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Conserved domains on  [gi|1085149888|gb|OGT40902|]
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hypothetical protein A3E81_04695 [Gammaproteobacteria bacterium RIFCSPHIGHO2_12_FULL_36_30]

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 ...
9-288 5.01e-162

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: 451.54  E-value: 5.01e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888   9 ELVLNADGSVYHLNLLPEEIADTIILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITM 88
Cdd:cd00436     1 ELILNPDGSIYHLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  89 NELDALHNIDLKNRVVKNNHKKLNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYDWKNNEAEKKLLTACREKFSA 168
Cdd:cd00436    81 NELDALVNIDFKTRTPKEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNLLNFYDHPNTDEEAELENAFIAHTSW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 169 TPFLNTLYVAAGAKSLIDLFEKNNlGLTGITLTCPGFYGPQNRQLRAQLSEPGIFSVARKIKVENHVITNLEMETAAIYG 248
Cdd:cd00436   161 FKGKPRPYVVKASPELLDALTGVG-YVVGITATAPGFYGPQGRQLRLPLADPDLLDKLSSFSYGGLRITNFEMETSAIYG 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1085149888 249 MARLLNHDACSINAILANRFTHSFSSNPDRVVEQMIQKVL 288
Cdd:cd00436   240 LSRLLGHRALSICAIIANRATGEFSKDYKKAVEKLIEKVL 279
 
Name Accession Description Interval E-value
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
9-288 5.01e-162

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: 451.54  E-value: 5.01e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888   9 ELVLNADGSVYHLNLLPEEIADTIILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITM 88
Cdd:cd00436     1 ELILNPDGSIYHLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  89 NELDALHNIDLKNRVVKNNHKKLNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYDWKNNEAEKKLLTACREKFSA 168
Cdd:cd00436    81 NELDALVNIDFKTRTPKEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNLLNFYDHPNTDEEAELENAFIAHTSW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 169 TPFLNTLYVAAGAKSLIDLFEKNNlGLTGITLTCPGFYGPQNRQLRAQLSEPGIFSVARKIKVENHVITNLEMETAAIYG 248
Cdd:cd00436   161 FKGKPRPYVVKASPELLDALTGVG-YVVGITATAPGFYGPQGRQLRLPLADPDLLDKLSSFSYGGLRITNFEMETSAIYG 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1085149888 249 MARLLNHDACSINAILANRFTHSFSSNPDRVVEQMIQKVL 288
Cdd:cd00436   240 LSRLLGHRALSICAIIANRATGEFSKDYKKAVEKLIEKVL 279
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
15-288 4.53e-83

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 250.08  E-value: 4.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  15 DGSVYHLNLLPEEIADTIILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELDAL 94
Cdd:COG2820     8 DGSQYHLGLKPGDVADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAAL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  95 hnidlknrvvknnhKKLNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYDWKNneaekklltacrekfsatpflnt 174
Cdd:COG2820    88 --------------GAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAE----------------------- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 175 lYVAAGAKSLIDLFEKN--NLGL---TGITLTCPGFYGPQNRQLRAQLSEPGIFSVARKIKVenhviTNLEMETAAIYGM 249
Cdd:COG2820   131 -YPAVADFELTRALVEAaeELGVdyhVGITASTDGFYAEQGRELRVDPDLDEKLEAWRKLGV-----LNVEMETAALFTL 204
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1085149888 250 ARLLNHDACSINAILANRFTHSFSSNPDRVVEQMIQKVL 288
Cdd:COG2820   205 ARLRGHRAGSVLAVSANRVTGEFSKDPEEAVERAIKVAL 243
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
18-272 4.84e-23

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: 94.96  E-value: 4.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  18 VYHLNLLPEEIADTIILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELdalhnI 97
Cdd:TIGR01718   1 VYHLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEEL-----A 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  98 DLKNRvvknnhkklNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYdwknneaekklltaCREKFSATPflNTLYV 177
Cdd:TIGR01718  76 QLGAR---------TFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHY--------------APLEFPAVA--DFEVT 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 178 AAGAKSLIDLFEKNNLGLTGITLTcpgFYGPQNRQlraqlSEPGIFSVARKIKVENHV---ITNLEMETAAIYGMARLLN 254
Cdd:TIGR01718 131 TALVEAAESIGVRHHVGVVASSDT---FYPGQERD-----TYSGRVVRHFKGSMEAWQamgVLNYEMESATLFTLCSSQG 202
                         250
                  ....*....|....*...
gi 1085149888 255 HDACSINAILANRFTHSF 272
Cdd:TIGR01718 203 LRAGMVAGVIVNRTQQEI 220
PRK11178 PRK11178
uridine phosphorylase; Provisional
18-267 3.52e-18

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 81.63  E-value: 3.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  18 VYHLNLLPEEI--ADTIILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELDALH 95
Cdd:PRK11178    4 VFHLGLTKADLqgATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  96 nidlknrvVKnnhkklNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYdwknneaekklltACRE-----KFSATp 170
Cdd:PRK11178   84 --------VR------TFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHF-------------APLEfpavaDFECT- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 171 flNTLYVAA---GAKSLIdlfeknnlgltGITLTCPGFYGPQNRQlraqlsepGIFS--VARKIK-----VENHVITNLE 240
Cdd:PRK11178  136 --TALVEAAksiGATTHV-----------GVTASSDTFYPGQERY--------DTYSgrVVRRFKgsmeeWQAMGVMNYE 194
                         250       260
                  ....*....|....*....|....*..
gi 1085149888 241 METAAIYGMARLLNHDACSINAILANR 267
Cdd:PRK11178  195 MESATLLTMCASQGLRAGMVAGVIVNR 221
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
32-263 3.58e-17

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: 78.54  E-value: 3.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  32 IILVGDPNRVKQVSKYFD-RIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDItMNELDALHNIDLKnrvvknnhkk 110
Cdd:pfam01048   3 AIIGGSPEELALLAELLDdETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAI-LAAIRLLKEFGVD---------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 111 lNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYdwkNNEAEKKLLTACRekFSATPFLNTLYVAAGAKSLIDLFEk 190
Cdd:pfam01048  72 -AIIRTGTAGGLNPDLKVGDVVIPTDAINHDGRSPLF---GPEGGPYFPDMAP--APADPELRALAKEAAERLGIPVHR- 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085149888 191 nnlgltGITLTCPGFYGPQNRQLRAqlsepgifsvARKIKVenhviTNLEMETAAIYGMARLLNHDACSINAI 263
Cdd:pfam01048 145 ------GVYATGDGFYFETPAEIRL----------LRRLGA-----DAVEMETAAEAQVAREAGIPFAAIRVV 196
 
Name Accession Description Interval E-value
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
9-288 5.01e-162

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: 451.54  E-value: 5.01e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888   9 ELVLNADGSVYHLNLLPEEIADTIILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITM 88
Cdd:cd00436     1 ELILNPDGSIYHLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  89 NELDALHNIDLKNRVVKNNHKKLNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYDWKNNEAEKKLLTACREKFSA 168
Cdd:cd00436    81 NELDALVNIDFKTRTPKEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNLLNFYDHPNTDEEAELENAFIAHTSW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 169 TPFLNTLYVAAGAKSLIDLFEKNNlGLTGITLTCPGFYGPQNRQLRAQLSEPGIFSVARKIKVENHVITNLEMETAAIYG 248
Cdd:cd00436   161 FKGKPRPYVVKASPELLDALTGVG-YVVGITATAPGFYGPQGRQLRLPLADPDLLDKLSSFSYGGLRITNFEMETSAIYG 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1085149888 249 MARLLNHDACSINAILANRFTHSFSSNPDRVVEQMIQKVL 288
Cdd:cd00436   240 LSRLLGHRALSICAIIANRATGEFSKDYKKAVEKLIEKVL 279
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
15-288 4.53e-83

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 250.08  E-value: 4.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  15 DGSVYHLNLLPEEIADTIILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELDAL 94
Cdd:COG2820     8 DGSQYHLGLKPGDVADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAAL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  95 hnidlknrvvknnhKKLNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYDWKNneaekklltacrekfsatpflnt 174
Cdd:COG2820    88 --------------GAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAE----------------------- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 175 lYVAAGAKSLIDLFEKN--NLGL---TGITLTCPGFYGPQNRQLRAQLSEPGIFSVARKIKVenhviTNLEMETAAIYGM 249
Cdd:COG2820   131 -YPAVADFELTRALVEAaeELGVdyhVGITASTDGFYAEQGRELRVDPDLDEKLEAWRKLGV-----LNVEMETAALFTL 204
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1085149888 250 ARLLNHDACSINAILANRFTHSFSSNPDRVVEQMIQKVL 288
Cdd:COG2820   205 ARLRGHRAGSVLAVSANRVTGEFSKDPEEAVERAIKVAL 243
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
19-285 3.87e-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: 147.59  E-value: 3.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  19 YHLNLLPEEIADTIILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELdalhnID 98
Cdd:cd17767     1 YHIGLKPGDVAPYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEEL-----AQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  99 LKNRVvknnhkklnFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYDWKNneaekklltacrekFSATP---FLNTL 175
Cdd:cd17767    76 LGAKT---------FIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPE--------------YPAVAdpeVVLAL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 176 YVAAgakslidlfekNNLGL---TGITLTCPGFYGPQNRQLRAQLSE-PGIFSVARKIKVenhviTNLEMETAAIYGMAR 251
Cdd:cd17767   133 VEAA-----------EELGVpyhVGITASKDSFYGGQGRPGPGLPPElPELLEEWQRAGV-----LNSEMESAALFTLAS 196
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1085149888 252 LLNHDACSINAILANRFTHSFSSNPDRV--VEQMIQ 285
Cdd:cd17767   197 LRGVRAGAVLAVVGNRVTDEAPDEEDVAagEERAIR 232
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
18-272 4.84e-23

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: 94.96  E-value: 4.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  18 VYHLNLLPEEIADTIILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELdalhnI 97
Cdd:TIGR01718   1 VYHLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEEL-----A 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  98 DLKNRvvknnhkklNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYdwknneaekklltaCREKFSATPflNTLYV 177
Cdd:TIGR01718  76 QLGAR---------TFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHY--------------APLEFPAVA--DFEVT 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 178 AAGAKSLIDLFEKNNLGLTGITLTcpgFYGPQNRQlraqlSEPGIFSVARKIKVENHV---ITNLEMETAAIYGMARLLN 254
Cdd:TIGR01718 131 TALVEAAESIGVRHHVGVVASSDT---FYPGQERD-----TYSGRVVRHFKGSMEAWQamgVLNYEMESATLFTLCSSQG 202
                         250
                  ....*....|....*...
gi 1085149888 255 HDACSINAILANRFTHSF 272
Cdd:TIGR01718 203 LRAGMVAGVIVNRTQQEI 220
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
32-290 8.03e-20

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: 85.42  E-value: 8.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  32 IILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELdalhnIDLKNRVvknnhkkl 111
Cdd:cd09005     2 AIIPGDPERVDVIDSKLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEEL-----CALGVDT-------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 112 nFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYdwknneaekklltACREKFSATPFLNTLyvaagaKSLIDLFEKN 191
Cdd:cd09005    69 -IIRVGSCGALREDIKVGDLVIADGAIRGDGVTPYY-------------VVGPPFAPEADPELT------AALEEAAKEL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 192 NLGL-TGITLTCPGFYGPQNRQLRAQLSEPGIfsvarkikvenhvitNLEMETAAIYGMARLLNHDACSINAILANRFT- 269
Cdd:cd09005   129 GLTVhVGTVWTTDAFYRETREESEKLRKLGAL---------------AVEMETSALATLAHLRGVKAASILAVSDNLITg 193
                         250       260
                  ....*....|....*....|...
gi 1085149888 270 -HSFSSNP-DRVVEQMIQKVLAL 290
Cdd:cd09005   194 eIGFVDEFlSEAEKKAIEIALDA 216
PRK11178 PRK11178
uridine phosphorylase; Provisional
18-267 3.52e-18

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 81.63  E-value: 3.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  18 VYHLNLLPEEI--ADTIILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELDALH 95
Cdd:PRK11178    4 VFHLGLTKADLqgATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  96 nidlknrvVKnnhkklNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYdwknneaekklltACRE-----KFSATp 170
Cdd:PRK11178   84 --------VR------TFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHF-------------APLEfpavaDFECT- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 171 flNTLYVAA---GAKSLIdlfeknnlgltGITLTCPGFYGPQNRQlraqlsepGIFS--VARKIK-----VENHVITNLE 240
Cdd:PRK11178  136 --TALVEAAksiGATTHV-----------GVTASSDTFYPGQERY--------DTYSgrVVRRFKgsmeeWQAMGVMNYE 194
                         250       260
                  ....*....|....*....|....*..
gi 1085149888 241 METAAIYGMARLLNHDACSINAILANR 267
Cdd:PRK11178  195 MESATLLTMCASQGLRAGMVAGVIVNR 221
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
32-281 1.94e-17

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: 79.93  E-value: 1.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  32 IILVGDPNRVKQVSKYFDRIE---VQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELDAlhnidlknrVVknnH 108
Cdd:cd17769     3 IITVGDPARARLIAKLLDKEPkvfELTSERGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREARA---------VV---D 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 109 KKLNFIRMGTSGALQDHIDVDSLLISSFGVGLDglvlyydwKNNEAEKkllTACREKFSATPFLNTLYVAAGaKSLIDLF 188
Cdd:cd17769    71 GPMAIIRLGSCGSLDPDVPVGSVVVPSASVAVT--------RNYDDDD---FAGPSTSSEKPYLISKPVPAD-PELSELL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 189 EKNNLG-------LTGITLTCPGFYGPQNRQL------RAQLSEpgifsvarKIKVENHVITNLEMETAAIYGMARLLNH 255
Cdd:cd17769   139 ESELKAslggevvVEGLNASADSFYSSQGRQDpnfpdhNENLID--------KLLKRYPGAASLEMETFHLFHLARCSRP 210
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1085149888 256 DACSINA-----ILANRFTHSFSSnPDRVVE 281
Cdd:cd17769   211 AQGKIRAaaahmVFANRTSNDFIS-PERVHE 240
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
32-263 3.58e-17

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: 78.54  E-value: 3.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  32 IILVGDPNRVKQVSKYFD-RIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDItMNELDALHNIDLKnrvvknnhkk 110
Cdd:pfam01048   3 AIIGGSPEELALLAELLDdETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAI-LAAIRLLKEFGVD---------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 111 lNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYdwkNNEAEKKLLTACRekFSATPFLNTLYVAAGAKSLIDLFEk 190
Cdd:pfam01048  72 -AIIRTGTAGGLNPDLKVGDVVIPTDAINHDGRSPLF---GPEGGPYFPDMAP--APADPELRALAKEAAERLGIPVHR- 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085149888 191 nnlgltGITLTCPGFYGPQNRQLRAqlsepgifsvARKIKVenhviTNLEMETAAIYGMARLLNHDACSINAI 263
Cdd:pfam01048 145 ------GVYATGDGFYFETPAEIRL----------LRRLGA-----DAVEMETAAEAQVAREAGIPFAAIRVV 196
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
20-290 4.18e-14

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: 69.74  E-value: 4.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  20 HLNLLPEEIADTIILVGDPNRVKQVS-KYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELDALHNID 98
Cdd:cd09006     1 HIEAKKGDIAKTVLMPGDPLRAKYIAeTFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  99 lknrvvknnhkklNFIRMGTSGALQDHIDVDSLLI-------SSFGVGLDGlvlYYDwknneaekklltacrekFSATP- 170
Cdd:cd09006    81 -------------NIIRIGTCGAYQPDLKLRDVVLamgastdSNYNRLRFG---GGD-----------------FAPIAd 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 171 -FLNTLYVAAGAKSLIDLfeknnlgLTGITLTCPGFYGPQNRQLRAqLSEPGIFSVarkikvenhvitnlEMETAAIYGM 249
Cdd:cd09006   128 fELLRKAVETAKELGIPV-------HVGNVFSSDVFYDDDPELWKK-LKKYGVLAV--------------EMEAAALYTN 185
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1085149888 250 ARLLNHDACSINAILANRFTHSFSSNPDRvvEQ----MIQkvLAL 290
Cdd:cd09006   186 AARLGKKALAILTVSDSLVTGEELSAEER--ETsftnMIE--LAL 226
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
20-290 1.04e-12

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 66.28  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  20 HLNLLPEEIADTIILVGDPNRVKQVSKYF--DRIEVQkTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELdaLHNI 97
Cdd:PRK13374    5 HINAQPGDFAETVLMPGDPLRAKYIAETYleDVVQVT-DVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHEL--IATF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  98 DLKnrvvknnhkklNFIRMGTSGALQDHIDVDSLLISSfGVGLDGlvlyydwKNNeaekklltacREKFSATPFLNTLYV 177
Cdd:PRK13374   82 GVK-----------NIIRVGSCGATQDDVKLMDVIIAQ-GASTDS-------KTN----------RIRFSGHDFAAIADY 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 178 AAGAKSLIDLFEKNNLGLTGITLTCPGFYGPqnrqlraqlsEPGIFSvarkiKVENHVITNLEMETAAIYGMARLLNHDA 257
Cdd:PRK13374  133 QLLEKAVETAREKGVPVKVGNVFSSDLFYDP----------DEDAIE-----AMERFGILGVDMEVAGLYGLAAYLGAEA 197
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1085149888 258 CSINAILANRFTHSFSSNPDRVVE--QMIQkvLAL 290
Cdd:PRK13374  198 LAILTVSDHIITGEETTAEERQLSfnDMIE--VAL 230
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
20-260 1.20e-12

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: 65.91  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  20 HLNLLPEEIADTIILVGDPNRVKQVSKYF--DRIEVQKTkREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELdaLHNI 97
Cdd:COG0813     5 HIGAKKGDIAETVLLPGDPLRAKYIAETFleDAVLVNEV-RGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYEL--ITEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  98 DLKnrvvknnhkklNFIRMGTSGALQDHIDVDSLLI----SSFGVGLDGLVLYYDwknneaekklltacrekFSATP--- 170
Cdd:COG0813    82 GVK-----------NIIRVGTCGALQEDVKVRDVVIamgaSTDSNVNRQRFGGGD-----------------FAPIAdfe 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 171 FLNTLYVAAGAKSlIDLFEknnlgltGITLTCPGFYGPqNRQLRAQLSEPGIFSVarkikvenhvitnlEMETAAIYGMA 250
Cdd:COG0813   134 LLRKAVEAAKELG-IKVHV-------GNVFSSDLFYRE-DPDLLEKLAKYGVLAV--------------EMEAAALYTLA 190
                         250
                  ....*....|
gi 1085149888 251 RLLNHDACSI 260
Cdd:COG0813   191 AKYGKRALAI 200
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
20-252 1.52e-12

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: 65.79  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  20 HLNLLPEEIADTIILVGDPNRVKQVSK-YFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELdalhnID 98
Cdd:cd17765     4 HIRAEPGDVAEAVLLPGDPGRATYIAEtFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEEL-----AQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  99 LKNRvvknnhkklNFIRMGTSGALQDHIDVDSLLISSFGVGLDGLVLYYdwknneaekklltACREKFSATP---FLNTL 175
Cdd:cd17765    79 LGVK---------RLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRAL-------------LGGEPYAPAAdfeLVEAL 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085149888 176 YVAAGAKSLidlfeKNNLGLtgiTLTCPGFYGPQNRQLRaQLSEPGIFSVarkikvenhvitnlEMETAAIYGMARL 252
Cdd:cd17765   137 YRAARAAGM-----PVHVGP---VATSDLFYDPTPDGVK-RWRRRGVLAV--------------EMEASALFTLAAL 190
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
20-278 6.42e-12

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 63.72  E-value: 6.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  20 HLNLLPEEIADTIILVGDPNRVKQVS-KYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELdaLHNID 98
Cdd:PRK05819    4 HINAKKGDIADTVLMPGDPLRAKYIAeTFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANEL--ITDYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  99 LKnrvvknnhkklNFIRMGTSGALQDHIDVDSLLISSfGVGLDGLVLYYDWKNNE----AEKKLLTACREkfsatpflnt 174
Cdd:PRK05819   82 VK-----------KLIRVGSCGALQEDVKVRDVVIAM-GASTDSNVNRIRFKGHDfapiADFDLLRKAYD---------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 175 lyvAAGAKslidlfeknnlGLT---GITLTCPGFYGPqNRQLRAQLSEPGIFSVarkikvenhvitnlEMETAAIYGMAR 251
Cdd:PRK05819  140 ---AAKEK-----------GITvhvGNVFSADLFYNP-DPEMFDVLEKYGVLGV--------------EMEAAALYGLAA 190
                         250       260
                  ....*....|....*....|....*..
gi 1085149888 252 LLNHDACSINAILANRFTHSFSSNPDR 278
Cdd:PRK05819  191 KYGVKALTILTVSDHIVTGEATTAEER 217
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
32-252 4.68e-10

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: 58.39  E-value: 4.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888  32 IILVGDPNRVKQVSKYFDRIEVQKTKREFVTHTGFIGKKHISVVGTGIGAGNIDITMNELdalhnIDLKNRVvknnhkkl 111
Cdd:cd17764     3 VIAVGDPGRVELLSTLLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEEL-----IMLGAKV-------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085149888 112 nFIRMGTSGALQDHIDVDSLLI----SSFGVGldGLVLYYDWKNNEAekklltacrekfSATPFLntlyvaagAKSLIDL 187
Cdd:cd17764    70 -IIRLGTAGGLVPELRVGDIVVatgaSYYPGG--GLGQYFPDVCPPA------------SPDPEL--------TLELVES 126
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085149888 188 FEKNNLGL-TGITLTCPGFYGpQNRQLRAQLSEPGIFSVarkikvenhvitnlEMETAAIYGMARL 252
Cdd:cd17764   127 LSKRGLKYyVGPVFSSDAFYA-EDEEFAERWSSLGFIAV--------------EMECATLFTLGWL 177
 
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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