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Conserved domains on  [gi|333805031|dbj|BAK26238|]
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phosphorylase family protein [Porphyromonas gingivalis TDC60]

Protein Classification

nucleoside phosphorylase( domain architecture ID 12903249)

nucleoside phosphorylase similar to Trypanosoma brucei uridine phosphorylase that 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_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
11-292 2.75e-155

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: 434.59  E-value: 2.75e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  11 ELIINTDGSVFHLHIRPEQLADKVILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVL 90
Cdd:cd00436    1 ELILNPDGSIYHLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  91 NELDALANIDFDTRQVKDRLRKLTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDTEKIRDAAFEAALQDQLEW 170
Cdd:cd00436   81 NELDALVNIDFKTRTPKEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNLLNFYDHPNTDEEAELENAFIAHTSW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 171 KIEGLKPYVIPADKTLSDRICREDILRGVTIAANGFYGPQGRRLRLPLKDEDLNRKIQAFDFNGSRITNYEMESSSLAGL 250
Cdd:cd00436  161 FKGKPRPYVVKASPELLDALTGVGYVVGITATAPGFYGPQGRQLRLPLADPDLLDKLSSFSYGGLRITNFEMETSAIYGL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 333805031 251 AALMGHEAITVCCIIAGRKSEKMNTSYQGSIEGLIDLVLERI 292
Cdd:cd00436  241 SRLLGHRALSICAIIANRATGEFSKDYKKAVEKLIEKVLEAL 282
 
Name Accession Description Interval E-value
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
11-292 2.75e-155

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: 434.59  E-value: 2.75e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  11 ELIINTDGSVFHLHIRPEQLADKVILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVL 90
Cdd:cd00436    1 ELILNPDGSIYHLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  91 NELDALANIDFDTRQVKDRLRKLTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDTEKIRDAAFEAALQDQLEW 170
Cdd:cd00436   81 NELDALVNIDFKTRTPKEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNLLNFYDHPNTDEEAELENAFIAHTSW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 171 KIEGLKPYVIPADKTLSDRICREDILRGVTIAANGFYGPQGRRLRLPLKDEDLNRKIQAFDFNGSRITNYEMESSSLAGL 250
Cdd:cd00436  161 FKGKPRPYVVKASPELLDALTGVGYVVGITATAPGFYGPQGRQLRLPLADPDLLDKLSSFSYGGLRITNFEMETSAIYGL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 333805031 251 AALMGHEAITVCCIIAGRKSEKMNTSYQGSIEGLIDLVLERI 292
Cdd:cd00436  241 SRLLGHRALSICAIIANRATGEFSKDYKKAVEKLIEKVLEAL 282
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
7-292 3.16e-88

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 263.18  E-value: 3.16e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031   7 IPPSELIintDGSVFHLHIRPEQLADKVILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNI 86
Cdd:COG2820    1 MKESELP---DGSQYHLGLKPGDVADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  87 DIVLNELDAlanidfdtrqvkdrLRKLTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDtekirdaafeaalqd 166
Cdd:COG2820   78 AIAVEELAA--------------LGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAP--------------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 167 qlewkieglKPYVIPADKTLSDRICRE------DILRGVTIAANGFYGPQGRRLRLplkDEDLNRKIQAfdFNGSRITNY 240
Cdd:COG2820  129 ---------AEYPAVADFELTRALVEAaeelgvDYHVGITASTDGFYAEQGRELRV---DPDLDEKLEA--WRKLGVLNV 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 333805031 241 EMESSSLAGLAALMGHEAITVCCIIAGRKSEKMNTSYQGSIEGLIDLVLERI 292
Cdd:COG2820  195 EMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEEAVERAIKVALEAL 246
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
34-264 1.56e-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: 98.57  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031   34 VILVGDPARVDAVASRFE-RIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVLNELdalanidfdtrqVKDRLRK 112
Cdd:pfam01048   3 AIIGGSPEELALLAELLDdETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIR------------LLKEFGV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  113 LTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDTEKIRDAAFEAAlqdqlewkieglkpyviPADKTLSDRICR 192
Cdd:pfam01048  71 DAIIRTGTAGGLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPA-----------------PADPELRALAKE 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333805031  193 E------DILRGVTIAANGFYGPQGRRLRLplkdedlnrkiqafdFNGSRITNYEMESSSLAGLAALMGHEAITVCCI 264
Cdd:pfam01048 134 AaerlgiPVHRGVYATGDGFYFETPAEIRL---------------LRRLGADAVEMETAAEAQVAREAGIPFAAIRVV 196
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
20-271 6.93e-20

uridine phosphorylase; This model represents a family of bacterial and archaeal uridine phosphorylases unrelated to the mammalian enzymes of the same name. The E. coli, Salmonella and Klebsiella genes have been characterized. Sequences from Clostridium, Streptomyces, Treponema, Halobacterium and Pyrobaculum were included above trusted on the basis of sequence homology and a PAM-based neighbor-joining tree. A clade including second sequences from Halobacterium and Vibrio was somewhat more distantly related and may represent a slightly different substrate specificity - these were placed below the noise cutoff. More distantly related is a clade of archaeal sequences which as related to the DeoD family of inosine phosphorylases (TIGR00107) as they are to these uridine phosphorylases. This clade includes a characterized protein from Sulfolobus solfataricus which has been mis-named as a methylthioadenosine phosphorylase, but which acts on inosine and guanosine - it is unclear whether uridine has been evaluated as a substrate. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130779  Cd Length: 245  Bit Score: 86.49  E-value: 6.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031   20 VFHLHIRPEQLADKVILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVLNELdALANI 99
Cdd:TIGR01718   1 VYHLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEEL-AQLGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  100 DfdtrqvkdrlrklTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDTEKIRDAAFE--AALQDQLEwkIEGLKP 177
Cdd:TIGR01718  80 R-------------TFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEvtTALVEAAE--SIGVRH 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  178 YVipadktlsdricredilrGVTIAANGFYGPQGRRLRLPLKDEDLNRKIQAfdFNGSRITNYEMESSSLAGLAALMGHE 257
Cdd:TIGR01718 145 HV------------------GVVASSDTFYPGQERDTYSGRVVRHFKGSMEA--WQAMGVLNYEMESATLFTLCSSQGLR 204
                         250
                  ....*....|....
gi 333805031  258 AITVCCIIAGRKSE 271
Cdd:TIGR01718 205 AGMVAGVIVNRTQQ 218
PRK11178 PRK11178
uridine phosphorylase; Provisional
20-268 1.08e-16

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 77.77  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  20 VFHLHIRPEQL--ADKVILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVLNELDALA 97
Cdd:PRK11178   4 VFHLGLTKADLqgATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  98 nidfdtrqvkdrLRklTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDTEKIRDAAFEAALQDQLEWKIEGLKP 177
Cdd:PRK11178  84 ------------VR--TFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 178 YVipadktlsdricredilrGVTIAANGFYGPQGRRlrlplkDEDLNRKIQAfdFNGSR-------ITNYEMESSSLAGL 250
Cdd:PRK11178 150 HV------------------GVTASSDTFYPGQERY------DTYSGRVVRR--FKGSMeewqamgVMNYEMESATLLTM 203
                        250
                 ....*....|....*...
gi 333805031 251 AALMGHEAITVCCIIAGR 268
Cdd:PRK11178 204 CASQGLRAGMVAGVIVNR 221
 
Name Accession Description Interval E-value
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
11-292 2.75e-155

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: 434.59  E-value: 2.75e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  11 ELIINTDGSVFHLHIRPEQLADKVILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVL 90
Cdd:cd00436    1 ELILNPDGSIYHLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  91 NELDALANIDFDTRQVKDRLRKLTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDTEKIRDAAFEAALQDQLEW 170
Cdd:cd00436   81 NELDALVNIDFKTRTPKEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNLLNFYDHPNTDEEAELENAFIAHTSW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 171 KIEGLKPYVIPADKTLSDRICREDILRGVTIAANGFYGPQGRRLRLPLKDEDLNRKIQAFDFNGSRITNYEMESSSLAGL 250
Cdd:cd00436  161 FKGKPRPYVVKASPELLDALTGVGYVVGITATAPGFYGPQGRQLRLPLADPDLLDKLSSFSYGGLRITNFEMETSAIYGL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 333805031 251 AALMGHEAITVCCIIAGRKSEKMNTSYQGSIEGLIDLVLERI 292
Cdd:cd00436  241 SRLLGHRALSICAIIANRATGEFSKDYKKAVEKLIEKVLEAL 282
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
7-292 3.16e-88

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 263.18  E-value: 3.16e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031   7 IPPSELIintDGSVFHLHIRPEQLADKVILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNI 86
Cdd:COG2820    1 MKESELP---DGSQYHLGLKPGDVADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  87 DIVLNELDAlanidfdtrqvkdrLRKLTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDtekirdaafeaalqd 166
Cdd:COG2820   78 AIAVEELAA--------------LGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAP--------------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 167 qlewkieglKPYVIPADKTLSDRICRE------DILRGVTIAANGFYGPQGRRLRLplkDEDLNRKIQAfdFNGSRITNY 240
Cdd:COG2820  129 ---------AEYPAVADFELTRALVEAaeelgvDYHVGITASTDGFYAEQGRELRV---DPDLDEKLEA--WRKLGVLNV 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 333805031 241 EMESSSLAGLAALMGHEAITVCCIIAGRKSEKMNTSYQGSIEGLIDLVLERI 292
Cdd:COG2820  195 EMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEEAVERAIKVALEAL 246
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
21-290 1.16e-43

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: 148.75  E-value: 1.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  21 FHLHIRPEQLADKVILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVLNEldaLANId 100
Cdd:cd17767    1 YHIGLKPGDVAPYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEE---LAQL- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 101 fdtrQVKdrlrklTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDTE-----------KIRDAAfeaalqdqle 169
Cdd:cd17767   77 ----GAK------TFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEypavadpevvlALVEAA---------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 170 wKIEGLKPYVipadktlsdricredilrGVTIAANGFYGPQGRRL-----RLPLKDEDLNRKiqafdfngsRITNYEMES 244
Cdd:cd17767  137 -EELGVPYHV------------------GITASKDSFYGGQGRPGpglppELPELLEEWQRA---------GVLNSEMES 188
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 333805031 245 SSLAGLAALMGHEAITVCCIIAGRKSEKMNTS--YQGSIEGLIDLVLE 290
Cdd:cd17767  189 AALFTLASLRGVRAGAVLAVVGNRVTDEAPDEedVAAGEERAIRVALE 236
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
34-290 1.13e-28

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: 109.30  E-value: 1.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  34 VILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVLNELDALanidfdtrQVKdrlrkl 113
Cdd:cd09005    2 AIIPGDPERVDVIDSKLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCAL--------GVD------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 114 TLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDtEKIRDAAFEAALQDQLE--WKIEGLKPYvipadktlsdric 191
Cdd:cd09005   68 TIIRVGSCGALREDIKVGDLVIADGAIRGDGVTPYYVV-GPPFAPEADPELTAALEeaAKELGLTVH------------- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 192 redilRGVTIAANGFYGPQGRRLRLPLKDEDLnrkiqafdfngsritNYEMESSSLAGLAALMGHEAITVCCI---IAGR 268
Cdd:cd09005  134 -----VGTVWTTDAFYRETREESEKLRKLGAL---------------AVEMETSALATLAHLRGVKAASILAVsdnLITG 193
                        250       260
                 ....*....|....*....|..
gi 333805031 269 KSEKMNTSYQGSIEGLIDLVLE 290
Cdd:cd09005  194 EIGFVDEFLSEAEKKAIEIALD 215
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
34-264 1.56e-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: 98.57  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031   34 VILVGDPARVDAVASRFE-RIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVLNELdalanidfdtrqVKDRLRK 112
Cdd:pfam01048   3 AIIGGSPEELALLAELLDdETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIR------------LLKEFGV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  113 LTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDTEKIRDAAFEAAlqdqlewkieglkpyviPADKTLSDRICR 192
Cdd:pfam01048  71 DAIIRTGTAGGLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPA-----------------PADPELRALAKE 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333805031  193 E------DILRGVTIAANGFYGPQGRRLRLplkdedlnrkiqafdFNGSRITNYEMESSSLAGLAALMGHEAITVCCI 264
Cdd:pfam01048 134 AaerlgiPVHRGVYATGDGFYFETPAEIRL---------------LRRLGADAVEMETAAEAQVAREAGIPFAAIRVV 196
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
20-271 6.93e-20

uridine phosphorylase; This model represents a family of bacterial and archaeal uridine phosphorylases unrelated to the mammalian enzymes of the same name. The E. coli, Salmonella and Klebsiella genes have been characterized. Sequences from Clostridium, Streptomyces, Treponema, Halobacterium and Pyrobaculum were included above trusted on the basis of sequence homology and a PAM-based neighbor-joining tree. A clade including second sequences from Halobacterium and Vibrio was somewhat more distantly related and may represent a slightly different substrate specificity - these were placed below the noise cutoff. More distantly related is a clade of archaeal sequences which as related to the DeoD family of inosine phosphorylases (TIGR00107) as they are to these uridine phosphorylases. This clade includes a characterized protein from Sulfolobus solfataricus which has been mis-named as a methylthioadenosine phosphorylase, but which acts on inosine and guanosine - it is unclear whether uridine has been evaluated as a substrate. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130779  Cd Length: 245  Bit Score: 86.49  E-value: 6.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031   20 VFHLHIRPEQLADKVILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVLNELdALANI 99
Cdd:TIGR01718   1 VYHLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEEL-AQLGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  100 DfdtrqvkdrlrklTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDTEKIRDAAFE--AALQDQLEwkIEGLKP 177
Cdd:TIGR01718  80 R-------------TFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEvtTALVEAAE--SIGVRH 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  178 YVipadktlsdricredilrGVTIAANGFYGPQGRRLRLPLKDEDLNRKIQAfdFNGSRITNYEMESSSLAGLAALMGHE 257
Cdd:TIGR01718 145 HV------------------GVVASSDTFYPGQERDTYSGRVVRHFKGSMEA--WQAMGVLNYEMESATLFTLCSSQGLR 204
                         250
                  ....*....|....
gi 333805031  258 AITVCCIIAGRKSE 271
Cdd:TIGR01718 205 AGMVAGVIVNRTQQ 218
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
34-270 1.06e-19

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: 86.09  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  34 VILVGDPARVDAVAS-------RFERiecnVSNREFHTVTGWYGDKRITVQSHGIGsdnidivlneldaLANIDFDTRQV 106
Cdd:cd17769    3 IITVGDPARARLIAKlldkepkVFEL----TSERGFLTITGRYKGVPVSIVAIGMG-------------APMMDFFVREA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 107 KDRL-RKLTLVRVGTSGGLQDNTPIGSYVAAERSIgfdGVMYFYSDTekirDAAFEAALQDqlewkieglKPYVI----P 181
Cdd:cd17769   66 RAVVdGPMAIIRLGSCGSLDPDVPVGSVVVPSASV---AVTRNYDDD----DFAGPSTSSE---------KPYLIskpvP 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 182 ADKTLSDRICREDIL--------RGVTIAANGFYGPQGRRL-RLPLKDEDLNRKIQAFDFNgsrITNYEMESSSLAGLAA 252
Cdd:cd17769  130 ADPELSELLESELKAslggevvvEGLNASADSFYSSQGRQDpNFPDHNENLIDKLLKRYPG---AASLEMETFHLFHLAR 206
                        250       260
                 ....*....|....*....|...
gi 333805031 253 LMGHEAITV----CCII-AGRKS 270
Cdd:cd17769  207 CSRPAQGKIraaaAHMVfANRTS 229
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
32-182 3.84e-17

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: 78.42  E-value: 3.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  32 DKVILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVLNELDAL-ANIdfdtrqvkdrl 110
Cdd:cd17764    1 ERVIAVGDPGRVELLSTLLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIMLgAKV----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 111 rkltLVRVGTSGGLQDNTPIGSYVAAErsigfdGVMYFYSDTEK--IRDAAFEAALQDQLEWKI------EGLKPYVIPA 182
Cdd:cd17764   70 ----IIRLGTAGGLVPELRVGDIVVAT------GASYYPGGGLGqyFPDVCPPASPDPELTLELveslskRGLKYYVGPV 139
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
22-262 4.32e-17

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: 78.50  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  22 HLHIRPEQLADKVILVGDPARVDAVASRF-ERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVLNELDALAnid 100
Cdd:cd17765    4 HIRAEPGDVAEAVLLPGDPGRATYIAETFfDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELAQLG--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 101 fdtrqVKdrlrklTLVRVGTSGGLQDNTPIGSYVAAERSIGFDG--VMYF-------YSDTEKIRdAAFEAAlqdqlewK 171
Cdd:cd17765   81 -----VK------RLIRVGTCGGLSSGLQLGDLIVATAAVPADGttRALLggepyapAADFELVE-ALYRAA-------R 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 172 IEGLKPYVIPadktlsdrICREDIlrgvtiaangFYGPqgrrlrlplkDEDLNRKIQAFDfngsrITNYEMESSSLAGLA 251
Cdd:cd17765  142 AAGMPVHVGP--------VATSDL----------FYDP----------TPDGVKRWRRRG-----VLAVEMEASALFTLA 188
                        250
                 ....*....|.
gi 333805031 252 ALMGHEAITVC 262
Cdd:cd17765  189 ALRGLRAGCIL 199
PRK11178 PRK11178
uridine phosphorylase; Provisional
20-268 1.08e-16

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 77.77  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  20 VFHLHIRPEQL--ADKVILVGDPARVDAVASRFERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVLNELDALA 97
Cdd:PRK11178   4 VFHLGLTKADLqgATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  98 nidfdtrqvkdrLRklTLVRVGTSGGLQDNTPIGSYVAAERSIGFDGVMYFYSDTEKIRDAAFEAALQDQLEWKIEGLKP 177
Cdd:PRK11178  84 ------------VR--TFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 178 YVipadktlsdricredilrGVTIAANGFYGPQGRRlrlplkDEDLNRKIQAfdFNGSR-------ITNYEMESSSLAGL 250
Cdd:PRK11178 150 HV------------------GVTASSDTFYPGQERY------DTYSGRVVRR--FKGSMeewqamgVMNYEMESATLLTM 203
                        250
                 ....*....|....*...
gi 333805031 251 AALMGHEAITVCCIIAGR 268
Cdd:PRK11178 204 CASQGLRAGMVAGVIVNR 221
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
22-262 8.10e-15

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: 72.05  E-value: 8.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  22 HLHIRPEQLADKVILVGDPARVDAVASRF-ERIECnvsnreFHTV------TGWYGDKRITVQSHGIGSDNIDIVLNELd 94
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFlEDAKL------VNSVrnmlgyTGTYKGKRVSVMGSGMGMPSIGIYAYEL- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  95 alanidFDTRQVKdrlrklTLVRVGTSGGLQDNTPIGSYVAAE---------RSIGFDGVMYFYSDTEKIRdAAFEAAlq 165
Cdd:cd09006   74 ------FKFYGVK------NIIRIGTCGAYQPDLKLRDVVLAMgastdsnynRLRFGGGDFAPIADFELLR-KAVETA-- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 166 dqlewKIEGLKPYVipadktlsdricredilrGVTIAANGFYGPqgrrlrlplkDEDLNRKIQAFDFNGSritnyEMESS 245
Cdd:cd09006  139 -----KELGIPVHV------------------GNVFSSDVFYDD----------DPELWKKLKKYGVLAV-----EMEAA 180
                        250
                 ....*....|....*..
gi 333805031 246 SLAGLAALMGHEAITVC 262
Cdd:cd09006  181 ALYTNAARLGKKALAIL 197
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
24-264 6.72e-14

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 69.50  E-value: 6.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  24 HI--RPEQLADKVILVGDPARVDAVASRF-ERIECNVSNREFHTVTGWYGDKRITVQSHGIGSDNIDIVLNELdalanI- 99
Cdd:PRK05819   4 HInaKKGDIADTVLMPGDPLRAKYIAETFlEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANEL-----It 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 100 DFDtrqVKdrlrklTLVRVGTSGGLQDNTPIGSYVAAERS--------IGFDGVMYF-YSDTEKIRdAAFEAAlqdqlew 170
Cdd:PRK05819  79 DYG---VK------KLIRVGSCGALQEDVKVRDVVIAMGAstdsnvnrIRFKGHDFApIADFDLLR-KAYDAA------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 171 KIEGLKPYVipadktlsdricredilrGVTIAANGFYGPqgrrlrlplkDEDLNRKIQAFDfngsrITNYEMESSSLAGL 250
Cdd:PRK05819 142 KEKGITVHV------------------GNVFSADLFYNP----------DPEMFDVLEKYG-----VLGVEMEAAALYGL 188
                        250
                 ....*....|....
gi 333805031 251 AALMGHEAITVCCI 264
Cdd:PRK05819 189 AAKYGVKALTILTV 202
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
34-268 4.15e-10

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: 59.39  E-value: 4.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031   34 VILVGDPARVDAVASRFER---IEC-----NVSNREFHTVTGWYGDkrITVQSHGIGSDNIDIVLNELDALANIDfdtrq 105
Cdd:TIGR01719  34 VCMGGTPSRMKAFARYVGAelgLSCgrdypNISERGDRFAMYKVGP--VLCVSHGMGIPSISIMLHELIKLLYYA----- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  106 vkdRLRKLTLVRVGTSGGLqdNTPIGSYVAAERsiGFDG------VMYFYSDTEKIRDAAFEAALQDQLEWKIEGLKPYV 179
Cdd:TIGR01719 107 ---RCKNPTFIRIGTSGGI--GVPPGTVVVSSE--AVDAclkpeyEQIVLGKRVIRPTQLDEALVQELLLCGAEGLDEFT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  180 IPADKTLSdricredilrgvtiaANGFYGPQGRrLRLPLKDEDLNRK---IQAFDFNGSRitNYEMESSSLAGLAALMGH 256
Cdd:TIGR01719 180 TVSGNTMC---------------TDDFYEGQGR-LDGAFCEYTEKDKmayLRKLYALGVR--NIEMESSMFAAMTSRAGF 241
                         250
                  ....*....|..
gi 333805031  257 EAITVCCIIAGR 268
Cdd:TIGR01719 242 KAAVVCVTLLNR 253
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
78-263 4.66e-10

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: 59.08  E-value: 4.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031  78 SHGIGSDNIDIVLNELDAL---ANidfdtrqVKDrlrkLTLVRVGTSGGLqdNTPIGSYVaaersigfdgvmyfysdtek 154
Cdd:cd17763   78 SHGMGIPSLSILLHELIKLlhyAG-------CKD----VTFIRIGTSGGI--GVEPGTVV-------------------- 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805031 155 IRDAAFEAALQDQLEWKIEGlKPYVIPA--DKTLSDRI---CRED----ILRGVTIAANGFYGPQGrRLRLPLKDEDLNR 225
Cdd:cd17763  125 ITTEAVDGELEPFYEQVILG-KVVKRPAvlDAQLAEELlecAKELddfpTVIGKTMCANDFYEGQG-RLDGAFCDYTEED 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 333805031 226 KiqaFDF------NGsrITNYEMESSSLAGLAALMGHEAITVCC 263
Cdd:cd17763  203 K---MAFlqklydAG--VRNIEMESLCFAAFCHRAGIKAAVVCV 241
 
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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