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Conserved domains on  [gi|2053492674|gb|QWS86766|]
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uridine phosphorylase [Enterobacter hormaechei]

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
 4-253 0e+00

uridine phosphorylase; Provisional


:

Pssm-ID: 183018  Cd Length: 251  Bit Score: 562.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   4 SDVFHLGLTKNDLQGATLAIVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQ 83
Cdd:PRK11178    2 SDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  84 LGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFY 163
Cdd:PRK11178   82 LGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 164 PGQERYDTFSGRVVSRFKGSMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 243
Cdd:PRK11178  162 PGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 241

                         250
                  ....*....|
gi 2053492674 244 IVVEAARRLI 253
Cdd:PRK11178  242 IVVEAARRLL 251
 
Name Accession Description Interval E-value
PRK11178 PRK11178
uridine phosphorylase; Provisional
 4-253 0e+00

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 562.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   4 SDVFHLGLTKNDLQGATLAIVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQ 83
Cdd:PRK11178    2 SDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  84 LGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFY 163
Cdd:PRK11178   82 LGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 164 PGQERYDTFSGRVVSRFKGSMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 243
Cdd:PRK11178  162 PGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 241

                         250
                  ....*....|
gi 2053492674 244 IVVEAARRLI 253
Cdd:PRK11178  242 IVVEAARRLL 251
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 6-253 1.98e-139

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: 391.18  E-value: 1.98e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   6 VFHLGLTKNDLQgaTLAIVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQLG 85
Cdd:TIGR01718   1 VYHLGLTKNDIQ--TYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  86 IRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPG 165
Cdd:TIGR01718  79 ARTFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 166 QERyDTFSGRVVSRFKGSMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIV 245
Cdd:TIGR01718 159 QER-DTYSGRVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVA 237


                  ....*...
gi 2053492674 246 VEAARRLI 253
Cdd:TIGR01718 238 VEAVKRLL 245
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 7-250 2.96e-125

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: 355.21  E-value: 2.96e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   7 FHLGLTKNDLqgATLAIVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQLGI 86
Cdd:cd17767     1 YHIGLKPGDV--APYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  87 RTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPGQ 166
Cdd:cd17767    79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 167 ERYDTFSGRvvsRFKGSMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVV 246
Cdd:cd17767   159 GRPGPGLPP---ELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVAL 235


                  ....
gi 2053492674 247 EAAR 250
Cdd:cd17767   236 EALK 239
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 6-253 3.00e-115

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 330.21  E-value: 3.00e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   6 VFHLGLTKNDLqgATLAIVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQLG 85
Cdd:COG2820    11 QYHLGLKPGDV--ADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAALG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  86 IRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPG 165
Cdd:COG2820    89 AKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGFYAE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 166 QERYDtfsgRVVSRFKGSMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAEtmKQTESHAVKIV 245
Cdd:COG2820   169 QGREL----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDP--EEAVERAIKVA 242


                  ....*...
gi 2053492674 246 VEAARRLI 253
Cdd:COG2820   243 LEALKKLI 250
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 20-253 1.04e-37

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: 132.08  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  20 TLAIVPGDPERVEKIAALMDKPVKL-AAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEE--LAQLGIRTFLRIGTTG 96
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVgPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  97 AIQPHINVGDVLVTTASVRLDGASL-------HFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPGQERY 169
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 170 dtfsgrvvsrfkgsMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGV--IVNRTQQEIPNAETMKQTESHAVKIVVE 247
Cdd:pfam01048 161 --------------IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVsdLAAGGADGELTHEEVEEFAERAAERAAA 226


                  ....*.
gi 2053492674 248 AARRLI 253
Cdd:pfam01048 227 LLLALL 232
 
Name Accession Description Interval E-value
PRK11178 PRK11178
uridine phosphorylase; Provisional
 4-253 0e+00

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 562.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   4 SDVFHLGLTKNDLQGATLAIVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQ 83
Cdd:PRK11178    2 SDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  84 LGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFY 163
Cdd:PRK11178   82 LGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 164 PGQERYDTFSGRVVSRFKGSMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 243
Cdd:PRK11178  162 PGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 241

                         250
                  ....*....|
gi 2053492674 244 IVVEAARRLI 253
Cdd:PRK11178  242 IVVEAARRLL 251
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 6-253 1.98e-139

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: 391.18  E-value: 1.98e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   6 VFHLGLTKNDLQgaTLAIVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQLG 85
Cdd:TIGR01718   1 VYHLGLTKNDIQ--TYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  86 IRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPG 165
Cdd:TIGR01718  79 ARTFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 166 QERyDTFSGRVVSRFKGSMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIV 245
Cdd:TIGR01718 159 QER-DTYSGRVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVA 237


                  ....*...
gi 2053492674 246 VEAARRLI 253
Cdd:TIGR01718 238 VEAVKRLL 245
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 7-250 2.96e-125

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: 355.21  E-value: 2.96e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   7 FHLGLTKNDLqgATLAIVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQLGI 86
Cdd:cd17767     1 YHIGLKPGDV--APYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  87 RTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPGQ 166
Cdd:cd17767    79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 167 ERYDTFSGRvvsRFKGSMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVV 246
Cdd:cd17767   159 GRPGPGLPP---ELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVAL 235


                  ....
gi 2053492674 247 EAAR 250
Cdd:cd17767   236 EALK 239
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 6-253 3.00e-115

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 330.21  E-value: 3.00e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   6 VFHLGLTKNDLqgATLAIVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQLG 85
Cdd:COG2820    11 QYHLGLKPGDV--ADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAALG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  86 IRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPG 165
Cdd:COG2820    89 AKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGFYAE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 166 QERYDtfsgRVVSRFKGSMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAEtmKQTESHAVKIV 245
Cdd:COG2820   169 QGREL----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDP--EEAVERAIKVA 242


                  ....*...
gi 2053492674 246 VEAARRLI 253
Cdd:COG2820   243 LEALKKLI 250
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 21-248 1.42e-67

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: 207.91  E-value: 1.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  21 LAIVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQP 100
Cdd:cd09005     1 YAIIPGDPERVDVIDSKLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALGVDTIIRVGSCGALRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 101 HINVGDVLVTTASVRLDGASLHF-APMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPGQERYdtfsgrvvsr 179
Cdd:cd09005    81 DIKVGDLVIADGAIRGDGVTPYYvVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETREE---------- 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 180 fkgsMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEI-PNAETMKQTESHAVKIVVEA 248
Cdd:cd09005   151 ----SEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIgFVDEFLSEAEKKAIEIALDA 216
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 8-249 8.56e-49

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: 160.55  E-value: 8.56e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   8 HLGLTKNDLQGATLaiVPGDPERVEKIAA-LMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQLGI 86
Cdd:cd17765     4 HIRAEPGDVAEAVL--LPGDPGRATYIAEtFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELAQLGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  87 RTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPME-FPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPG 165
Cdd:cd17765    82 KRLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEpYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFYDP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 166 QErydtfsgrvvsrfkGSMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGV--IVNRTQQEIPNAEtMKQTESHAVK 243
Cdd:cd17765   162 TP--------------DGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVsdLIGDPERRIDDEE-LRAGVDRMTE 226


                  ....*.
gi 2053492674 244 IVVEAA 249
Cdd:cd17765   227 VALEAV 232
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 23-248 4.87e-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: 153.15  E-value: 4.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  23 IVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHI 102
Cdd:cd17764     4 IAVGDPGRVELLSTLLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIMLGAKVIIRLGTAGGLVPEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 103 NVGD-VLVTTASVRLDGA-SLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPGQERYdtfsgrvvsrf 180
Cdd:cd17764    84 RVGDiVVATGASYYPGGGlGQYFPDVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEF----------- 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2053492674 181 kgsMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAgVIVN---RTQQEIPNAETMKQTESHAVKIVVEA 248
Cdd:cd17764   153 ---AERWSSLGFIAVEMECATLFTLGWLRGVKAGAVL-VVSDnlvKGGKLMLTKEELEEKVMKAAKAVLEA 219
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 20-253 1.04e-37

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: 132.08  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  20 TLAIVPGDPERVEKIAALMDKPVKL-AAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEE--LAQLGIRTFLRIGTTG 96
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVgPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  97 AIQPHINVGDVLVTTASVRLDGASL-------HFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPGQERY 169
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 170 dtfsgrvvsrfkgsMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGV--IVNRTQQEIPNAETMKQTESHAVKIVVE 247
Cdd:pfam01048 161 --------------IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVsdLAAGGADGELTHEEVEEFAERAAERAAA 226


                  ....*.
gi 2053492674 248 AARRLI 253
Cdd:pfam01048 227 LLLALL 232
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 8-249 1.68e-34

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: 123.69  E-value: 1.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   8 HLGLTKNDLqgATLAIVPGDPERVEKIAA-LMDKPVKLAAHRE---FT-TWRaeldGKAVIVCSTGIGGPSTSIAVEELA 82
Cdd:COG0813     5 HIGAKKGDI--AETVLLPGDPLRAKYIAEtFLEDAVLVNEVRGmlgYTgTYK----GKRVSVMGSGMGIPSISIYAYELI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  83 Q-LGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDG-ASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSD 160
Cdd:COG0813    79 TeYGVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNvNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 161 TFYpgQERYDTFsgrvvsrfkgsmEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGV---IVnrTQQEIPnAETMKQT 237
Cdd:COG0813   159 LFY--REDPDLL------------EKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVsdhLV--TGEETT-AEERQTT 221

                         250
                  ....*....|..
gi 2053492674 238 ESHAVKIVVEAA 249
Cdd:COG0813   222 FNDMMEIALEAA 233
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 6-248 9.04e-34

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: 122.97  E-value: 9.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674   6 VFHLGLTKNDLqgATLAIVPGDPERVEKIAALMDKPVKLAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEEL---- 81
Cdd:cd00436    10 IYHLHLKPEDL--ADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVLNELdalv 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  82 ----------AQLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTAL----------- 140
Cdd:cd00436    88 nidfktrtpkEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNLLNFYDHPNTDEEAELENAFIAhtswfkgkprp 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 141 --VEAAKSV-----GATTHVGVTASSDTFYPGQerydtfsGRVVSR------FKGSME--EWQSMGVMNYEMESATLLTM 205
Cdd:cd00436   168 yvVKASPELldaltGVGYVVGITATAPGFYGPQ-------GRQLRLpladpdLLDKLSsfSYGGLRITNFEMETSAIYGL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2053492674 206 CASQGLRAGMVAGVIVNRTQQEIpnAETMKQTESHAVKIVVEA 248
Cdd:cd00436   241 SRLLGHRALSICAIIANRATGEF--SKDYKKAVEKLIEKVLEA 281
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 23-219 6.98e-31

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: 114.04  E-value: 6.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  23 IVPGDPERVEKIA-ALMDKPVklaahrEFTTWRAEL------DGKAVIVCSTGIGGPSTSIAVEELAQL-GIRTFLRIGT 94
Cdd:cd09006    14 LMPGDPLRAKYIAeTFLEDAK------LVNSVRNMLgytgtyKGKRVSVMGSGMGMPSIGIYAYELFKFyGVKNIIRIGT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  95 TGAIQPHINVGD-VLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPGQERYdtfs 173
Cdd:cd09006    88 CGAYQPDLKLRDvVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDDPEL---- 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2053492674 174 grvvsrfkgsMEEWQSMGVMNYEMESATLLTMCASQGLRAGMVAGV 219
Cdd:cd09006   164 ----------WKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTV 199
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
25-213 1.69e-30

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 113.41  E-value: 1.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  25 PGDPERVEKIA-ALMDKPVKLAAHRE---FT-TWRaeldGKAVIVCSTGIGGPSTSIAVEELAQ-LGIRTFLRIGTTGAI 98
Cdd:PRK05819   19 PGDPLRAKYIAeTFLEDVVCVNEVRGmlgFTgTYK----GKRVSVMGTGMGIPSISIYANELITdYGVKKLIRVGSCGAL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  99 QPHINVGDV-LVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYpgQERYDTFsgrvv 177
Cdd:PRK05819   95 QEDVKVRDVvIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY--NPDPEMF----- 167

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2053492674 178 srfkgsmEEWQSMGVMNYEMESATLLTMCASQGLRA 213
Cdd:PRK05819  168 -------DVLEKYGVLGVEMEAAALYGLAAKYGVKA 196
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 53-217 5.95e-21

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: 87.54  E-value: 5.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  53 WRAELDGKAVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVA 132
Cdd:cd09007    38 YRLEYDGEEVGVVGPPVGAPAAVLVLEELIALGAKKFIVVGSCGSLDPDLAVGDIILPTSALRDEGTSYHYLPPSRYIEP 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 133 DFECTTALVEAAKSVGATTHVGVTASSDTFYpgQErydTfsgrvvsrfKGSMEEWQSMGVMNYEMESATLLTMCASQGLR 212
Cdd:cd09007   118 DPELLDALEEALEKAGIPYVRGKTWTTDAPY--RE---T---------RAKVARRRAEGCLAVEMEAAALFAVAQFRGVE 183


                  ....*
gi 2053492674 213 AGMVA 217
Cdd:cd09007   184 LAQLL 188
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
23-213 1.61e-20

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 87.08  E-value: 1.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  23 IVPGDPERVEKIAALMdkpvkLAAHREFTTWRAEL------DGKAVIVCSTGIGGPSTSIAVEEL-AQLGIRTFLRIGTT 95
Cdd:PRK13374   18 LMPGDPLRAKYIAETY-----LEDVVQVTDVRNMFgftgtyKGKKVSVMGHGMGIPSMVIYVHELiATFGVKNIIRVGSC 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  96 GAIQPHINVGDVLVTT-ASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTFYPGQErydtfsg 174
Cdd:PRK13374   93 GATQDDVKLMDVIIAQgASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFYDPDE------- 165

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2053492674 175 rvvsrfkGSMEEWQSMGVMNYEMESATLLTMCASQGLRA 213
Cdd:PRK13374  166 -------DAIEAMERFGILGVDMEVAGLYGLAAYLGAEA 197
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 26-248 6.08e-19

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: 83.01  E-value: 6.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  26 GDPERVEKIAALMDKPVK---LAAHREFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELAQL--GIRTFLRIGTTGAIQP 100
Cdd:cd17769     7 GDPARARLIAKLLDKEPKvfeLTSERGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREARAVvdGPMAIIRLGSCGSLDP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 101 HINVGDVLVTTASV----RLDGASLHFAP--------MEFPAVADFECTTALVEAAKSVGATTHV--GVTASSDTFYPGQ 166
Cdd:cd17769    87 DVPVGSVVVPSASVavtrNYDDDDFAGPStssekpylISKPVPADPELSELLESELKASLGGEVVveGLNASADSFYSSQ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 167 ERYDT-FSGR---VVSRFKGSMEEWQSMgvmnyEMESATLLTMCAS-----QGLRAGMVAGVIVNRTQQEIPNAETMKQT 237
Cdd:cd17769   167 GRQDPnFPDHnenLIDKLLKRYPGAASL-----EMETFHLFHLARCsrpaqGKIRAAAAHMVFANRTSNDFISPERVHEL 241

                         250
                  ....*....|.
gi 2053492674 238 ESHAVKIVVEA 248
Cdd:cd17769   242 ERWAGRACLDA 252
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 62-247 7.30e-18

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: 80.65  E-value: 7.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  62 VIVCSTGIGGPSTSIAVEELAQL----GIR--TFLRIGTTGAI--QPhinvGDVLVTTASVrlDGASLHFAPM------- 126
Cdd:cd17763    74 VLSVSHGMGIPSLSILLHELIKLlhyaGCKdvTFIRIGTSGGIgvEP----GTVVITTEAV--DGELEPFYEQvilgkvv 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 127 EFPAVADFECTTALVEAAKSVGATTHV-GVTASSDTFYPGQERYD-TFSGRVVSRFKGSMEEWQSMGVMNYEMESATLLT 204
Cdd:cd17763   148 KRPAVLDAQLAEELLECAKELDDFPTViGKTMCANDFYEGQGRLDgAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAA 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2053492674 205 MCASQGLRAGMVAGVIVNR--TQQEIPNAETMKQTESHAVKIVVE 247
Cdd:cd17763   228 FCHRAGIKAAVVCVTLLNRleGDQITSSKETLEEWQQRPQRLVSR 272
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 62-223 2.01e-14

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: 70.94  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  62 VIVCSTGIGGPSTSIAVEEL------AQLGIRTFLRIGTTGAIQphINVGDVLVTTASVRLDGASLHFAPMEFPAVADF- 134
Cdd:TIGR01719  80 VLCVSHGMGIPSISIMLHELikllyyARCKNPTFIRIGTSGGIG--VPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPt 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 135 ECTTALVEAAKSVGA------TTHVGVTASSDTFYPGQERYDTFSGRVVSRFKGSMEEW-QSMGVMNYEMESATLLTMCA 207
Cdd:TIGR01719 158 QLDEALVQELLLCGAegldefTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKlYALGVRNIEMESSMFAAMTS 237

                         170
                  ....*....|....*.
gi 2053492674 208 SQGLRAGMVAGVIVNR 223
Cdd:TIGR01719 238 RAGFKAAVVCVTLLNR 253
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 23-216 4.51e-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: 69.17  E-value: 4.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  23 IVPGDPERVEKIAALMDKPVKLAAHREFttWRAELDGKAVIVCSTGIGGPSTSIAVEEL-AQLGIRTFLRIGTTGAIQPH 101
Cdd:COG0775     6 IGAMEEEVAALLEALEDKKEVQIAGFTF--YLGTLGGKEVVLVNSGIGKVNAATATTLLiARFRPDAVINTGVAGGLDPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 102 INVGDVLVTTASVRLDG--ASLHFAPMEFPAV-ADFECTTALVEAAKSV----GATTHVGVTASSDTFYPGQERYDtfsg 174
Cdd:COG0775    84 LKIGDVVLATEVVQHDVdvTAFGYPRGQVPGMpALFEADPALLEAAKEAakesGLKVVTGTIATGDRFVWSAEEKR---- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2053492674 175 RVVSRFKGsmeewqSMGVmnyEMESATLLTMCASQGLRAGMV 216
Cdd:COG0775   160 RLRERFPG------ALAV---DMEGAAIAQVCYRFGVPFLVI 192
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 23-200 9.92e-12

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: 62.51  E-value: 9.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  23 IVPGDPErVEKIAALMDKP-VKLAAHREFttWRAELDGKAVIVCSTGIGGPSTSIAveelAQLGIRTF-----LRIGTTG 96
Cdd:cd09008     4 IGAMEEE-IAPLLELLENVeEETIAGRTF--YEGTLGGKEVVLVQSGIGKVNAAIA----TQLLIDRFkpdaiINTGVAG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  97 AIQPHINVGDVLVTTASVRLD-GASLHFAPMEFPA--VADFECTTALVEAAKSV----GATTHVGVTASSDTFYPGQER- 168
Cdd:cd09008    77 GLDPDLKIGDVVIATKVVYHDvDATAFGYEGGQPPgmPAYFPADPELLELAKKAakelGPKVHTGLIASGDQFVASSEKk 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2053492674 169 ---YDTFSGRVVsrfkgsmeewqsmgvmnyEMESA 200
Cdd:cd09008   157 eelRENFPALAV------------------EMEGA 173
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 31-204 4.22e-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: 58.33  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  31 VEKIAALMDKPVKlAAHREFTTWRAELDGKAVIvcSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHINVGDVLVT 110
Cdd:cd17762    33 VDEFAERTGVPIR-GGSVQMPAAHLKKEGITII--NFGVGSPNAATITDLLAVLRPKAVLMLGHCGGLRNSQEIGDFVLP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674 111 TASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSVGATTHVGVTASSDtfypgqER---YDTfsgrvvsRFKGSMEEW 187
Cdd:cd17762   110 IAAIRGEGTSDDYLPPEVPALPSFELQRALSDALREVGLDYRTGTVYTTD------RRnweFDE-------AFKEYLRES 176

                         170
                  ....*....|....*..
gi 2053492674 188 QSMGVmnyEMESATLLT 204
Cdd:cd17762   177 RAIAI---DMESATIFA 190
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
20-170 1.09e-09

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 57.05  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  20 TLAIVPGDPERVEKIAALMDKPVKLA-AHREFttWRAELDGKAVIVCSTGIGGPSTSIAVEELAQ-LGIRTFLRIGTTGA 97
Cdd:PRK05584    2 KIGIIGAMEEEVTLLLDKLENAQTITlAGREF--YTGTLHGHEVVLVLSGIGKVAAALTATILIEhFKVDAVINTGVAGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  98 IQPHINVGDVLVTTASVR--LDGASLHFAPMEFPAV-ADFECTTALVEAAKSV----GATTHVGVTASSDTFYPGQERYD 170
Cdd:PRK05584   80 LAPGLKVGDVVVADELVQhdVDVTAFGYPYGQVPGLpAAFKADEKLVALAEKAakelNLNVHRGLIASGDQFIAGAEKVA 159
PRK07115 PRK07115
AMP nucleosidase; Provisional
 68-204 5.94e-08

AMP nucleosidase; Provisional


Pssm-ID: 235940  Cd Length: 258  Bit Score: 52.27  E-value: 5.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  68 GIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVADFECTTALVEAAKSV 147
Cdd:PRK07115   68 GMGSPNAATIMDLLSALNPKAVLFLGKCGGLKSKYQVGDYFLPIAAIRGEGTSDDYFPPEVPALPNFVLQKAVSSIIRDK 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2053492674 148 GATTHVGVTassdtfYPGQERYDTFSgrvvSRFKGSMEEWQSMGVmnyEMESATLLT 204
Cdd:PRK07115  148 GLDYWTGTV------YTTNRRFWEHD----KEFKEYLYETRAQAI---DMETATLFA 191
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 21-162 1.20e-05

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: 44.98  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  21 LAIVPGDPERVEKIAALMDKPVKLAAHReFTTWRAELDGKAVIVCSTGIGGPSTSIAVEELA-QLGIRTFLRIGTTGAIQ 99
Cdd:cd17877     1 IGIIAAMPEEISPLLRRIEVLQKVRLGG-FRFYRGTLGGHPVVLVESGMGKANAARAAQLLLeHFQPDLIISTGFAGGLD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2053492674 100 PHINVGDVLVTTASVRLDGASlhfapmEFPAVADFECTTALVEAAKSVGATTHVGVTASSDTF 162
Cdd:cd17877    80 PGLAVGDLVIADRVLYHDGDV------PAGLEADEKLVALAEELAAGLNLKVHRGTIITVDAI 136
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 55-155 3.10e-03

bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 38.45  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053492674  55 AELDGKAVIVCSTGIGGPSTSIAVEELA-QLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMeFPAVAD 133
Cdd:PRK06698   37 GEFMGTEVIVTRCGVGKVNAAACTQTLIhKFDVDAIINTGVAGGLHPDVKVGDIVISTNVTHHDVSKTQMKNL-FPFQEE 115

                          90       100
                  ....*....|....*....|....
gi 2053492674 134 FECTTALVEAAKSV--GATTHVGV 155
Cdd:PRK06698  116 FIASKELVELARKAcnSSSLHMEI 139
 
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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