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Conserved domains on  [gi|488429473|ref|WP_002498858|]
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purine-nucleoside phosphorylase [Staphylococcus epidermidis]

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;
4-236 4.39e-158

DeoD-type purine-nucleoside phosphorylase;


:

Pssm-ID: 180275  Cd Length: 235  Bit Score: 437.37  E-value: 4.39e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   4 STPHINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFF 83
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  84 DVDTIIRVGSCGALQEDVNLYDVIIAQAASTNSNYVD-QFNiPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTF 162
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRiRFK-GHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLF 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488429473 163 YNADSTFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMMEIALEIAE 236
Cdd:PRK05819 160 YNPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAI 233
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
4-236 4.39e-158

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 437.37  E-value: 4.39e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   4 STPHINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFF 83
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  84 DVDTIIRVGSCGALQEDVNLYDVIIAQAASTNSNYVD-QFNiPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTF 162
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRiRFK-GHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLF 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488429473 163 YNADSTFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMMEIALEIAE 236
Cdd:PRK05819 160 YNPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAI 233
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 4-235 8.80e-155

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: 428.76  E-value: 8.80e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   4 STPHINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFF 83
Cdd:COG0813    2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  84 DVDTIIRVGSCGALQEDVNLYDVIIAQAASTNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFY 163
Cdd:COG0813   82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488429473 164 NADSTFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMMEIALEIA 235
Cdd:COG0813  162 REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIALEAA 233
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 7-234 2.24e-150

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: 417.57  E-value: 2.24e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   7 HINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVD 86
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  87 TIIRVGSCGALQEDVNLYDVIIAQAASTNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNAD 166
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488429473 167 STFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMMEIALEI 234
Cdd:cd09006  161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELALET 228
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 7-235 1.00e-99

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: 289.75  E-value: 1.00e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473    7 HINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVD 86
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   87 TIIRVGSCGALQEDVNLYDVIIAQAASTNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNAD 166
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488429473  167 STFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMMEIALEIA 235
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILALESV 229
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 17-236 1.96e-35

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: 125.53  E-value: 1.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   17 KTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGI-YSYELYHFFDVDTIIRVGSCG 95
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAIlAAIRLLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   96 ALQEDVNLYDVIIAQAA------STNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNADSTF 169
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAinhdgrSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488429473  170 NDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILR--DEATSAEERQTSFTQMMEIALEIAE 236
Cdd:pfam01048 161 IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGgaDGELTHEEVEEFAERAAERAAALLL 229
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
4-236 4.39e-158

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 437.37  E-value: 4.39e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   4 STPHINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFF 83
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  84 DVDTIIRVGSCGALQEDVNLYDVIIAQAASTNSNYVD-QFNiPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTF 162
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRiRFK-GHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLF 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488429473 163 YNADSTFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMMEIALEIAE 236
Cdd:PRK05819 160 YNPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAI 233
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 4-235 8.80e-155

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: 428.76  E-value: 8.80e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   4 STPHINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFF 83
Cdd:COG0813    2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  84 DVDTIIRVGSCGALQEDVNLYDVIIAQAASTNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFY 163
Cdd:COG0813   82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488429473 164 NADSTFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMMEIALEIA 235
Cdd:COG0813  162 REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIALEAA 233
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 7-234 2.24e-150

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: 417.57  E-value: 2.24e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   7 HINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVD 86
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  87 TIIRVGSCGALQEDVNLYDVIIAQAASTNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNAD 166
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488429473 167 STFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMMEIALEI 234
Cdd:cd09006  161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELALET 228
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
4-235 9.01e-123

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 347.86  E-value: 9.01e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   4 STPHINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFF 83
Cdd:PRK13374   2 STPHINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELIATF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  84 DVDTIIRVGSCGALQEDVNLYDVIIAQAASTNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFY 163
Cdd:PRK13374  82 GVKNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFY 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488429473 164 NADSTFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMMEIALEIA 235
Cdd:PRK13374 162 DPDEDAIEAMERFGILGVDMEVAGLYGLAAYLGAEALAILTVSDHIITGEETTAEERQLSFNDMIEVALETA 233
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 7-235 1.00e-99

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: 289.75  E-value: 1.00e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473    7 HINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVD 86
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   87 TIIRVGSCGALQEDVNLYDVIIAQAASTNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNAD 166
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488429473  167 STFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMMEIALEIA 235
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILALESV 229
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 7-233 2.60e-70

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: 214.86  E-value: 2.60e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   7 HINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELyHFFDVD 86
Cdd:cd17765    4 HIRAEPGDVAEAVLLPGDPGRATYIAETFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEEL-AQLGVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  87 TIIRVGSCGALQEDVNLYDVIIAQAASTNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNAD 166
Cdd:cd17765   83 RLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEPYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFYDPT 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488429473 167 STFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEAT-SAEERQTSFTQMMEIALE 233
Cdd:cd17765  163 PDGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVSDLIGDPERRiDDEELRAGVDRMTEVALE 230
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 6-233 1.95e-58

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: 184.95  E-value: 1.95e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   6 PHINPNGVKIAKTVLMPGDPLRAQYIAEnLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFdV 85
Cdd:cd17767    1 YHIGLKPGDVAPYVLLPGDPGRVERIAE-LLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLG-A 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  86 DTIIRVGSCGALQEDVNLYDVIIAQAA----STNSNYVdqfniPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDT 161
Cdd:cd17767   79 KTFIRVGTCGALQPDIKLGDLVIATGAvrdeGTSKHYV-----PPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473 162 FY-----------NADSTFNDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMMEI 230
Cdd:cd17767  154 FYggqgrpgpglpPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRV 233


                 ...
gi 488429473 231 ALE 233
Cdd:cd17767  234 ALE 236
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 19-233 1.53e-55

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: 176.71  E-value: 1.53e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  19 VLMPGDPLRAQYIAEnLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELyHFFDVDTIIRVGSCGALQ 98
Cdd:cd09005    2 AIIPGDPERVDVIDS-KLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEEL-CALGVDTIIRVGSCGALR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  99 EDVNLYDVIIAQAASTNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNADSTFNDSWKKMGI 178
Cdd:cd09005   80 EDIKVGDLVIADGAIRGDGVTPYYVVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETREESEKLRKLGA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488429473 179 LGIEMESAGLYLNAIHANKKALGIFTVSDHILRDE-ATSAEERQTSFTQMMEIALE 233
Cdd:cd09005  160 LAVEMETSALATLAHLRGVKAASILAVSDNLITGEiGFVDEFLSEAEKKAIEIALD 215
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 1-233 1.47e-52

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 170.35  E-value: 1.47e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   1 MTESTPHINPNGVKIAKTVLMPGDPLRAQYIAEnLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELY 80
Cdd:COG2820    7 PDGSQYHLGLKPGDVADYVILPGDPGRVELIAS-YLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  81 HFfDVDTIIRVGSCGALQEDVNLYDVIIAQAA----STNSNYVdqfniPGHFAPIADFNLVAKAKKAADEIGAISHVGNV 156
Cdd:COG2820   86 AL-GAKTFIRVGTSGALQPDIPVGDLVIATGAvrldGTSNFYA-----PAEYPAVADFELTRALVEAAEELGVDYHVGIT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473 157 LSSDTFY-------NADSTFN---DSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERqtSFTQ 226
Cdd:COG2820  160 ASTDGFYaeqgrelRVDPDLDeklEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEE--AVER 237


                 ....*..
gi 488429473 227 MMEIALE 233
Cdd:COG2820  238 AIKVALE 244
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 17-233 2.59e-42

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: 142.75  E-value: 2.59e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  17 KTVLMPGDPLRAQYIAEnLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELyHFFDVDTIIRVGSCGA 96
Cdd:cd17764    1 ERVIAVGDPGRVELLST-LLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEEL-IMLGAKVIIRLGTAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  97 LQEDVNLYDVIIAQAAS-----TNSNYVDQFNIPghfaPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNADSTFND 171
Cdd:cd17764   79 LVPELRVGDIVVATGASyypggGLGQYFPDVCPP----ASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEFAE 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488429473 172 SWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEA--TSAEERQTSFTQMMEIALE 233
Cdd:cd17764  155 RWSSLGFIAVEMECATLFTLGWLRGVKAGAVLVVSDNLVKGGKlmLTKEELEEKVMKAAKAVLE 218
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 17-236 1.96e-35

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: 125.53  E-value: 1.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   17 KTVLMPGDPLRAQYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGI-YSYELYHFFDVDTIIRVGSCG 95
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAIlAAIRLLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   96 ALQEDVNLYDVIIAQAA------STNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNADSTF 169
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAinhdgrSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488429473  170 NDSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILR--DEATSAEERQTSFTQMMEIALEIAE 236
Cdd:pfam01048 161 IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGgaDGELTHEEVEEFAERAAERAAALLL 229
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 7-236 1.22e-32

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: 118.84  E-value: 1.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473    7 HINPNGVKIAKTVLMPGDPLRAQYIAENLLENVEqFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFfDVD 86
Cdd:TIGR01718   3 HLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVK-VASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQL-GAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   87 TIIRVGSCGALQEDVNLYDVIIAQAA----STNSNYVdqfniPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTF 162
Cdd:TIGR01718  81 TFIRVGTTGAIQPHINVGDVLITTAAvrldGASLHYA-----PLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  163 YNADSTFN-------------DSWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHILRDEATSAEERQTSFTQMME 229
Cdd:TIGR01718 156 YPGQERDTysgrvvrhfkgsmEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIK 235


                  ....*..
gi 488429473  230 IALEIAE 236
Cdd:TIGR01718 236 VAVEAVK 242
PRK11178 PRK11178
uridine phosphorylase; Provisional
 16-189 3.27e-28

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 107.44  E-value: 3.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  16 AKTVLMPGDPLRAQYIAEnLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFfDVDTIIRVGSCG 95
Cdd:PRK11178  17 ATLAIVPGDPERVEKIAA-LMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQL-GVRTFLRIGTTG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  96 ALQEDVNLYDVIIAQAAstnsnyVDQFNIPGHFAP-----IADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNAD---- 166
Cdd:PRK11178  95 AIQPHINVGDVLVTTAS------VRLDGASLHFAPlefpaVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQeryd 168

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488429473 167 -------STFNDS---WKKMGILGIEMESAGLY 189
Cdd:PRK11178 169 tysgrvvRRFKGSmeeWQAMGVMNYEMESATLL 201
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 18-189 9.91e-22

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: 89.95  E-value: 9.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  18 TVlmpGDPLRAQYIAENLLEN--VEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVD-TIIRVGSC 94
Cdd:cd17769    5 TV---GDPARARLIAKLLDKEpkVFELTSERGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREARAVVDGPmAIIRLGSC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  95 GALQEDVNLYDVIIAQAAST---NSNYVDQFN----------IPGHFAPIADF-NLVAKAKKAADEiGAISHVGNVLSSD 160
Cdd:cd17769   82 GSLDPDVPVGSVVVPSASVAvtrNYDDDDFAGpstssekpylISKPVPADPELsELLESELKASLG-GEVVVEGLNASAD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488429473 161 TFYNA----DSTFNDSWKKM---------GILGIEMESAGLY 189
Cdd:cd17769  161 SFYSSqgrqDPNFPDHNENLidkllkrypGAASLEMETFHLF 202
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 34-219 7.37e-19

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: 81.77  E-value: 7.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  34 NLLENVEQFNTVRNMFgYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVDTIIRVGSCGALQEDVNLYDVIIAQAA- 112
Cdd:cd09008   16 ELLENVEEETIAGRTF-YEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDPDLKIGDVVIATKVv 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473 113 -----STNSNYVDQFNIPGHFAPIADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNADSTFNDSWKKMGILGIEMESAG 187
Cdd:cd09008   95 yhdvdATAFGYEGGQPPGMPAYFPADPELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKEELRENFPALAVEMEGAA 174

                        170       180       190
                 ....*....|....*....|....*....|..
gi 488429473 188 LYLNAIHANKKALGIFTVSDHILRDEATSAEE 219
Cdd:cd09008  175 IAQVCYLNGVPFLVIRSISDLADGEADEDFEE 206
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 15-234 2.03e-18

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: 80.61  E-value: 2.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  15 IAKTVLMP--GDPLRAqYIAENLLENVEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELyHFFDVDTIIRVG 92
Cdd:cd09007    1 LPEKCVLVfsGDLLEY-LLEEYGAEKIGELSSAGHTPLYRLEYDGEEVGVVGPPVGAPAAVLVLEEL-IALGAKKFIVVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  93 SCGALQEDVNLYDVIIAQAAstnsnYVDQfnipG---HFAPIADF-----NLVAKAKKAADEIGAISHVGNVLSSDTFY- 163
Cdd:cd09007   79 SCGSLDPDLAVGDIILPTSA-----LRDE----GtsyHYLPPSRYiepdpELLDALEEALEKAGIPYVRGKTWTTDAPYr 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488429473 164 ------NAdstfndsWKKMGILGIEMESAGLYLNAIHANKKALGIFTVSDHI--LRDEATSAEERQTSFTQMMEIALEI 234
Cdd:cd09007  150 etrakvAR-------RRAEGCLAVEMEAAALFAVAQFRGVELAQLLYVSDSLagEEWDPRGRDEGKDAREKALELALEA 221
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 8-234 2.95e-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: 78.28  E-value: 2.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   8 INPNGV---------KIAKTVLMPGDPLRAQYIAENLL------ENVEqFNTVrnmfgyTGTYKGKEVSVMGSGMGIPSI 72
Cdd:cd00436    4 LNPDGSiyhlhlkpeDLADTIILVGDPGRVPKVSKHFDsiefkkQNRE-FVTH------TGTYKGKRITVISTGIGTDNI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  73 GIYSYELYHFFDVD-------------TIIRVGSCGALQEDVNLYDVIIAQAA------------STNSNYVDQFNIPGH 127
Cdd:cd00436   77 DIVLNELDALVNIDfktrtpkeektslNIIRLGTSGALQPDIPVGSLVISSYAigldnllnfydhPNTDEEAELENAFIA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473 128 FAPIADFNLVAKAKKAADEI-----GAISHVGNVLSSDTFY----------NADSTFND-----SWKKMGILGIEMESAG 187
Cdd:cd00436  157 HTSWFKGKPRPYVVKASPELldaltGVGYVVGITATAPGFYgpqgrqlrlpLADPDLLDklssfSYGGLRITNFEMETSA 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488429473 188 LY------------LNAIHANkkalgiftvsdhilRDEATSAEERQTSFTQMMEIALEI 234
Cdd:cd00436  237 IYglsrllghralsICAIIAN--------------RATGEFSKDYKKAVEKLIEKVLEA 281
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 34-207 2.11e-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: 75.33  E-value: 2.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  34 NLLENVEQFNTVRNMFgYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVDTIIRVGSCGALQEDVNLYDVIIAQAAS 113
Cdd:COG0775   18 EALEDKKEVQIAGFTF-YLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGLDPDLKIGDVVLATEVV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473 114 TNSNYVDQFNIPGHFAPI------ADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNADSTFNDSWKKM-GILGIEMESA 186
Cdd:COG0775   97 QHDVDVTAFGYPRGQVPGmpalfeADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRRLRERFpGALAVDMEGA 176

                        170       180
                 ....*....|....*....|..
gi 488429473 187 GLYLNAiHANKKALGIF-TVSD 207
Cdd:COG0775  177 AIAQVC-YRFGVPFLVIrAISD 197
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
35-186 2.25e-12

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 63.99  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  35 LLENVEQFNTVR---NMFgYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVDTIIRVGSCGALQEDVNLYDVIIAqa 111
Cdd:PRK05584  16 LLDKLENAQTITlagREF-YTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGLAPGLKVGDVVVA-- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473 112 asTNSNYVD----QFNIPGHFAP------IADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNAD-------STFNDswk 174
Cdd:PRK05584  93 --DELVQHDvdvtAFGYPYGQVPglpaafKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAekvaairAEFPD--- 167

                        170
                 ....*....|..
gi 488429473 175 kmgILGIEMESA 186
Cdd:PRK05584 168 ---ALAVEMEGA 176
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 17-188 1.26e-09

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: 56.77  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  17 KTVLMPGDPLR----AQYIAENLLENVEQFNTVRNMFGYTGTY---KGKEVSVMGSGMGIPSIGIYSYE----LYHFFDV 85
Cdd:cd17763   24 KFVCMGGSPGRmenfAEYLAKELGIKLPAGAALVNLSKTTDRYsmyKVGPVLSVSHGMGIPSLSILLHEliklLHYAGCK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  86 D-TIIRVGSCGALqeDVNLYDVIIAQAAstnsnyVDQFNIPGH----------FAPIADFNLVAKAKKAADEIGAISHV- 153
Cdd:cd17763  104 DvTFIRIGTSGGI--GVEPGTVVITTEA------VDGELEPFYeqvilgkvvkRPAVLDAQLAEELLECAKELDDFPTVi 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488429473 154 GNVLSSDTFYNA----DSTFND--SWKKM---------GILGIEMESAGL 188
Cdd:cd17763  176 GKTMCANDFYEGqgrlDGAFCDytEEDKMaflqklydaGVRNIEMESLCF 225
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 35-162 2.19e-08

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 53.09  E-value: 2.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  35 LLEN--VEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVDTIIRVGSCGALQEDVNLYDVIIAQAA 112
Cdd:PRK14697  17 LLEKlvVQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNV 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488429473 113 STNSNYVDQFN--IPGHFAPIADFNLVAKAKKA--ADEIGAISHVGNVLSSDTF 162
Cdd:PRK14697  97 THHDVSKTQMKnlFPFQEEFIASKELVELARKAcnSSSLHIEIHEGRIVSGECF 150
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 51-219 2.69e-08

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: 52.29  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  51 YTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVDTIIRVGSCGALQEDVNLYDVIIAqaasTNSNYVDQfniPGHFAP 130
Cdd:cd17877   32 YRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDPGLAVGDLVIA----DRVLYHDG---DVPAGL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473 131 IADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNADSTfndswKKM-----GILGIEMESAGLYLNAIHANKKALGIFTV 205
Cdd:cd17877  105 EADEKLVALAEELAAGLNLKVHRGTIITVDAIVRKSAE-----KAAlaarfPALAVDMESAAIAQVAAARGIPFLAIRAI 179

                        170
                 ....*....|....
gi 488429473 206 SDHILRDEATSAEE 219
Cdd:cd17877  180 SDPADEELPFSIEE 193
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 31-231 3.56e-08

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase which acts on its two substrates at the same active site. This enzyme is involved in the recycling of the components of S-adenosylmethionine after it has donated one of its two non-ribose sulfur ligands to an acceptor. In the case of 5-methylthioadenosine this represents the first step of the methionine salvage pathway in bacteria. This enzyme is widely distributed in bacteria, especially those that lack adenosylhomocysteinase (EC 3.3.1.1). One clade of bacteria including Agrobacterium, Mesorhizobium, Sinorhizobium and Brucella includes sequences annotated as MTA/SAH nucleotidase, but differs significantly in homology and has no independent experimental evidence. There are homologs of this enzyme in plants, some of which score between trusted and noise cutoffs here, but there is no experimental evidence to validate this function at this time. [Central intermediary metabolism, Other, Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130765  Cd Length: 228  Bit Score: 52.42  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   31 IAENLLENVEQfNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVDTIIRVGSCGALQEDVNLYDVIIAQ 110
Cdd:TIGR01704  14 LLRDKIENRQT-ISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  111 AASTNSNYVDQFN-----IPGHFAP-IADFNLVAKAKKAADEIGAISHVGNVLSSDTFYNADSTFNDSWKKMGIL-GIEM 183
Cdd:TIGR01704  93 EARYHDADVTAFGyeygqLPGCPAGfKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAiAVEM 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 488429473  184 ESAGLYLNAIHANKKALGIFTVSDhilrdeaTSAEERQTSFTQMMEIA 231
Cdd:TIGR01704 173 EATAIAHVCHNFNVPFVVVRAISD-------VADQQSHLSFDEFLAVA 213
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 35-162 1.44e-06

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 48.47  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473  35 LLEN--VEQFNTVRNMFGYTGTYKGKEVSVMGSGMGIPSIGIYSYELYHFFDVDTIIRVGSCGALQEDVNLYDVIIAQAA 112
Cdd:PRK06698  17 LLEKliMQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNV 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488429473 113 STNSNYVDQFN--IPGHFAPIADFNLVAKAKKAAD--EIGAISHVGNVLSSDTF 162
Cdd:PRK06698  97 THHDVSKTQMKnlFPFQEEFIASKELVELARKACNssSLHMEIHEGRIVSGECF 150
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 17-186 1.27e-05

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: 45.14  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   17 KTVLMPGDPLRAQYIAENLLE--NVEQFNTVRNMFGYT---GTYKGKEVSVMGSGMGIPSIGIYSYELY---HFFDVD-- 86
Cdd:TIGR01719  32 KFVCMGGTPSRMKAFARYVGAelGLSCGRDYPNISERGdrfAMYKVGPVLCVSHGMGIPSISIMLHELIkllYYARCKnp 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488429473   87 TIIRVGSCGALqeDVNLYDVIIAQAAsTNSNYVDQFNI---------PGHFAPIADFNLVAKAKKAADEIGAIShvGNVL 157
Cdd:TIGR01719 112 TFIRIGTSGGI--GVPPGTVVVSSEA-VDACLKPEYEQivlgkrvirPTQLDEALVQELLLCGAEGLDEFTTVS--GNTM 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 488429473  158 SSDTFYNA----DSTFNDSWKKM-----------GILGIEMESA 186
Cdd:TIGR01719 187 CTDDFYEGqgrlDGAFCEYTEKDkmaylrklyalGVRNIEMESS 230
 
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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