.91e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   1 MTKKIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIKVAAD 80
Cdd:PRK10443   1 MALPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  81 IHGESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPAKtITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEANA 160
Cdd:PRK10443  81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEP-VTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMGLGNW 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 161 SAVAEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQ-NFDAPPV 239
Cdd:PRK10443 160 TPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFMEYHKDEKwGFVGAPL 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510996702 240 HDPCAVAYVIDPTVMTTKKVPVDIELNGTLTRGMTVADFSYPIPEDCQTSVAVKLDHAKFWGLVEDALR 308
Cdd:PRK10443 240 HDPCTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQLTGNKPNATVLVDVDRQGFVDLLAERLK 308
rihB PRK09955
ribosylpyrimidine nucleosidase;
3-308 9.70e-93

ribosylpyrimidine nucleosidase;


Pssm-ID: 182166 [Multi-domain]  Cd Length: 313  Bit Score: 277.98  E-value: 9.70e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   3 KKIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMhDVPIAAGCSRPLIEEIKVAADIH 82
Cdd:PRK09955   4 RKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEI-NVPVYAGMPQPIMRQQIVADNIH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  83 GESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPAKtITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEANASA 162
Cdd:PRK09955  83 GETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGD-ITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 163 VAEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQNFDAPPVHDP 242
Cdd:PRK09955 162 SAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHDA 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996702 243 CAVAYVIDPTVMTTKKVPVDIELNGTLTRGMTVADFSYPIPEDCQTSVAVKLDHAKFWGLVEDALR 308
Cdd:PRK09955 242 TCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVR 307
nuc_hydro_CaPnhB cd02650
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ...
 4-295 1.83e-92

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: 276.85  E-value: 1.83e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   4 KIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIK-VAADIH 82
Cdd:cd02650    1 KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPFrIATFVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  83 GESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPaKTITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGY-HEANAS 161
Cdd:cd02650   81 GDNGLGDVELPAPPRQPEDESAADFLIELANEYP-GELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFtVPGNVT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 162 AVAEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQNFDAPPVHD 241
Cdd:cd02650  160 PAAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSGGKAGQFLADMLDYYIDFYQESPGLRGCALHD 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 510996702 242 PCAVAYVIDPTVMTTKKVPVDIELNGtLTRGMTVADFSYPIPEDCQTSVAVKLD 295
Cdd:cd02650  240 PLAVAAAVDPSLFTTREGVVRVETEG-PTRGRTIGDRDGRRFWDSSPNATVAVD 292
PRK10768 PRK10768
ribonucleoside hydrolase RihC; Provisional
 1-308 5.08e-92

ribonucleoside hydrolase RihC; Provisional


Pssm-ID: 182713 [Multi-domain]  Cd Length: 304  Bit Score: 275.63  E-value: 5.08e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   1 MTKKIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGmHDVPIAAGCSRPLIEEIKVAAD 80
Cdd:PRK10768   1 MRLPIILDTDPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFN-SDVPVAQGAAKPLVRPLRDAAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  81 IHGESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPAKtITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEANA 160
Cdd:PRK10768  80 VHGESGMEGYDFPEHTRKPLSIPAVEAMRDALMNAPEP-VTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSAGRGNV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 161 SAVAEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHtETSAFvvdLLAFFRDmYKKGQNFDAPPVH 240
Cdd:PRK10768 159 TPNAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPELN-RTGKM---LHALFSH-YRSGSMQTGLRMH 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 241 DPCAVAYVIDPTVMTTKKVPVDIELNGTLTRGMTVADF--SYPIPEDCQtsVAVKLDHAKFWGLVEDALR 308
Cdd:PRK10768 234 DVCAIAYLLRPELFTLKPCFVDVETQGEFTAGATVVDIdgRLGKPANAQ--VALDIDVDGFQKWFAEVLA 301
nuc_hydro_CeIAG cd02649
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ...
 3-277 1.13e-72

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: 226.37  E-value: 1.13e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   3 KKIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIKVAADIH 82
Cdd:cd02649    1 RKLIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGPGPTAAYFH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  83 GESGLDGVVLP--KPTVELEKIHAVDLIIDLIMSHPAKtITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYH-EAN 159
Cdd:cd02649   81 GKDGFGDVGFPepKDELELQKEHAVDAIIRLVREYPGE-ITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREgVGN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 160 ASAVAEFNIKFDPEAAKIVFNA-GWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQNFDAPP 238
Cdd:cd02649  160 TTPAAEFNFHVDPEAAHIVLNSfGCPITIVPWETTLLAFPLDWEFEDKWANRLEKALFAESLNRREYAFASEGLGGDGWV 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 510996702 239 VHDPCAVAYVIDPTVMT-TKKVPVDIELNGTLTRGMTVAD 277
Cdd:cd02649  240 PCDALAVAAALDPSIITrRLTYAVDVELHGELTRGQMVVD 279
nuc_hydro_3 cd02653
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 4-279 5.19e-66

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: 209.92  E-value: 5.19e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   4 KIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIKVAADIHG 83
Cdd:cd02653    1 KVIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKPLAGPLTTAQDTHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  84 ESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPaKTITLVpTGALTNIAMAARKEPKIIDRVKEVVLMGGGY-HEANASA 162
Cdd:cd02653   81 PDGLGYAELPASTRTLSDESAAQAWVDLARAHP-DLIGLA-TGPLTNLALALREEPELPRLLRRLVIMGGAFnSRGNTSP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 163 VAEFNIKFDPEAAKIVFNAGWQ----VTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMY-KKGQNFDAp 237
Cdd:cd02653  159 VAEWNYWVDPEAAKEVLAAFGGhpvrPTICGLDVTRAVVLTPNLLERLARAKDSVGAFIEDALRFYFEFHwAYGHGYGA- 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 510996702 238 PVHDPCAVAYVIDPTVMTTKKVPVDIELNGTLTrGMTVADFS 279
Cdd:cd02653  238 VIHDPLAAAVALNPNLARGRPAYVDVECTGVLT-GQTVVDWA 278
PLN02717 PLN02717
uridine nucleosidase
 3-277 4.54e-63

uridine nucleosidase


Pssm-ID: 178319 [Multi-domain]  Cd Length: 316  Bit Score: 202.14  E-value: 4.54e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   3 KKIILDCDPGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEEIK--VAAD 80
Cdd:PLN02717   1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKprIADF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  81 IHGESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPAKtITLVPTGALTNIAMAARKEPKIIDRVKEVVLMGGGYHEA-N 159
Cdd:PLN02717  81 VHGSDGLGNTNLPPPKGKKIEKSAAEFLVEKVSEYPGE-VTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNgN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 160 ASAVAEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAFFRDMYKKGQNFDAPPV 239
Cdd:PLN02717 160 VNPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSKGKYAQFLCDICKFYRDWHRKSYGIDGIYL 239

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 510996702 240 HDPCAVAYVIDPTVMTTKKVPVDIELNGtLTRGMTVAD 277
Cdd:PLN02717 240 HDPTALLAAVRPSLFTYKEGVVRVETEG-ICRGLTLFD 276
nuc_hydro_1 cd02648
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ...
 4-277 4.00e-36

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: 133.09  E-value: 4.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   4 KIILDCDPGHDDAVAMMLAHGNP-EIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDV------------------PI- 63
Cdd:cd02648    3 PIIIDTDPGVDDVLAILLALSSPeEVDVALISLTFGNTTLDHALRNVLRLFHVLERERAwratpgvryrafsadaekPIv 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  64 AAGCSRPLIEEIKVAADIHGESGLDGV--VLPKPT---VELEKIH---------AVDLIIDLIMSHPAKTITLVPTGALT 129
Cdd:cd02648   83 ASGSDQPLEGERLTASYFHGRDGLSGVhwLHPDFTpveTWIPEIVapltpsdkpAYDVILDILREEPDHTVTIAALGPLT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 130 NIAMAARKEPKIIDRVKEVVLMGGGY-HEANASAVAEFNIKFDPEAAKIVFNAG----------WQVTMVGLDLThqala 198
Cdd:cd02648  163 NLAAAARKDPETFAKVGEVVVMGGAIdVPGNTSPVAEFNCFADPYAAAVVIDEPpstapearrkLPLQVFPLDIT----- 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 199 TPDIVSEIKAIHT-----------------ETSAFVVDLLAFFRDMYKKGQNFDAPPV---HDPCAVAYVIDPTVMTTKK 258
Cdd:cd02648  238 TGHTLPYSSLFATyvtprdapergsplarwLEHVFISTFLTHPRAFTPEEFLPDRSELfemHDPLAVWYAIFADMPATGS 317

                        330       340
                 ....*....|....*....|....*....
gi 510996702 259 VPVD----------IELNGTLTRGMTVAD 277
Cdd:cd02648  318 IDGNgwkhtprdfrVETSGQWTRGMCVVD 346
nuc_hydro_CjNH cd02654
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ...
 4-257 8.81e-35

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: 128.44  E-value: 8.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   4 KIILDCD----PGHDDAVAMMLAHGNPEIDLLAVTTVAANQTLTKVTRNALAVATMIGMHDVPIAAGCSRPLIEE---IK 76
Cdd:cd02654    1 KVILDNDiamgRDTDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANTPLGRTnraFH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  77 VAADIHGESGLDGVVLP--------KPTVELEKIHAVDLIIDLIMSHPaKTITLVPTGALTNIAMAARKEPKIIDRVKEV 148
Cdd:cd02654   81 AWESLYGAYLWQGAWSPeysdmytnASIIRNASIPAALFMIEMVRKHP-HEVSIVAAGPLTNLALALRIDPDFAPLAKEL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 149 VLMGGGYHEA----NASAVAEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPdivsEIKAIHTETSAFVVDLLAFF 224
Cdd:cd02654  160 VIMGGYLDDIgefvNRHYASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTP----EQIKADDPLRDFIRETLDLP 235

                        250       260       270
                 ....*....|....*....|....*....|....
gi 510996702 225 RDMYKKGQ-NFDAPPVHDPCAVAYVIDPTVMTTK 257
Cdd:cd02654  236 IDYAKEFVgTGDGLPMWDELASAVALDPELATSS 269
nuc_hydro_TvIAG cd02647
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ...
 3-277 1.51e-31

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: 119.83  E-value: 1.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   3 KKIILDCDPGHDDAVAMMLAHGNPEIDLLAVT----------TVAANQTLTKVTRnalavatMIGMHDVPIAAGCSRPLI 72
Cdd:cd02647    1 KNVIFDHDGNVDDLVALLLLLKNEKVDLKGIGvsgidadcyvEPAVSVTRKLIDR-------LGQRDAIPVGKGGSRAVN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  73 ---EEIKVAADIHGESGLDGVVLPKPTVELEKIHAVDLIIDLIMSHPAKtITLVPTGALTNIAMAARKEPKIIDRVKEVV 149
Cdd:cd02647   74 pfpRSWRRDAAFSVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEP-VTLLVTGPLTNLARALDSDPDISSNIEEVY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 150 LMGGGYH------EANASAVAEFNIKFDPEAAKIVFNAGWQVTMVGLDLTHQALATPDIVSEIKAIHTETSAFVVDLLAF 223
Cdd:cd02647  153 IMGGGVDapgnvfTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFLETDRQRFAAQRLPASDLAGQ 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 510996702 224 FRDMYKKGQNFDAPPVHDPCAVAYVIDPTVMTTKKVPV-DIELNGtLTRGMTVAD 277
Cdd:cd02647  233 GYALVKPLEFNSTYYMWDVLTTLVLGAKEVDNTKESLIlEVDTDG-LSAGQTVTS 286
nuc_hydro_2 cd02652
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 5-179 9.11e-12

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: 64.44  E-value: 9.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   5 IILDCDPGHD--DAVAMMLAHGNPEIDLLAVTTVAANQTltkVTRNALAVATMIGMHDVPIAAGCSRPLIEEIKVAADIH 82
Cdd:cd02652    1 LILDTDIGGDpdDALALALAHALQKCDLLAVTITLADAS---ARRAIDAVNRFYGRGDIPIGADYHGWPEDAKDHAKFLL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  83 GESGLDGVVLPKPTVElekiHAVDLIIDLIMSHPAKTITLVPTGALTNIAMAARKEPKIID-------RVKEVVLMGGGY 155
Cdd:cd02652   78 EGDRLHHDLESAEDAL----DAVKALRRLLASAEDASVTIVSIGPLTNLAALLDADADPLTgpelvrqKVKRLVVMGGAF 153

                        170       180
                 ....*....|....*....|....*
gi 510996702 156 HEANASAVA-EFNIKFDPEAAKIVF 179
Cdd:cd02652  154 YDPDGNVQHrEYNFVTDPKAAQRVA 178
PTZ00313 PTZ00313
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
 1-274 8.14e-11

inosine-adenosine-guanosine-nucleoside hydrolase; Provisional


Pssm-ID: 140334 [Multi-domain]  Cd Length: 326  Bit Score: 61.80  E-value: 8.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702   1 MTKKIILDCDPGHDDAVAMMLAHGNPE-IDLLAVTTVAANQtltkVTRNALAVA--TMIGMHDV------PIAAGCSR-- 69
Cdd:PTZ00313   1 MPKPVILDHDGNHDDLVALALLLGNPEkVKVIGCICTDADC----FVDDAFNVTgkLMCMMHAReatplfPIGKSSFKgv 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702  70 -PLIEEIKVAADihGESGLDGVVLPKPTV-------ELEKIHAVDLIIDLIMSHPAKtITLVPTGALTNIAMAARKE-PK 140
Cdd:PTZ00313  77 nPFPSEWRWSAK--NMDDLPCLNIPEHVAiweklkpENEALVGEELLADLVMSSPEK-VTICVTGPLSNVAWCIEKYgEE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996702 141 IIDRVKEVVLMGGGYHEA------NASAVAEFNIKFDPEAAKIVFNA-GWQVTMVGLDLTHQALATPDIVSEIKAIHTET 213
Cdd:PTZ00313 154 FTKKVEECVIMGGAVDVGgnvflpGTDGSAEWNIYWDPPAAKTVLMCpHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYL 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996702 214 -SAFVVDLLAF--FRDMYKKGQNFDAppvHDPCAVAYVIDPTVMTTKKVPVDIELNGTLTRGMT 274
Cdd:PTZ00313 234 lSQFVGSTWAMctHHELLRPGDGYYA---WDVLTAAYVIERNLAELEPVPLEVVVEKAKNEGRT 294
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH