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Conserved domains on  [gi|491579945|ref|WP_005437517|]
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MULTISPECIES: uridine phosphorylase [Vibrio]

Protein Classification

uridine phosphorylase( domain architecture ID 10013750)

uridine phosphorylase (UP), a key enzyme in the pyrimidine salvage pathway, catalyzes the reversible phosphorolysis of uridine or 2'-deoxyuridine to uracil and ribose 1-phosphate or 2'-deoxyribose 1-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11178 PRK11178
uridine phosphorylase; Provisional
 5-252 0e+00

uridine phosphorylase; Provisional


:

Pssm-ID: 183018  Cd Length: 251  Bit Score: 529.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   5 VFHLGVTEADLNGATLAIIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLG 84
Cdd:PRK11178   4 VFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  85 VRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPG 164
Cdd:PRK11178  84 VRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 165 QERYDTFSGRVVKRFQGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGVIINRTQKEIPDHSTLKETEARSIKVV 244
Cdd:PRK11178 164 QERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIV 243


                 ....*...
gi 491579945 245 VEAARKML 252
Cdd:PRK11178 244 VEAARRLL 251
 
Name Accession Description Interval E-value
PRK11178 PRK11178
uridine phosphorylase; Provisional
 5-252 0e+00

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 529.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   5 VFHLGVTEADLNGATLAIIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLG 84
Cdd:PRK11178   4 VFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  85 VRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPG 164
Cdd:PRK11178  84 VRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 165 QERYDTFSGRVVKRFQGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGVIINRTQKEIPDHSTLKETEARSIKVV 244
Cdd:PRK11178 164 QERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIV 243


                 ....*...
gi 491579945 245 VEAARKML 252
Cdd:PRK11178 244 VEAARRLL 251
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 6-249 1.85e-120

uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine phosphorylase (UP) is specific for pyrimidines, and is involved in pyrimidine salvage and in the maintenance of uridine homeostasis. In addition to E. coli Udp, this subfamily includes Shewanella oneidensis MR-1 UP and Plasmodium falciparum purine nucleoside phosphorylase (PfPNP). PfPNP is an outlier in terms of genetic distance from the other families of PNPs. PfPNP is catalytically active for inosine and guanosine, and in addition, has a weak UP activity. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350167  Cd Length: 239  Bit Score: 342.89  E-value: 1.85e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   6 FHLGVTEADLngATLAIIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLGV 85
Cdd:cd17767    1 YHIGLKPGDV--APYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  86 RTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPGQ 165
Cdd:cd17767   79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 166 ERYDTFSGRvvkRFQGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGVIINRTQKEIPDHSTLKETEARSIKVVV 245
Cdd:cd17767  159 GRPGPGLPP---ELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVAL 235


                 ....
gi 491579945 246 EAAR 249
Cdd:cd17767  236 EALK 239
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 5-252 1.57e-115

uridine phosphorylase; This model represents a family of bacterial and archaeal uridine phosphorylases unrelated to the mammalian enzymes of the same name. The E. coli, Salmonella and Klebsiella genes have been characterized. Sequences from Clostridium, Streptomyces, Treponema, Halobacterium and Pyrobaculum were included above trusted on the basis of sequence homology and a PAM-based neighbor-joining tree. A clade including second sequences from Halobacterium and Vibrio was somewhat more distantly related and may represent a slightly different substrate specificity - these were placed below the noise cutoff. More distantly related is a clade of archaeal sequences which as related to the DeoD family of inosine phosphorylases (TIGR00107) as they are to these uridine phosphorylases. This clade includes a characterized protein from Sulfolobus solfataricus which has been mis-named as a methylthioadenosine phosphorylase, but which acts on inosine and guanosine - it is unclear whether uridine has been evaluated as a substrate. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130779  Cd Length: 245  Bit Score: 330.70  E-value: 1.57e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945    5 VFHLGVTEADLngATLAIIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLG 84
Cdd:TIGR01718   1 VYHLGLTKNDI--QTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   85 VRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPG 164
Cdd:TIGR01718  79 ARTFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  165 QERyDTFSGRVVKRFQGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGVIINRTQKEIPDHSTLKETEARSIKVV 244
Cdd:TIGR01718 159 QER-DTYSGRVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVA 237


                  ....*...
gi 491579945  245 VEAARKML 252
Cdd:TIGR01718 238 VEAVKRLL 245
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 5-251 3.28e-110

Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 442068  Cd Length: 251  Bit Score: 317.49  E-value: 3.28e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   5 VFHLGVTEADLngATLAIIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLG 84
Cdd:COG2820   11 QYHLGLKPGDV--ADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAALG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  85 VRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPG 164
Cdd:COG2820   89 AKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGFYAE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 165 QERYDtfsgRVVKRFQGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGVIINRTQKEIPDHStlKETEARSIKVV 244
Cdd:COG2820  169 QGREL----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDP--EEAVERAIKVA 242


                 ....*..
gi 491579945 245 VEAARKM 251
Cdd:COG2820  243 LEALKKL 249
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 19-249 1.41e-39

Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase)


Pssm-ID: 426013  Cd Length: 233  Bit Score: 136.71  E-value: 1.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   19 TLAIIPGDPARVQKIAEEMENPV-FLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEE--LAQLGVRTFLRVGTTG 95
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETpVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   96 AIQPHVNVGDMIVTTGSVRLDGASL-------HFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPGQERY 168
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  169 dtfsgrvvkrfqgsMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAgVIINRTQKEIPDHSTLKETEARSIKVVVEAA 248
Cdd:pfam01048 161 --------------IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIR-VVSDLAAGGADGELTHEEVEEFAERAAERAA 225


                  .
gi 491579945  249 R 249
Cdd:pfam01048 226 A 226
 
Name Accession Description Interval E-value
PRK11178 PRK11178
uridine phosphorylase; Provisional
 5-252 0e+00

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 529.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   5 VFHLGVTEADLNGATLAIIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLG 84
Cdd:PRK11178   4 VFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  85 VRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPG 164
Cdd:PRK11178  84 VRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 165 QERYDTFSGRVVKRFQGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGVIINRTQKEIPDHSTLKETEARSIKVV 244
Cdd:PRK11178 164 QERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIV 243


                 ....*...
gi 491579945 245 VEAARKML 252
Cdd:PRK11178 244 VEAARRLL 251
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 6-249 1.85e-120

uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine phosphorylase (UP) is specific for pyrimidines, and is involved in pyrimidine salvage and in the maintenance of uridine homeostasis. In addition to E. coli Udp, this subfamily includes Shewanella oneidensis MR-1 UP and Plasmodium falciparum purine nucleoside phosphorylase (PfPNP). PfPNP is an outlier in terms of genetic distance from the other families of PNPs. PfPNP is catalytically active for inosine and guanosine, and in addition, has a weak UP activity. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350167  Cd Length: 239  Bit Score: 342.89  E-value: 1.85e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   6 FHLGVTEADLngATLAIIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLGV 85
Cdd:cd17767    1 YHIGLKPGDV--APYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  86 RTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPGQ 165
Cdd:cd17767   79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 166 ERYDTFSGRvvkRFQGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGVIINRTQKEIPDHSTLKETEARSIKVVV 245
Cdd:cd17767  159 GRPGPGLPP---ELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVAL 235


                 ....
gi 491579945 246 EAAR 249
Cdd:cd17767  236 EALK 239
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 5-252 1.57e-115

uridine phosphorylase; This model represents a family of bacterial and archaeal uridine phosphorylases unrelated to the mammalian enzymes of the same name. The E. coli, Salmonella and Klebsiella genes have been characterized. Sequences from Clostridium, Streptomyces, Treponema, Halobacterium and Pyrobaculum were included above trusted on the basis of sequence homology and a PAM-based neighbor-joining tree. A clade including second sequences from Halobacterium and Vibrio was somewhat more distantly related and may represent a slightly different substrate specificity - these were placed below the noise cutoff. More distantly related is a clade of archaeal sequences which as related to the DeoD family of inosine phosphorylases (TIGR00107) as they are to these uridine phosphorylases. This clade includes a characterized protein from Sulfolobus solfataricus which has been mis-named as a methylthioadenosine phosphorylase, but which acts on inosine and guanosine - it is unclear whether uridine has been evaluated as a substrate. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130779  Cd Length: 245  Bit Score: 330.70  E-value: 1.57e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945    5 VFHLGVTEADLngATLAIIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLG 84
Cdd:TIGR01718   1 VYHLGLTKNDI--QTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   85 VRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPG 164
Cdd:TIGR01718  79 ARTFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  165 QERyDTFSGRVVKRFQGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGVIINRTQKEIPDHSTLKETEARSIKVV 244
Cdd:TIGR01718 159 QER-DTYSGRVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVA 237


                  ....*...
gi 491579945  245 VEAARKML 252
Cdd:TIGR01718 238 VEAVKRLL 245
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 5-251 3.28e-110

Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 442068  Cd Length: 251  Bit Score: 317.49  E-value: 3.28e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   5 VFHLGVTEADLngATLAIIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLG 84
Cdd:COG2820   11 QYHLGLKPGDV--ADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAALG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  85 VRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPG 164
Cdd:COG2820   89 AKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGFYAE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 165 QERYDtfsgRVVKRFQGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGVIINRTQKEIPDHStlKETEARSIKVV 244
Cdd:COG2820  169 QGREL----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDP--EEAVERAIKVA 242


                 ....*..
gi 491579945 245 VEAARKM 251
Cdd:COG2820  243 LEALKKL 249
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 20-247 3.39e-64

nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases such as purine nucleoside phosphorylase (PNP, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases such as AMP nucleosidase (AMN, EC 3.2.2.4) and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Members of this family display different physiologically relevant quaternary structures: hexameric (trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP); homotrimeric (human PNP and Escherichia coli PNPII or XapA); hexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD); or homodimeric such as human and Trypanosoma brucei UP. The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350156  Cd Length: 216  Bit Score: 199.44  E-value: 3.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  20 LAIIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLGVRTFLRVGTTGAIQP 99
Cdd:cd09005    1 YAIIPGDPERVDVIDSKLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALGVDTIIRVGSCGALRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 100 HVNVGDMIVTTGSVRLDGASLHF-APMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPGQerydtfsgrvvkr 178
Cdd:cd09005   81 DIKVGDLVIADGAIRGDGVTPYYvVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRET------------- 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 179 fQGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGVIINRTQKEI-PDHSTLKETEARSIKVVVEA 247
Cdd:cd09005  148 -REESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIgFVDEFLSEAEKKAIEIALDA 216
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 23-248 2.95e-55

purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside phosphorylase (PNP) catalyzes the reversible phosphorolysis of purine nucleosides. Thermus thermophiles PNP catalyzes the phosphorolysis of guanosine but not adenosine. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350165  Cd Length: 234  Bit Score: 177.11  E-value: 2.95e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  23 IPGDPARVQKIAEemenpVFLASHREYTLYRAEL------DGKPVVVCSTGIGGPSTSIAVEELAQLGVRTFLRVGTTGA 96
Cdd:cd17765   18 LPGDPGRATYIAE-----TFFDGPRLYNDHRGLLgytgtyKGKPVSVQTTGMGCPSAAIVVEELAQLGVKRLIRVGTCGG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  97 IQPHVNVGDMIVTTGSVRLDGASLHFAPME-FPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPGQErydtfsgrv 175
Cdd:cd17765   93 LSSGLQLGDLIVATAAVPADGTTRALLGGEpYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFYDPTP--------- 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491579945 176 vkrfqGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGV--IINRTQKEIPDhSTLKETEARSIKVVVEAA 248
Cdd:cd17765  164 -----DGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVsdLIGDPERRIDD-EELRAGVDRMTEVALEAV 232
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 22-247 1.06e-46

5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP) catalyzes the reversible phosphorolysis of 5'-deoxy-5'-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate. Sulfolobus solfataricus MTAPI will utilize inosine, guanosine, and adenosine as substrates, in addition to MTA. Two MTAPs have been isolated from S. solfataricus: SsMTAP1 and SsMTAPII, SsMTAPII belongs to a different subfamily of the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-I family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350164  Cd Length: 220  Bit Score: 154.69  E-value: 1.06e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  22 IIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLGVRTFLRVGTTGAIQPHV 101
Cdd:cd17764    4 IAVGDPGRVELLSTLLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIMLGAKVIIRLGTAGGLVPEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 102 NVGDMIVTTGSVRLDGA--SLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPGQERYdtfsgrvVKRf 179
Cdd:cd17764   84 RVGDIVVATGASYYPGGglGQYFPDVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEF-------AER- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491579945 180 qgsmqeWQDMGVLNFEMESATLLTMCASSGLKAGCVAgVIIN---RTQKEIPDHSTLKETEARSIKVVVEA 247
Cdd:cd17764  156 ------WSSLGFIAVEMECATLFTLGWLRGVKAGAVL-VVSDnlvKGGKLMLTKEELEEKVMKAAKAVLEA 219
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 19-249 1.41e-39

Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase)


Pssm-ID: 426013  Cd Length: 233  Bit Score: 136.71  E-value: 1.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   19 TLAIIPGDPARVQKIAEEMENPV-FLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEE--LAQLGVRTFLRVGTTG 95
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETpVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   96 AIQPHVNVGDMIVTTGSVRLDGASL-------HFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPGQERY 168
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  169 dtfsgrvvkrfqgsMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAgVIINRTQKEIPDHSTLKETEARSIKVVVEAA 248
Cdd:pfam01048 161 --------------IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIR-VVSDLAAGGADGELTHEEVEEFAERAAERAA 225


                  .
gi 491579945  249 R 249
Cdd:pfam01048 226 A 226
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 24-215 7.70e-39

Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside phosphorylase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440575  Cd Length: 236  Bit Score: 134.86  E-value: 7.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  24 PGDPARVQKIAEE-MENPVFLASHRE---YT-LYRaeldGKPVVVCSTGIGGPSTSIAVEELAQ-LGVRTFLRVGTTGAI 97
Cdd:COG0813   20 PGDPLRAKYIAETfLEDAVLVNEVRGmlgYTgTYK----GKRVSVMGSGMGIPSISIYAYELITeYGVKNIIRVGTCGAL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  98 QPHVNVGDMIVTTGSVRLDG-ASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFY-PGQERYDTfsgrv 175
Cdd:COG0813   96 QEDVKVRDVVIAMGASTDSNvNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFYrEDPDLLEK----- 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491579945 176 vkrfqgsmqeWQDMGVLNFEMESATLLTMCASSGLKAGCV 215
Cdd:COG0813  171 ----------LAKYGVLAVEMEAAALYTLAAKYGKRALAI 200
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 24-218 6.88e-37

purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas vaginalis PNP; Escherichia coli purine nucleoside phosphorylase (PNP)-I (or DeoD) accepts both 6-oxo and 6-amino purine nucleosides as substrates. Trichomonas vaginalis PNP has broad substrate specificity, having phosphorolytic catalytic activity with adenosine, inosine, and guanosine (with adenosine as the preferred substrate). This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350157  Cd Length: 228  Bit Score: 129.83  E-value: 6.88e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  24 PGDPARVQKIAEE-MENPVFLASHRE---YT-LYRaeldGKPVVVCSTGIGGPSTSIAVEELAQL-GVRTFLRVGTTGAI 97
Cdd:cd09006   16 PGDPLRAKYIAETfLEDAKLVNSVRNmlgYTgTYK----GKRVSVMGSGMGMPSIGIYAYELFKFyGVKNIIRIGTCGAY 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  98 QPHVNVGDMIVTTGSVRLDG-ASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFY-PGQERYDTfsgrv 175
Cdd:cd09006   92 QPDLKLRDVVLAMGASTDSNyNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYdDDPELWKK----- 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 491579945 176 vkrfqgsmqeWQDMGVLNFEMESATLLTMCASSGLKAGCVAGV 218
Cdd:cd09006  167 ----------LKKYGVLAVEMEAAALYTNAARLGKKALAILTV 199
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
24-215 1.50e-33

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 121.12  E-value: 1.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  24 PGDPARVQKIAEE-MENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQ-LGVRTFLRVGTTGAIQPHV 101
Cdd:PRK05819  19 PGDPLRAKYIAETfLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITdYGVKKLIRVGSCGALQEDV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 102 NVGDMIVTTGS------VRLDgaslhFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYpgQERYDTFsgrv 175
Cdd:PRK05819  99 KVRDVVIAMGAstdsnvNRIR-----FKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY--NPDPEMF---- 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491579945 176 vkrfqgsmQEWQDMGVLNFEMESATLLTMCASSGLKAGCV 215
Cdd:PRK05819 168 --------DVLEKYGVLGVEMEAAALYGLAAKYGVKALTI 199
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 5-247 1.80e-30

uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate. Trypanosoma brucei UP has a high specificity for uracil-containing (deoxy)nucleosides, and may function as a dimer. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350155  Cd Length: 282  Bit Score: 114.49  E-value: 1.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   5 VFHLGVTEADLngATLAIIPGDPARVQKIAEEMENPVFLASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEEL---- 80
Cdd:cd00436   10 IYHLHLKPEDL--ADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVLNELdalv 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  81 ----------AQLGVRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGAsLHFAPMEFPAVADFEIATAMKA--------- 141
Cdd:cd00436   88 nidfktrtpkEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNL-LNFYDHPNTDEEAELENAFIAHtswfkgkpr 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 142 --AVEES--------GATVHMGVTASSDTFYPGQerydtfsGRVVKR------FQGSMQ--EWQDMGVLNFEMESATLLT 203
Cdd:cd00436  167 pyVVKASpelldaltGVGYVVGITATAPGFYGPQ-------GRQLRLpladpdLLDKLSsfSYGGLRITNFEMETSAIYG 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 491579945 204 MCASSGLKAGCVAGVIINRTQKEIPDHStlKETEARSIKVVVEA 247
Cdd:cd00436  240 LSRLLGHRALSICAIIANRATGEFSKDY--KKAVEKLIEKVLEA 281
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 43-216 1.17e-24

uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed of uncharacterized members including Streptococcus pneumoniae hypothetical protein spr0068. The nucleoside phosphorylase-I (NP-I) family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases such as purine nucleoside phosphorylase (PNP, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases such as AMP nucleosidase (AMN, EC 3.2.2.4) and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Members of the NP-I family display different physiologically relevant quaternary structures: hexameric (trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP); homotrimeric (human PNP and Escherichia coli PNPII or XapA); hexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD); or homodimeric such as human and Trypanosoma brucei UP. The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350158 [Multi-domain]  Cd Length: 221  Bit Score: 97.55  E-value: 1.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  43 LASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQLGVRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHF 122
Cdd:cd09007   29 LSSAGHTPLYRLEYDGEEVGVVGPPVGAPAAVLVLEELIALGAKKFIVVGSCGSLDPDLAVGDIILPTSALRDEGTSYHY 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 123 APMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFY---PGQERYdtfsgrvvkrfqgsmqeWQDMGVLNFEMESA 199
Cdd:cd09007  109 LPPSRYIEPDPELLDALEEALEKAGIPYVRGKTWTTDAPYretRAKVAR-----------------RRAEGCLAVEMEAA 171

                        170
                 ....*....|....*..
gi 491579945 200 TLLTMCASSGLKAGCVA 216
Cdd:cd09007  172 ALFAVAQFRGVELAQLL 188
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 25-250 9.80e-23

uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate. Human UPP1 has a role in the activation of pyrimidine nucleoside analogues used in chemotherapy, such as 5-fluorouracil. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350163  Cd Length: 276  Bit Score: 93.75  E-value: 9.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  25 GDPARVQK----IAEEMENPV--------FLASHREYTLYRAeldgKPVVVCSTGIGGPSTSIAVEELAQL----GVR-- 86
Cdd:cd17763   30 GSPGRMENfaeyLAKELGIKLpagaalvnLSKTTDRYSMYKV----GPVLSVSHGMGIPSLSILLHELIKLlhyaGCKdv 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  87 TFLRVGTTGAIQphVNVGDMIVTTGSVrlDGASLHFAPM-------EFPAVADFEIAT-AMKAAVEESGATVHMGVTASS 158
Cdd:cd17763  106 TFIRIGTSGGIG--VEPGTVVITTEAV--DGELEPFYEQvilgkvvKRPAVLDAQLAEeLLECAKELDDFPTVIGKTMCA 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 159 DTFYPGQERYD-TFSGRVVKRFQGSMQEWQDMGVLNFEMESATLLTMCASSGLKAGCVAGVIINRTQKE--IPDHSTLKE 235
Cdd:cd17763  182 NDFYEGQGRLDgAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVCVTLLNRLEGDqiTSSKETLEE 261

                        250
                 ....*....|....*
gi 491579945 236 TEARSIKVVVEAARK 250
Cdd:cd17763  262 WQQRPQRLVSRYIKK 276
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
22-212 1.65e-21

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 89.39  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  22 IIPGDPARVQKIAEEmenpvFLASHREYTLYRAEL------DGKPVVVCSTGIGGPSTSIAVEEL-AQLGVRTFLRVGTT 94
Cdd:PRK13374  18 LMPGDPLRAKYIAET-----YLEDVVQVTDVRNMFgftgtyKGKKVSVMGHGMGIPSMVIYVHELiATFGVKNIIRVGSC 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  95 GAIQPHVNVGDMIVTTG-SVRLDGASLHFAPMEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFY-PGQERYDtfs 172
Cdd:PRK13374  93 GATQDDVKLMDVIIAQGaSTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFYdPDEDAIE--- 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491579945 173 grvvkrfqgsmqEWQDMGVLNFEMESATLLTMCASSGLKA 212
Cdd:PRK13374 170 ------------AMERFGILGVDMEVAGLYGLAAYLGAEA 197
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 25-250 8.65e-18

nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily is composed of mostly uncharacterized proteins with similarity to Toxoplasma gondii uridine phosphorylase (TgUPase). Toxoplasma gondii appears to have a single non-specific uridine phosphorylase which catalyzes the reversible phosphorolysis of uridine, deoxyuridine and thymidine, rather than the two distinct enzymes of mammalian cells: uridine phosphorylase (nucleoside phosphorylase-I family) and thymidine phosphorylase (nucleoside phosphorylase-II family). TgUPase is a potential target for intervention against toxoplasmosis. It belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350169  Cd Length: 255  Bit Score: 79.93  E-value: 8.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  25 GDPARVQKIAEEM--ENPVF-LASHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELAQL--GVRTFLRVGTTGAIQP 99
Cdd:cd17769    7 GDPARARLIAKLLdkEPKVFeLTSERGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREARAVvdGPMAIIRLGSCGSLDP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 100 HVNVGDMIVTTGSV----RLDGASLHFAP--------MEFPAVADFEIATAMKAAVEES--GATVHMGVTASSDTFYPGQ 165
Cdd:cd17769   87 DVPVGSVVVPSASVavtrNYDDDDFAGPStssekpylISKPVPADPELSELLESELKASlgGEVVVEGLNASADSFYSSQ 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 166 ERYDT-FSGR---VVKRFQGsmqewQDMGVLNFEMESATLLTMCASSG-----LKAGCVAGVIINRTQKEIPDHSTLKET 236
Cdd:cd17769  167 GRQDPnFPDHnenLIDKLLK-----RYPGAASLEMETFHLFHLARCSRpaqgkIRAAAAHMVFANRTSNDFISPERVHEL 241

                        250
                 ....*....|....
gi 491579945 237 EARSIKVVVEAARK 250
Cdd:cd17769  242 ERWAGRACLDALVA 255
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 60-252 6.70e-15

uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine phosphorylases. Genes from human and mouse have been characterized. This enzyme is a member of the PHP/UDP subfamily (pfam01048) and is closely related to the bacterial uridine (TIGR01718) and inosine (TIGR00107) phosphorylase equivalogs. In addition to the eukaryotes, a gene from Mycobacterium leprae is included in this equivalog and may have resulted from lateral gene transfer. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130780 [Multi-domain]  Cd Length: 287  Bit Score: 72.49  E-value: 6.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945   60 PVVVCSTGIGGPSTSIAVEEL------AQLGVRTFLRVGTTGAIQphVNVGDMIVTTGSVRLD----------GASLHFA 123
Cdd:TIGR01719  79 PVLCVSHGMGIPSISIMLHELikllyyARCKNPTFIRIGTSGGIG--VPPGTVVVSSEAVDAClkpeyeqivlGKRVIRP 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  124 PMEFPAVADfeiATAMKAAVEESGATVHMGVTASSDTFYPGQERYDtfsGRVVKRFQGSMQEW----QDMGVLNFEMESA 199
Cdd:TIGR01719 157 TQLDEALVQ---ELLLCGAEGLDEFTTVSGNTMCTDDFYEGQGRLD---GAFCEYTEKDKMAYlrklYALGVRNIEMESS 230

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 491579945  200 TLLTMCASSGLKAGCVAGVIINR---TQKEIPdHSTLKETEARSIKVVVEAARKML 252
Cdd:TIGR01719 231 MFAAMTSRAGFKAAVVCVTLLNRlegDQITIT-RDQLHEFEQRPQRLVSRYIKKKL 285
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 19-215 1.75e-14

Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB [Nucleotide transport and metabolism, Coenzyme transport and metabolism]; Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440538  Cd Length: 231  Bit Score: 70.32  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  19 TLAIIPGDPARVQKIAEEMENPVFLaSHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEEL-AQLGVRTFLRVGTTGAI 97
Cdd:COG0775    2 TIGIIGAMEEEVAALLEALEDKKEV-QIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLiARFRPDAVINTGVAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  98 QPHVNVGDMIVTTGSVRLDGASLHF---------APMEFPavADFEIATAMKAAVEESGATVHMGVTASSDTFypgqery 168
Cdd:COG0775   81 DPDLKIGDVVLATEVVQHDVDVTAFgyprgqvpgMPALFE--ADPALLEAAKEAAKESGLKVVTGTIATGDRF------- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491579945 169 dTFSGRVVKRFQgsmQEWQDMGVLnfEMESATLLTMCASSGLKAGCV 215
Cdd:COG0775  152 -VWSAEEKRRLR---ERFPGALAV--DMEGAAIAQVCYRFGVPFLVI 192
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 30-199 4.54e-11

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs): bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350159  Cd Length: 222  Bit Score: 60.59  E-value: 4.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  30 VQKIAEEMENP-VFLASHREYtlYRAELDGKPVVVCSTGIGGPSTSIAVEELAQL-GVRTFLRVGTTGAIQPHVNVGDMI 107
Cdd:cd09008   11 IAPLLELLENVeEETIAGRTF--YEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRfKPDAIINTGVAGGLDPDLKIGDVV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 108 VTTGSVRLDGASLHFA---------PMEFPavADFEIATAMKAAVEESGATVHMGVTASSDTFYPGQERYDtfsgRVVKR 178
Cdd:cd09008   89 IATKVVYHDVDATAFGyeggqppgmPAYFP--ADPELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKE----ELREN 162

                        170       180
                 ....*....|....*....|.
gi 491579945 179 FqgsmqewqdmGVLNFEMESA 199
Cdd:cd09008  163 F----------PALAVEMEGA 173
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 67-203 1.63e-10

AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate and adenine. It is a prokaryotic enzyme which plays a role in purine nucleoside salvage and intracellular AMP level regulation. AMN is active as a homohexamer; each monomer is comprised of a catalytic domain and a putative regulatory domain. This model represents the catalytic domain. AMN belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350162  Cd Length: 242  Bit Score: 59.49  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  67 GIGGPSTSIAVEELAQLGVRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHFAPMEFPAVADFEIATAMKAAVEES 146
Cdd:cd17762   67 GVGSPNAATITDLLAVLRPKAVLMLGHCGGLRNSQEIGDFVLPIAAIRGEGTSDDYLPPEVPALPSFELQRALSDALREV 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491579945 147 GATVHMGVTASSDtfypgqERYDTFSGRVVKRFQGSmqewQDMGVlnfEMESATLLT 203
Cdd:cd17762  147 GLDYRTGTVYTTD------RRNWEFDEAFKEYLRES----RAIAI---DMESATIFA 190
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
19-199 6.66e-10

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 57.44  E-value: 6.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  19 TLAIIPGDPARVQKIAEEMENP--VFLAShREYtlYRAELDGKPVVVCSTGIGGPSTSIAVEELAQ-LGVRTFLRVGTTG 95
Cdd:PRK05584   2 KIGIIGAMEEEVTLLLDKLENAqtITLAG-REF--YTGTLHGHEVVLVLSGIGKVAAALTATILIEhFKVDAVINTGVAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  96 AIQPHVNVGDMIVTTgSVR---LDGASLHFAPMEFPA-----VADFEIATAMKAAVEESGATVHMGVTASSDTFYPGQER 167
Cdd:PRK05584  79 GLAPGLKVGDVVVAD-ELVqhdVDVTAFGYPYGQVPGlpaafKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAEK 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 491579945 168 YDtfsgRVVKRFQgsmqewqdmGVLNFEMESA 199
Cdd:PRK05584 158 VA----AIRAEFP---------DALAVEMEGA 176
PRK07115 PRK07115
AMP nucleosidase; Provisional
 67-203 1.63e-08

AMP nucleosidase; Provisional


Pssm-ID: 235940  Cd Length: 258  Bit Score: 53.81  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  67 GIGGPSTSIAVEELAQLGVRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASLHFAPMEFPAVADFEIATAMKAAVEES 146
Cdd:PRK07115  68 GMGSPNAATIMDLLSALNPKAVLFLGKCGGLKSKYQVGDYFLPIAAIRGEGTSDDYFPPEVPALPNFVLQKAVSSIIRDK 147

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491579945 147 GATVHMGVTassdtfYPGQERYDTFSgrvvKRFQGSMQEWQDMGVlnfEMESATLLT 203
Cdd:PRK07115 148 GLDYWTGTV------YTTNRRFWEHD----KEFKEYLYETRAQAI---DMETATLFA 191
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 45-210 4.14e-06

nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs), as well as futalosine nucleosidase and adenosylhopane nucleosidase. Bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350170 [Multi-domain]  Cd Length: 210  Bit Score: 46.13  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945  45 SHREYTLYRAELDGKPVVVCSTGIGGPSTSIAVEELA-QLGVRTFLRVGTTGAIQPHVNVGDMIVTTGSVRLDGASlhfa 123
Cdd:cd17877   25 RLGGFRFYRGTLGGHPVVLVESGMGKANAARAAQLLLeHFQPDLIISTGFAGGLDPGLAVGDLVIADRVLYHDGDV---- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491579945 124 pmEFPAVADFEIATAMKAAVEESGATVHMGVTASSDTFYPGQERydtfsgrvvKRFQGsmqewQDMGVLNFEMESATLLT 203
Cdd:cd17877  101 --PAGLEADEKLVALAEELAAGLNLKVHRGTIITVDAIVRKSAE---------KAALA-----ARFPALAVDMESAAIAQ 164


                 ....*..
gi 491579945 204 MCASSGL 210
Cdd:cd17877  165 VAAARGI 171
 
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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