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Conserved domains on  [gi|3323355|gb|AAC65977|]
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uridine phosphorylase (udp) [Treponema pallidum subsp. pallidum str. Nichols]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 10-252 2.55e-146

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: 408.90  E-value: 2.55e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355     10 EYHIGLKASDIGHYVILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGAH 89
Cdd:TIGR01718   1 VYHLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355     90 TFIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYGQHS 169
Cdd:TIGR01718  81 TFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPGQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    170 PHTMP--VHAELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLVIGNQTRRAQGLEDIQVHDTENAIRVAVEA 247
Cdd:TIGR01718 161 RDTYSgrVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVAVEA 240


                  ....*
gi 3323355    248 VKLLI 252
Cdd:TIGR01718 241 VKRLL 245
 
Name Accession Description Interval E-value
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 10-252 2.55e-146

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: 408.90  E-value: 2.55e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355     10 EYHIGLKASDIGHYVILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGAH 89
Cdd:TIGR01718   1 VYHLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355     90 TFIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYGQHS 169
Cdd:TIGR01718  81 TFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPGQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    170 PHTMP--VHAELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLVIGNQTRRAQGLEDIQVHDTENAIRVAVEA 247
Cdd:TIGR01718 161 RDTYSgrVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVAVEA 240


                  ....*
gi 3323355    248 VKLLI 252
Cdd:TIGR01718 241 VKRLL 245
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 11-249 8.05e-132

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: 371.78  E-value: 8.05e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   11 YHIGLKASDIGHYVILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGAHT 90
Cdd:cd17767   1 YHIGLKPGDVAPYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGAKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   91 FIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYGQHSP 170
Cdd:cd17767  81 FIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQGR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3323355  171 HTMPVHAELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLVIGNQTRRAQGLEDIQVHDTENAIRVAVEAVK 249
Cdd:cd17767 161 PGPGLPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVALEALK 239
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 11-252 2.07e-112

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 323.27  E-value: 2.07e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   11 YHIGLKASDIGHYVILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGAHT 90
Cdd:COG2820  12 YHLGLKPGDVADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAALGAKT 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   91 FIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYGQHSP 170
Cdd:COG2820  92 FIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGFYAEQGR 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  171 HTmPVHAELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLVIGNQTrRAQGLEDIQvHDTENAIRVAVEAVKL 250
Cdd:COG2820 172 EL-RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRV-TGEFSKDPE-EAVERAIKVALEALKK 248


                ..
gi 3323355  251 LI 252
Cdd:COG2820 249 LI 250
PRK11178 PRK11178
uridine phosphorylase; Provisional
 11-252 2.40e-63

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 198.73  E-value: 2.40e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    11 YHIGLKASDI--GHYVILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGA 88
Cdd:PRK11178   5 FHLGLTKADLqgATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    89 HTFIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFY-GQ 167
Cdd:PRK11178  85 RTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYpGQ 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   168 --HSPHTMPVHAELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLVIGNQTRraQGLEDIQ-VHDTEN-AIRV 243
Cdd:PRK11178 165 erYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQ--QEIPNAEtMKQTEShAVKI 242


                 ....*....
gi 3323355   244 AVEAVKLLI 252
Cdd:PRK11178 243 VVEAARRLL 251
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 23-253 2.93e-30

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: 112.82  E-value: 2.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355     23 YVILPGDPARSEKIAQHFSHPHKVG-HNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEE--LIHLGAHTFIRVGTSGG 99
Cdd:pfam01048   2 IAIIGGSPEELALLAELLDDETPVGpPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    100 MQPDILAGTVVIATGAIRFEGTSK-------EYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYGQhspht 172
Cdd:pfam01048  82 LNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFE----- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    173 mpVHAELtQKWHAWIAcntLASEMESAALFVLGSVRRVRTGAVLLVIGNQTRRAQGLEDIQVHDtENAIRVAVEAVKLLI 252
Cdd:pfam01048 157 --TPAEI-RLLRRLGA---DAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADGELTHEEVE-EFAERAAERAAALLL 229


                  .
gi 3323355    253 T 253
Cdd:pfam01048 230 A 230
 
Name Accession Description Interval E-value
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 10-252 2.55e-146

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: 408.90  E-value: 2.55e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355     10 EYHIGLKASDIGHYVILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGAH 89
Cdd:TIGR01718   1 VYHLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355     90 TFIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYGQHS 169
Cdd:TIGR01718  81 TFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPGQE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    170 PHTMP--VHAELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLVIGNQTRRAQGLEDIQVHDTENAIRVAVEA 247
Cdd:TIGR01718 161 RDTYSgrVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVAVEA 240


                  ....*
gi 3323355    248 VKLLI 252
Cdd:TIGR01718 241 VKRLL 245
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 11-249 8.05e-132

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: 371.78  E-value: 8.05e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   11 YHIGLKASDIGHYVILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGAHT 90
Cdd:cd17767   1 YHIGLKPGDVAPYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGAKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   91 FIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYGQHSP 170
Cdd:cd17767  81 FIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQGR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3323355  171 HTMPVHAELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLVIGNQTRRAQGLEDIQVHDTENAIRVAVEAVK 249
Cdd:cd17767 161 PGPGLPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVALEALK 239
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 11-252 2.07e-112

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 323.27  E-value: 2.07e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   11 YHIGLKASDIGHYVILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGAHT 90
Cdd:COG2820  12 YHLGLKPGDVADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAALGAKT 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   91 FIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYGQHSP 170
Cdd:COG2820  92 FIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGFYAEQGR 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  171 HTmPVHAELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLVIGNQTrRAQGLEDIQvHDTENAIRVAVEAVKL 250
Cdd:COG2820 172 EL-RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRV-TGEFSKDPE-EAVERAIKVALEALKK 248


                ..
gi 3323355  251 LI 252
Cdd:COG2820 249 LI 250
PRK11178 PRK11178
uridine phosphorylase; Provisional
 11-252 2.40e-63

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 198.73  E-value: 2.40e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    11 YHIGLKASDI--GHYVILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGA 88
Cdd:PRK11178   5 FHLGLTKADLqgATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    89 HTFIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFY-GQ 167
Cdd:PRK11178  85 RTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYpGQ 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   168 --HSPHTMPVHAELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLVIGNQTRraQGLEDIQ-VHDTEN-AIRV 243
Cdd:PRK11178 165 erYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQ--QEIPNAEtMKQTEShAVKI 242


                 ....*....
gi 3323355   244 AVEAVKLLI 252
Cdd:PRK11178 243 VVEAARRLL 251
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 12-248 7.39e-58

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: 184.05  E-value: 7.39e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   12 HIGLKASDIGHYVILPGDPARSEKIAQHF-SHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGAHT 90
Cdd:cd17765   4 HIRAEPGDVAEAVLLPGDPGRATYIAETFfDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELAQLGVKR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   91 FIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVE-FPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYGQHs 169
Cdd:cd17765  84 LIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEpYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFYDPT- 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  170 PHTMPvhaeltqkwhAWIACNTLASEMESAALFVLGSVRRVRTGAVLLV---IGNQTRRAqGLEDIQvHDTENAIRVAVE 246
Cdd:cd17765 163 PDGVK----------RWRRRGVLAVEMEASALFTLAALRGLRAGCILTVsdlIGDPERRI-DDEELR-AGVDRMTEVALE 230


                ..
gi 3323355  247 AV 248
Cdd:cd17765 231 AV 232
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 23-247 4.68e-56

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: 179.02  E-value: 4.68e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   23 YVILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGAHTFIRVGTSGGMQP 102
Cdd:cd09005   1 YAIIPGDPERVDVIDSKLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALGVDTIIRVGSCGALRE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  103 DILAGTVVIATGAIRFEGTSKEY-APVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYgqhsphtmpvhAELTQ 181
Cdd:cd09005  81 DIKVGDLVIADGAIRGDGVTPYYvVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFY-----------RETRE 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3323355  182 KWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLVIGNQTRRAQGLEDIQVHDTEN-AIRVAVEA 247
Cdd:cd09005 150 ESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEFLSEAEKkAIEIALDA 216
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 24-221 1.17e-51

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: 167.79  E-value: 1.17e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   24 VILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGAHTFIRVGTSGGMQPD 103
Cdd:cd17764   3 VIAVGDPGRVELLSTLLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIMLGAKVIIRLGTAGGLVPE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  104 ILAGTVVIATGAIRFE-GTSKEYAP-VEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYgqhsphtmpvhAELTQ 181
Cdd:cd17764  83 LRVGDIVVATGASYYPgGGLGQYFPdVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFY-----------AEDEE 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 3323355  182 KWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLVIGN 221
Cdd:cd17764 152 FAERWSSLGFIAVEMECATLFTLGWLRGVKAGAVLVVSDN 191
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 12-251 5.08e-45

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: 151.04  E-value: 5.08e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   12 HIGLKASDIGHYVILPGDPARSEKIAQHF-SHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIH-LGAH 89
Cdd:COG0813   5 HIGAKKGDIAETVLLPGDPLRAKYIAETFlEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITeYGVK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   90 TFIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYA-PVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYGqh 168
Cdd:COG0813  85 NIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFgGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFYR-- 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  169 sphtmpvhaELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVL-----LVIGNQT---RRAQGLEDiqvhdtenA 240
Cdd:COG0813 163 ---------EDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILtvsdhLVTGEETtaeERQTTFND--------M 225

                       250
                ....*....|.
gi 3323355  241 IRVAVEAVKLL 251
Cdd:COG0813 226 MEIALEAALKL 236
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 12-218 2.67e-41

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: 141.39  E-value: 2.67e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   12 HIGLKASDIGHYVILPGDPARSEKIAQHF-SHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHL-GAH 89
Cdd:cd09006   1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFlEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFyGVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   90 TFIRVGTSGGMQPDILAGTVVIATGAirfeGTSKEYA-----PVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNF 164
Cdd:cd09006  81 NIIRIGTCGAYQPDLKLRDVVLAMGA----STDSNYNrlrfgGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVF 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 3323355  165 YGqhsphtmpvhaELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLV 218
Cdd:cd09006 157 YD-----------DDPELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTV 199
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
12-218 7.65e-36

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 127.28  E-value: 7.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    12 HIGLKASDIGHYVILPGDPARSEKIAQHF-SHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIH-LGAH 89
Cdd:PRK05819   4 HINAKKGDIADTVLMPGDPLRAKYIAETFlEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITdYGVK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    90 TFIRVGTSGGMQPDILAGTVVIATGA--------IRFEgtskeyaPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCK 161
Cdd:PRK05819  84 KLIRVGSCGALQEDVKVRDVVIAMGAstdsnvnrIRFK-------GHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 3323355   162 DNFYGqhsphtmpvhaELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGAVLLV 218
Cdd:PRK05819 157 DLFYN-----------PDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTV 202
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 11-247 7.45e-32

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: 118.34  E-value: 7.45e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   11 YHIGLKASDIGHYVILPGDPARSEKIAQHFSHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEEL-----IH 85
Cdd:cd00436  11 YHLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVLNELdalvnID 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   86 LGAHT---------FIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALKH-----------A 145
Cdd:cd00436  91 FKTRTpkeektslnIIRLGTSGALQPDIPVGSLVISSYAIGLDNLLNFYDHPNTDEEAELENAFIAHTswfkgkprpyvV 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  146 AEDVQVRHALGVVQCKDN-------FYG-QH----SPHTMPvhaELTQKwhawiacntLAS-----------EMESAALF 202
Cdd:cd00436 171 KASPELLDALTGVGYVVGitatapgFYGpQGrqlrLPLADP---DLLDK---------LSSfsygglritnfEMETSAIY 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 3323355  203 VLGSVRRVRTGAVLLVIGNqtrRAQGLEDIQVHDT-ENAIRVAVEA 247
Cdd:cd00436 239 GLSRLLGHRALSICAIIAN---RATGEFSKDYKKAvEKLIEKVLEA 281
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 23-253 2.93e-30

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: 112.82  E-value: 2.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355     23 YVILPGDPARSEKIAQHFSHPHKVG-HNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEE--LIHLGAHTFIRVGTSGG 99
Cdd:pfam01048   2 IAIIGGSPEELALLAELLDDETPVGpPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    100 MQPDILAGTVVIATGAIRFEGTSK-------EYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNFYGQhspht 172
Cdd:pfam01048  82 LNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFE----- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    173 mpVHAELtQKWHAWIAcntLASEMESAALFVLGSVRRVRTGAVLLVIGNQTRRAQGLEDIQVHDtENAIRVAVEAVKLLI 252
Cdd:pfam01048 157 --TPAEI-RLLRRLGA---DAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADGELTHEEVE-EFAERAAERAAALLL 229


                  .
gi 3323355    253 T 253
Cdd:pfam01048 230 A 230
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 55-247 3.31e-24

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


Pssm-ID: 350158 [Multi-domain]  Cd Length: 221  Bit Score: 96.40  E-value: 3.31e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   55 YTGTLCETPVSVMSTGIGGPSTAIGVEELIHLGAHTFIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVP 134
Cdd:cd09007  38 YRLEYDGEEVGVVGPPVGAPAAVLVLEELIALGAKKFIVVGSCGSLDPDLAVGDIILPTSALRDEGTSYHYLPPSRYIEP 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  135 DFTVTAALKHAAEDVQVRHALGVVQCKDNFYgqhsphtmpvhAELTQKWHAWIACNTLASEMESAALFVLGSVRRVRTGA 214
Cdd:cd09007 118 DPELLDALEEALEKAGIPYVRGKTWTTDAPY-----------RETRAKVARRRAEGCLAVEMEAAALFAVAQFRGVELAQ 186

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 3323355  215 vLLVIGN---QTRRAQGLEDIQVHDTENAIRVAVEA 247
Cdd:cd09007 187 -LLYVSDslaGEEWDPRGRDEGKDAREKALELALEA 221
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
12-218 1.98e-22

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 92.08  E-value: 1.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    12 HIGLKASDIGHYVILPGDPARSEKIAQHFSHPHK-VGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIH-LGAH 89
Cdd:PRK13374   5 HINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVqVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELIAtFGVK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    90 TFIRVGTSGGMQPDILAGTVVIATGAirfeGT-----SKEYAPVEFPAVPDFTVTAALKHAAEDVQVRHALGVVQCKDNF 164
Cdd:PRK13374  85 NIIRVGSCGATQDDVKLMDVIIAQGA----STdsktnRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLF 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 3323355   165 YgqhSPHTmpvhaELTQKWHAWiacNTLASEMESAALFVLGSVRRVRTGAVLLV 218
Cdd:PRK13374 161 Y---DPDE-----DAIEAMERF---GILGVDMEVAGLYGLAAYLGAEALAILTV 203
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 64-218 1.57e-17

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: 79.14  E-value: 1.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   64 VSVMSTGIGGPSTAIGVEELIHLGAHTFIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALK 143
Cdd:cd17762  61 ITIINFGVGSPNAATITDLLAVLRPKAVLMLGHCGGLRNSQEIGDFVLPIAAIRGEGTSDDYLPPEVPALPSFELQRALS 140

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3323355  144 HAAEDVQVRHALGVVQCKDNFYGQHSPHTmpvhAELTQKWHAwiacntLASEMESAALFVLGSVRRVRTGAVLLV 218
Cdd:cd17762 141 DALREVGLDYRTGTVYTTDRRNWEFDEAF----KEYLRESRA------IAIDMESATIFAVGFANRVPYGALLLV 205
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 28-247 8.92e-16

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: 74.54  E-value: 8.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   28 GDPARSEKIAQHF---SHPHKVGHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELIHL--GAHTFIRVGTSGGMQP 102
Cdd:cd17769   7 GDPARARLIAKLLdkePKVFELTSERGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREARAVvdGPMAIIRLGSCGSLDP 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  103 DILAGTVVIATGAI------RFEGTSKEYAPVE--------FPAVPDFT--VTAALKHAAEDVQVRHALGVvqCKDNFY- 165
Cdd:cd17769  87 DVPVGSVVVPSASVavtrnyDDDDFAGPSTSSEkpyliskpVPADPELSelLESELKASLGGEVVVEGLNA--SADSFYs 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  166 --GQHSPHtMPVH-----AELTQKWHawiacNTLASEMESAALFVLGSVRR-----VRTGAVLLVIGNQTRRaQGLEDIQ 233
Cdd:cd17769 165 sqGRQDPN-FPDHnenliDKLLKRYP-----GAASLEMETFHLFHLARCSRpaqgkIRAAAAHMVFANRTSN-DFISPER 237

                       250
                ....*....|....*
gi 3323355  234 VHDTEN-AIRVAVEA 247
Cdd:cd17769 238 VHELERwAGRACLDA 252
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 11-167 4.06e-12

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: 64.48  E-value: 4.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   11 YHIGLKASDIG--------HYVILPGDPARSEKIAQ------HFSHPHKV-------GHNReYVTY-TGtlcetPVSVMS 68
Cdd:cd17763   5 YHLGLDTSSHDlkkmfgdvKFVCMGGSPGRMENFAEylakelGIKLPAGAalvnlskTTDR-YSMYkVG-----PVLSVS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   69 TGIGGPSTAIGVEELIHLGAH------TFIRVGTSGGMqpDILAGTVVIATGAIRFEGTSK-EYA----PVEFPAVPDFT 137
Cdd:cd17763  79 HGMGIPSLSILLHELIKLLHYagckdvTFIRIGTSGGI--GVEPGTVVITTEAVDGELEPFyEQVilgkVVKRPAVLDAQ 156

                       170       180       190
                ....*....|....*....|....*....|..
gi 3323355  138 VTAALK-HAAEDVQVRHALGVVQCKDNFY-GQ 167
Cdd:cd17763 157 LAEELLeCAKELDDFPTVIGKTMCANDFYeGQ 188
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 36-218 1.36e-11

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: 62.24  E-value: 1.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   36 IAQHFSHPHKVgHNREYVTYTGTLCETPVSVMSTGIGGPSTAIGVEELI-HLGAHTFIRVGTSGGMQPDILAGTVVIATG 114
Cdd:COG0775  16 LLEALEDKKEV-QIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIaRFRPDAVINTGVAGGLDPDLKIGDVVLATE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  115 AIRFEG--TSKEYAPVEFPAVP-----DFTVTAALKHAAEDVQVRHALGVVQCKDNFygqhsphtmpvHAELTQKwhAWI 187
Cdd:COG0775  95 VVQHDVdvTAFGYPRGQVPGMPalfeaDPALLEAAKEAAKESGLKVVTGTIATGDRF-----------VWSAEEK--RRL 161

                       170       180       190
                ....*....|....*....|....*....|....
gi 3323355  188 ACNT---LASEMESAALFVLGSVRRVRTGAVLLV 218
Cdd:COG0775 162 RERFpgaLAVDMEGAAIAQVCYRFGVPFLVIRAI 195
PRK07115 PRK07115
AMP nucleosidase; Provisional
 64-252 1.94e-10

AMP nucleosidase; Provisional


Pssm-ID: 235940  Cd Length: 258  Bit Score: 59.59  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    64 VSVMSTGIGGPSTAIGVEELIHLGAHTFIRVGTSGGMQPDILAGTVVIATGAIRFEGTSKEYAPVEFPAVPDFTVTAALK 143
Cdd:PRK07115  62 ITIINFGMGSPNAATIMDLLSALNPKAVLFLGKCGGLKSKYQVGDYFLPIAAIRGEGTSDDYFPPEVPALPNFVLQKAVS 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   144 HAAEDVqvrhalgvvqckdnfygQHSPHTMPVHaelTQKWHAW----------IACNTLASEMESAALFVLGSVRRVRTG 213
Cdd:PRK07115 142 SIIRDK-----------------GLDYWTGTVY---TTNRRFWehdkefkeylYETRAQAIDMETATLFAAGFANNIPTG 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 3323355   214 AvLLVIGNQTRRAQGLE----DIQVHD--TENAIRVAVEAVKLLI 252
Cdd:PRK07115 202 A-LLLISDLPLRPEGVKtkesDNKVTKtyTEEHIEIGIEALKSLR 245
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 8-116 1.41e-07

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: 51.30  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355      8 DCEYHIGLKAS---------DIgHYVILPGDPARSEKIAQHFSHPHKVGHNREYVTytgtLCET----------PVSVMS 68
Cdd:TIGR01719  10 DILYHFGINTSthdfpavfgDV-KFVCMGGTPSRMKAFARYVGAELGLSCGRDYPN----ISERgdrfamykvgPVLCVS 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 3323355     69 TGIGGPSTAIGVEELIHLGAH------TFIRVGTSGGMqpDILAGTVVIATGAI 116
Cdd:TIGR01719  85 HGMGIPSISIMLHELIKLLYYarcknpTFIRIGTSGGI--GVPPGTVVVSSEAV 136
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 34-200 2.44e-07

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: 50.19  E-value: 2.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   34 EKIAQHFSHPHKVGH-NREYvtYTGTLCETPVSVMSTGIGGPSTAIGVEELI-HLGAHTFIRVGTSGGMQPDILAGTVVI 111
Cdd:cd09008  12 APLLELLENVEEETIaGRTF--YEGTLGGKEVVLVQSGIGKVNAAIATQLLIdRFKPDAIINTGVAGGLDPDLKIGDVVI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355  112 AT---------GAIRFEGTSKEYAPVEFPAvpDFTVTAALKHAAEDVQVRHALGVVQCKDNFygqhsPHTMPVHAELTQK 182
Cdd:cd09008  90 ATkvvyhdvdaTAFGYEGGQPPGMPAYFPA--DPELLELAKKAAKELGPKVHTGLIASGDQF-----VASSEKKEELREN 162

                       170
                ....*....|....*...
gi 3323355  183 WHAwiacntLASEMESAA 200
Cdd:cd09008 163 FPA------LAVEMEGAA 174
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 55-146 8.73e-05

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 42.69  E-value: 8.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    55 YTGTLCETPVSVMSTGIGGPSTAIGVEELIH-LGAHTFIRVGTSGGMQPDILAGTVVIATGAIRFEgTSKEYAPVEFPAV 133
Cdd:PRK14697  35 YVGEFMGTEVIVTRCGVGKVNAAACTQTLIHkFDVDAIINTGVAGGLHPDVKVGDIVISTNVTHHD-VSKTQMKNLFPFQ 113

                         90
                 ....*....|...
gi 3323355   134 PDFTVTAALKHAA 146
Cdd:PRK14697 114 EEFIASKELVELA 126
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
49-200 8.86e-05

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 42.42  E-value: 8.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    49 NREYvtYTGTLCETPVSVMSTGIGGPSTAIGVEELI-HLGAHTFIRVGTSGGMQPDILAGTVVIAT---------GAIRF 118
Cdd:PRK05584  30 GREF--YTGTLHGHEVVLVLSGIGKVAAALTATILIeHFKVDAVINTGVAGGLAPGLKVGDVVVADelvqhdvdvTAFGY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355   119 E-----GTskeyaPVEFPAvpDFTVTAALKHAAEDVQVRHALGVVQCKDNFygqhsphtmpVHAELTQKWHAWIACNTLA 193
Cdd:PRK05584 108 PygqvpGL-----PAAFKA--DEKLVALAEKAAKELNLNVHRGLIASGDQF----------IAGAEKVAAIRAEFPDALA 170


                 ....*..
gi 3323355   194 SEMESAA 200
Cdd:PRK05584 171 VEMEGAA 177
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 55-146 5.61e-04

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 40.77  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3323355    55 YTGTLCETPVSVMSTGIGGPSTAIGVEELIH-LGAHTFIRVGTSGGMQPDILAGTVVIATGAIRFEgTSKEYAPVEFPAV 133
Cdd:PRK06698  35 YVGEFMGTEVIVTRCGVGKVNAAACTQTLIHkFDVDAIINTGVAGGLHPDVKVGDIVISTNVTHHD-VSKTQMKNLFPFQ 113

                         90
                 ....*....|...
gi 3323355   134 PDFTVTAALKHAA 146
Cdd:PRK06698 114 EEFIASKELVELA 126
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 52-113 1.97e-03

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: 38.43  E-value: 1.97e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3323355   52 YVTYTGTLCETPVSVMSTGIGGPSTAIGVEELI-HLGAHTFIRVGTSGGMQPDILAGTVVIAT 113
Cdd:cd17877  29 FRFYRGTLGGHPVVLVESGMGKANAARAAQLLLeHFQPDLIISTGFAGGLDPGLAVGDLVIAD 91
 
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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