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Conserved domains on  [gi|37538021|sp|O95045|]
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RecName: Full=Uridine phosphorylase 2; Short=UPase 2; Short=UrdPase 2

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 ...
37-311 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: 501.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021  37 EDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFALFMHKELGFEE-AEEDIKDICAGTDRYCMYKTGPVLAISHG 115
Cdd:cd17763   1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLpAGAALVNLSKTTDRYSMYKVGPVLSVSHG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 116 MGIPSISIMLHELIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRFEQVILDNIVTRSTELDKELSEE 195
Cdd:cd17763  81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 196 LFNCSKEIPNFPTLVGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAFKAGVRNIEMESTVFAAMCGLCGLKAAVVC 275
Cdd:cd17763 161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 37538021 276 VTLLDRLDCDQINLPHDVLVEYQQRPQLLISNFIRR 311
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 ...
37-311 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: 501.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021  37 EDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFALFMHKELGFEE-AEEDIKDICAGTDRYCMYKTGPVLAISHG 115
Cdd:cd17763   1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLpAGAALVNLSKTTDRYSMYKVGPVLSVSHG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 116 MGIPSISIMLHELIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRFEQVILDNIVTRSTELDKELSEE 195
Cdd:cd17763  81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 196 LFNCSKEIPNFPTLVGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAFKAGVRNIEMESTVFAAMCGLCGLKAAVVC 275
Cdd:cd17763 161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 37538021 276 VTLLDRLDCDQINLPHDVLVEYQQRPQLLISNFIRR 311
Cdd:cd17763 241 VTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
29-314 2.60e-143

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: 405.68  E-value: 2.60e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021    29 NPYLDLMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFALFMHKELGFEEAEeDIKDICAGTDRYCMYKTGP 108
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSCGR-DYPNISERGDRFAMYKVGP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   109 VLAISHGMGIPSISIMLHELIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRFEQVILDNIVTRSTEL 188
Cdd:TIGR01719  80 VLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   189 DKELSEELFNCSKE-IPNFPTLVGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAFKAGVRNIEMESTVFAAMCGLC 267
Cdd:TIGR01719 160 DEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 37538021   268 GLKAAVVCVTLLDRLDCDQINLPHDVLVEYQQRPQLLISNFIRRRLG 314
Cdd:TIGR01719 240 GFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLS 286
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
36-292 6.41e-26

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 103.32  E-value: 6.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021  36 DEDILYHLDLGtkthnlPAMFGDVKFVCvgGSPNRMKAFALFmhkelgFEEAEedikdiCAGTDR-YCMYkTG-----PV 109
Cdd:COG2820   7 PDGSQYHLGLK------PGDVADYVILP--GDPGRVELIASY------LDDVE------LVAENReFRTY-TGtykgkRI 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 110 LAISHGMGIPSISIMLHELIKLlhHARccdvTIIRIGTSGGI--GIAPGTVVITDIAVdsffkpRFEQ-----VILDNIV 182
Cdd:COG2820  66 TVISTGIGGPSAAIAVEELAAL--GAK----TFIRVGTSGALqpDIPVGDLVIATGAV------RLDGtsnfyAPAEYPA 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 183 TRSTELDKELSEELfncskEIPNFPTLVGHTMCTYDFYEGQGRLDGALCSFsrEKKLDYLKrafKAGVRNIEMESTVFAA 262
Cdd:COG2820 134 VADFELTRALVEAA-----EELGVDYHVGITASTDGFYAEQGRELRVDPDL--DEKLEAWR---KLGVLNVEMETAALFT 203
                       250       260       270
                ....*....|....*....|....*....|
gi 37538021 263 MCGLCGLKAAVVCVTLLDRLDCDQINLPHD 292
Cdd:COG2820 204 LARLRGHRAGSVLAVSANRVTGEFSKDPEE 233
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
60-310 1.36e-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: 99.34  E-value: 1.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021    60 KFVCVGGSPNRMKAFALFMHKELGFEeaeedikDICAGTDRY-CMYKTGPVLAISHGMGIPSISIMlhELIKLLHHARCc 138
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVG-------PPSRGGKFYtGTLGGVPVVLVRHGIGPPNAAIL--AAIRLLKEFGV- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   139 dVTIIRIGTSGGI--GIAPGTVVITDIAVD-----SFFKPRFEQVILDnivTRSTELDKELSEELFNCSKEIpNFPTLVG 211
Cdd:pfam01048  71 -DAIIRTGTAGGLnpDLKVGDVVIPTDAINhdgrsPLFGPEGGPYFPD---MAPAPADPELRALAKEAAERL-GIPVHRG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   212 HTMCTYDFYegqgrldgalcsFSREKKLDYLKRAfkaGVRNIEMESTVFAAMCGLCGLKAAVVCVtLLDRLDCD-----Q 286
Cdd:pfam01048 146 VYATGDGFY------------FETPAEIRLLRRL---GADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGadgelT 209
                         250       260
                  ....*....|....*....|....
gi 37538021   287 INLPHDVLVEYQQRPQLLISNFIR 310
Cdd:pfam01048 210 HEEVEEFAERAAERAAALLLALLA 233
PRK11178 PRK11178
uridine phosphorylase; Provisional
41-281 1.17e-12

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 66.60  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   41 YHLDLgTKthnlpAMFGDVKFVCVGGSPNRMKAFALFM--------HKELGFEEAEEDIKdicagtdrycmyktgPVLAI 112
Cdd:PRK11178   5 FHLGL-TK-----ADLQGATLAIVPGDPERVEKIAALMdnpvflasHREFTSWRAELDGK---------------PVIVC 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021  113 SHGMGIPSISIMLHELIKLLHHarccdvTIIRIGTSGGI--GIAPGTVVITDIAV-----DSFFKP-RFEQVIldnivtr 184
Cdd:PRK11178  64 STGIGGPSTSIAVEELAQLGVR------TFLRIGTTGAIqpHINVGDVLVTTASVrldgaSLHFAPlEFPAVA------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021  185 stelDKELSEELFNCSKEIpNFPTLVGHTMCTYDFYEGQGRLDgalcSFSrekklDYLKRAFKA--------GVRNIEME 256
Cdd:PRK11178 131 ----DFECTTALVEAAKSI-GATTHVGVTASSDTFYPGQERYD----TYS-----GRVVRRFKGsmeewqamGVMNYEME 196
                        250       260
                 ....*....|....*....|....*
gi 37538021  257 STVFAAMCGLCGLKAAVVCVTLLDR 281
Cdd:PRK11178 197 SATLLTMCASQGLRAGMVAGVIVNR 221
 
Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
37-311 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: 501.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021  37 EDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFALFMHKELGFEE-AEEDIKDICAGTDRYCMYKTGPVLAISHG 115
Cdd:cd17763   1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLpAGAALVNLSKTTDRYSMYKVGPVLSVSHG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 116 MGIPSISIMLHELIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRFEQVILDNIVTRSTELDKELSEE 195
Cdd:cd17763  81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 196 LFNCSKEIPNFPTLVGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAFKAGVRNIEMESTVFAAMCGLCGLKAAVVC 275
Cdd:cd17763 161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 37538021 276 VTLLDRLDCDQINLPHDVLVEYQQRPQLLISNFIRR 311
Cdd:cd17763 241 VTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
29-314 2.60e-143

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: 405.68  E-value: 2.60e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021    29 NPYLDLMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFALFMHKELGFEEAEeDIKDICAGTDRYCMYKTGP 108
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSCGR-DYPNISERGDRFAMYKVGP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   109 VLAISHGMGIPSISIMLHELIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRFEQVILDNIVTRSTEL 188
Cdd:TIGR01719  80 VLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   189 DKELSEELFNCSKE-IPNFPTLVGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAFKAGVRNIEMESTVFAAMCGLC 267
Cdd:TIGR01719 160 DEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 37538021   268 GLKAAVVCVTLLDRLDCDQINLPHDVLVEYQQRPQLLISNFIRRRLG 314
Cdd:TIGR01719 240 GFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLS 286
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
61-308 8.73e-36

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: 128.56  E-value: 8.73e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021  61 FVCVGGSPNRMKAFALFmhkelgFEEAEEdikdICAGtDRYCMYkTG-----PVLAISHGMGIPSISIMLHELIKLlhha 135
Cdd:cd09005   1 YAIIPGDPERVDVIDSK------LENPQK----VSSF-RGYTMY-TGkyngkRVTVVNGGMGSPSAAIVVEELCAL---- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 136 rCCDvTIIRIGTSGGIG--IAPGTVVITDIAVDSFFKPRFEQVILDnivtRSTELDKELSEELFNCSKEIpNFPTLVGHT 213
Cdd:cd09005  65 -GVD-TIIRVGSCGALRedIKVGDLVIADGAIRGDGVTPYYVVGPP----FAPEADPELTAALEEAAKEL-GLTVHVGTV 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 214 MCTYDFYEGQGrldgalcsfsrekklDYLKRAFKAGVRNIEMESTVFAAMCGLCGLKAAVVCVTlLDRLDCDQINLPHDV 293
Cdd:cd09005 138 WTTDAFYRETR---------------EESEKLRKLGALAVEMETSALATLAHLRGVKAASILAV-SDNLITGEIGFVDEF 201
                       250
                ....*....|....*
gi 37538021 294 LVEYQQRPQLLISNF 308
Cdd:cd09005 202 LSEAEKKAIEIALDA 216
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
36-292 6.41e-26

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 103.32  E-value: 6.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021  36 DEDILYHLDLGtkthnlPAMFGDVKFVCvgGSPNRMKAFALFmhkelgFEEAEedikdiCAGTDR-YCMYkTG-----PV 109
Cdd:COG2820   7 PDGSQYHLGLK------PGDVADYVILP--GDPGRVELIASY------LDDVE------LVAENReFRTY-TGtykgkRI 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 110 LAISHGMGIPSISIMLHELIKLlhHARccdvTIIRIGTSGGI--GIAPGTVVITDIAVdsffkpRFEQ-----VILDNIV 182
Cdd:COG2820  66 TVISTGIGGPSAAIAVEELAAL--GAK----TFIRVGTSGALqpDIPVGDLVIATGAV------RLDGtsnfyAPAEYPA 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 183 TRSTELDKELSEELfncskEIPNFPTLVGHTMCTYDFYEGQGRLDGALCSFsrEKKLDYLKrafKAGVRNIEMESTVFAA 262
Cdd:COG2820 134 VADFELTRALVEAA-----EELGVDYHVGITASTDGFYAEQGRELRVDPDL--DEKLEAWR---KLGVLNVEMETAALFT 203
                       250       260       270
                ....*....|....*....|....*....|
gi 37538021 263 MCGLCGLKAAVVCVTLLDRLDCDQINLPHD 292
Cdd:COG2820 204 LARLRGHRAGSVLAVSANRVTGEFSKDPEE 233
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
60-310 1.36e-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: 99.34  E-value: 1.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021    60 KFVCVGGSPNRMKAFALFMHKELGFEeaeedikDICAGTDRY-CMYKTGPVLAISHGMGIPSISIMlhELIKLLHHARCc 138
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVG-------PPSRGGKFYtGTLGGVPVVLVRHGIGPPNAAIL--AAIRLLKEFGV- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   139 dVTIIRIGTSGGI--GIAPGTVVITDIAVD-----SFFKPRFEQVILDnivTRSTELDKELSEELFNCSKEIpNFPTLVG 211
Cdd:pfam01048  71 -DAIIRTGTAGGLnpDLKVGDVVIPTDAINhdgrsPLFGPEGGPYFPD---MAPAPADPELRALAKEAAERL-GIPVHRG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   212 HTMCTYDFYegqgrldgalcsFSREKKLDYLKRAfkaGVRNIEMESTVFAAMCGLCGLKAAVVCVtLLDRLDCD-----Q 286
Cdd:pfam01048 146 VYATGDGFY------------FETPAEIRLLRRL---GADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGadgelT 209
                         250       260
                  ....*....|....*....|....
gi 37538021   287 INLPHDVLVEYQQRPQLLISNFIR 310
Cdd:pfam01048 210 HEEVEEFAERAAERAAALLLALLA 233
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
41-289 5.91e-24

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: 97.51  E-value: 5.91e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021  41 YHLDLGTkthnlpamfGDV-KFVCVGGSPNRMKAFALFmhkelgFEEAEEdikdicAGTDRycMYKTG-------PVLAI 112
Cdd:cd17767   1 YHIGLKP---------GDVaPYVLLPGDPGRVERIAEL------LDDAEE------VADNR--EYRTYtgtykgvPVSVC 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 113 SHGMGIPSISIMLHELIKLlhHARccdvTIIRIGTSGGI--GIAPGTVVITDIAVdsffkpRFEQVildnivtrSTEL-- 188
Cdd:cd17767  58 STGIGGPSAAIAVEELAQL--GAK----TFIRVGTCGALqpDIKLGDLVIATGAV------RDEGT--------SKHYvp 117
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 189 -------DKELSEELFNCSKEIpNFPTLVGhTMCTYD-FYEGQGRLDGALCSFSREkKLDYLKRafkAGVRNIEME-STV 259
Cdd:cd17767 118 peypavaDPEVVLALVEAAEEL-GVPYHVG-ITASKDsFYGGQGRPGPGLPPELPE-LLEEWQR---AGVLNSEMEsAAL 191
                       250       260       270
                ....*....|....*....|....*....|
gi 37538021 260 FaAMCGLCGLKAAVVCVTLLDRLDCDQINL 289
Cdd:cd17767 192 F-TLASLRGVRAGAVLAVVGNRVTDEAPDE 220
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
104-281 6.67e-14

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: 70.58  E-value: 6.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 104 YKTGPVLAISHGMGIPSISIMLHEL------------IKLLHHArccdVTIIRIGTSGGI--GIAPGTVVITDIAV--DS 167
Cdd:cd00436  59 YKGKRITVISTGIGTDNIDIVLNELdalvnidfktrtPKEEKTS----LNIIRLGTSGALqpDIPVGSLVISSYAIglDN 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 168 F-----FKPRFEQVILDNIVTRSTELDKEL--------SEELFNCskeIPNFPTLVGHTMCTYDFYEGQGR--------- 225
Cdd:cd00436 135 LlnfydHPNTDEEAELENAFIAHTSWFKGKprpyvvkaSPELLDA---LTGVGYVVGITATAPGFYGPQGRqlrlpladp 211
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37538021 226 -LDGALCSFSREkkldylkrafkaGVR--NIEMEStvfAAMCGLCGL---KAAVVCVTLLDR 281
Cdd:cd00436 212 dLLDKLSSFSYG------------GLRitNFEMET---SAIYGLSRLlghRALSICAIIANR 258
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
103-275 1.15e-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: 66.27  E-value: 1.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 103 MYKTGPVLAISHGMGIPSISIMLHELIKllHHarccDV-TIIRIGTSGGIG--IAPGTVVITDIAV-DSFFkprfeQVIL 178
Cdd:cd09006  48 TYKGKRVSVMGSGMGMPSIGIYAYELFK--FY----GVkNIIRIGTCGAYQpdLKLRDVVLAMGAStDSNY-----NRLR 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 179 DNIVTRSTELDKELSEELFNCSKEIpNFPTLVGHTMCTYDFYegqgrldgalcsfsrEKKLDYLKRAFKAGVRNIEMEST 258
Cdd:cd09006 117 FGGGDFAPIADFELLRKAVETAKEL-GIPVHVGNVFSSDVFY---------------DDDPELWKKLKKYGVLAVEMEAA 180
                       170
                ....*....|....*..
gi 37538021 259 VFAAMCGLCGLKAAVVC 275
Cdd:cd09006 181 ALYTNAARLGKKALAIL 197
PRK11178 PRK11178
uridine phosphorylase; Provisional
41-281 1.17e-12

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 66.60  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   41 YHLDLgTKthnlpAMFGDVKFVCVGGSPNRMKAFALFM--------HKELGFEEAEEDIKdicagtdrycmyktgPVLAI 112
Cdd:PRK11178   5 FHLGL-TK-----ADLQGATLAIVPGDPERVEKIAALMdnpvflasHREFTSWRAELDGK---------------PVIVC 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021  113 SHGMGIPSISIMLHELIKLLHHarccdvTIIRIGTSGGI--GIAPGTVVITDIAV-----DSFFKP-RFEQVIldnivtr 184
Cdd:PRK11178  64 STGIGGPSTSIAVEELAQLGVR------TFLRIGTTGAIqpHINVGDVLVTTASVrldgaSLHFAPlEFPAVA------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021  185 stelDKELSEELFNCSKEIpNFPTLVGHTMCTYDFYEGQGRLDgalcSFSrekklDYLKRAFKA--------GVRNIEME 256
Cdd:PRK11178 131 ----DFECTTALVEAAKSI-GATTHVGVTASSDTFYPGQERYD----TYS-----GRVVRRFKGsmeewqamGVMNYEME 196
                        250       260
                 ....*....|....*....|....*
gi 37538021  257 STVFAAMCGLCGLKAAVVCVTLLDR 281
Cdd:PRK11178 197 SATLLTMCASQGLRAGMVAGVIVNR 221
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
104-294 2.26e-11

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: 62.71  E-value: 2.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 104 YKTGPVLAISHGMGIPSISIMLHELIKLLhhARccdvTIIRIGTSGGI--GIAPGTVVITDIAVDSFFKPRfeqvILDNI 181
Cdd:cd17765  52 YKGKPVSVQTTGMGCPSAAIVVEELAQLG--VK----RLIRVGTCGGLssGLQLGDLIVATAAVPADGTTR----ALLGG 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 182 VTRSTELDKELSEELFNCSKEIpNFPTLVGHTMCTYDFYEGQgrldgalcsfsrekkLDYLKRAFKAGVRNIEMESTVFA 261
Cdd:cd17765 122 EPYAPAADFELVEALYRAARAA-GMPVHVGPVATSDLFYDPT---------------PDGVKRWRRRGVLAVEMEASALF 185
                       170       180       190
                ....*....|....*....|....*....|...
gi 37538021 262 AMCGLCGLKAAVVCvTLLDRLDCDQINLPHDVL 294
Cdd:cd17765 186 TLAALRGLRAGCIL-TVSDLIGDPERRIDDEEL 217
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
104-275 1.30e-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: 60.51  E-value: 1.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 104 YKTGPVLAISHGMGIPSISIMLHELIKLLhharccDV-TIIRIGTSGGI--GIAPGTVVITDIAV-DS-FFKPRFEQVIL 178
Cdd:COG0813  53 YKGKRVSVMGSGMGIPSISIYAYELITEY------GVkNIIRVGTCGALqeDVKVRDVVIAMGAStDSnVNRQRFGGGDF 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 179 dnivtrSTELDKELSEELFNCSKEIpNFPTLVGHTMCTYDFYegqgrldgalcsfsrEKKLDYLKRAFKAGVRNIEMEST 258
Cdd:COG0813 127 ------APIADFELLRKAVEAAKEL-GIKVHVGNVFSSDLFY---------------REDPDLLEKLAKYGVLAVEMEAA 184
                       170
                ....*....|....*..
gi 37538021 259 VFAAMCGLCGLKAAVVC 275
Cdd:COG0813 185 ALYTLAAKYGKRALAIL 201
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
103-257 3.95e-10

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: 59.13  E-value: 3.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 103 MYKTGPVLAISHGMGIPSISIMLHElikllhhARCC---DVTIIRIGTSGGIG--IAPGTVVITDIAV-------DSFFK 170
Cdd:cd17769  40 RYKGVPVSIVAIGMGAPMMDFFVRE-------ARAVvdgPMAIIRLGSCGSLDpdVPVGSVVVPSASVavtrnydDDDFA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 171 PRFEQV----ILDNIVTRSTELDKELSEELFNCSKEIPNFPTLVGhTMCTydFYEGQGRLDGalcSF--SREKKLDYLKR 244
Cdd:cd17769 113 GPSTSSekpyLISKPVPADPELSELLESELKASLGGEVVVEGLNA-SADS--FYSSQGRQDP---NFpdHNENLIDKLLK 186
                       170
                ....*....|...
gi 37538021 245 AFKaGVRNIEMES 257
Cdd:cd17769 187 RYP-GAASLEMET 198
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
104-277 3.09e-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: 53.38  E-value: 3.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 104 YKTGPVLAISHGMGIPSISIMLHELIKLlhHARccdvTIIRIGTSGGI--GIAPGTVVitdIAVDSFFKP--RFEQVILD 179
Cdd:cd17764  38 YKGEEVTIATHGIGGPSAAIVFEELIML--GAK----VIIRLGTAGGLvpELRVGDIV---VATGASYYPggGLGQYFPD 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021 180 NIVTRST--ELDKELSEELfncSKEipNFPTLVGHTMCTYDFYEgqgrldgalcsfsrEKKlDYLKRAFKAGVRNIEMES 257
Cdd:cd17764 109 VCPPASPdpELTLELVESL---SKR--GLKYYVGPVFSSDAFYA--------------EDE-EFAERWSSLGFIAVEMEC 168
                       170       180
                ....*....|....*....|
gi 37538021 258 TVFAAMCGLCGLKAAVVCVT 277
Cdd:cd17764 169 ATLFTLGWLRGVKAGAVLVV 188
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
103-151 4.27e-08

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 52.94  E-value: 4.27e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37538021  103 MYKTGPVLAISHGMGIPSISIMLHELIKLLhharccDV-TIIRIGTSGGI 151
Cdd:PRK05819  51 TYKGKRVSVMGTGMGIPSISIYANELITDY------GVkKLIRVGSCGAL 94
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
104-275 1.27e-05

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: 45.53  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   104 YKTGPVLAISHGMGIPSISIMLHELIKLLhharccDV-TIIRIGTSGGIGiapGTVVITDIAV------DSFF-KPRFEQ 175
Cdd:TIGR00107  49 YKGKKISVMGHGMGIPSISIYVYELIKFY------EVkTIIRVGSCGAIR---PDVKLRDVIIamgastDSKYnRVRFVE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   176 VilDNIVTRstelDKELSEELFNCSKEIpNFPTLVGHTMCTYDFYEGQGrldgalcsfsrekklDYLKRAFKAGVRNIEM 255
Cdd:TIGR00107 120 V--DFAAIA----DFELVENAYDAAKAK-GVDVHVGNVFSADAFYQPDK---------------DVFDLMAKYGILGVEM 177
                         170       180
                  ....*....|....*....|
gi 37538021   256 ESTVFAAMCGLCGLKAAVVC 275
Cdd:TIGR00107 178 EAAALYANAAELGAKALTIL 197
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
49-151 3.40e-05

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 44.32  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37538021   49 THNLPAMFGDV-KFVCVGGSPNRMKAFAlfmhkelgfEEAEEDIKDIC--------AGTdrycmYKTGPVLAISHGMGIP 119
Cdd:PRK13374   3 TPHINAQPGDFaETVLMPGDPLRAKYIA---------ETYLEDVVQVTdvrnmfgfTGT-----YKGKKVSVMGHGMGIP 68
                         90       100       110
                 ....*....|....*....|....*....|..
gi 37538021  120 SISIMLHELIKLLHHARccdvtIIRIGTSGGI 151
Cdd:PRK13374  69 SMVIYVHELIATFGVKN-----IIRVGSCGAT 95
 
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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