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Conserved domains on  [gi|281364312|ref|NP_001162855|]
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uncharacterized protein Dmel_CG17224, isoform C [Drosophila melanogaster]

Protein Classification

nucleoside phosphorylase-I family protein; purine-nucleoside phosphorylase( domain architecture ID 10019827)

nucleoside phosphorylase-I family protein| purine-nucleoside phosphorylase catalyzes the phosphorolysis of purine nucleoside to form the corresponding free purine base and pentose-1-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
10-300 9.22e-180

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: 496.98  E-value: 9.22e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312   10 NPHLETARSDYLYHLDINVantrDTSELQNRFGDVRVICMGGTGSRMRQLALYLRDILVVSESGDPVDLCERGNRYAMYK 89
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINT----STHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSCGRDYPNISERGDRFAMYK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312   90 VGPVLCVSHGVGSSSFSVVLHELIKLLKYARCQDPVLLRIGTCGGLGVPPGTVVASKNAFNGLLRNEHEIAILGQRVVRP 169
Cdd:TIGR01719  77 VGPVLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  170 AQFSEDVIRDLLAFGVDANDGFQTISANTMGTDCFYEGQGRTDGAICEYSEKDKMEFLQKCHDLGIRNIEMEASMFASVT 249
Cdd:TIGR01719 157 TQLDEALVQELLLCGAEGLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMT 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281364312  250 QKVGVKAGDVCVTLIDRLKGDQITITIDQKHEFEQRPFFVVGRYIKRLLQQ 300
Cdd:TIGR01719 237 SRAGFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
 
Name Accession Description Interval E-value
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
10-300 9.22e-180

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: 496.98  E-value: 9.22e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312   10 NPHLETARSDYLYHLDINVantrDTSELQNRFGDVRVICMGGTGSRMRQLALYLRDILVVSESGDPVDLCERGNRYAMYK 89
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINT----STHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSCGRDYPNISERGDRFAMYK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312   90 VGPVLCVSHGVGSSSFSVVLHELIKLLKYARCQDPVLLRIGTCGGLGVPPGTVVASKNAFNGLLRNEHEIAILGQRVVRP 169
Cdd:TIGR01719  77 VGPVLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  170 AQFSEDVIRDLLAFGVDANDGFQTISANTMGTDCFYEGQGRTDGAICEYSEKDKMEFLQKCHDLGIRNIEMEASMFASVT 249
Cdd:TIGR01719 157 TQLDEALVQELLLCGAEGLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMT 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281364312  250 QKVGVKAGDVCVTLIDRLKGDQITITIDQKHEFEQRPFFVVGRYIKRLLQQ 300
Cdd:TIGR01719 237 SRAGFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
18-296 1.37e-155

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: 435.42  E-value: 1.37e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  18 SDYLYHLDINVANTrdtsELQNRFGDVRVICMGGTGSRMRQLALYLRDILVVSESGD--PVDLCERGNRYAMYKVGPVLC 95
Cdd:cd17763    1 VDFLYHLGLDTSSH----DLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPAGaaLVNLSKTTDRYSMYKVGPVLS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  96 VSHGVGSSSFSVVLHELIKLLKYARCQDPVLLRIGTCGGLGVPPGTVVASKNAFNGLLRNEHEIAILGQRVVRPAQFSED 175
Cdd:cd17763   77 VSHGMGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 176 VIRDLLAFGVDANDgFQTISANTMGTDCFYEGQGRTDGAICEYSEKDKMEFLQKCHDLGIRNIEMEASMFASVTQKVGVK 255
Cdd:cd17763  157 LAEELLECAKELDD-FPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIK 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 281364312 256 AGDVCVTLIDRLKGDQITITIDQKHEFEQRPFFVVGRYIKR 296
Cdd:cd17763  236 AAVVCVTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
88-275 2.96e-20

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 87.53  E-value: 2.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  88 YKVGPVLCVSHGVGSSSFSVVLHELIKLlkYARcqdpVLLRIGTCGGL--GVPPGTVVASKNA--FNGLLrneHEIAILG 163
Cdd:COG2820   60 YKGKRITVISTGIGGPSAAIAVEELAAL--GAK----TFIRVGTSGALqpDIPVGDLVIATGAvrLDGTS---NFYAPAE 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 164 QrvvrPAQFSEDVIRDLLAFGVDAndGFQTISANTMGTDCFYEGQGRTDGAICEYseKDKMEFLQKchdLGIRNIEMEAS 243
Cdd:COG2820  131 Y----PAVADFELTRALVEAAEEL--GVDYHVGITASTDGFYAEQGRELRVDPDL--DEKLEAWRK---LGVLNVEMETA 199
                        170       180       190
                 ....*....|....*....|....*....|..
gi 281364312 244 MFASVTQKVGVKAGDVCVTLIDRLKGDQITIT 275
Cdd:COG2820  200 ALFTLARLRGHRAGSVLAVSANRVTGEFSKDP 231
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
45-283 1.19e-15

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: 74.69  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312   45 RVICMGGTGSRMRQLALYLRDILvvsESGDPvdlcERGNRYA--MYKVGPVLCVSHGVGSSSFSVVL-HELIKLLKyarc 121
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDET---PVGPP----SRGGKFYtgTLGGVPVVLVRHGIGPPNAAILAaIRLLKEFG---- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  122 qDPVLLRIGTCGGL--GVPPGTVVASKNAFNGLLRNEHEIAILGQRVV--RPAQFSEDVIRdlLAFGVDANDGFQTISAN 197
Cdd:pfam01048  70 -VDAIIRTGTAGGLnpDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPdmAPAPADPELRA--LAKEAAERLGIPVHRGV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  198 TMGTDCFYegqgrtdgaiceYSEKDKMEFLQkchDLGIRNIEMEASMFASVTQKVGVKAGDVCVTLidrlkgDQITITID 277
Cdd:pfam01048 147 YATGDGFY------------FETPAEIRLLR---RLGADAVEMETAAEAQVAREAGIPFAAIRVVS------DLAAGGAD 205

                  ....*.
gi 281364312  278 QKHEFE 283
Cdd:pfam01048 206 GELTHE 211
 
Name Accession Description Interval E-value
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
10-300 9.22e-180

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: 496.98  E-value: 9.22e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312   10 NPHLETARSDYLYHLDINVantrDTSELQNRFGDVRVICMGGTGSRMRQLALYLRDILVVSESGDPVDLCERGNRYAMYK 89
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINT----STHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSCGRDYPNISERGDRFAMYK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312   90 VGPVLCVSHGVGSSSFSVVLHELIKLLKYARCQDPVLLRIGTCGGLGVPPGTVVASKNAFNGLLRNEHEIAILGQRVVRP 169
Cdd:TIGR01719  77 VGPVLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  170 AQFSEDVIRDLLAFGVDANDGFQTISANTMGTDCFYEGQGRTDGAICEYSEKDKMEFLQKCHDLGIRNIEMEASMFASVT 249
Cdd:TIGR01719 157 TQLDEALVQELLLCGAEGLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMT 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281364312  250 QKVGVKAGDVCVTLIDRLKGDQITITIDQKHEFEQRPFFVVGRYIKRLLQQ 300
Cdd:TIGR01719 237 SRAGFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
18-296 1.37e-155

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: 435.42  E-value: 1.37e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  18 SDYLYHLDINVANTrdtsELQNRFGDVRVICMGGTGSRMRQLALYLRDILVVSESGD--PVDLCERGNRYAMYKVGPVLC 95
Cdd:cd17763    1 VDFLYHLGLDTSSH----DLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPAGaaLVNLSKTTDRYSMYKVGPVLS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  96 VSHGVGSSSFSVVLHELIKLLKYARCQDPVLLRIGTCGGLGVPPGTVVASKNAFNGLLRNEHEIAILGQRVVRPAQFSED 175
Cdd:cd17763   77 VSHGMGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 176 VIRDLLAFGVDANDgFQTISANTMGTDCFYEGQGRTDGAICEYSEKDKMEFLQKCHDLGIRNIEMEASMFASVTQKVGVK 255
Cdd:cd17763  157 LAEELLECAKELDD-FPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIK 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 281364312 256 AGDVCVTLIDRLKGDQITITIDQKHEFEQRPFFVVGRYIKR 296
Cdd:cd17763  236 AAVVCVTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
88-275 2.96e-20

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 87.53  E-value: 2.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  88 YKVGPVLCVSHGVGSSSFSVVLHELIKLlkYARcqdpVLLRIGTCGGL--GVPPGTVVASKNA--FNGLLrneHEIAILG 163
Cdd:COG2820   60 YKGKRITVISTGIGGPSAAIAVEELAAL--GAK----TFIRVGTSGALqpDIPVGDLVIATGAvrLDGTS---NFYAPAE 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 164 QrvvrPAQFSEDVIRDLLAFGVDAndGFQTISANTMGTDCFYEGQGRTDGAICEYseKDKMEFLQKchdLGIRNIEMEAS 243
Cdd:COG2820  131 Y----PAVADFELTRALVEAAEEL--GVDYHVGITASTDGFYAEQGRELRVDPDL--DEKLEAWRK---LGVLNVEMETA 199
                        170       180       190
                 ....*....|....*....|....*....|..
gi 281364312 244 MFASVTQKVGVKAGDVCVTLIDRLKGDQITIT 275
Cdd:COG2820  200 ALFTLARLRGHRAGSVLAVSANRVTGEFSKDP 231
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
46-284 5.05e-18

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: 80.80  E-value: 5.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  46 VICMGGTGSRMRQLALYLRDILVVSESgdpvdlcergNRYAMYKVG----PVLCVSHGVGSSSFSVVLHELIKLLkyARc 121
Cdd:cd09005    1 YAIIPGDPERVDVIDSKLENPQKVSSF----------RGYTMYTGKyngkRVTVVNGGMGSPSAAIVVEELCALG--VD- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 122 qdpVLLRIGTCGGLG--VPPGTVVASknafNGLLRNEHeiaILGQRVVRPAqFSEDVIRDLLAFGVDAND--GFQTISAN 197
Cdd:cd09005   68 ---TIIRVGSCGALRedIKVGDLVIA----DGAIRGDG---VTPYYVVGPP-FAPEADPELTAALEEAAKelGLTVHVGT 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 198 TMGTDCFYEGQgrtdgaiceysekdkMEFLQKCHDLGIRNIEMEASMFASVTQKVGVKAGDVCVTLIDRLKGDQITITID 277
Cdd:cd09005  137 VWTTDAFYRET---------------REESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEF 201

                 ....*..
gi 281364312 278 QKHEFEQ 284
Cdd:cd09005  202 LSEAEKK 208
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
92-272 3.92e-17

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: 78.64  E-value: 3.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  92 PVLCVSHGVGSSSFSVVLHELIkllkyaRCQDPVLLRIGTCGGL--GVPPGTVVASknafNGLLRNE---HEIAilgqrv 166
Cdd:cd17767   53 PVSVCSTGIGGPSAAIAVEELA------QLGAKTFIRVGTCGALqpDIKLGDLVIA----TGAVRDEgtsKHYV------ 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 167 vrPAQF----SEDVIRDLLAfgvdandgfqtiSANTMG----------TDCFYEGQGRTDGAIcEYSEKDKMEFLQKchd 232
Cdd:cd17767  117 --PPEYpavaDPEVVLALVE------------AAEELGvpyhvgitasKDSFYGGQGRPGPGL-PPELPELLEEWQR--- 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 281364312 233 LGIRNIEMEASMFASVTQKVGVKAGDVCVTLIDRLKGDQI 272
Cdd:cd17767  179 AGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAP 218
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
45-283 1.19e-15

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: 74.69  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312   45 RVICMGGTGSRMRQLALYLRDILvvsESGDPvdlcERGNRYA--MYKVGPVLCVSHGVGSSSFSVVL-HELIKLLKyarc 121
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDET---PVGPP----SRGGKFYtgTLGGVPVVLVRHGIGPPNAAILAaIRLLKEFG---- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  122 qDPVLLRIGTCGGL--GVPPGTVVASKNAFNGLLRNEHEIAILGQRVV--RPAQFSEDVIRdlLAFGVDANDGFQTISAN 197
Cdd:pfam01048  70 -VDAIIRTGTAGGLnpDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPdmAPAPADPELRA--LAKEAAERLGIPVHRGV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  198 TMGTDCFYegqgrtdgaiceYSEKDKMEFLQkchDLGIRNIEMEASMFASVTQKVGVKAGDVCVTLidrlkgDQITITID 277
Cdd:pfam01048 147 YATGDGFY------------FETPAEIRLLR---RLGADAVEMETAAEAQVAREAGIPFAAIRVVS------DLAAGGAD 205

                  ....*.
gi 281364312  278 QKHEFE 283
Cdd:pfam01048 206 GELTHE 211
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
45-275 2.69e-09

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: 56.08  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  45 RVICMGGTGsRMRQLALYLRDILVVSESgdpvdlceRG-NRY-AMYKVGPVLCVSHGVGSSSFSVVLHELIKLlkYARcq 122
Cdd:cd17764    2 RVIAVGDPG-RVELLSTLLEDPRLVNEN--------RGlLVYtGKYKGEEVTIATHGIGGPSAAIVFEELIML--GAK-- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 123 dpVLLRIGTCGGL--GVPPGTVVASKNA--FNGllrneheiAILGQ---RVVRPAQFSEDVIRDLL-AFgvdANDGFQTI 194
Cdd:cd17764   69 --VIIRLGTAGGLvpELRVGDIVVATGAsyYPG--------GGLGQyfpDVCPPASPDPELTLELVeSL---SKRGLKYY 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 195 SANTMGTDCFyegqgrtdgaiceYSEKDkmEFLQKCHDLGIRNIEMEASMFASVTQKVGVKAGDVCVTLIDRLKGDQITI 274
Cdd:cd17764  136 VGPVFSSDAF-------------YAEDE--EFAERWSSLGFIAVEMECATLFTLGWLRGVKAGAVLVVSDNLVKGGKLML 200

                 .
gi 281364312 275 T 275
Cdd:cd17764  201 T 201
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
125-283 7.35e-08

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: 52.20  E-value: 7.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 125 VLLRIGTCGGLG--VPPGTVVASKNAFnGLLRNEHEIAILGQ--------RVVRPAQFSEDVIRDLLAFGVDANDG---F 191
Cdd:cd17769   74 AIIRLGSCGSLDpdVPVGSVVVPSASV-AVTRNYDDDDFAGPstssekpyLISKPVPADPELSELLESELKASLGGevvV 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 192 QTISANTmgtDCFYEGQGRTDGAICEYSEkDKMEFLQKCHdLGIRNIEMEASMF---ASVTQKVG--VKAGDVCVTLIDR 266
Cdd:cd17769  153 EGLNASA---DSFYSSQGRQDPNFPDHNE-NLIDKLLKRY-PGAASLEMETFHLfhlARCSRPAQgkIRAAAAHMVFANR 227
                        170
                 ....*....|....*..
gi 281364312 267 LKGDqiTITIDQKHEFE 283
Cdd:cd17769  228 TSND--FISPERVHELE 242
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
65-269 3.51e-06

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: 47.47  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  65 DILVVsesGDP--VDL---------CERGNR--YAM---YKVGPVLCVSHGVGSSSFSVVLHEL---------------- 112
Cdd:cd00436   23 TIILV---GDPgrVPKvskhfdsieFKKQNRefVTHtgtYKGKRITVISTGIGTDNIDIVLNELdalvnidfktrtpkee 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 113 IKLLKyarcqdpvLLRIGTCGGL--GVPPGTVVASKNA--FNGLLR------NEHEIAIL---------GQRVVRP--AQ 171
Cdd:cd00436  100 KTSLN--------IIRLGTSGALqpDIPVGSLVISSYAigLDNLLNfydhpnTDEEAELEnafiahtswFKGKPRPyvVK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 172 FSEDVIRDLLafGVDANDGFqTISANtmGtdcFYEGQGR---TDGAICEYSEKdkmefLQKCHDLGIR--NIEMEASMFA 246
Cdd:cd00436  172 ASPELLDALT--GVGYVVGI-TATAP--G---FYGPQGRqlrLPLADPDLLDK-----LSSFSYGGLRitNFEMETSAIY 238
                        250       260
                 ....*....|....*....|...
gi 281364312 247 SVTQKVGVKAGDVCVTLIDRLKG 269
Cdd:cd00436  239 GLSRLLGHRALSICAIIANRATG 261
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
98-260 6.31e-06

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: 46.26  E-value: 6.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  98 HGVGSSSFSVVLHELIKLLkyaRCQDpvLLRIGTCGGL--GVPPGTVVASKNA-----FNGLLRNEHEIAILgqrvvrpA 170
Cdd:COG0813   63 SGMGIPSISIYAYELITEY---GVKN--IIRVGTCGALqeDVKVRDVVIAMGAstdsnVNRQRFGGGDFAPI-------A 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 171 QFsedvirDLLAFGVDAND--GFQTISANTMGTDCFYEgqgrtdgaiceysekDKMEFLQKCHDLGIRNIEMEASMFASV 248
Cdd:COG0813  131 DF------ELLRKAVEAAKelGIKVHVGNVFSSDLFYR---------------EDPDLLEKLAKYGVLAVEMEAAALYTL 189
                        170
                 ....*....|..
gi 281364312 249 TQKVGVKAGDVC 260
Cdd:COG0813  190 AAKYGKRALAIL 201
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
88-275 1.14e-05

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: 45.76  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312  88 YKVGPVLCVSHGVGSSSFSVVLHELIKLLkyARcqdpVLLRIGTCGGL--GVPPG-TVVA-SKNAFNGLLRneheiAILG 163
Cdd:cd17765   52 YKGKPVSVQTTGMGCPSAAIVVEELAQLG--VK----RLIRVGTCGGLssGLQLGdLIVAtAAVPADGTTR-----ALLG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364312 164 QRVVRP-AQFSedvirdLLAFGVDAndgfqtisANTMG----------TDCFYEGQgrtdgaiceysekdkMEFLQKCHD 232
Cdd:cd17765  121 GEPYAPaADFE------LVEALYRA--------ARAAGmpvhvgpvatSDLFYDPT---------------PDGVKRWRR 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 281364312 233 LGIRNIEMEASMFASVTQKVGVKAGDVCvTLIDRLKGDQITIT 275
Cdd:cd17765  172 RGVLAVEMEASALFTLAALRGLRAGCIL-TVSDLIGDPERRID 213
 
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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