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Conserved domains on  [gi|502626321|ref|WP_012863042|]
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nucleoside hydrolase [Sebaldella termitidis]

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

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List of domain hits

 Name Accession Description Interval E-value
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
 3-304 5.60e-159

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: 445.45  E-value: 5.60e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   3 KIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGI-DVPVYKGMPGPMVREQVIADDIHG 81
Cdd:cd02651    1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRtDVPVAAGAARPLVRPLITASDIHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  82 ETGLDGPDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQLGNSTPAA 161
Cdd:cd02651   81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 162 EFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDVFgWSAPPVHDPTT 241
Cdd:cd02651  161 EFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAETYGSAF-TEGPPLHDPCA 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502626321 242 VAYLIDPSCIETKPMYCKIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWNIVYETL 304
Cdd:cd02651  240 VAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
 
Name Accession Description Interval E-value
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
 3-304 5.60e-159

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: 445.45  E-value: 5.60e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   3 KIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGI-DVPVYKGMPGPMVREQVIADDIHG 81
Cdd:cd02651    1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRtDVPVAAGAARPLVRPLITASDIHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  82 ETGLDGPDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQLGNSTPAA 161
Cdd:cd02651   81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 162 EFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDVFgWSAPPVHDPTT 241
Cdd:cd02651  161 EFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAETYGSAF-TEGPPLHDPCA 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502626321 242 VAYLIDPSCIETKPMYCKIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWNIVYETL 304
Cdd:cd02651  240 VAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 1-307 1.41e-155

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: 436.89  E-value: 1.41e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   1 MKKIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGI-DVPVYKGMPGPMVREQVIADDI 79
Cdd:COG1957    2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRtDVPVAAGAARPLVRPLVTAEHV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  80 HGETGLDGPDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQ-LGNST 158
Cdd:COG1957   82 HGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFvPGNVT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 159 PAAEFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDVFGWSAPPVHD 238
Cdd:COG1957  162 PVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCPLHD 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502626321 239 PTTVAYLIDPSCIETKPMYCKIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWNIVYETLKLY 307
Cdd:COG1957  242 PLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLARL 310
rihB PRK09955
ribosylpyrimidine nucleosidase;
2-307 3.30e-148

ribosylpyrimidine nucleosidase;


Pssm-ID: 182166 [Multi-domain]  Cd Length: 313  Bit Score: 418.58  E-value: 3.30e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   2 KKIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGIDVPVYKGMPGPMVREQVIADDIHG 81
Cdd:PRK09955   4 RKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRQQIVADNIHG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  82 ETGLDGPDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQLGNSTPAA 161
Cdd:PRK09955  84 ETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPSA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 162 EFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDVFGWSAPPVHDPTT 241
Cdd:PRK09955 164 EFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHDATC 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502626321 242 VAYLIDPSCIETKPMYCKIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWNIVYETLKLY 307
Cdd:PRK09955 244 IGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGY 309
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
4-298 6.20e-113

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 326.86  E-value: 6.20e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321    4 IILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGID-VPVYKGmpgpmvreqviaddihge 82
Cdd:pfam01156   1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDdIPVYAG------------------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   83 tgldgpdfgeitkkgetmhavdyiieKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQL-GNSTPAA 161
Cdd:pfam01156  63 --------------------------EAIREPGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVrGNVTPAA 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  162 EFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDVFGWSAPPVHDPTT 241
Cdd:pfam01156 117 EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDPLA 196

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 502626321  242 VAYLIDPSCIETKPMYCKIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWN 298
Cdd:pfam01156 197 VAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFWE 253
 
Name Accession Description Interval E-value
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
 3-304 5.60e-159

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: 445.45  E-value: 5.60e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   3 KIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGI-DVPVYKGMPGPMVREQVIADDIHG 81
Cdd:cd02651    1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRtDVPVAAGAARPLVRPLITASDIHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  82 ETGLDGPDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQLGNSTPAA 161
Cdd:cd02651   81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 162 EFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDVFgWSAPPVHDPTT 241
Cdd:cd02651  161 EFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAETYGSAF-TEGPPLHDPCA 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502626321 242 VAYLIDPSCIETKPMYCKIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWNIVYETL 304
Cdd:cd02651  240 VAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 1-307 1.41e-155

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: 436.89  E-value: 1.41e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   1 MKKIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGI-DVPVYKGMPGPMVREQVIADDI 79
Cdd:COG1957    2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRtDVPVAAGAARPLVRPLVTAEHV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  80 HGETGLDGPDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQ-LGNST 158
Cdd:COG1957   82 HGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFvPGNVT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 159 PAAEFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDVFGWSAPPVHD 238
Cdd:COG1957  162 PVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCPLHD 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502626321 239 PTTVAYLIDPSCIETKPMYCKIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWNIVYETLKLY 307
Cdd:COG1957  242 PLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLARL 310
rihB PRK09955
ribosylpyrimidine nucleosidase;
2-307 3.30e-148

ribosylpyrimidine nucleosidase;


Pssm-ID: 182166 [Multi-domain]  Cd Length: 313  Bit Score: 418.58  E-value: 3.30e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   2 KKIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGIDVPVYKGMPGPMVREQVIADDIHG 81
Cdd:PRK09955   4 RKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRQQIVADNIHG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  82 ETGLDGPDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQLGNSTPAA 161
Cdd:PRK09955  84 ETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPSA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 162 EFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDVFGWSAPPVHDPTT 241
Cdd:PRK09955 164 EFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHDATC 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502626321 242 VAYLIDPSCIETKPMYCKIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWNIVYETLKLY 307
Cdd:PRK09955 244 IGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGY 309
rihA PRK10443
ribonucleoside hydrolase 1; Provisional
 1-307 3.00e-113

ribonucleoside hydrolase 1; Provisional


Pssm-ID: 182465 [Multi-domain]  Cd Length: 311  Bit Score: 329.71  E-value: 3.00e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   1 MKKIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLG-IDVPVYKGMPGPMVREQVIADDI 79
Cdd:PRK10443   2 ALPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNrTDIPVAGGAVKPLMRELIIADNV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  80 HGETGLDGPDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQLGNSTP 159
Cdd:PRK10443  82 HGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMGLGNWTP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 160 AAEFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHD-VFGWSAPPVHD 238
Cdd:PRK10443 162 AAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFMEYHKDeKWGFVGAPLHD 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502626321 239 PTTVAYLIDPSCIETKPMYCKIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWNIVYETLKLY 307
Cdd:PRK10443 242 PCTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQLTGNKPNATVLVDVDRQGFVDLLAERLKFY 310
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
4-298 6.20e-113

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 326.86  E-value: 6.20e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321    4 IILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGID-VPVYKGmpgpmvreqviaddihge 82
Cdd:pfam01156   1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDdIPVYAG------------------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   83 tgldgpdfgeitkkgetmhavdyiieKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQL-GNSTPAA 161
Cdd:pfam01156  63 --------------------------EAIREPGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVrGNVTPAA 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  162 EFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDVFGWSAPPVHDPTT 241
Cdd:pfam01156 117 EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDPLA 196

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 502626321  242 VAYLIDPSCIETKPMYCKIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWN 298
Cdd:pfam01156 197 VAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFWE 253
PRK10768 PRK10768
ribonucleoside hydrolase RihC; Provisional
 1-306 1.05e-107

ribonucleoside hydrolase RihC; Provisional


Pssm-ID: 182713 [Multi-domain]  Cd Length: 304  Bit Score: 315.31  E-value: 1.05e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   1 MKKIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGIDVPVYKGMPGPMVREQVIADDIH 80
Cdd:PRK10768   2 RLPIILDTDPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFNSDVPVAQGAAKPLVRPLRDAASVH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  81 GETGLDGPDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQLGNSTPA 160
Cdd:PRK10768  82 GESGMEGYDFPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSAGRGNVTPN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 161 AEFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLnNKASKLFVDLMeffaktQHDVFGWSAP--PVHD 238
Cdd:PRK10768 162 AEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPEL-NRTGKMLHALF------SHYRSGSMQTglRMHD 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502626321 239 PTTVAYLIDPSCIETKPMYCKIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWNIVYETLKL 306
Cdd:PRK10768 235 VCAIAYLLRPELFTLKPCFVDVETQGEFTAGATVVDIDGRLGKPANAQVALDIDVDGFQKWFAEVLAL 302
nuc_hydro_CaPnhB cd02650
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ...
 3-292 1.25e-85

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: 259.13  E-value: 1.25e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   3 KIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGI-DVPVYKGMPGPMVREQV-IADDIH 80
Cdd:cd02650    1 KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRpDVPVAEGAAKPLTRPPFrIATFVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  81 GETGLDGPDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQ-LGNSTP 159
Cdd:cd02650   81 GDNGLGDVELPAPPRQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTvPGNVTP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 160 AAEFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDVFGWSAPPVHDP 239
Cdd:cd02650  161 AAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSGGKAGQFLADMLDYYIDFYQESPGLRGCALHDP 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502626321 240 TTVAYLIDPSCIETKPMYCKIELKSEdSYGRTLCD----YFGILKKEPNVDVAVKLD 292
Cdd:cd02650  241 LAVAAAVDPSLFTTREGVVRVETEGP-TRGRTIGDrdgrRFWDSSPNATVAVDVDVD 296
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 4-298 6.16e-84

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: 254.56  E-value: 6.16e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   4 IILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGI-DVPVYKGMPGPMVREQVIADDIHGE 82
Cdd:cd00455    1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRlDIPVYAGATRPLTGEIPAAYPEIHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  83 TGLDGPDFGEITKKGEtMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQ-LGNSTPAA 161
Cdd:cd00455   81 EGGLGLPIPPIIEADD-PEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLvPGNVTPVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 162 EFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKlFVDLMEFFAKTQHDVFGWSAPPVHDPTT 241
Cdd:cd00455  160 EANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGL-LIKPMIDYYYKAYQKPGIEGSPIHDPLA 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502626321 242 VAYLIDPSCIETKPMYCKIELkSEDSYGRTLCDyFGILKKEPNVDVAVKLDFDKFWN 298
Cdd:cd00455  239 VAYLLNPSMFDYSKVPVDVDT-DGLTRGQTIAD-FRENPGNGVTRVAVNLDYPDFIE 293
nuc_hydro_CeIAG cd02649
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ...
 2-301 5.09e-77

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: 237.16  E-value: 5.09e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   2 KKIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLG-IDVPVYKGMPGPMVREQVIADDIH 80
Cdd:cd02649    1 RKLIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGrRDIPVYRGASKPLLGPGPTAAYFH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  81 GETGLDGPDFGE--ITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQ-LGNS 157
Cdd:cd02649   81 GKDGFGDVGFPEpkDELELQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREgVGNT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 158 TPAAEFNIFADPEAAYVVF-SSGLPVVMMGLDLTRQA--LATKEVVDKIG--SLNNKASKLFVDLMEFFAKTQHDVfGWS 232
Cdd:cd02649  161 TPAAEFNFHVDPEAAHIVLnSFGCPITIVPWETTLLAfpLDWEFEDKWANrlEKALFAESLNRREYAFASEGLGGD-GWV 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 233 APpvhDPTTVAYLIDPSCIETKPMYC-KIELKSEDSYGRTLCDYFGILKKEPNVDVAVKLDFDKFWNIVY 301
Cdd:cd02649  240 PC---DALAVAAALDPSIITRRLTYAvDVELHGELTRGQMVVDWLGTLKKKPNARVITKIDREKFKELLY 306
PLN02717 PLN02717
uridine nucleosidase
 2-304 1.65e-63

uridine nucleosidase


Pssm-ID: 178319 [Multi-domain]  Cd Length: 316  Bit Score: 202.91  E-value: 1.65e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   2 KKIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLG-IDVPVYKGMPGPMVREQV--IADD 78
Cdd:PLN02717   1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGrPDVPVAEGSHEPLKGGTKprIADF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  79 IHGETGLDGPDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQ-LGNS 157
Cdd:PLN02717  81 VHGSDGLGNTNLPPPKGKKIEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFvNGNV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 158 TPAAEFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDVFGWSAPPVH 237
Cdd:PLN02717 161 NPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSKGKYAQFLCDICKFYRDWHRKSYGIDGIYLH 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502626321 238 DPTTVAYLIDPSCIETKPMYCKIElKSEDSYGRTLCDyfGILKK---------EPNVDVAVKLDFDKFWNIVYETL 304
Cdd:PLN02717 241 DPTALLAAVRPSLFTYKEGVVRVE-TEGICRGLTLFD--NGLKRwngenawtgRPPVKVAVTVDAPAVVELVKERL 313
nuc_hydro_3 cd02653
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 3-304 2.83e-62

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: 199.91  E-value: 2.83e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   3 KIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLG-IDVPVYKGMPGPMVREQVIADDIHG 81
Cdd:cd02653    1 KVIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGrTDIPVYLGADKPLAGPLTTAQDTHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  82 ETGLDGPDFGEITKKGETMHAVDYIIEkLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGGAYQL-GNSTPA 160
Cdd:cd02653   81 PDGLGYAELPASTRTLSDESAAQAWVD-LARAHPDLIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSrGNTSPV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 161 AEFNIFADPEAAYVVF--SSGLPV--VMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFFAKTQHDV-FGWSApP 235
Cdd:cd02653  160 AEWNYWVDPEAAKEVLaaFGGHPVrpTICGLDVTRAVVLTPNLLERLARAKDSVGAFIEDALRFYFEFHWAYgHGYGA-V 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502626321 236 VHDPTTVAYLIDPSCIETKPMYCKIELKSEDSyGRTLCDYFGILKKEPNVDVAVKLDFDKFWNIVYETL 304
Cdd:cd02653  239 IHDPLAAAVALNPNLARGRPAYVDVECTGVLT-GQTVVDWAGFWGKGANAEILTKVDSQDFMALFIERV 306
nuc_hydro_1 cd02648
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ...
 3-246 1.41e-34

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: 128.85  E-value: 1.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   3 KIILDVDPGHDDAVAIMLA-AFNPEIDLLGITVVAGNQTLEKTFNNALKVCS-------------------HLGIDVP-V 61
Cdd:cd02648    3 PIIIDTDPGVDDVLAILLAlSSPEEVDVALISLTFGNTTLDHALRNVLRLFHvlererawratpgvryrafSADAEKPiV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  62 YKGMPGPMVREQVIADDIHGETGLDG-----PDFGEITKKGETMH---------AVDYIIEKLLGS-DEKITLVPTGPLS 126
Cdd:cd02648   83 ASGSDQPLEGERLTASYFHGRDGLSGvhwlhPDFTPVETWIPEIVapltpsdkpAYDVILDILREEpDHTVTIAALGPLT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 127 NIGMALRKEPRIKEKIEQIVLMGGAYQL-GNSTPAAEFNIFADPEAAYVVFSSG----------LPVVMMGLDLT----- 190
Cdd:cd02648  163 NLAAAARKDPETFAKVGEVVVMGGAIDVpGNTSPVAEFNCFADPYAAAVVIDEPpstapearrkLPLQVFPLDITtghtl 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502626321 191 -RQALATKEVVDKIGSlnNKASKLFVDLMEFFAKT----------------QHDVFGwsappVHDPTTVAYLI 246
Cdd:cd02648  243 pYSSLFATYVTPRDAP--ERGSPLARWLEHVFISTflthpraftpeeflpdRSELFE-----MHDPLAVWYAI 308
nuc_hydro_TvIAG cd02647
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ...
 2-271 1.84e-33

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: 124.84  E-value: 1.84e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   2 KKIILDVDPGHDDAVAIMLAAFNPEIDLLGITVVAGNQ-TLEKTFNNA-LKVCSHLGI--DVPVYKG---MPGPMVRE-Q 73
Cdd:cd02647    1 KNVIFDHDGNVDDLVALLLLLKNEKVDLKGIGVSGIDAdCYVEPAVSVtRKLIDRLGQrdAIPVGKGgsrAVNPFPRSwR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  74 VIADDihgeTGLDGP---DFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQIVLMGG 150
Cdd:cd02647   81 RDAAF----SVDHLPilnERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 151 AYQL-GN-----STPAAEFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLM-EFFAK 223
Cdd:cd02647  157 GVDApGNvftppSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFLETDRQRFAAQRLPASDLAgQGYAL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 502626321 224 TQHDVFGwSAPPVHDPTTVAYLIDPSCIETKPMYCKIELKSEDSYGRT 271
Cdd:cd02647  237 VKPLEFN-STYYMWDVLTTLVLGAKEVDNTKESLILEVDTDGLSAGQT 283
nuc_hydro_CjNH cd02654
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ...
 3-298 8.27e-26

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: 104.17  E-value: 8.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   3 KIILDVD----PGHDDAVAIMLAAFNPEIDLLGITVVAGNQTLEKTFNNALKVCSHLGID-VPVYKGMPGPMVRE----- 72
Cdd:cd02654    1 KVILDNDiamgRDTDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADaIPVYAGANTPLGRTnrafh 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  73 -------QVIADDIHGETGLDGpDFGEITKKGETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKEPRIKEKIEQI 145
Cdd:cd02654   81 aweslygAYLWQGAWSPEYSDM-YTNASIIRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAKEL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 146 VLMGGAYQLG----NSTPAAEFNIFADPEAAYVVFSSGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLMEFF 221
Cdd:cd02654  160 VIMGGYLDDIgefvNRHYASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQIKADDPLRDFIRETLDLPIDYA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 222 AKTQHDVFGWsapPVHDPTTVAYLIDPSCIETKP-MYCKIELKSEDSYGRTLCDYFGILK--KEPNVDVAVKLDFDKFWN 298
Cdd:cd02654  240 KEFVGTGDGL---PMWDELASAVALDPELATSSEtFYIDVQTDSDGGGQLIWPEDLLLAKglRPYHVKVITAVDVAAFLN 316
PTZ00313 PTZ00313
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
 2-294 1.50e-17

inosine-adenosine-guanosine-nucleoside hydrolase; Provisional


Pssm-ID: 140334 [Multi-domain]  Cd Length: 326  Bit Score: 81.45  E-value: 1.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   2 KKIILDVDPGHDDAVAIMLAAFNPE-IDLLGITVVAGNQTLEKTFNNALKVCS--HLGIDVPVY-------KGM-PGPMv 70
Cdd:PTZ00313   3 KPVILDHDGNHDDLVALALLLGNPEkVKVIGCICTDADCFVDDAFNVTGKLMCmmHAREATPLFpigkssfKGVnPFPS- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  71 REQVIADDIHGETGLDGPDFGEITKK----GETMHAVDYIIEKLLGSDEKITLVPTGPLSNIGMALRKE-PRIKEKIEQI 145
Cdd:PTZ00313  82 EWRWSAKNMDDLPCLNIPEHVAIWEKlkpeNEALVGEELLADLVMSSPEKVTICVTGPLSNVAWCIEKYgEEFTKKVEEC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 146 VLMGGAYQLGNST------PAAEFNIFADPEAAYVVFS-SGLPVVMMGLDLTRQALATKEVVDKIGSLNNKASKLFVDLM 218
Cdd:PTZ00313 162 VIMGGAVDVGGNVflpgtdGSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVGST 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 219 eFFAKTQHDV-------FGWsappvhDPTTVAYLIDPSCIETKPMYCKIELKSEDSYGRTL-------CDYfgiLKKEPN 284
Cdd:PTZ00313 242 -WAMCTHHELlrpgdgyYAW------DVLTAAYVIERNLAELEPVPLEVVVEKAKNEGRTRraaegaaCTY---VAKNTN 311

                        330
                 ....*....|
gi 502626321 285 VDVAVKLDFD 294
Cdd:PTZ00313 312 AELFYDMVLD 321
nuc_hydro_2 cd02652
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 4-249 5.43e-11

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: 62.13  E-value: 5.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321   4 IILDVDPGHD--DAVAIMLAAFNPEIDLLGITVVAGNqtlEKTFNNALKVCSHLG-IDVPV---YKGMPGPMVReqviad 77
Cdd:cd02652    1 LILDTDIGGDpdDALALALAHALQKCDLLAVTITLAD---ASARRAIDAVNRFYGrGDIPIgadYHGWPEDAKD------ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321  78 diHGETGLDGPDFGEITKKGE-TMHAVDYIIEKLL-GSDEKITLVPTGPLSNIGMALRKE--PR-----IKEKIEQIVLM 148
Cdd:cd02652   72 --HAKFLLEGDRLHHDLESAEdALDAVKALRRLLAsAEDASVTIVSIGPLTNLAALLDADadPLtgpelVRQKVKRLVVM 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502626321 149 GGA--YQLGNSTpAAEFNIFADPEAAYVVFSSG------LPVVMMGLDLTrQALATKEVVDKIGSLNNKASKLFvdlmef 220
Cdd:cd02652  150 GGAfyDPDGNVQ-HREYNFVTDPKAAQRVAGRAqhlgipVRIVWSGYELG-EAVSYPHVLVIAHPFNTPVFAAY------ 221

                        250       260       270
                 ....*....|....*....|....*....|..
gi 502626321 221 faktqhdvfgWSAP---PVHDPTTVAYLIDPS 249
Cdd:cd02652  222 ----------WPRShrrPLWDPLTLLAAVRGG 243
 
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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