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Conserved domains on  [gi|1907143827|ref|XP_036018568|]
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uridine phosphorylase 2 isoform X5 [Mus musculus]

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: 507.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  37 EDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEGD-GEDIEDICAGTDRYCMFKTGPVLSVSHG 115
Cdd:cd17763     1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 116 MGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTELDKELAND 195
Cdd:cd17763    81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 196 LFNCSREIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLCGLRAAVVC 275
Cdd:cd17763   161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907143827 276 VTLLDRLESDQINLSHDVLVEYQQRPQLLISNFIKK 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: 507.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  37 EDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEGD-GEDIEDICAGTDRYCMFKTGPVLSVSHG 115
Cdd:cd17763     1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 116 MGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTELDKELAND 195
Cdd:cd17763    81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 196 LFNCSREIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLCGLRAAVVC 275
Cdd:cd17763   161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907143827 276 VTLLDRLESDQINLSHDVLVEYQQRPQLLISNFIKK 311
Cdd:cd17763   241 VTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
29-314 1.71e-141

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: 401.06  E-value: 1.71e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  29 NPYLEGMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEgDGEDIEDICAGTDRYCMFKTGP 108
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLS-CGRDYPNISERGDRFAMYKVGP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 109 VLSVSHGMGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTEL 188
Cdd:TIGR01719  80 VLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 189 DKELANDLFNCSRE-IPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLC 267
Cdd:TIGR01719 160 DEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907143827 268 GLRAAVVCVTLLDRLESDQINLSHDVLVEYQQRPQLLISNFIKKQLG 314
Cdd:TIGR01719 240 GFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLS 286
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
36-287 9.65e-27

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 105.63  E-value: 9.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  36 DEDILYHLDLGtkthnlPAMFGDVKFVCvgGSPNRMKAFAQFMhkelrlegdgEDIEDIcAGTDRYCMFkTG-----PVL 110
Cdd:COG2820     7 PDGSQYHLGLK------PGDVADYVILP--GDPGRVELIASYL----------DDVELV-AENREFRTY-TGtykgkRIT 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 111 SVSHGMGIPSISIMLHELIKLlhHAHccdvTIIRIGTSGGI--GIAPGSVVITDTAVdsffkpRFEQ-----VILDNVVT 183
Cdd:COG2820    67 VISTGIGGPSAAIAVEELAAL--GAK----TFIRVGTSGALqpDIPVGDLVIATGAV------RLDGtsnfyAPAEYPAV 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 184 RSTELDKELANDLfncsrEIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFsrEKKLDYLKrayRAGVRNIEMESTVFAAM 263
Cdd:COG2820   135 ADFELTRALVEAA-----EELGVDYHVGITASTDGFYAEQGRELRVDPDL--DEKLEAWR---KLGVLNVEMETAALFTL 204
                         250       260
                  ....*....|....*....|....
gi 1907143827 264 CGLCGLRAAVVCVTLLDRLESDQI 287
Cdd:COG2820   205 ARLRGHRAGSVLAVSANRVTGEFS 228
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
60-310 5.00e-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: 97.80  E-value: 5.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  60 KFVCVGGSPNRMKAFAQFMHKELRLEgdgedieDICAGTDRY-CMFKTGPVLSVSHGMGIPSISIMlhELIKLLHHAHCc 138
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVG-------PPSRGGKFYtGTLGGVPVVLVRHGIGPPNAAIL--AAIRLLKEFGV- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 139 dVTIIRIGTSGGI--GIAPGSVVITDTAVD-----SFFKPRFEQVILDnvvTRSTELDKELANDLFNCSREIpNVPTLIG 211
Cdd:pfam01048  71 -DAIIRTGTAGGLnpDLKVGDVVIPTDAINhdgrsPLFGPEGGPYFPD---MAPAPADPELRALAKEAAERL-GIPVHRG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 212 HTMCTYDFYegqgrldgalcsFSREKKLDYLKRAyraGVRNIEMESTVFAAMCGLCGLRAAVVCVT----LLDRLESDQI 287
Cdd:pfam01048 146 VYATGDGFY------------FETPAEIRLLRRL---GADAVEMETAAEAQVAREAGIPFAAIRVVsdlaAGGADGELTH 210
                         250       260
                  ....*....|....*....|...
gi 1907143827 288 NLSHDVLVEYQQRPQLLISNFIK 310
Cdd:pfam01048 211 EEVEEFAERAAERAAALLLALLA 233
PRK11178 PRK11178
uridine phosphorylase; Provisional
41-281 6.89e-14

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 70.07  E-value: 6.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  41 YHLDLgTKthnlpAMFGDVKFVCVGGSPNRMKAFAQFM--------HKEL---RLEGDGEdiedicagtdrycmfktgPV 109
Cdd:PRK11178    5 FHLGL-TK-----ADLQGATLAIVPGDPERVEKIAALMdnpvflasHREFtswRAELDGK------------------PV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 110 LSVSHGMGIPSISIMLHELIKLLHHahccdvTIIRIGTSGGI--GIAPGSVVITDTAV-----DSFFKP-RFEQVIldnv 181
Cdd:PRK11178   61 IVCSTGIGGPSTSIAVEELAQLGVR------TFLRIGTTGAIqpHINVGDVLVTTASVrldgaSLHFAPlEFPAVA---- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 182 vtrstelDKELANDLFNCSREIpNVPTLIGHTMCTYDFYEGQGRLDgalcSFSrekkldylKRAYRA-----------GV 250
Cdd:PRK11178  131 -------DFECTTALVEAAKSI-GATTHVGVTASSDTFYPGQERYD----TYS--------GRVVRRfkgsmeewqamGV 190
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907143827 251 RNIEMESTVFAAMCGLCGLRAAVVCVTLLDR 281
Cdd:PRK11178  191 MNYEMESATLLTMCASQGLRAGMVAGVIVNR 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: 507.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  37 EDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEGD-GEDIEDICAGTDRYCMFKTGPVLSVSHG 115
Cdd:cd17763     1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 116 MGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTELDKELAND 195
Cdd:cd17763    81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 196 LFNCSREIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLCGLRAAVVC 275
Cdd:cd17763   161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907143827 276 VTLLDRLESDQINLSHDVLVEYQQRPQLLISNFIKK 311
Cdd:cd17763   241 VTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
29-314 1.71e-141

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: 401.06  E-value: 1.71e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  29 NPYLEGMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEgDGEDIEDICAGTDRYCMFKTGP 108
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLS-CGRDYPNISERGDRFAMYKVGP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 109 VLSVSHGMGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTEL 188
Cdd:TIGR01719  80 VLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 189 DKELANDLFNCSRE-IPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLC 267
Cdd:TIGR01719 160 DEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907143827 268 GLRAAVVCVTLLDRLESDQINLSHDVLVEYQQRPQLLISNFIKKQLG 314
Cdd:TIGR01719 240 GFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLS 286
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
61-308 4.36e-34

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: 123.94  E-value: 4.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  61 FVCVGGSPNRMKAFAQFMhkelrlegdgEDIEDICAGtDRYCMFkTG-----PVLSVSHGMGIPSISIMLHELIkllhhA 135
Cdd:cd09005     1 YAIIPGDPERVDVIDSKL----------ENPQKVSSF-RGYTMY-TGkyngkRVTVVNGGMGSPSAAIVVEELC-----A 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 136 HCCDvTIIRIGTSGGIG--IAPGSVVITDTAVDSFFKPRFEQVILDnvvtRSTELDKELANDLFNCSREIpNVPTLIGHT 213
Cdd:cd09005    64 LGVD-TIIRVGSCGALRedIKVGDLVIADGAIRGDGVTPYYVVGPP----FAPEADPELTAALEEAAKEL-GLTVHVGTV 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 214 MCTYDFYEGQGrldgalcsfsrekklDYLKRAYRAGVRNIEMESTVFAAMCGLCGLRAAVVCVTlLDRLESDQINLSHDV 293
Cdd:cd09005   138 WTTDAFYRETR---------------EESEKLRKLGALAVEMETSALATLAHLRGVKAASILAV-SDNLITGEIGFVDEF 201
                         250
                  ....*....|....*
gi 1907143827 294 LVEYQQRPQLLISNF 308
Cdd:cd09005   202 LSEAEKKAIEIALDA 216
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
36-287 9.65e-27

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 105.63  E-value: 9.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  36 DEDILYHLDLGtkthnlPAMFGDVKFVCvgGSPNRMKAFAQFMhkelrlegdgEDIEDIcAGTDRYCMFkTG-----PVL 110
Cdd:COG2820     7 PDGSQYHLGLK------PGDVADYVILP--GDPGRVELIASYL----------DDVELV-AENREFRTY-TGtykgkRIT 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 111 SVSHGMGIPSISIMLHELIKLlhHAHccdvTIIRIGTSGGI--GIAPGSVVITDTAVdsffkpRFEQ-----VILDNVVT 183
Cdd:COG2820    67 VISTGIGGPSAAIAVEELAAL--GAK----TFIRVGTSGALqpDIPVGDLVIATGAV------RLDGtsnfyAPAEYPAV 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 184 RSTELDKELANDLfncsrEIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFsrEKKLDYLKrayRAGVRNIEMESTVFAAM 263
Cdd:COG2820   135 ADFELTRALVEAA-----EELGVDYHVGITASTDGFYAEQGRELRVDPDL--DEKLEAWR---KLGVLNVEMETAALFTL 204
                         250       260
                  ....*....|....*....|....
gi 1907143827 264 CGLCGLRAAVVCVTLLDRLESDQI 287
Cdd:COG2820   205 ARLRGHRAGSVLAVSANRVTGEFS 228
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
41-289 4.59e-26

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: 103.29  E-value: 4.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  41 YHLDLGTkthnlpamfGDV-KFVCVGGSPNRMKAFAQFMhkelrlegdgEDIEDIcaGTDRycMFKTG-------PVLSV 112
Cdd:cd17767     1 YHIGLKP---------GDVaPYVLLPGDPGRVERIAELL----------DDAEEV--ADNR--EYRTYtgtykgvPVSVC 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 113 SHGMGIPSISIMLHELIKLlhHAHccdvTIIRIGTSGGI--GIAPGSVVITDTAVdsffkpRFEQVildnvvtrSTEL-- 188
Cdd:cd17767    58 STGIGGPSAAIAVEELAQL--GAK----TFIRVGTCGALqpDIKLGDLVIATGAV------RDEGT--------SKHYvp 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 189 -------DKELANDLFNCSREIpNVPTLIGhTMCTYD-FYEGQGRLDGALCSFSREkKLDYLKrayRAGVRNIEME-STV 259
Cdd:cd17767   118 peypavaDPEVVLALVEAAEEL-GVPYHVG-ITASKDsFYGGQGRPGPGLPPELPE-LLEEWQ---RAGVLNSEMEsAAL 191
                         250       260       270
                  ....*....|....*....|....*....|
gi 1907143827 260 FaAMCGLCGLRAAVVCVTLLDRLESDQINL 289
Cdd:cd17767   192 F-TLASLRGVRAGAVLAVVGNRVTDEAPDE 220
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
60-310 5.00e-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: 97.80  E-value: 5.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  60 KFVCVGGSPNRMKAFAQFMHKELRLEgdgedieDICAGTDRY-CMFKTGPVLSVSHGMGIPSISIMlhELIKLLHHAHCc 138
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVG-------PPSRGGKFYtGTLGGVPVVLVRHGIGPPNAAIL--AAIRLLKEFGV- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 139 dVTIIRIGTSGGI--GIAPGSVVITDTAVD-----SFFKPRFEQVILDnvvTRSTELDKELANDLFNCSREIpNVPTLIG 211
Cdd:pfam01048  71 -DAIIRTGTAGGLnpDLKVGDVVIPTDAINhdgrsPLFGPEGGPYFPD---MAPAPADPELRALAKEAAERL-GIPVHRG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 212 HTMCTYDFYegqgrldgalcsFSREKKLDYLKRAyraGVRNIEMESTVFAAMCGLCGLRAAVVCVT----LLDRLESDQI 287
Cdd:pfam01048 146 VYATGDGFY------------FETPAEIRLLRRL---GADAVEMETAAEAQVAREAGIPFAAIRVVsdlaAGGADGELTH 210
                         250       260
                  ....*....|....*....|...
gi 1907143827 288 NLSHDVLVEYQQRPQLLISNFIK 310
Cdd:pfam01048 211 EEVEEFAERAAERAAALLLALLA 233
PRK11178 PRK11178
uridine phosphorylase; Provisional
41-281 6.89e-14

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 70.07  E-value: 6.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  41 YHLDLgTKthnlpAMFGDVKFVCVGGSPNRMKAFAQFM--------HKEL---RLEGDGEdiedicagtdrycmfktgPV 109
Cdd:PRK11178    5 FHLGL-TK-----ADLQGATLAIVPGDPERVEKIAALMdnpvflasHREFtswRAELDGK------------------PV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 110 LSVSHGMGIPSISIMLHELIKLLHHahccdvTIIRIGTSGGI--GIAPGSVVITDTAV-----DSFFKP-RFEQVIldnv 181
Cdd:PRK11178   61 IVCSTGIGGPSTSIAVEELAQLGVR------TFLRIGTTGAIqpHINVGDVLVTTASVrldgaSLHFAPlEFPAVA---- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 182 vtrstelDKELANDLFNCSREIpNVPTLIGHTMCTYDFYEGQGRLDgalcSFSrekkldylKRAYRA-----------GV 250
Cdd:PRK11178  131 -------DFECTTALVEAAKSI-GATTHVGVTASSDTFYPGQERYD----TYS--------GRVVRRfkgsmeewqamGV 190
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907143827 251 RNIEMESTVFAAMCGLCGLRAAVVCVTLLDR 281
Cdd:PRK11178  191 MNYEMESATLLTMCASQGLRAGMVAGVIVNR 221
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
112-281 1.98e-12

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: 66.34  E-value: 1.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 112 VSHGMGIPSISIMLHELikllhHA-HCCD------------VTIIRIGTSGGI--GIAPGSVVITDTAV--DSF-----F 169
Cdd:cd00436    67 ISTGIGTDNIDIVLNEL-----DAlVNIDfktrtpkeektsLNIIRLGTSGALqpDIPVGSLVISSYAIglDNLlnfydH 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 170 KPRFEQVILDNVVTRSTELDKELAN--------DLFNCsreIPNVPTLIGHTMCTYDFYEGQGR----------LDGALC 231
Cdd:cd00436   142 PNTDEEAELENAFIAHTSWFKGKPRpyvvkaspELLDA---LTGVGYVVGITATAPGFYGPQGRqlrlpladpdLLDKLS 218
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907143827 232 SFSREkkldylkrayraGVR--NIEMEStvfAAMCGLCGL---RAAVVCVTLLDR 281
Cdd:cd00436   219 SFSYG------------GLRitNFEMET---SAIYGLSRLlghRALSICAIIANR 258
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
111-275 2.98e-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: 65.12  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 111 SV-SHGMGIPSISIMLHELIKllHHahccDV-TIIRIGTSGGIG--IAPGSVVITDTAV-DSFFkprfeQVILDNVVTRS 185
Cdd:cd09006    55 SVmGSGMGMPSIGIYAYELFK--FY----GVkNIIRIGTCGAYQpdLKLRDVVLAMGAStDSNY-----NRLRFGGGDFA 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 186 TELDKELANDLFNCSREIpNVPTLIGHTMCTYDFYegqgrldgalcsfsrEKKLDYLKRAYRAGVRNIEMESTVFAAMCG 265
Cdd:cd09006   124 PIADFELLRKAVETAKEL-GIPVHVGNVFSSDVFY---------------DDDPELWKKLKKYGVLAVEMEAAALYTNAA 187
                         170
                  ....*....|
gi 1907143827 266 LCGLRAAVVC 275
Cdd:cd09006   188 RLGKKALAIL 197
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
110-275 1.31e-11

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: 63.21  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 110 LSV-SHGMGIPSISIMLHELIKLLhhahccDV-TIIRIGTSGGI--GIAPGSVVITDTAV-DS-FFKPRFEQVILdnvvt 183
Cdd:COG0813    58 VSVmGSGMGIPSISIYAYELITEY------GVkNIIRVGTCGALqeDVKVRDVVIAMGAStDSnVNRQRFGGGDF----- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 184 rSTELDKELANDLFNCSREIpNVPTLIGHTMCTYDFYegqgrldgalcsfsrEKKLDYLKRAYRAGVRNIEMESTVFAAM 263
Cdd:COG0813   127 -APIADFELLRKAVEAAKEL-GIKVHVGNVFSSDLFY---------------REDPDLLEKLAKYGVLAVEMEAAALYTL 189
                         170
                  ....*....|..
gi 1907143827 264 CGLCGLRAAVVC 275
Cdd:COG0813   190 AAKYGKRALAIL 201
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
110-294 2.34e-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: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 110 LSV-SHGMGIPSISIMLHELIKLLHHahccdvTIIRIGTSGGI--GIAPGSVVITDTAVDSFFKPRfeqvILDNVVTRST 186
Cdd:cd17765    57 VSVqTTGMGCPSAAIVVEELAQLGVK------RLIRVGTCGGLssGLQLGDLIVATAAVPADGTTR----ALLGGEPYAP 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 187 ELDKELANDLFNCSREIpNVPTLIGHTMCTYDFYEGQgrldgalcsfsrekkLDYLKRAYRAGVRNIEMESTVFAAMCGL 266
Cdd:cd17765   127 AADFELVEALYRAARAA-GMPVHVGPVATSDLFYDPT---------------PDGVKRWRRRGVLAVEMEASALFTLAAL 190
                         170       180
                  ....*....|....*....|....*...
gi 1907143827 267 CGLRAAVVCvTLLDRLESDQINLSHDVL 294
Cdd:cd17765   191 RGLRAGCIL-TVSDLIGDPERRIDDEEL 217
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
103-287 1.41e-09

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: 57.59  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 103 MFKTGPVLSVSHGMGIPSISIMLHELikllhhAHCCD--VTIIRIGTSGGIG--IAPGSVVITDTAV-------DSFFKP 171
Cdd:cd17769    40 RYKGVPVSIVAIGMGAPMMDFFVREA------RAVVDgpMAIIRLGSCGSLDpdVPVGSVVVPSASVavtrnydDDDFAG 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 172 RFEQVILDNVVTRSTELDKELANDLF-NCSREIPNVPTLIGHTMCTYDFYEGQGRLDGalcSF--SREKKLDYLKRAYRa 248
Cdd:cd17769   114 PSTSSEKPYLISKPVPADPELSELLEsELKASLGGEVVVEGLNASADSFYSSQGRQDP---NFpdHNENLIDKLLKRYP- 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907143827 249 GVRNIEMESTVF---AAMC-GLCG-LRAAVVCVTLLDRLESDQI 287
Cdd:cd17769   190 GAASLEMETFHLfhlARCSrPAQGkIRAAAAHMVFANRTSNDFI 233
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
111-151 2.94e-07

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 50.63  E-value: 2.94e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1907143827 111 SV-SHGMGIPSISIMLHELIKLLhhahccDV-TIIRIGTSGGI 151
Cdd:PRK05819   58 SVmGTGMGIPSISIYANELITDY------GVkKLIRVGSCGAL 94
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
104-277 2.37e-06

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: 47.60  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 104 FKTGPVLSVSHGMGIPSISIMLHELIKLlhHAHccdvTIIRIGTSGGI--GIAPGSVVItdtAVDSFFKP--RFEQVILD 179
Cdd:cd17764    38 YKGEEVTIATHGIGGPSAAIVFEELIML--GAK----VIIRLGTAGGLvpELRVGDIVV---ATGASYYPggGLGQYFPD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827 180 nvVTRSTELDKELANDLFNCSREIpNVPTLIGHTMCTYDFYEgqgrldgalcsfsrEKKlDYLKRAYRAGVRNIEMESTV 259
Cdd:cd17764   109 --VCPPASPDPELTLELVESLSKR-GLKYYVGPVFSSDAFYA--------------EDE-EFAERWSSLGFIAVEMECAT 170
                         170
                  ....*....|....*...
gi 1907143827 260 FAAMCGLCGLRAAVVCVT 277
Cdd:cd17764   171 LFTLGWLRGVKAGAVLVV 188
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
114-151 2.50e-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: 41.68  E-value: 2.50e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907143827 114 HGMGIPSISIMLHELIKLLhhahccDV-TIIRIGTSGGI 151
Cdd:TIGR00107  59 HGMGIPSISIYVYELIKFY------EVkTIIRVGSCGAI 91
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
49-151 3.55e-04

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 41.24  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143827  49 THNLPAMFGDV-KFVCVGGSPNRMKAFAQ-FMhkelrlegdgEDIEDICA--GTDRYCMFKTGPVLSV-SHGMGIPSISI 123
Cdd:PRK13374    3 TPHINAQPGDFaETVLMPGDPLRAKYIAEtYL----------EDVVQVTDvrNMFGFTGTYKGKKVSVmGHGMGIPSMVI 72
                          90       100
                  ....*....|....*....|....*....
gi 1907143827 124 MLHELIkllhhaHCCDV-TIIRIGTSGGI 151
Cdd:PRK13374   73 YVHELI------ATFGVkNIIRVGSCGAT 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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