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Conserved domains on  [gi|1384008279|ref|NP_001349703|]
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uridine phosphorylase 1 isoform a [Homo sapiens]

Protein Classification

uridine phosphorylase( domain architecture ID 13027119)

uridine phosphorylase catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 31-305 0e+00

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: 511.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  31 EDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCP-GRDYPNICAGTDRYAMYKVGPVLSVSHG 109
Cdd:cd17763     1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 110 MGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQE 189
Cdd:cd17763    81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 190 LLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVC 269
Cdd:cd17763   161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1384008279 270 VTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKK 305
Cdd:cd17763   241 VTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
 
Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 31-305 0e+00

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: 511.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  31 EDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCP-GRDYPNICAGTDRYAMYKVGPVLSVSHG 109
Cdd:cd17763     1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 110 MGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQE 189
Cdd:cd17763    81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 190 LLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVC 269
Cdd:cd17763   161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1384008279 270 VTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKK 305
Cdd:cd17763   241 VTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 23-309 0e+00

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: 504.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  23 NPNIAKMKEDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCpGRDYPNICAGTDRYAMYKVGP 102
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSC-GRDYPNISERGDRFAMYKVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 103 VLSVSHGMGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDL 182
Cdd:TIGR01719  80 VLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 183 NKKLVQELLLCSAE-LSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSAC 261
Cdd:TIGR01719 160 DEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1384008279 262 GLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKKKLSK 309
Cdd:TIGR01719 240 GFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 98-286 1.42e-28

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 110.26  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  98 YKVGPVLSVSHGMGIPSISIMLHELikllyyARCSNVTIIRIGTSGGI--GLEPGTVVITEQAV----------DTCFKA 165
Cdd:COG2820    60 YKGKRITVISTGIGGPSAAIAVEEL------AALGAKTFIRVGTSGALqpDIPVGDLVIATGAVrldgtsnfyaPAEYPA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 166 EFEqivlgkrvirkTDLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDgalcsYTEKDKQAYLEAAYAAGVR 245
Cdd:COG2820   134 VAD-----------FELTRALVE-----AAEELGVDYHVGITASTDGFYAEQGREL-----RVDPDLDEKLEAWRKLGVL 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1384008279 246 NIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRN 286
Cdd:COG2820   193 NVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEE 233
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 54-304 6.90e-24

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: 97.41  E-value: 6.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  54 KFVCVGGSPSRMKAFIRCVGAELGldcpgrdYPNICAGTDRYA-MYKVGPVLSVSHGMGIPSISIML-HELIKLLyyarc 131
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETP-------VGPPSRGGKFYTgTLGGVPVVLVRHGIGPPNAAILAaIRLLKEF----- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 132 sNV-TIIRIGTSGGI--GLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTD--LNKKLVQELLLCSAELsEFTTVVGN 206
Cdd:pfam01048  69 -GVdAIIRTGTAGGLnpDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPapADPELRALAKEAAERL-GIPVHRGV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 207 TMCTLDFYEGQgrldgalcsytekdkQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVtLLNRLEGD-----QI 281
Cdd:pfam01048 147 YATGDGFYFET---------------PAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGadgelTH 210

                         250       260
                  ....*....|....*....|...
gi 1384008279 282 SSPRNVLSEYQQRPQRLVSYFIK 304
Cdd:pfam01048 211 EEVEEFAERAAERAAALLLALLA 233
PRK11178 PRK11178
uridine phosphorylase; Provisional
 102-275 5.87e-11

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 61.60  E-value: 5.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 102 PVLSVSHGMGIPSISIMLHELIKLlyyarcsNV-TIIRIGTSGGI--GLEPGTVVITEQAVdTCFKAEFEQIVLGKRVIR 178
Cdd:PRK11178   59 PVIVCSTGIGGPSTSIAVEELAQL-------GVrTFLRIGTTGAIqpHINVGDVLVTTASV-RLDGASLHFAPLEFPAVA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 179 KTDLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDgALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMC 258
Cdd:PRK11178  131 DFECTTALVE-----AAKSIGATTHVGVTASSDTFYPGQERYD-TYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMC 204

                         170
                  ....*....|....*..
gi 1384008279 259 SACGLQAAVVCVTLLNR 275
Cdd:PRK11178  205 ASQGLRAGMVAGVIVNR 221
 
Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 31-305 0e+00

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: 511.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  31 EDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCP-GRDYPNICAGTDRYAMYKVGPVLSVSHG 109
Cdd:cd17763     1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 110 MGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQE 189
Cdd:cd17763    81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 190 LLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVC 269
Cdd:cd17763   161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1384008279 270 VTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKK 305
Cdd:cd17763   241 VTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 23-309 0e+00

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: 504.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  23 NPNIAKMKEDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCpGRDYPNICAGTDRYAMYKVGP 102
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSC-GRDYPNISERGDRFAMYKVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 103 VLSVSHGMGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDL 182
Cdd:TIGR01719  80 VLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 183 NKKLVQELLLCSAE-LSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSAC 261
Cdd:TIGR01719 160 DEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1384008279 262 GLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKKKLSK 309
Cdd:TIGR01719 240 GFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 55-302 1.05e-46

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: 156.68  E-value: 1.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  55 FVCVGGSPSRMKAFircvgaelglDCPGRDYPNICAGtDRYAMYKVG----PVLSVSHGMGIPSISIMLHELIKLLyyar 130
Cdd:cd09005     1 YAIIPGDPERVDVI----------DSKLENPQKVSSF-RGYTMYTGKyngkRVTVVNGGMGSPSAAIVVEELCALG---- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 131 csNVTIIRIGTSGGIGLE--PGTVVITEQAVDTCFKAEFEqivlGKRVIRKTDLNKKLVQELLLCSAELsEFTTVVGNTM 208
Cdd:cd09005    66 --VDTIIRVGSCGALREDikVGDLVIADGAIRGDGVTPYY----VVGPPFAPEADPELTAALEEAAKEL-GLTVHVGTVW 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 209 CTLDFYEGQgrldgalcsytekdkQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDqISSPRNVL 288
Cdd:cd09005   139 TTDAFYRET---------------REESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGE-IGFVDEFL 202

                         250
                  ....*....|....
gi 1384008279 289 SEYQQRPQRLVSYF 302
Cdd:cd09005   203 SEAEKKAIEIALDA 216
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 98-286 1.42e-28

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 110.26  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  98 YKVGPVLSVSHGMGIPSISIMLHELikllyyARCSNVTIIRIGTSGGI--GLEPGTVVITEQAV----------DTCFKA 165
Cdd:COG2820    60 YKGKRITVISTGIGGPSAAIAVEEL------AALGAKTFIRVGTSGALqpDIPVGDLVIATGAVrldgtsnfyaPAEYPA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 166 EFEqivlgkrvirkTDLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDgalcsYTEKDKQAYLEAAYAAGVR 245
Cdd:COG2820   134 VAD-----------FELTRALVE-----AAEELGVDYHVGITASTDGFYAEQGREL-----RVDPDLDEKLEAWRKLGVL 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1384008279 246 NIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRN 286
Cdd:COG2820   193 NVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEE 233
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 54-304 6.90e-24

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: 97.41  E-value: 6.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  54 KFVCVGGSPSRMKAFIRCVGAELGldcpgrdYPNICAGTDRYA-MYKVGPVLSVSHGMGIPSISIML-HELIKLLyyarc 131
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETP-------VGPPSRGGKFYTgTLGGVPVVLVRHGIGPPNAAILAaIRLLKEF----- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 132 sNV-TIIRIGTSGGI--GLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTD--LNKKLVQELLLCSAELsEFTTVVGN 206
Cdd:pfam01048  69 -GVdAIIRTGTAGGLnpDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPapADPELRALAKEAAERL-GIPVHRGV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 207 TMCTLDFYEGQgrldgalcsytekdkQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVtLLNRLEGD-----QI 281
Cdd:pfam01048 147 YATGDGFYFET---------------PAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGadgelTH 210

                         250       260
                  ....*....|....*....|...
gi 1384008279 282 SSPRNVLSEYQQRPQRLVSYFIK 304
Cdd:pfam01048 211 EEVEEFAERAAERAAALLLALLA 233
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 102-281 5.69e-22

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: 92.12  E-value: 5.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 102 PVLSVSHGMGIPSISIMLHELIkllyyaRCSNVTIIRIGTSGGI--GLEPGTVVITEQAV----------DTCFKAefeq 169
Cdd:cd17767    53 PVSVCSTGIGGPSAAIAVEELA------QLGAKTFIRVGTCGALqpDIKLGDLVIATGAVrdegtskhyvPPEYPA---- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 170 ivlgkrvIRKTDLNKKLVQelllcSAELSEFTTVVGnTMCTLD-FYEGQGRLDgalcSYTEKDKQAYLEAAYAAGVRNIE 248
Cdd:cd17767   123 -------VADPEVVLALVE-----AAEELGVPYHVG-ITASKDsFYGGQGRPG----PGLPPELPELLEEWQRAGVLNSE 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1384008279 249 MESSVFAAMCSACGLQAAVVCVTLLNRLEGDQI 281
Cdd:cd17767   186 MESAALFTLASLRGVRAGAVLAVVGNRVTDEAP 218
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 106-278 4.49e-17

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: 79.44  E-value: 4.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 106 VSHGMGIPSISIMLHEL------------IKllyyARCSNVTIIRIGTSGGI--GLEPGTVVITEQAV--DTC-----FK 164
Cdd:cd00436    67 ISTGIGTDNIDIVLNELdalvnidfktrtPK----EEKTSLNIIRLGTSGALqpDIPVGSLVISSYAIglDNLlnfydHP 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 165 AEFEQIVLGKRVIRKTDLNKKLVQ--------ELLlcsAELSEFTTVVGNTMCTLDFYEGQGR----------LDGALCS 226
Cdd:cd00436   143 NTDEEAELENAFIAHTSWFKGKPRpyvvkaspELL---DALTGVGYVVGITATAPGFYGPQGRqlrlpladpdLLDKLSS 219

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1384008279 227 YTEKDKQayleaayaagVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEG 278
Cdd:cd00436   220 FSYGGLR----------ITNFEMETSAIYGLSRLLGHRALSICAIIANRATG 261
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 97-269 1.33e-12

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: 65.89  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  97 MYKVGPVlSV-SHGMGIPSISIMLHELIKllYYarcsNV-TIIRIGTSGGIG--LEPGTVVITEQA-------------V 159
Cdd:cd09006    48 TYKGKRV-SVmGSGMGMPSIGIYAYELFK--FY----GVkNIIRIGTCGAYQpdLKLRDVVLAMGAstdsnynrlrfggG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 160 DTCFKAEFEqivlgkrvirktdLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEgqgrldgalcsytekDKQAYLEAA 239
Cdd:cd09006   121 DFAPIADFE-------------LLRKAVE-----TAKELGIPVHVGNVFSSDVFYD---------------DDPELWKKL 167

                         170       180       190
                  ....*....|....*....|....*....|
gi 1384008279 240 YAAGVRNIEMESSVFAAMCSACGLQAAVVC 269
Cdd:cd09006   168 KKYGVLAVEMEAAALYTNAARLGKKALAIL 197
PRK11178 PRK11178
uridine phosphorylase; Provisional
 102-275 5.87e-11

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 61.60  E-value: 5.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 102 PVLSVSHGMGIPSISIMLHELIKLlyyarcsNV-TIIRIGTSGGI--GLEPGTVVITEQAVdTCFKAEFEQIVLGKRVIR 178
Cdd:PRK11178   59 PVIVCSTGIGGPSTSIAVEELAQL-------GVrTFLRIGTTGAIqpHINVGDVLVTTASV-RLDGASLHFAPLEFPAVA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 179 KTDLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDgALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMC 258
Cdd:PRK11178  131 DFECTTALVE-----AAKSIGATTHVGVTASSDTFYPGQERYD-TYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMC 204

                         170
                  ....*....|....*..
gi 1384008279 259 SACGLQAAVVCVTLLNR 275
Cdd:PRK11178  205 ASQGLRAGMVAGVIVNR 221
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 98-269 1.62e-10

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: 60.13  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  98 YKVGPVlSV-SHGMGIPSISIMLHELIKllYYarcsNV-TIIRIGTSGGI--GLEPGTVVI-----TEQAVDtcfkaefE 168
Cdd:COG0813    53 YKGKRV-SVmGSGMGIPSISIYAYELIT--EY----GVkNIIRVGTCGALqeDVKVRDVVIamgasTDSNVN-------R 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 169 QIVLGKRVIRKTD--LNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEgqgrldgalcsyTEKDKQAYLeAAYaaGVRN 246
Cdd:COG0813   119 QRFGGGDFAPIADfeLLRKAVE-----AAKELGIKVHVGNVFSSDLFYR------------EDPDLLEKL-AKY--GVLA 178

                         170       180
                  ....*....|....*....|...
gi 1384008279 247 IEMESSVFAAMCSACGLQAAVVC 269
Cdd:COG0813   179 VEMEAAALYTLAAKYGKRALAIL 201
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 98-290 1.80e-08

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: 54.23  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  98 YKVGPVlSV-SHGMGIPSISIMLHELIKLLyyARcsnvTIIRIGTSGGI--GLEPGTVVITEQAV--DTCFKAEFEQIvl 172
Cdd:cd17765    52 YKGKPV-SVqTTGMGCPSAAIVVEELAQLG--VK----RLIRVGTCGGLssGLQLGDLIVATAAVpaDGTTRALLGGE-- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 173 GKRVIRKTDLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYtekdkqayleaayaaGVRNIEMESS 252
Cdd:cd17765   123 PYAPAADFELVEALYR-----AARAAGMPVHVGPVATSDLFYDPTPDGVKRWRRR---------------GVLAVEMEAS 182

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1384008279 253 VFAAMCSACGLQAAVVCvTLLNRLEGDQISSPRNVLSE 290
Cdd:cd17765   183 ALFTLAALRGLRAGCIL-TVSDLIGDPERRIDDEELRA 219
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
97-145 8.25e-08

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 52.17  E-value: 8.25e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1384008279  97 MYKvGPVLSV-SHGMGIPSISIMLHELIKllYYarcsNV-TIIRIGTSGGI 145
Cdd:PRK05819   51 TYK-GKRVSVmGTGMGIPSISIYANELIT--DY----GVkKLIRVGSCGAL 94
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 98-158 8.50e-08

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: 51.84  E-value: 8.50e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1384008279  98 YKVGPVLSVSHGMGIPSISIMLHELIKLlyYARcsnvTIIRIGTSGGI--GLEPGTVVITEQA 158
Cdd:cd17764    38 YKGEEVTIATHGIGGPSAAIVFEELIML--GAK----VIIRLGTAGGLvpELRVGDIVVATGA 94
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 97-282 2.43e-06

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: 47.96  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279  97 MYKVGPVLSVSHGMGIPSISIMLHElikllyyarCSNVT-----IIRIGTSGGIG--LEPGTVVITEQAV-------DTC 162
Cdd:cd17769    40 RYKGVPVSIVAIGMGAPMMDFFVRE---------ARAVVdgpmaIIRLGSCGSLDpdVPVGSVVVPSASVavtrnydDDD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384008279 163 FKAEFEQIV----LGKRVIRKTDLNKKLVQELLLCSAELSEFTTVVGnTMCTldFYEGQGRLDGalcSYTEKDKQ--AYL 236
Cdd:cd17769   111 FAGPSTSSEkpylISKPVPADPELSELLESELKASLGGEVVVEGLNA-SADS--FYSSQGRQDP---NFPDHNENliDKL 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1384008279 237 EAAYaAGVRNIEMESSVF---AAMCSACG--LQAAVVCVTLLNRLEGDQIS 282
Cdd:cd17769   185 LKRY-PGAASLEMETFHLfhlARCSRPAQgkIRAAAAHMVFANRTSNDFIS 234
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
98-145 9.68e-05

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 42.78  E-value: 9.68e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1384008279  98 YKvGPVLSV-SHGMGIPSISIMLHELIKLLYYARcsnvtIIRIGTSGGI 145
Cdd:PRK13374   53 YK-GKKVSVmGHGMGIPSMVIYVHELIATFGVKN-----IIRVGSCGAT 95
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 98-145 2.11e-04

purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called inosine phosphorylase) is a purine salvage enzyme. Purine nucleosides, such as guanosine, inosine, or xanthosine, plus orthophosphate, can be converted to their respective purine bases (guanine, hypoxanthine, or xanthine) plus ribose-1-phosphate. This family of purine nucleoside phosphorylase is restricted to the bacteria. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 188024  Cd Length: 232  Bit Score: 42.07  E-value: 2.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1384008279  98 YKVGPVLSVSHGMGIPSISIMLHELIKlLYYARcsnvTIIRIGTSGGI 145
Cdd:TIGR00107  49 YKGKKISVMGHGMGIPSISIYVYELIK-FYEVK----TIIRVGSCGAI 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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