NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16131680|ref|NP_418275|]
View 

uridine phosphorylase [Escherichia coli str. K-12 substr. MG1655]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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: 569.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680    4 SDVFHLGLTKNDLQGATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQ 83
Cdd:PRK11178   2 SDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   84 LGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY 163
Cdd:PRK11178  82 LGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  164 PGQERYDTYSGRVVRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 243
Cdd:PRK11178 162 PGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 241

                        250
                 ....*....|
gi 16131680  244 IVVEAARRLL 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: 569.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680    4 SDVFHLGLTKNDLQGATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQ 83
Cdd:PRK11178   2 SDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   84 LGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY 163
Cdd:PRK11178  82 LGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  164 PGQERYDTYSGRVVRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 243
Cdd:PRK11178 162 PGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 241

                        250
                 ....*....|
gi 16131680  244 IVVEAARRLL 253
Cdd:PRK11178 242 IVVEAARRLL 251
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 6-253 3.27e-145

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: 405.82  E-value: 3.27e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680     6 VFHLGLTKNDLQgaTLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLG 85
Cdd:TIGR01718   1 VYHLGLTKNDIQ--TYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680    86 IRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPG 165
Cdd:TIGR01718  79 ARTFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   166 QERyDTYSGRVVRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIV 245
Cdd:TIGR01718 159 QER-DTYSGRVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVA 237


                  ....*...
gi 16131680   246 VEAARRLL 253
Cdd:TIGR01718 238 VEAVKRLL 245
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 7-250 1.95e-128

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: 363.30  E-value: 1.95e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   7 FHLGLTKNDLqgATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGI 86
Cdd:cd17767   1 YHIGLKPGDV--APYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  87 RTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQ 166
Cdd:cd17767  79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQ 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 167 ERYDTYsgrVVRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVV 246
Cdd:cd17767 159 GRPGPG---LPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVAL 235


                ....
gi 16131680 247 EAAR 250
Cdd:cd17767 236 EALK 239
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 6-252 6.72e-117

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 334.44  E-value: 6.72e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   6 VFHLGLTKNDLqgATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLG 85
Cdd:COG2820  11 QYHLGLKPGDV--ADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAALG 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  86 IRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPG 165
Cdd:COG2820  89 AKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGFYAE 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 166 QERYDtysgRVVRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAEtmKQTESHAVKIV 245
Cdd:COG2820 169 QGREL----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDP--EEAVERAIKVA 242


                ....*..
gi 16131680 246 VEAARRL 252
Cdd:COG2820 243 LEALKKL 249
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 20-253 1.04e-38

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: 134.78  E-value: 1.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680    20 TLAIVPGDPDRVEKIAALMDKPVKLAS-HREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEE--LAQLGIRTFLRIGTTG 96
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVGPpSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680    97 AIQPHINVGDVLVTTASVRLDGASL-------HFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQERY 169
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   170 dtysgrvvrhfkgsMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGV--IVNRTQQEIPNAETMKQTESHAVKIVVE 247
Cdd:pfam01048 161 --------------IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVsdLAAGGADGELTHEEVEEFAERAAERAAA 226


                  ....*.
gi 16131680   248 AARRLL 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: 569.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680    4 SDVFHLGLTKNDLQGATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQ 83
Cdd:PRK11178   2 SDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   84 LGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY 163
Cdd:PRK11178  82 LGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  164 PGQERYDTYSGRVVRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 243
Cdd:PRK11178 162 PGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVK 241

                        250
                 ....*....|
gi 16131680  244 IVVEAARRLL 253
Cdd:PRK11178 242 IVVEAARRLL 251
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 6-253 3.27e-145

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: 405.82  E-value: 3.27e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680     6 VFHLGLTKNDLQgaTLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLG 85
Cdd:TIGR01718   1 VYHLGLTKNDIQ--TYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680    86 IRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPG 165
Cdd:TIGR01718  79 ARTFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   166 QERyDTYSGRVVRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIV 245
Cdd:TIGR01718 159 QER-DTYSGRVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVA 237


                  ....*...
gi 16131680   246 VEAARRLL 253
Cdd:TIGR01718 238 VEAVKRLL 245
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 7-250 1.95e-128

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: 363.30  E-value: 1.95e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   7 FHLGLTKNDLqgATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGI 86
Cdd:cd17767   1 YHIGLKPGDV--APYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  87 RTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQ 166
Cdd:cd17767  79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQ 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 167 ERYDTYsgrVVRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVV 246
Cdd:cd17767 159 GRPGPG---LPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVAL 235


                ....
gi 16131680 247 EAAR 250
Cdd:cd17767 236 EALK 239
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 6-252 6.72e-117

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 334.44  E-value: 6.72e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   6 VFHLGLTKNDLqgATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLG 85
Cdd:COG2820  11 QYHLGLKPGDV--ADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAALG 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  86 IRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPG 165
Cdd:COG2820  89 AKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGFYAE 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 166 QERYDtysgRVVRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAEtmKQTESHAVKIV 245
Cdd:COG2820 169 QGREL----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDP--EEAVERAIKVA 242


                ....*..
gi 16131680 246 VEAARRL 252
Cdd:COG2820 243 LEALKKL 249
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 21-248 1.50e-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: 1.50e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  21 LAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQP 100
Cdd:cd09005   1 YAIIPGDPERVDVIDSKLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALGVDTIIRVGSCGALRE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 101 HINVGDVLVTTASVRLDGASLHF-APLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQERYdtysgrvvrh 179
Cdd:cd09005  81 DIKVGDLVIADGAIRGDGVTPYYvVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETREE---------- 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 180 fkgsMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEI-PNAETMKQTESHAVKIVVEA 248
Cdd:cd09005 151 ----SEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIgFVDEFLSEAEKKAIEIALDA 216
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 8-249 8.21e-50

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: 163.25  E-value: 8.21e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   8 HLGLTKNDLQGATLaiVPGDPDRVEKIAA-LMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGI 86
Cdd:cd17765   4 HIRAEPGDVAEAVL--LPGDPGRATYIAEtFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELAQLGV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  87 RTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLE-FPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPG 165
Cdd:cd17765  82 KRLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEpYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFYDP 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 166 QErydtysgrvvrhfkGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGV--IVNRTQQEIPNAEtMKQTESHAVK 243
Cdd:cd17765 162 TP--------------DGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVsdLIGDPERRIDDEE-LRAGVDRMTE 226


                ....*.
gi 16131680 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 1.02e-47

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: 157.39  E-value: 1.02e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  23 IVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHI 102
Cdd:cd17764   4 IAVGDPGRVELLSTLLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIMLGAKVIIRLGTAGGLVPEL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 103 NVGD-VLVTTASVRLDGA-SLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQERYdtysgrvvrhf 180
Cdd:cd17764  84 RVGDiVVATGASYYPGGGlGQYFPDVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEF----------- 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131680 181 kgsMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAgVIVN---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-38

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: 134.78  E-value: 1.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680    20 TLAIVPGDPDRVEKIAALMDKPVKLAS-HREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEE--LAQLGIRTFLRIGTTG 96
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVGPpSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680    97 AIQPHINVGDVLVTTASVRLDGASL-------HFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQERY 169
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   170 dtysgrvvrhfkgsMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGV--IVNRTQQEIPNAETMKQTESHAVKIVVE 247
Cdd:pfam01048 161 --------------IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVsdLAAGGADGELTHEEVEEFAERAAERAAA 226


                  ....*.
gi 16131680   248 AARRLL 253
Cdd:pfam01048 227 LLLALL 232
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 8-249 2.84e-36

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: 128.31  E-value: 2.84e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   8 HLGLTKNDLqgATLAIVPGDPDRVEKIAA-LMDKPVKLASHRE---FT-TWRaeldGKPVIVCSTGIGGPSTSIAVEELA 82
Cdd:COG0813   5 HIGAKKGDI--AETVLLPGDPLRAKYIAEtFLEDAVLVNEVRGmlgYTgTYK----GKRVSVMGSGMGIPSISIYAYELI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  83 Q-LGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDG-ASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSD 160
Cdd:COG0813  79 TeYGVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNvNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 161 TFYpgQERYDTYsgrvvrhfkgsmEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGV---IVnrTQQEIPnAETMKQT 237
Cdd:COG0813 159 LFY--REDPDLL------------EKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVsdhLV--TGEETT-AEERQTT 221

                       250
                ....*....|..
gi 16131680 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 3.19e-36

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: 129.51  E-value: 3.19e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   6 VFHLGLTKNDLqgATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEEL---- 81
Cdd:cd00436  10 IYHLHLKPEDL--ADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVLNELdalv 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  82 ----------AQLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGaSLHFAPLEfPAVADFECTTAL----------- 140
Cdd:cd00436  88 nidfktrtpkEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDN-LLNFYDHP-NTDEEAELENAFiahtswfkgkp 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 141 ----VEAAKSI-----GATTHVGVTASSDTFYPGQerydtysGRVVR------HFKGSMEEWQAMG--VMNYEMESATLL 203
Cdd:cd00436 166 rpyvVKASPELldaltGVGYVVGITATAPGFYGPQ-------GRQLRlpladpDLLDKLSSFSYGGlrITNFEMETSAIY 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 16131680 204 TMCASQGLRAGMVAGVIVNRTQQEIpnAETMKQTESHAVKIVVEA 248
Cdd:cd00436 239 GLSRLLGHRALSICAIIANRATGEF--SKDYKKAVEKLIEKVLEA 281
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 23-219 2.14e-32

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: 117.89  E-value: 2.14e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  23 IVPGDPDRVEKIA-ALMDKPVKLASHRE---FT-TWRaeldGKPVIVCSTGIGGPSTSIAVEELAQL-GIRTFLRIGTTG 96
Cdd:cd09006  14 LMPGDPLRAKYIAeTFLEDAKLVNSVRNmlgYTgTYK----GKRVSVMGSGMGMPSIGIYAYELFKFyGVKNIIRIGTCG 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  97 AIQPHINVGD-VLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQERYdtysgr 175
Cdd:cd09006  90 AYQPDLKLRDvVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDDPEL------ 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 16131680 176 vvrhfkgsMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGV 219
Cdd:cd09006 164 --------WKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTV 199
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
25-213 4.34e-31

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 114.95  E-value: 4.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   25 PGDPDRVEKIA-ALMDKPVKLASHRE---FT-TWRaeldGKPVIVCSTGIGGPSTSIAVEELAQ-LGIRTFLRIGTTGAI 98
Cdd:PRK05819  19 PGDPLRAKYIAeTFLEDVVCVNEVRGmlgFTgTYK----GKRVSVMGTGMGIPSISIYANELITdYGVKKLIRVGSCGAL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   99 QPHINVGDV-LVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYpgQERYDTYsgrvv 177
Cdd:PRK05819  95 QEDVKVRDVvIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY--NPDPEMF----- 167

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 16131680  178 rhfkgsmEEWQAMGVMNYEMESATLLTMCASQGLRA 213
Cdd:PRK05819 168 -------DVLEKYGVLGVEMEAAALYGLAAKYGVKA 196
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 53-217 7.00e-22

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: 90.24  E-value: 7.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  53 WRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVA 132
Cdd:cd09007  38 YRLEYDGEEVGVVGPPVGAPAAVLVLEELIALGAKKFIVVGSCGSLDPDLAVGDIILPTSALRDEGTSYHYLPPSRYIEP 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 133 DFECTTALVEAAKSIGATTHVGVTASSDTFYpgqerydtysgrvvRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLR 212
Cdd:cd09007 118 DPELLDALEEALEKAGIPYVRGKTWTTDAPY--------------RETRAKVARRRAEGCLAVEMEAAALFAVAQFRGVE 183


                ....*
gi 16131680 213 AGMVA 217
Cdd:cd09007 184 LAQLL 188
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
23-213 1.56e-20

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 87.08  E-value: 1.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   23 IVPGDPDRVEKIAALMdkpvkLASHREFTTWRAEL------DGKPVIVCSTGIGGPSTSIAVEEL-AQLGIRTFLRIGTT 95
Cdd:PRK13374  18 LMPGDPLRAKYIAETY-----LEDVVQVTDVRNMFgftgtyKGKKVSVMGHGMGIPSMVIYVHELiATFGVKNIIRVGSC 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   96 GAIQPHINVGDVLVTT-ASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQErydtysg 174
Cdd:PRK13374  93 GATQDDVKLMDVIIAQgASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFYDPDE------- 165

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 16131680  175 rvvrhfkGSMEEWQAMGVMNYEMESATLLTMCASQGLRA 213
Cdd:PRK13374 166 -------DAIEAMERFGILGVDMEVAGLYGLAAYLGAEA 197
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 61-247 3.06e-20

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: 86.82  E-value: 3.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  61 PVIVCSTGIGGPSTSIAVEELAQL----GIR--TFLRIGTTGAI--QPhinvGDVLVTTASVrlDGASLHFAPL------ 126
Cdd:cd17763  73 PVLSVSHGMGIPSLSILLHELIKLlhyaGCKdvTFIRIGTSGGIgvEP----GTVVITTEAV--DGELEPFYEQvilgkv 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 127 -EFPAVADFECTTALVEAAKSIGATTHV-GVTASSDTFYPGQERYD----TYSGRVVRHFkgsMEEWQAMGVMNYEMESA 200
Cdd:cd17763 147 vKRPAVLDAQLAEELLECAKELDDFPTViGKTMCANDFYEGQGRLDgafcDYTEEDKMAF---LQKLYDAGVRNIEMESL 223

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16131680 201 TLLTMCASQGLRAGMVAGVIVNR--TQQEIPNAETMKQTESHAVKIVVE 247
Cdd:cd17763 224 CFAAFCHRAGIKAAVVCVTLLNRleGDQITSSKETLEEWQQRPQRLVSR 272
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 26-248 7.09e-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: 7.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  26 GDPDRVEKIAALMDKPVK---LASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQL--GIRTFLRIGTTGAIQP 100
Cdd:cd17769   7 GDPARARLIAKLLDKEPKvfeLTSERGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREARAVvdGPMAIIRLGSCGSLDP 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 101 HINVGDVLVTTASV----RLDGASLHFA------PLEF--PAVADFECTTALVEAAKSIGATTHV--GVTASSDTFYPGQ 166
Cdd:cd17769  87 DVPVGSVVVPSASVavtrNYDDDDFAGPstssekPYLIskPVPADPELSELLESELKASLGGEVVveGLNASADSFYSSQ 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 167 ERYDTysgrvvrHF----KGSMEEWQAM--GVMNYEMESATLLTMCAS-----QGLRAGMVAGVIVNRTQQEIPNAETMK 235
Cdd:cd17769 167 GRQDP-------NFpdhnENLIDKLLKRypGAASLEMETFHLFHLARCsrpaqGKIRAAAAHMVFANRTSNDFISPERVH 239

                       250
                ....*....|...
gi 16131680 236 QTESHAVKIVVEA 248
Cdd:cd17769 240 ELERWAGRACLDA 252
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 61-223 3.79e-16

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: 75.95  E-value: 3.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680    61 PVIVCSTGIGGPSTSIAVEEL------AQLGIRTFLRIGTTGAIQphINVGDVLVTTASV-----------RLDGASLHF 123
Cdd:TIGR01719  79 PVLCVSHGMGIPSISIMLHELikllyyARCKNPTFIRIGTSGGIG--VPPGTVVVSSEAVdaclkpeyeqiVLGKRVIRP 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   124 APLeFPAVADFECTTAlVEAAKSIgaTTHVGVTASSDTFYPGQERYDTYSGRVVRHFKGSMEEW-QAMGVMNYEMESATL 202
Cdd:TIGR01719 157 TQL-DEALVQELLLCG-AEGLDEF--TTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKlYALGVRNIEMESSMF 232

                         170       180
                  ....*....|....*....|.
gi 16131680   203 LTMCASQGLRAGMVAGVIVNR 223
Cdd:TIGR01719 233 AAMTSRAGFKAAVVCVTLLNR 253
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 34-216 7.97e-15

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: 71.48  E-value: 7.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  34 IAALMDKPVKLASHREFttWRAELDGKPVIVCSTGIGGPSTSIAVEEL-AQLGIRTFLRIGTTGAIQPHINVGDVLVTTA 112
Cdd:COG0775  17 LEALEDKKEVQIAGFTF--YLGTLGGKEVVLVNSGIGKVNAATATTLLiARFRPDAVINTGVAGGLDPDLKIGDVVLATE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 113 SVRLDG--ASLHFAPLEFPAV-ADFECTTALVEAAKSI----GATTHVGVTASSDTFYPGQERYDtysgRVVRHFKGsme 185
Cdd:COG0775  95 VVQHDVdvTAFGYPRGQVPGMpALFEADPALLEAAKEAakesGLKVVTGTIATGDRFVWSAEEKR----RLRERFPG--- 167

                       170       180       190
                ....*....|....*....|....*....|.
gi 16131680 186 ewqAMGVmnyEMESATLLTMCASQGLRAGMV 216
Cdd:COG0775 168 ---ALAV---DMEGAAIAQVCYRFGVPFLVI 192
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 31-200 5.02e-13

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: 66.37  E-value: 5.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  31 VEKIAALMDKP-VKLASHREFttWRAELDGKPVIVCSTGIGGPSTSIAveelAQLGIRTF-----LRIGTTGAIQPHINV 104
Cdd:cd09008  11 IAPLLELLENVeEETIAGRTF--YEGTLGGKEVVLVQSGIGKVNAAIA----TQLLIDRFkpdaiINTGVAGGLDPDLKI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 105 GDVLVTTASVRLD-GASLHFAPLEFPA--VADFECTTALVEAAKSI----GATTHVGVTASSDTFYPGQERYDtysgRVV 177
Cdd:cd09008  85 GDVVIATKVVYHDvDATAFGYEGGQPPgmPAYFPADPELLELAKKAakelGPKVHTGLIASGDQFVASSEKKE----ELR 160

                       170       180
                ....*....|....*....|...
gi 16131680 178 RHFKgsmeewqAMGVmnyEMESA 200
Cdd:cd09008 161 ENFP-------ALAV---EMEGA 173
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 31-204 9.04e-11

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: 60.26  E-value: 9.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  31 VEKIAALMDKPVKlASHREFTTWRAELDGKPVIvcSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHINVGDVLVT 110
Cdd:cd17762  33 VDEFAERTGVPIR-GGSVQMPAAHLKKEGITII--NFGVGSPNAATITDLLAVLRPKAVLMLGHCGGLRNSQEIGDFVLP 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680 111 TASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTfypgqerydtysgRVVRH---FKGSMEEW 187
Cdd:cd17762 110 IAAIRGEGTSDDYLPPEVPALPSFELQRALSDALREVGLDYRTGTVYTTDR-------------RNWEFdeaFKEYLRES 176

                       170
                ....*....|....*..
gi 16131680 188 QAMGVmnyEMESATLLT 204
Cdd:cd17762 177 RAIAI---DMESATIFA 190
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
20-200 1.84e-09

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 56.28  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   20 TLAIVPGDPDRVEKIAALMDKP--VKLAShREFttWRAELDGKPVIVCSTGIGGPSTSIAVEELAQ-LGIRTFLRIGTTG 96
Cdd:PRK05584   2 KIGIIGAMEEEVTLLLDKLENAqtITLAG-REF--YTGTLHGHEVVLVLSGIGKVAAALTATILIEhFKVDAVINTGVAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   97 AIQPHINVGDVLVTTASVR--LDGASLHFAPLEFPAV-ADFECTTALVE----AAKSIGATTHVGVTASSDTFYPGQERY 169
Cdd:PRK05584  79 GLAPGLKVGDVVVADELVQhdVDVTAFGYPYGQVPGLpAAFKADEKLVAlaekAAKELNLNVHRGLIASGDQFIAGAEKV 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 16131680  170 DtysgRVVRHFKgsmeewQAMGVmnyEMESA 200
Cdd:PRK05584 159 A----AIRAEFP------DALAV---EMEGA 176
PRK07115 PRK07115
AMP nucleosidase; Provisional
 68-204 2.35e-09

AMP nucleosidase; Provisional


Pssm-ID: 235940  Cd Length: 258  Bit Score: 56.12  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   68 GIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSI 147
Cdd:PRK07115  68 GMGSPNAATIMDLLSALNPKAVLFLGKCGGLKSKYQVGDYFLPIAAIRGEGTSDDYFPPEVPALPNFVLQKAVSSIIRDK 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  148 GATTHVGVTassdtfypgqerYDTySGRVVRH---FKGSMEEWQAMGVmnyEMESATLLT 204
Cdd:PRK07115 148 GLDYWTGTV------------YTT-NRRFWEHdkeFKEYLYETRAQAI---DMETATLFA 191
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 21-162 2.31e-07

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: 49.98  E-value: 2.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680  21 LAIVPGDPDRVEKIAALMdKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELA-QLGIRTFLRIGTTGAIQ 99
Cdd:cd17877   1 IGIIAAMPEEISPLLRRI-EVLQKVRLGGFRFYRGTLGGHPVVLVESGMGKANAARAAQLLLeHFQPDLIISTGFAGGLD 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131680 100 PHINVGDVLVTTASVRLDGASlhfaPLEFPavADFECTTALVEAAKSIGATTHVGVTASSDTF 162
Cdd:cd17877  80 PGLAVGDLVIADRVLYHDGDV----PAGLE--ADEKLVALAEELAAGLNLKVHRGTIITVDAI 136
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 55-162 1.81e-03

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 39.22  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131680   55 AELDGKPVIVCSTGIGGPSTSIAVEELA-QLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLeFPAVAD 133
Cdd:PRK06698  37 GEFMGTEVIVTRCGVGKVNAAACTQTLIhKFDVDAIINTGVAGGLHPDVKVGDIVISTNVTHHDVSKTQMKNL-FPFQEE 115

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 16131680  134 FECTTALVEAAK------SIGATTHVGVTASSDTF 162
Cdd:PRK06698 116 FIASKELVELARkacnssSLHMEIHEGRIVSGECF 150
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH