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Conserved domains on  [gi|502737515|ref|WP_012972499|]
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MULTISPECIES: purine-nucleoside phosphorylase [Streptococcus]

Protein Classification

purine-nucleoside phosphorylase( domain architecture ID 10012601)

purine-nucleoside phosphorylase catalyzes the phosphorolysis of purine nucleoside to form the corresponding free purine base and pentose-1-phosphate

EC:  2.4.2.1
Gene Ontology:  GO:0004731|GO:0009164|GO:0042278
PubMed:  24479338

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
1-235 2.16e-148

DeoD-type purine-nucleoside phosphorylase;


:

Pssm-ID: 180275  Cd Length: 235  Bit Score: 412.71  E-value: 2.16e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   1 MSIHIAAQQGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDY 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502737515 161 SNYFEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNpDEDTTAEERQNTFTDMMKVGLETLIA 235
Cdd:PRK05819 161 NPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVT-GEATTAEERQTTFNDMIEIALESAIL 234
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
1-235 2.16e-148

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 412.71  E-value: 2.16e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   1 MSIHIAAQQGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDY 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502737515 161 SNYFEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNpDEDTTAEERQNTFTDMMKVGLETLIA 235
Cdd:PRK05819 161 NPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVT-GEATTAEERQTTFNDMIEIALESAIL 234
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 1-235 5.81e-140

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: 391.40  E-value: 5.81e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   1 MSIHIAAQQGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDY 80
Cdd:COG0813    2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFY 160
Cdd:COG0813   82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502737515 161 SNYFEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNpDEDTTAEERQNTFTDMMKVGLETLIA 235
Cdd:COG0813  162 REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVT-GEETTAEERQTTFNDMMEIALEAALK 235
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 4-232 5.09e-133

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: 373.66  E-value: 5.09e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   4 HIAAQQGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVK 83
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  84 KLIRVGTAGSLNEDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFYSNY 163
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502737515 164 FEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNpDEDTTAEERQNTFTDMMKVGLET 232
Cdd:cd09006  161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVT-GEELSAEERETSFTNMIELALET 228
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 4-231 2.53e-85

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: 253.16  E-value: 2.53e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515    4 HIAAQQGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVK 83
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   84 KLIRVGTAGSLNEDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFYSNY 163
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502737515  164 FEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNpDEDTTAEERQNTFTDMMKVGLE 231
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVT-HEATTAEERQTTFKDMIILALE 227
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 16-235 4.33e-37

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: 129.77  E-value: 4.33e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   16 ILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISI-YARELIVDYGVKKLIRVGTAGSL 94
Cdd:pfam01048   3 AIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAIlAAIRLLKEFGVDAIIRTGTAGGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   95 NEDVHVRELVLAQAAA---TNSNIIRNDWPQYDFPQ---IASFDLLDKAYHIAKELGMTTHVGNVLSSDVFYSNYFEKNI 168
Cdd:pfam01048  83 NPDLKVGDVVIPTDAInhdGRSPLFGPEGGPYFPDMapaPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAEIR 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502737515  169 ELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLvnpDEDTTAEERQNTFTDMMKVGLETLIA 235
Cdd:pfam01048 163 LLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLA---AGGADGELTHEEVEEFAERAAERAAA 226
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
1-235 2.16e-148

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 412.71  E-value: 2.16e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   1 MSIHIAAQQGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDY 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502737515 161 SNYFEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNpDEDTTAEERQNTFTDMMKVGLETLIA 235
Cdd:PRK05819 161 NPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVT-GEATTAEERQTTFNDMIEIALESAIL 234
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 1-235 5.81e-140

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: 391.40  E-value: 5.81e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   1 MSIHIAAQQGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDY 80
Cdd:COG0813    2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFY 160
Cdd:COG0813   82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502737515 161 SNYFEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNpDEDTTAEERQNTFTDMMKVGLETLIA 235
Cdd:COG0813  162 REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVT-GEETTAEERQTTFNDMMEIALEAALK 235
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 4-232 5.09e-133

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: 373.66  E-value: 5.09e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   4 HIAAQQGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVK 83
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  84 KLIRVGTAGSLNEDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFYSNY 163
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502737515 164 FEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNpDEDTTAEERQNTFTDMMKVGLET 232
Cdd:cd09006  161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVT-GEELSAEERETSFTNMIELALET 228
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
1-232 7.15e-99

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 287.38  E-value: 7.15e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   1 MSIHIAAQQGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDY 80
Cdd:PRK13374   2 STPHINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELIATF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFY 160
Cdd:PRK13374  82 GVKNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFY 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502737515 161 S---NYFEKnieLGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNpDEDTTAEERQNTFTDMMKVGLET 232
Cdd:PRK13374 162 DpdeDAIEA---MERFGILGVDMEVAGLYGLAAYLGAEALAILTVSDHIIT-GEETTAEERQLSFNDMIEVALET 232
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 4-231 2.53e-85

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: 253.16  E-value: 2.53e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515    4 HIAAQQGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVK 83
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   84 KLIRVGTAGSLNEDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFYSNY 163
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502737515  164 FEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNpDEDTTAEERQNTFTDMMKVGLE 231
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVT-HEATTAEERQTTFKDMIILALE 227
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 1-235 1.99e-75

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: 227.96  E-value: 1.99e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   1 MSIHIAAQQGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIvDY 80
Cdd:cd17765    1 MPIHIRAEPGDVAEAVLLPGDPGRATYIAETFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELA-QL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFY 160
Cdd:cd17765   80 GVKRLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEPYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502737515 161 SNYFEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNPDEDTTAEERQNTFTDMMKVGLETLIA 235
Cdd:cd17765  160 DPTPDGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVSDLIGDPERRIDDEELRAGVDRMTEVALEAVVA 234
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 16-232 4.32e-54

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: 172.86  E-value: 4.32e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  16 ILLPGDPLRAKFIAEnFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIvDYGVKKLIRVGTAGSLN 95
Cdd:cd09005    2 AIIPGDPERVDVIDS-KLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELC-ALGVDTIIRVGSCGALR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  96 EDVHVRELVLAQAAATNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFYSNYFEKNIELGKWGV 175
Cdd:cd09005   80 EDIKVGDLVIADGAIRGDGVTPYYVVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETREESEKLRKLGA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502737515 176 KAVEMEAAALYYLAAQHHVDALAIMTISDSLVNPDEDTTAEERQNTFTDMMKVGLET 232
Cdd:cd09005  160 LAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEFLSEAEKKAIEIALDA 216
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 4-234 1.95e-49

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: 161.84  E-value: 1.95e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   4 HIAAQQGEIADKILLPGDPLRAKFIAEnFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIvDYGVK 83
Cdd:cd17767    2 HIGLKPGDVAPYVLLPGDPGRVERIAE-LLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELA-QLGAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  84 KLIRVGTAGSLNEDVHVRELVLAQAAatnsniIRNDW--PQY---DFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDV 158
Cdd:cd17767   80 TFIRVGTCGALQPDIKLGDLVIATGA------VRDEGtsKHYvppEYPAVADPEVVLALVEAAEELGVPYHVGITASKDS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515 159 FYSNYF-----------EKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNpDEDTTAEERQNTFTDMMK 227
Cdd:cd17767  154 FYGGQGrpgpglppelpELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVT-DEAPDEEDVAAGEERAIR 232


                 ....*..
gi 502737515 228 VGLETLI 234
Cdd:cd17767  233 VALEALK 239
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 4-234 6.27e-48

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 158.41  E-value: 6.27e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   4 HIAAQQGEIADKILLPGDPLRAKFIAEnFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIvDYGVK 83
Cdd:COG2820   13 HLGLKPGDVADYVILPGDPGRVELIAS-YLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELA-ALGAK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  84 KLIRVGTAGSLNEDVHVRELVLAQAAatnsniIRND-----WPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDV 158
Cdd:COG2820   91 TFIRVGTSGALQPDIPVGDLVIATGA------VRLDgtsnfYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515 159 FY----------SNYFEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDslvNPDEDTTAEERQNTFTDMMKV 228
Cdd:COG2820  165 FYaeqgrelrvdPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSA---NRVTGEFSKDPEEAVERAIKV 241


                 ....*.
gi 502737515 229 GLETLI 234
Cdd:COG2820  242 ALEALK 247
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 14-233 3.76e-43

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: 145.06  E-value: 3.76e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  14 DKILLPGDPLRAKFIAEnFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVdYGVKKLIRVGTAGS 93
Cdd:cd17764    1 ERVIAVGDPGRVELLST-LLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIM-LGAKVIIRLGTAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  94 LNEDVHVRELVLAQAAA-TNSNIIRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFYSNYFEKNIELGK 172
Cdd:cd17764   79 LVPELRVGDIVVATGASyYPGGGLGQYFPDVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEFAERWSS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502737515 173 WGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLVNPDEDT-TAEERQNTFTDMMKVGLETL 233
Cdd:cd17764  159 LGFIAVEMECATLFTLGWLRGVKAGAVLVVSDNLVKGGKLMlTKEELEEKVMKAAKAVLEAL 220
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 16-235 4.33e-37

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: 129.77  E-value: 4.33e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   16 ILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISI-YARELIVDYGVKKLIRVGTAGSL 94
Cdd:pfam01048   3 AIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAIlAAIRLLKEFGVDAIIRTGTAGGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   95 NEDVHVRELVLAQAAA---TNSNIIRNDWPQYDFPQ---IASFDLLDKAYHIAKELGMTTHVGNVLSSDVFYSNYFEKNI 168
Cdd:pfam01048  83 NPDLKVGDVVIPTDAInhdGRSPLFGPEGGPYFPDMapaPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAEIR 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502737515  169 ELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTISDSLvnpDEDTTAEERQNTFTDMMKVGLETLIA 235
Cdd:pfam01048 163 LLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLA---AGGADGELTHEEVEEFAERAAERAAA 226
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 16-161 5.29e-21

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: 88.02  E-value: 5.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  16 ILLPGDPLRAKFIAENFLEDAVCFnEV---RNMFGYTGTYKGHRVSVMGTGMGMPSISIYAREL--IVDyGVKKLIRVGT 90
Cdd:cd17769    3 IITVGDPARARLIAKLLDKEPKVF-ELtseRGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREAraVVD-GPMAIIRLGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  91 AGSLNEDVHVRELVLAQAAATnsnIIRNDWPQYDFPQiasFDLLDKAYHIAK--------------ELGM---TTHVGNV 153
Cdd:cd17769   81 CGSLDPDVPVGSVVVPSASVA---VTRNYDDDDFAGP---STSSEKPYLISKpvpadpelsellesELKAslgGEVVVEG 154

                        170
                 ....*....|
gi 502737515 154 L--SSDVFYS 161
Cdd:cd17769  155 LnaSADSFYS 164
PRK11178 PRK11178
uridine phosphorylase; Provisional
 17-160 2.59e-20

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 86.25  E-value: 2.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  17 LLPGDPLRAKFIAEnFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELiVDYGVKKLIRVGTAGSLNE 96
Cdd:PRK11178  21 IVPGDPERVEKIAA-LMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEEL-AQLGVRTFLRIGTTGAIQP 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502737515  97 DVHVRELVLAQAAatnsniIRND-----WPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFY 160
Cdd:PRK11178  99 HINVGDVLVTTAS------VRLDgaslhFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY 161
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 2-109 2.75e-17

uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate. Trypanosoma brucei UP has a high specificity for uracil-containing (deoxy)nucleosides, and may function as a dimer. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350155  Cd Length: 282  Bit Score: 78.67  E-value: 2.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   2 SI-HIAAQQGEIADKILLPGDPLRAKFIAENFleDAVCF-NEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYAREL--I 77
Cdd:cd00436    9 SIyHLHLKPEDLADTIILVGDPGRVPKVSKHF--DSIEFkKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVLNELdaL 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 502737515  78 VDYGVK-----------KLIRVGTAGSLNEDVHVRELVLAQAA 109
Cdd:cd00436   87 VNIDFKtrtpkeektslNIIRLGTSGALQPDIPVGSLVISSYA 129
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 48-217 1.55e-16

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs): bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. 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: 350159  Cd Length: 222  Bit Score: 75.61  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  48 YTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVKKLIRVGTAGSLNEDVHVRELVLAQAA------ATnsniIRNDWP 121
Cdd:cd09008   32 YEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDPDLKIGDVVIATKVvyhdvdAT----AFGYEG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515 122 QYDFPQIASF----DLLDKAYHIAKELGMTTHVGNVLSSDVFYSNYFEKNIELGKWGVKAVEMEAAALYYLAAQHHVDAL 197
Cdd:cd09008  108 GQPPGMPAYFpadpELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKEELRENFPALAVEMEGAAIAQVCYLNGVPFL 187

                        170       180
                 ....*....|....*....|
gi 502737515 198 AIMTISDsLVNPDEDTTAEE 217
Cdd:cd09008  188 VIRSISD-LADGEADEDFEE 206
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 48-220 4.58e-16

Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB [Nucleotide transport and metabolism, Coenzyme transport and metabolism]; Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440538  Cd Length: 231  Bit Score: 74.56  E-value: 4.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  48 YTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVKKLIRVGTAGSLNEDVHVRELVLAQAA------ATNSNIIRNDWP 121
Cdd:COG0775   34 YLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGLDPDLKIGDVVLATEVvqhdvdVTAFGYPRGQVP 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515 122 QYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFYSNYFEKNiELGK--WGVKAVEMEAAALYYLAAQHHVDALAI 199
Cdd:COG0775  114 GMPALFEADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKR-RLRErfPGALAVDMEGAAIAQVCYRFGVPFLVI 192

                        170       180
                 ....*....|....*....|.
gi 502737515 200 MTISDslvNPDEDTTAEERQN 220
Cdd:COG0775  193 RAISD---LAGEKAPNDFDEF 210
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 16-232 2.90e-12

uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed of uncharacterized members including Streptococcus pneumoniae hypothetical protein spr0068. The nucleoside phosphorylase-I (NP-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 the NP-I 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: 350158 [Multi-domain]  Cd Length: 221  Bit Score: 63.66  E-value: 2.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  16 ILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVdYGVKKLIRVGTAGSLN 95
Cdd:cd09007    6 VLVFSGDLLEYLLEEYGAEKIGELSSAGHTPLYRLEYDGEEVGVVGPPVGAPAAVLVLEELIA-LGAKKFIVVGSCGSLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  96 EDVHVRELVLAQAAatnsniIR-----------NDWPQydfpqiASFDLLDKAYHIAKELGMTTHVGNVLSSDVFYSNYF 164
Cdd:cd09007   85 PDLAVGDIILPTSA------LRdegtsyhylppSRYIE------PDPELLDALEEALEKAGIPYVRGKTWTTDAPYRETR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515 165 EKnIELGKW-GVKAVEMEaaalyylaaqHHVDALAIMTISDSLVNPDEDT-TAEERQNTFTDMMKVGLET 232
Cdd:cd09007  153 AK-VARRRAeGCLAVEMEaaalfavaqfRGVELAQLLYVSDSLAGEEWDPrGRDEGKDAREKALELALEA 221
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 48-204 1.30e-10

nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs), as well as futalosine nucleosidase and adenosylhopane nucleosidase. Bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. 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: 350170 [Multi-domain]  Cd Length: 210  Bit Score: 58.84  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  48 YTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVKKLIRVGTAGSLNEDVHVRELVLAQAAAtnsniirnDWPQYDfpq 127
Cdd:cd17877   32 YRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDPGLAVGDLVIADRVL--------YHDGDV--- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515 128 IASFDLLDKAYHIAKE----LGMTTHVGNVLSSDVFYSNYFEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMTIS 203
Cdd:cd17877  101 PAGLEADEKLVALAEElaagLNLKVHRGTIITVDAIVRKSAEKAALAARFPALAVDMESAAIAQVAAARGIPFLAIRAIS 180


                 .
gi 502737515 204 D 204
Cdd:cd17877  181 D 181
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
5-181 1.39e-09

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 56.28  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   5 IAAQQGEIAdkillpgdPLRAKfiaenfLEDAVCFNEVRNMFgYTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVKK 84
Cdd:PRK05584   6 IGAMEEEVT--------LLLDK------LENAQTITLAGREF-YTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  85 LIRVGTAGSLNEDVHVRELVLAQAAAtnsniirndwpQYD-------FP--QIA----SFD----LLDKAYHIAKELGMT 147
Cdd:PRK05584  71 VINTGVAGGLAPGLKVGDVVVADELV-----------QHDvdvtafgYPygQVPglpaAFKadekLVALAEKAAKELNLN 139

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 502737515 148 THVGNVLSSDVFYSNYfEKNIELGK--WGVKAVEME 181
Cdd:PRK05584 140 VHRGLIASGDQFIAGA-EKVAAIRAefPDALAVEME 174
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 48-205 1.21e-07

bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Provisional


Pssm-ID: 184794  Cd Length: 233  Bit Score: 50.78  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  48 YTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVKKLIRVGTAGSLNEDVHVRELVLAQAAA---TNSNIIRNDWP-QY 123
Cdd:PRK14697  35 YVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNVThhdVSKTQMKNLFPfQE 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515 124 DFpqIASFDLLDKAYHI--AKELGMTTHVGNVLSSDVFYSNYFEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMT 201
Cdd:PRK14697 115 EF--IASKELVELARKAcnSSSLHIEIHEGRIVSGECFVEDSKLKAKLIDEYAPHCTEMEGAAIGHVAYINEVPFLVIRC 192


                 ....
gi 502737515 202 ISDS 205
Cdd:PRK14697 193 ISDS 196
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 48-205 5.20e-06

bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 46.54  E-value: 5.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  48 YTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVKKLIRVGTAGSLNEDVHVRELVLAQAAA---TNSNIIRNDWP-QY 123
Cdd:PRK06698  35 YVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNVThhdVSKTQMKNLFPfQE 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515 124 DFpqIASFDLLDKAYHI--AKELGMTTHVGNVLSSDVFYSNYFEKNIELGKWGVKAVEMEAAALYYLAAQHHVDALAIMT 201
Cdd:PRK06698 115 EF--IASKELVELARKAcnSSSLHMEIHEGRIVSGECFVEDSKLKAKLIDEYAPHCTEMEGAAIGHVAYINEVPFLVIRC 192


                 ....
gi 502737515 202 ISDS 205
Cdd:PRK06698 193 ISDS 196
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 63-181 1.25e-05

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: 45.22  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515  63 GMGMPSISIYARELIvdygvkKL-----------IRVGTAGSLneDVHVRELVLAQAAATnsNIIRNDWPQY------DF 125
Cdd:cd17763   80 GMGIPSLSILLHELI------KLlhyagckdvtfIRIGTSGGI--GVEPGTVVITTEAVD--GELEPFYEQVilgkvvKR 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502737515 126 PQIASFDLLDKAYHIAKELGMTTHV-GNVLSSDVFYS------------------NYFEKnieLGKWGVKAVEME 181
Cdd:cd17763  150 PAVLDAQLAEELLECAKELDDFPTViGKTMCANDFYEgqgrldgafcdyteedkmAFLQK---LYDAGVRNIEME 221
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 16-181 1.71e-04

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: 41.67  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   16 ILLPGDPLRAKFIAENFLEDAV--CFNEVRNMFGYT---GTYKGHRVSVMGTGMGMPSISIYARELI--VDY-GVKK--L 85
Cdd:TIGR01719  34 VCMGGTPSRMKAFARYVGAELGlsCGRDYPNISERGdrfAMYKVGPVLCVSHGMGIPSISIMLHELIklLYYaRCKNptF 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502737515   86 IRVGTAGSLNED----VHVRELVLAQAAATNSNII---RNDWPQYDFPqiasfDLLDKAYHIAKEL--GMTTHVGNVLSS 156
Cdd:TIGR01719 114 IRIGTSGGIGVPpgtvVVSSEAVDACLKPEYEQIVlgkRVIRPTQLDE-----ALVQELLLCGAEGldEFTTVSGNTMCT 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 502737515  157 DVFYSNYF-----------EKNIELGKW----GVKAVEME 181
Cdd:TIGR01719 189 DDFYEGQGrldgafceyteKDKMAYLRKlyalGVRNIEME 228
 
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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