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Conserved domains on  [gi|489819600|ref|WP_003723411|]
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MULTISPECIES: purine-nucleoside phosphorylase [Listeria]

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;
1-233 3.77e-166

DeoD-type purine-nucleoside phosphorylase;


:

Pssm-ID: 180275  Cd Length: 235  Bit Score: 457.40  E-value: 3.77e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   1 MSVHIEAKQGEIAETILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSY 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  81 DVKNLIRVGTMGGIQADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489819600 161 NDQLD-KQQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEAAIK 233
Cdd:PRK05819 161 NPDPEmFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAIL 234
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
1-233 3.77e-166

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 457.40  E-value: 3.77e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   1 MSVHIEAKQGEIAETILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSY 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  81 DVKNLIRVGTMGGIQADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489819600 161 NDQLD-KQQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEAAIK 233
Cdd:PRK05819 161 NPDPEmFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAIL 234
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 1-233 8.34e-165

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: 454.19  E-value: 8.34e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   1 MSVHIEAKQGEIAETILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSY 80
Cdd:COG0813    2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  81 DVKNLIRVGTMGGIQADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFY 160
Cdd:COG0813   82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489819600 161 NDQLDK-QQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEAAIK 233
Cdd:COG0813  162 REDPDLlEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIALEAALK 235
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 4-230 1.34e-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: 417.96  E-value: 1.34e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   4 HIEAKQGEIAETILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSYDVK 83
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  84 NLIRVGTMGGIQADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQ 163
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489819600 164 LD-KQQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEA 230
Cdd:cd09006  161 PElWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELALET 228
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 4-233 1.67e-117

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: 334.43  E-value: 1.67e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600    4 HIEAKQGEIAETILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSYDVK 83
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   84 NLIRVGTMGGIQADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQ 163
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489819600  164 LDK-QQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEAAIK 233
Cdd:TIGR00107 161 KDVfDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILALESVSQ 231
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 16-232 2.92e-38

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: 132.85  E-value: 2.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   16 ILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVN-ELIQSYDVKNLIRVGTMGGI 94
Cdd:pfam01048   3 AIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAiRLLKEFGVDAIIRTGTAGGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   95 QADVKVRDVVIAQAA------STDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQLDKQQ 168
Cdd:pfam01048  83 NPDLKVGDVVIPTDAinhdgrSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAEIR 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489819600  169 -LADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEAAI 232
Cdd:pfam01048 163 lLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADGELTHEEVEEFAERAAERAAAL 227
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
1-233 3.77e-166

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 457.40  E-value: 3.77e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   1 MSVHIEAKQGEIAETILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSY 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  81 DVKNLIRVGTMGGIQADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489819600 161 NDQLD-KQQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEAAIK 233
Cdd:PRK05819 161 NPDPEmFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAIL 234
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 1-233 8.34e-165

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: 454.19  E-value: 8.34e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   1 MSVHIEAKQGEIAETILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSY 80
Cdd:COG0813    2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  81 DVKNLIRVGTMGGIQADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFY 160
Cdd:COG0813   82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489819600 161 NDQLDK-QQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEAAIK 233
Cdd:COG0813  162 REDPDLlEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIALEAALK 235
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 4-230 1.34e-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: 417.96  E-value: 1.34e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   4 HIEAKQGEIAETILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSYDVK 83
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  84 NLIRVGTMGGIQADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQ 163
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489819600 164 LD-KQQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEA 230
Cdd:cd09006  161 PElWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELALET 228
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
1-231 4.34e-124

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 351.32  E-value: 4.34e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   1 MSVHIEAKQGEIAETILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSY 80
Cdd:PRK13374   2 STPHINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELIATF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  81 DVKNLIRVGTMGGIQADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFY 160
Cdd:PRK13374  82 GVKNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFY 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489819600 161 N-DQLDKQQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEAA 231
Cdd:PRK13374 162 DpDEDAIEAMERFGILGVDMEVAGLYGLAAYLGAEALAILTVSDHIITGEETTAEERQLSFNDMIEVALETA 233
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 4-233 1.67e-117

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: 334.43  E-value: 1.67e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600    4 HIEAKQGEIAETILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSYDVK 83
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   84 NLIRVGTMGGIQADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQ 163
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489819600  164 LDK-QQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEAAIK 233
Cdd:TIGR00107 161 KDVfDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILALESVSQ 231
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 1-231 8.14e-92

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: 269.56  E-value: 8.14e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   1 MSVHIEAKQGEIAETILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQsY 80
Cdd:cd17765    1 MPIHIRAEPGDVAEAVLLPGDPGRATYIAETFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELAQ-L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  81 DVKNLIRVGTMGGIQADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFY 160
Cdd:cd17765   80 GVKRLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEPYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489819600 161 NDQLDK-QQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEET-SAEERQTTFNDMIVVALEAA 231
Cdd:cd17765  160 DPTPDGvKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVSDLIGDPERRiDDEELRAGVDRMTEVALEAV 232
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 4-233 9.95e-70

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 213.88  E-value: 9.95e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   4 HIEAKQGEIAETILLPGDPLRAKYIAEtFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSyDVK 83
Cdd:COG2820   13 HLGLKPGDVADYVILPGDPGRVELIAS-YLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAAL-GAK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  84 NLIRVGTMGGIQADVKVRDVVIAQAAStdsqinR-----NTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADR 158
Cdd:COG2820   91 TFIRVGTSGALQPDIPVGDLVIATGAV------RldgtsNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600 159 FYNDQLDK-----------QQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERqtTFNDMIVVA 227
Cdd:COG2820  165 FYAEQGRElrvdpdldeklEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEE--AVERAIKVA 242


                 ....*.
gi 489819600 228 LEAAIK 233
Cdd:COG2820  243 LEALKK 248
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 4-232 2.41e-64

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: 199.59  E-value: 2.41e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   4 HIEAKQGEIAETILLPGDPLRAKYIAEtFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQsYDVK 83
Cdd:cd17767    2 HIGLKPGDVAPYVLLPGDPGRVERIAE-LLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQ-LGAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  84 NLIRVGTMGGIQADVKVRDVVIAQAA------StdsqinrNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSAD 157
Cdd:cd17767   80 TFIRVGTCGALQPDIKLGDLVIATGAvrdegtS-------KHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600 158 RFYNDQLDK------------QQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIV 225
Cdd:cd17767  153 SFYGGQGRPgpglppelpellEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIR 232


                 ....*..
gi 489819600 226 VALEAAI 232
Cdd:cd17767  233 VALEALK 239
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 16-230 1.92e-59

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: 186.73  E-value: 1.92e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  16 ILLPGDPLRAKYIAEtFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSYdVKNLIRVGTMGGIQ 95
Cdd:cd09005    2 AIIPGDPERVDVIDS-KLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALG-VDTIIRVGSCGALR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  96 ADVKVRDVVIAQAASTDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQLDK-QQLADYGV 174
Cdd:cd09005   80 EDIKVGDLVIADGAIRGDGVTPYYVVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETREEsEKLRKLGA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489819600 175 LGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGE-ETSAEERQTTFNDMIVVALEA 230
Cdd:cd09005  160 LAVEMETSALATLAHLRGVKAASILAVSDNLITGEiGFVDEFLSEAEKKAIEIALDA 216
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 14-230 1.05e-47

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: 156.62  E-value: 1.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  14 ETILLPGDPLRAKYIAETfLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSyDVKNLIRVGTMGG 93
Cdd:cd17764    1 ERVIAVGDPGRVELLSTL-LEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIML-GAKVIIRLGTAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  94 IQADVKVRDVVIAQAAS-TDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQLDK-QQLAD 171
Cdd:cd17764   79 LVPELRVGDIVVATGASyYPGGGLGQYFPDVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEFaERWSS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489819600 172 YGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEE--TSAEERQTTFNDMIVVALEA 230
Cdd:cd17764  159 LGFIAVEMECATLFTLGWLRGVKAGAVLVVSDNLVKGGKlmLTKEELEEKVMKAAKAVLEA 219
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 16-232 2.92e-38

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: 132.85  E-value: 2.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   16 ILLPGDPLRAKYIAETFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVN-ELIQSYDVKNLIRVGTMGGI 94
Cdd:pfam01048   3 AIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAiRLLKEFGVDAIIRTGTAGGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   95 QADVKVRDVVIAQAA------STDSQINRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQLDKQQ 168
Cdd:pfam01048  83 NPDLKVGDVVIPTDAinhdgrSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAEIR 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489819600  169 -LADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEAAI 232
Cdd:pfam01048 163 lLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADGELTHEEVEEFAERAAERAAAL 227
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 4-230 5.46e-29

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: 109.87  E-value: 5.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   4 HIEAKQGEIAETILLPGDPLRAKYIAETFleDVVLF-NQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNEL------ 76
Cdd:cd00436   12 HLHLKPEDLADTIILVGDPGRVPKVSKHF--DSIEFkKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVLNELdalvni 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  77 -IQSYDVK------NLIRVGTMGGIQADVKVRDVVIAQAA----------STDSQINRNTFAGVDFAPVADFSLLKKAY- 138
Cdd:cd00436   90 dFKTRTPKeektslNIIRLGTSGALQPDIPVGSLVISSYAigldnllnfyDHPNTDEEAELENAFIAHTSWFKGKPRPYv 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600 139 -DAGIE-----KGLSLKVGNVFSADRFY----------------NDQLDKQQLADYGVLGIEMEAAALYTLAQKYGRRAL 196
Cdd:cd00436  170 vKASPElldalTGVGYVVGITATAPGFYgpqgrqlrlpladpdlLDKLSSFSYGGLRITNFEMETSAIYGLSRLLGHRAL 249

                        250       260       270
                 ....*....|....*....|....*....|....
gi 489819600 197 AILTVSDHIFTGeeTSAEERQTTFNDMIVVALEA 230
Cdd:cd00436  250 SICAIIANRATG--EFSKDYKKAVEKLIEKVLEA 281
PRK11178 PRK11178
uridine phosphorylase; Provisional
 13-231 7.42e-27

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 103.58  E-value: 7.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  13 AETILLPGDPLRAKYIAEtFLEDVVLFNQVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQsYDVKNLIRVGTMG 92
Cdd:PRK11178  17 ATLAIVPGDPERVEKIAA-LMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQ-LGVRTFLRIGTTG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  93 GIQADVKVRDVVIAQAASTDSQINRNtFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQ--LDK---- 166
Cdd:PRK11178  95 AIQPHINVGDVLVTTASVRLDGASLH-FAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQerYDTysgr 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489819600 167 ---------QQLADYGVLGIEMEAAALYTLAQKYGRRALAILTVSDHIFTGEETSAEERQTTFNDMIVVALEAA 231
Cdd:PRK11178 174 vvrrfkgsmEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVVEAA 247
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 16-205 4.40e-25

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: 98.81  E-value: 4.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  16 ILLPGDPLRAKYIAETFLEDVVLFNQV--RGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELiqSYDVK---NLIRVGT 90
Cdd:cd17769    3 IITVGDPARARLIAKLLDKEPKVFELTseRGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREA--RAVVDgpmAIIRLGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  91 MGGIQADVKVRDVVIAQAASTdsqINRNTFAGVDFAPV--------------ADFSLLKKAYDAGIEKGLSLKVGNVF-- 154
Cdd:cd17769   81 CGSLDPDVPVGSVVVPSASVA---VTRNYDDDDFAGPStssekpyliskpvpADPELSELLESELKASLGGEVVVEGLna 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489819600 155 SADRFY-------------NDQLDKQQLADY-GVLGIEMEAAALYTLAQKYGRRALAILTVSDHI 205
Cdd:cd17769  158 SADSFYssqgrqdpnfpdhNENLIDKLLKRYpGAASLEMETFHLFHLARCSRPAQGKIRAAAAHM 222
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 41-233 6.28e-19

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: 81.88  E-value: 6.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  41 QVRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSYDVKNLIRVGTMGGIQADVKVRDVVIAQAA------STDSQ 114
Cdd:COG0775   27 QIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGLDPDLKIGDVVLATEVvqhdvdVTAFG 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600 115 INRNTFAGVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQLDKQQLADY--GVLGIEMEAAALYTLAQKYG 192
Cdd:COG0775  107 YPRGQVPGMPALFEADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRRLRERfpGALAVDMEGAAIAQVCYRFG 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489819600 193 RRALAILTVSDhiFTGEETSAEerqttFNDMIVVALEAAIK 233
Cdd:COG0775  187 VPFLVIRAISD--LAGEKAPND-----FDEFLEEAAKNAAE 220
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 41-215 5.02e-17

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: 76.77  E-value: 5.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  41 QVRGMLGFTGTYKGEKVSVMGTGMGIpsisiyVN------ELIQSYDVKNLIRVGTMGGIQADVKVRDVVIAQAA---ST 111
Cdd:cd09008   25 TIAGRTFYEGTLGGKEVVLVQSGIGK------VNaaiatqLLIDRFKPDAIINTGVAGGLDPDLKIGDVVIATKVvyhDV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600 112 DSQINRNTFAGVDFAPV---ADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQLDKQQL-ADYGVLGIEMEAAALYTL 187
Cdd:cd09008   99 DATAFGYEGGQPPGMPAyfpADPELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKEELrENFPALAVEMEGAAIAQV 178

                        170       180
                 ....*....|....*....|....*...
gi 489819600 188 AQKYGRRALAILTVSDHIFTGEETSAEE 215
Cdd:cd09008  179 CYLNGVPFLVIRSISDLADGEADEDFEE 206
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 48-230 5.50e-14

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: 68.28  E-value: 5.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  48 FTGTYKGEKVSVMGTGMGIPSISIYVNELIqSYDVKNLIRVGTMGGIQADVKVRDVVIAqaastdsqinrnTFAGVD--- 124
Cdd:cd09007   38 YRLEYDGEEVGVVGPPVGAPAAVLVLEELI-ALGAKKFIVVGSCGSLDPDLAVGDIILP------------TSALRDegt 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600 125 ---FAPVADFS-----LLKKAYDAGIEKGLSLKVGNVFSADRFYNDQLDK-QQLADYGVLGIEMEAAALYTLAQKYGRRA 195
Cdd:cd09007  105 syhYLPPSRYIepdpeLLDALEEALEKAGIPYVRGKTWTTDAPYRETRAKvARRRAEGCLAVEMEAAALFAVAQFRGVEL 184

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489819600 196 LAILTVSDHIFTGEE--TSAEERQTTFNDMIVVALEA 230
Cdd:cd09007  185 AQLLYVSDSLAGEEWdpRGRDEGKDAREKALELALEA 221
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 48-203 2.21e-11

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: 61.15  E-value: 2.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  48 FTGTYKGEKVSVMGTGMGIPSISIYVNELIQSYDVKNLIRVGTMGGIQADVKVRDVVIAQAAstdsqinRNTFAGVDFAP 127
Cdd:cd17877   32 YRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDPGLAVGDLVIADRV-------LYHDGDVPAGL 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489819600 128 VADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQLDKQQLA-DYGVLGIEMEAAALYTLAQKYGRRALAILTVSD 203
Cdd:cd17877  105 EADEKLVALAEELAAGLNLKVHRGTIITVDAIVRKSAEKAALAaRFPALAVDMESAAIAQVAAARGIPFLAIRAISD 181
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 63-214 4.35e-11

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: 61.01  E-value: 4.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  63 GMGIPSISIYVNELI------QSYDVKnLIRVGTMGGIqaDVKVRDVVIAQAASTDSQINRNTFA--G--VDFAPVADFS 132
Cdd:cd17763   80 GMGIPSLSILLHELIkllhyaGCKDVT-FIRIGTSGGI--GVEPGTVVITTEAVDGELEPFYEQVilGkvVKRPAVLDAQ 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600 133 LLKKAYDAGIE-KGLSLKVGNVFSADRFYNDQ--LD----------K----QQLADYGVLGIEMEAAALYTLAQKYGRRA 195
Cdd:cd17763  157 LAEELLECAKElDDFPTVIGKTMCANDFYEGQgrLDgafcdyteedKmaflQKLYDAGVRNIEMESLCFAAFCHRAGIKA 236

                        170       180
                 ....*....|....*....|....*.
gi 489819600 196 lAILTV-------SDHIFTGEETSAE 214
Cdd:cd17763  237 -AVVCVtllnrleGDQITSSKETLEE 261
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 32-222 3.07e-09

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 55.40  E-value: 3.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  32 FLEDVVLFNQ--VRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSYDVKNLIRVGTMGGIQADVKVRDVVIAQAA 109
Cdd:PRK14697  17 LLEKLVVQEEqiIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600 110 sTDSQINRNTFAGV---DFAPVADFSLLKKAYDAGIEKGLSLKV--GNVFSADRFYNDQLDKQQLAD-YGVLGIEMEAAA 183
Cdd:PRK14697  97 -THHDVSKTQMKNLfpfQEEFIASKELVELARKACNSSSLHIEIheGRIVSGECFVEDSKLKAKLIDeYAPHCTEMEGAA 175

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489819600 184 LYTLAQKYGRRALAILTVSDhiftgeeTSAEERQTTFND 222
Cdd:PRK14697 176 IGHVAYINEVPFLVIRCISD-------SADDEAQISYDD 207
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
48-203 4.12e-09

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 54.74  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  48 FTGTYKGEKVSVMGTGMGIPSISIYVNELIQSYDVKNLIRVGTMGGIQADVKVRDVVIAQA-ASTDSQIN-----RNTFA 121
Cdd:PRK05584  34 YTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGLAPGLKVGDVVVADElVQHDVDVTafgypYGQVP 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600 122 GVDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYNDQLDKQQLAD--YGVLGIEMEAAALYTLAQKYGRRALAIL 199
Cdd:PRK05584 114 GLPAAFKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAEKVAAIRAefPDALAVEMEGAAIAQVCHEFGVPFVVVR 193


                 ....
gi 489819600 200 TVSD 203
Cdd:PRK05584 194 AISD 197
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 51-202 1.48e-08

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: 54.00  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   51 TYKGEKVSVMGTGMGIPSISIYVNELIQ---SYDVKN--LIRVGTMGGIqaDVKVRDVVIA-QAASTDSQ-INRNTFAGV 123
Cdd:TIGR01719  74 MYKVGPVLCVSHGMGIPSISIMLHELIKllyYARCKNptFIRIGTSGGI--GVPPGTVVVSsEAVDACLKpEYEQIVLGK 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  124 DFAPVADF--SLLKKAYDAGIE--KGLSLKVGNVFSADRFYNDQL------------DK----QQLADYGVLGIEMEAAA 183
Cdd:TIGR01719 152 RVIRPTQLdeALVQELLLCGAEglDEFTTVSGNTMCTDDFYEGQGrldgafceytekDKmaylRKLYALGVRNIEMESSM 231

                         170
                  ....*....|....*....
gi 489819600  184 LYTLAQKYGRRAlAILTVS 202
Cdd:TIGR01719 232 FAAMTSRAGFKA-AVVCVT 249
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 42-227 1.21e-07

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 51.55  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  42 VRGMLGFTGTYKGEKVSVMGTGMGIPSISIYVNELIQSYDVKNLIRVGTMGGIQADVKVRDVVIAQAAsTDSQINRNTFA 121
Cdd:PRK06698  29 IAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNV-THHDVSKTQMK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600 122 GV-----DFapVADFSLLKKAYDAGIEKGLSLKV--GNVFSADRFYNDQLDKQQLAD-YGVLGIEMEAAALYTLAQKYGR 193
Cdd:PRK06698 108 NLfpfqeEF--IASKELVELARKACNSSSLHMEIheGRIVSGECFVEDSKLKAKLIDeYAPHCTEMEGAAIGHVAYINEV 185

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489819600 194 RALAILTVSDhiftgeeTSAEERQTTFNDMIVVA 227
Cdd:PRK06698 186 PFLVIRCISD-------SADDEAQISYDDFAKTA 212
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 49-203 5.55e-06

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: 45.87  E-value: 5.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600   49 TGTYKGEKVSVMGTGMGIPSISIYVNELIQSYDVKNLIRVGTMGGIQADVKVRDVVIAQAAS------TDSQINRNTFAG 122
Cdd:TIGR01704  34 TGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARyhdadvTAFGYEYGQLPG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  123 VDFAPVADFSLLKKAYDAGIEKGLSLKVGNVFSADRFYND--QLDKQQLADYGVLGIEMEAAALYTLAQKYGRRALAILT 200
Cdd:TIGR01704 114 CPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGsvGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRA 193


                  ...
gi 489819600  201 VSD 203
Cdd:TIGR01704 194 ISD 196
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 51-209 6.42e-05

AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate and adenine. It is a prokaryotic enzyme which plays a role in purine nucleoside salvage and intracellular AMP level regulation. AMN is active as a homohexamer; each monomer is comprised of a catalytic domain and a putative regulatory domain. This model represents the catalytic domain. AMN 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: 350162  Cd Length: 242  Bit Score: 42.93  E-value: 6.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600  51 TYKGEKVSVMGTGMGiPSISIYVNELIQSYDVKNLIRVGTMGGIQADVKVRDVVIAQAASTDSQINrNTFAGVDFAPVAD 130
Cdd:cd17762   55 HLKKEGITIINFGVG-SPNAATITDLLAVLRPKAVLMLGHCGGLRNSQEIGDFVLPIAAIRGEGTS-DDYLPPEVPALPS 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819600 131 FSLLKKAYDAGIEKGLSLKVGNVFSAD-RF--YNDQLdKQQLADYGVLGIEMEAAALYTLAQKY----GrralAILTVSD 203
Cdd:cd17762  133 FELQRALSDALREVGLDYRTGTVYTTDrRNweFDEAF-KEYLRESRAIAIDMESATIFAVGFANrvpyG----ALLLVSD 207


                 ....*.
gi 489819600 204 HIFTGE 209
Cdd:cd17762  208 KPLHPE 213
 
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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