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Conserved domains on  [gi|518139402|ref|WP_019309610|]
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MULTISPECIES: purine-nucleoside phosphorylase [Kocuria]

Protein Classification

DeoD family protein( domain architecture ID 10002776)

DeoD family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 5-232 5.11e-129

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: 364.05  E-value: 5.11e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   5 STPHIKPDGAPIAETILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHEF 84
Cdd:COG0813    2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  85 GCRKLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQFDLPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFY 164
Cdd:COG0813   82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518139402 165 HAQDDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRQTGFAQMIELA 232
Cdd:COG0813  162 REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIA 229
 
Name Accession Description Interval E-value
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 5-232 5.11e-129

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: 364.05  E-value: 5.11e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   5 STPHIKPDGAPIAETILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHEF 84
Cdd:COG0813    2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  85 GCRKLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQFDLPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFY 164
Cdd:COG0813   82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518139402 165 HAQDDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRQTGFAQMIELA 232
Cdd:COG0813  162 REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIA 229
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 8-232 4.44e-127

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: 358.64  E-value: 4.44e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   8 HIKPDGAPIAETILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHEFGCR 87
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  88 KLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQFDLPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHAQ 167
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518139402 168 DDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRQTGFAQMIELA 232
Cdd:cd09006  161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELA 225
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
5-232 2.96e-121

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 344.15  E-value: 2.96e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   5 STPHIKPDGAPIAETILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHEF 84
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  85 GCRKLVRIGSCGGLTPELGLNDIVLAQAASTDSNY-LAQFDlPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTF 163
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVnRIRFK-GHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLF 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518139402 164 YHAQDDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRQTGFAQMIELA 232
Cdd:PRK05819 160 YNPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIA 228
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 8-232 4.09e-81

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: 242.37  E-value: 4.09e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402    8 HIKPDGAPIAETILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHEFGCR 87
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   88 KLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQFDLPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHAQ 167
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518139402  168 DDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRQTGFAQMIELA 232
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILA 225
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 20-190 2.40e-29

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: 109.74  E-value: 2.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   20 ILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMA-LYSWELIHEFGCRKLVRIGSCGGL 98
Cdd:pfam01048   3 AIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAiLAAIRLLKEFGVDAIIRTGTAGGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   99 TPELGLNDIVLAQAASTDSNYLAQFDLPGTW------APTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHAQDDTTQ 172
Cdd:pfam01048  83 NPDLKVGDVVIPTDAINHDGRSPLFGPEGGPyfpdmaPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAEIR 162

                         170
                  ....*....|....*...
gi 518139402  173 RWARMGVLAVEMETVGLY 190
Cdd:pfam01048 163 LLRRLGADAVEMETAAEA 180
 
Name Accession Description Interval E-value
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 5-232 5.11e-129

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: 364.05  E-value: 5.11e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   5 STPHIKPDGAPIAETILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHEF 84
Cdd:COG0813    2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  85 GCRKLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQFDLPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFY 164
Cdd:COG0813   82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518139402 165 HAQDDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRQTGFAQMIELA 232
Cdd:COG0813  162 REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIA 229
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 8-232 4.44e-127

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: 358.64  E-value: 4.44e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   8 HIKPDGAPIAETILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHEFGCR 87
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  88 KLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQFDLPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHAQ 167
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518139402 168 DDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRQTGFAQMIELA 232
Cdd:cd09006  161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELA 225
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
5-232 2.96e-121

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 344.15  E-value: 2.96e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   5 STPHIKPDGAPIAETILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHEF 84
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  85 GCRKLVRIGSCGGLTPELGLNDIVLAQAASTDSNY-LAQFDlPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTF 163
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVnRIRFK-GHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLF 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518139402 164 YHAQDDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRQTGFAQMIELA 232
Cdd:PRK05819 160 YNPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIA 228
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
5-232 2.61e-101

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 293.54  E-value: 2.61e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   5 STPHIKPDGAPIAETILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHEF 84
Cdd:PRK13374   2 STPHINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELIATF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  85 GCRKLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQFDLPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFY 164
Cdd:PRK13374  82 GVKNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFY 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518139402 165 HAQDDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRQTGFAQMIELA 232
Cdd:PRK13374 162 DPDEDAIEAMERFGILGVDMEVAGLYGLAAYLGAEALAILTVSDHIITGEETTAEERQLSFNDMIEVA 229
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 8-232 4.09e-81

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: 242.37  E-value: 4.09e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402    8 HIKPDGAPIAETILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHEFGCR 87
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   88 KLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQFDLPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHAQ 167
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518139402  168 DDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRQTGFAQMIELA 232
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILA 225
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 8-232 1.47e-66

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: 205.62  E-value: 1.47e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   8 HIKPDGAPIAETILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIhEFGCR 87
Cdd:cd17765    4 HIRAEPGDVAEAVLLPGDPGRATYIAETFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELA-QLGVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  88 KLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQFdLPG-TWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHA 166
Cdd:cd17765   83 RLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRAL-LGGePYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFYDP 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518139402 167 QDDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHE-EMSPEDRQTGFAQMIELA 232
Cdd:cd17765  162 TPDGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVSDLIGDPErRIDDEELRAGVDRMTEVA 228
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 20-232 7.04e-47

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: 154.75  E-value: 7.04e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  20 ILLPGDPLRAQYIAEtFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIhEFGCRKLVRIGSCGGLT 99
Cdd:cd09005    2 AIIPGDPERVDVIDS-KLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELC-ALGVDTIIRVGSCGALR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402 100 PELGLNDIVLAQAASTDSNYLAQFDLPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHAQDDTTQRWARMGV 179
Cdd:cd09005   80 EDIKVGDLVIADGAIRGDGVTPYYVVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETREESEKLRKLGA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 518139402 180 LAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSP-EDRQTGFAQMIELA 232
Cdd:cd09005  160 LAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVdEFLSEAEKKAIEIA 213
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 2-232 3.09e-45

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 151.47  E-value: 3.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   2 PRTSTPHI--KPDGapIAETILLPGDPLRAQYIAEtFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWE 79
Cdd:COG2820    7 PDGSQYHLglKPGD--VADYVILPGDPGRVELIAS-YLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  80 LIHeFGCRKLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQFdLPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVS 159
Cdd:COG2820   84 LAA-LGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFY-APAEYPAVADFELTRALVEAAEELGVDYHVGITAS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402 160 SDTFYHAQ----------DDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRqtGFAQMI 229
Cdd:COG2820  162 TDGFYAEQgrelrvdpdlDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEE--AVERAI 239


                 ...
gi 518139402 230 ELA 232
Cdd:COG2820  240 KVA 242
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 18-218 1.76e-41

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: 140.82  E-value: 1.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  18 ETILLPGDPLRAQYIAETfLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIhEFGCRKLVRIGSCGG 97
Cdd:cd17764    1 ERVIAVGDPGRVELLSTL-LEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELI-MLGAKVIIRLGTAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  98 LTPELGLNDIVLAQAAS-TDSNYLAQFdLPGTWAPTG-SFRLLDHVYRGAAERGITAHAGNVVSSDTFYHAQDDTTQRWA 175
Cdd:cd17764   79 LVPELRVGDIVVATGASyYPGGGLGQY-FPDVCPPASpDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEFAERWS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 518139402 176 RMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSP 218
Cdd:cd17764  158 SLGFIAVEMECATLFTLGWLRGVKAGAVLVVSDNLVKGGKLML 200
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 7-232 4.34e-41

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: 140.27  E-value: 4.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   7 PHIKPDGAPIAETILLPGDPLRAQYIAEtFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHeFGC 86
Cdd:cd17767    1 YHIGLKPGDVAPYVLLPGDPGRVERIAE-LLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQ-LGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  87 RKLVRIGSCGGLTPELGLNDIVLAQAA----STDSNYLaqfdlPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDT 162
Cdd:cd17767   79 KTFIRVGTCGALQPDIKLGDLVIATGAvrdeGTSKHYV-----PPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402 163 FYHAQ-----------DDTTQRWARMGVLAVEMETVGLYANAAAAGVEALAMFTVSDNLVTHEEMSPEDRQTGFAQMIEL 231
Cdd:cd17767  154 FYGGQgrpgpglppelPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRV 233


                 .
gi 518139402 232 A 232
Cdd:cd17767  234 A 234
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 20-190 2.40e-29

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: 109.74  E-value: 2.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   20 ILLPGDPLRAQYIAETFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMA-LYSWELIHEFGCRKLVRIGSCGGL 98
Cdd:pfam01048   3 AIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAiLAAIRLLKEFGVDAIIRTGTAGGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   99 TPELGLNDIVLAQAASTDSNYLAQFDLPGTW------APTGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHAQDDTTQ 172
Cdd:pfam01048  83 NPDLKVGDVVIPTDAINHDGRSPLFGPEGGPyfpdmaPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAEIR 162

                         170
                  ....*....|....*...
gi 518139402  173 RWARMGVLAVEMETVGLY 190
Cdd:pfam01048 163 LLRRLGADAVEMETAAEA 180
PRK11178 PRK11178
uridine phosphorylase; Provisional
 12-190 3.97e-20

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 85.86  E-value: 3.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  12 DGAPIAetiLLPGDPLRAQYIAEtFLEDAVQFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIhEFGCRKLVR 91
Cdd:PRK11178  15 QGATLA---IVPGDPERVEKIAA-LMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELA-QLGVRTFLR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  92 IGSCGGLTPELGLNDIVLAQAA---STDSNYLAQFDLPGTwaptGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHAQD 168
Cdd:PRK11178  90 IGTTGAIQPHINVGDVLVTTASvrlDGASLHFAPLEFPAV----ADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQE 165

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 518139402 169 --DT------------TQRWARMGVLAVEMETVGLY 190
Cdd:PRK11178 166 ryDTysgrvvrrfkgsMEEWQAMGVMNYEMESATLL 201
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 20-190 1.17e-19

nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily is composed of mostly uncharacterized proteins with similarity to Toxoplasma gondii uridine phosphorylase (TgUPase). Toxoplasma gondii appears to have a single non-specific uridine phosphorylase which catalyzes the reversible phosphorolysis of uridine, deoxyuridine and thymidine, rather than the two distinct enzymes of mammalian cells: uridine phosphorylase (nucleoside phosphorylase-I family) and thymidine phosphorylase (nucleoside phosphorylase-II family). TgUPase is a potential target for intervention against toxoplasmosis. It belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350169  Cd Length: 255  Bit Score: 84.55  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  20 ILLPGDPLRAQYIAETFLEDAV--QFNSVRNMLGYTGTFNGRELSVMGTGMGIPSMALysweLIHEfgCRKLV------- 90
Cdd:cd17769    3 IITVGDPARARLIAKLLDKEPKvfELTSERGFLTITGRYKGVPVSIVAIGMGAPMMDF----FVRE--ARAVVdgpmaii 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  91 RIGSCGGLTPELGLNDIVLAQAASTDS-NYLAQFDLPGTWAPTGSFR----------LLDHVYR--GAAERGITAHAGNV 157
Cdd:cd17769   77 RLGSCGSLDPDVPVGSVVVPSASVAVTrNYDDDDFAGPSTSSEKPYLiskpvpadpeLSELLESelKASLGGEVVVEGLN 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 518139402 158 VSSDTFYHAQ--------DDTTQRWARM-----GVLAVEMETVGLY 190
Cdd:cd17769  157 ASADSFYSSQgrqdpnfpDHNENLIDKLlkrypGAASLEMETFHLF 202
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 52-190 5.86e-17

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: 76.75  E-value: 5.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  52 YTGTFNGRELSVMGTGMGIPSMALYSWELIHeFGCRKLVRIGSCGGLTPELGLNDIVLAQAA----STDSNYLAqfdlPG 127
Cdd:cd09007   38 YRLEYDGEEVGVVGPPVGAPAAVLVLEELIA-LGAKKFIVVGSCGSLDPDLAVGDIILPTSAlrdeGTSYHYLP----PS 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518139402 128 TWAPTGSfRLLDHVYRGAAERGITAHAGNVVSSDTFY---HAQddtTQRWARMGVLAVEMETVGLY 190
Cdd:cd09007  113 RYIEPDP-ELLDALEEALEKAGIPYVRGKTWTTDAPYretRAK---VARRRAEGCLAVEMEAAALF 174
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 37-186 6.52e-16

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


Pssm-ID: 440538  Cd Length: 231  Bit Score: 74.18  E-value: 6.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  37 LEDAVQFNSVRNMLG---YTGTFNGRELSVMGTGMGIPSMALYSWELIHEFGCRKLVRIGSCGGLTPELGLNDIVLAQAA 113
Cdd:COG0775   16 LLEALEDKKEVQIAGftfYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGLDPDLKIGDVVLATEV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402 114 ------STDSNYlAQFDLPGTWAP-TGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHaqDDTTQRWAR---MGVLAVE 183
Cdd:COG0775   96 vqhdvdVTAFGY-PRGQVPGMPALfEADPALLEAAKEAAKESGLKVVTGTIATGDRFVW--SAEEKRRLRerfPGALAVD 172


                 ...
gi 518139402 184 MET 186
Cdd:COG0775  173 MEG 175
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 52-186 1.47e-15

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: 72.91  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  52 YTGTFNGRELSVMGTGMGIPSMALYSWELIHEFGCRKLVRIGSCGGLTPELGLNDIVLA-QAASTDSNYLAQFDLPGTWA 130
Cdd:cd09008   32 YEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDPDLKIGDVVIAtKVVYHDVDATAFGYEGGQPP 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518139402 131 PTGSF-----RLLDHVYRGAAERGITAHAGNVVSSDTFYHAQDDTTQRWARMGVLAVEMET 186
Cdd:cd09008  112 GMPAYfpadpELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKEELRENFPALAVEMEG 172
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 8-190 4.74e-14

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: 69.42  E-value: 4.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   8 HIKPDgaPIAETILLPGDPLRAQYIAETFleDAVQF-NSVRNMLGYTGTFNGRELSVMGTGMGIPSM--------ALYSW 78
Cdd:cd00436   14 HLKPE--DLADTIILVGDPGRVPKVSKHF--DSIEFkKQNREFVTHTGTYKGKRITVISTGIGTDNIdivlneldALVNI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  79 EL----IHEFgCRKL--VRIGSCGGLTPELGLNDIVLAQAA---------------STDSNYLAQFDLPGTWAPT----- 132
Cdd:cd00436   90 DFktrtPKEE-KTSLniIRLGTSGALQPDIPVGSLVISSYAigldnllnfydhpntDEEAELENAFIAHTSWFKGkprpy 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518139402 133 ---GSFRLLDHVYRGAAERGITAHAGNvvssdtFY---------HAQDD------TTQRWARMGVLAVEMETVGLY 190
Cdd:cd00436  169 vvkASPELLDALTGVGYVVGITATAPG------FYgpqgrqlrlPLADPdlldklSSFSYGGLRITNFEMETSAIY 238
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
52-185 6.26e-11

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 60.13  E-value: 6.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  52 YTGTFNGRELSVMGTGMGIPSMALYSWELIHEFGCRKLVRIGSCGGLTPELGLNDIVLAQAastdsnyLAQFDL------ 125
Cdd:PRK05584  34 YTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGLAPGLKVGDVVVADE-------LVQHDVdvtafg 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518139402 126 ------PGTWAptgSF----RLLDHVYRGAAERGITAHAGNVVSSDTFYHaqDDTTQRWAR---MGVLAVEME 185
Cdd:PRK05584 107 ypygqvPGLPA---AFkadeKLVALAEKAAKELNLNVHRGLIASGDQFIA--GAEKVAAIRaefPDALAVEME 174
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 52-186 9.35e-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: 59.23  E-value: 9.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  52 YTGTFNGRELSVMGTGMGIPSMALYSWELIHEFGCRKLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQfdlpgtwAP 131
Cdd:cd17877   32 YRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDPGLAVGDLVIADRVLYHDGDVPA-------GL 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518139402 132 TGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHAQDDTTQRWARMGVLAVEMET 186
Cdd:cd17877  105 EADEKLVALAEELAAGLNLKVHRGTIITVDAIVRKSAEKAALAARFPALAVDMES 159
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 52-163 9.16e-06

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 45.39  E-value: 9.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  52 YTGTFNGRELSVMGTGMGIPSMALYSWELIHEFGCRKLVRIGSCGGLTPELGLNDIVLAQAAS---TDSNYLAQ-FDLPG 127
Cdd:PRK14697  35 YVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNVThhdVSKTQMKNlFPFQE 114

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 518139402 128 TWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSDTF 163
Cdd:PRK14697 115 EFIASKELVELARKACNSSSLHIEIHEGRIVSGECF 150
adenosylhopane_nucleosidase_HpnG-like cd17768
adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; ...
 79-187 2.61e-04

adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; similar to Burkholderia cenocepacia HpnG; adenosylhopane nucleosidase HpnG, catalyzes the second step in hopanoid side-chain biosynthesis. Hopanoids are bacterial membrane lipids. This CD belongs to the PNP_UDP_1 superfamily which includes members which accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. PNP_UDP_1 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). Superfamily members have different physiologically relevant quaternary structures: hexameric such as the trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP, homotrimeric such as human PNP and Escherichia coli PNPII (XapA), homohexameric (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 PNP_UDP_2 (nucleoside phosphorylase-II family) is a different structural family.


Pssm-ID: 350168  Cd Length: 188  Bit Score: 40.60  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  79 ELIHEFGCRKLVRIGSCGGLTPELGLNDIVLAQAASTDsnylaqfdlpGTWAPTGSfRLLDHVYRgAAERGITAHAGNVV 158
Cdd:cd17768   40 ERLLAAGARALISFGVAGGLDPALKPGDLVLPEAVVAD----------GERYPTDP-AWRRRLLR-ALPAGLRVVAGPLA 107

                         90       100
                 ....*....|....*....|....*....
gi 518139402 159 SSDTFYHAQDDTTQRWARMGVLAVEMETV 187
Cdd:cd17768  108 GSDAPVLSVADKAALHAATGAVAVDMESG 136
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 45-110 2.76e-04

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 41.54  E-value: 2.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518139402  45 SVRNMLGYTGTFNGRELSVMGTGMGIPSMALYSWELIHEFGCRKLVRIGSCGGLTPELGLNDIVLA 110
Cdd:PRK06698  28 IIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVIS 93
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 53-238 2.77e-03

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: 37.78  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402   53 TGTFNGRELSVMGTGMGIPSMALYSWELIHEFGCRKLVRIGSCGGLTPELGLNDIVLAQAASTDSNYLAQFD-------- 124
Cdd:TIGR01704  34 TGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGyeygqlpg 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  125 LPGTWAptGSFRLLDHVYRGAAERGITAHAGNVVSSDTFYHAQDDTTQRWARMGVL-AVEMETVGLYANAAAAGVEALAM 203
Cdd:TIGR01704 114 CPAGFK--ADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAiAVEMEATAIAHVCHNFNVPFVVV 191

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 518139402  204 FTVSDnlvtheeMSPEDRQTGFAQMIELAAT-VTEL 238
Cdd:TIGR01704 192 RAISD-------VADQQSHLSFDEFLAVAAKqSSLM 220
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 92-186 3.16e-03

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: 37.92  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  92 IGSCGGLTPELGLNDIVLAQAASTDSNYLAQFDLPGTWAPTgSFRLLDHVYRGAAERGITAHAGNVVSSDT-FYHAQDDT 170
Cdd:cd17762   91 LGHCGGLRNSQEIGDFVLPIAAIRGEGTSDDYLPPEVPALP-SFELQRALSDALREVGLDYRTGTVYTTDRrNWEFDEAF 169

                         90
                 ....*....|....*.
gi 518139402 171 TQRWARMGVLAVEMET 186
Cdd:cd17762  170 KEYLRESRAIAIDMES 185
PRK07077 PRK07077
phosphorylase;
85-185 3.44e-03

phosphorylase;


Pssm-ID: 235926  Cd Length: 238  Bit Score: 37.71  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518139402  85 GCRKLVRIGSCGGLTPELGLNDIVLAQAAstdSNYLAQFDLPGTWAPTGSFRLLDHVYRGAAERGITAHAGNVVSSdtfy 164
Cdd:PRK07077  53 GCAGIVSFGVAGGLDPDLAPGDLVVATAV---DAPFGRVDTDARWSARLAAALELTPVARRVVRGGLAGVEAPVVG---- 125

                         90       100
                 ....*....|....*....|.
gi 518139402 165 haQDDTTQRWARMGVLAVEME 185
Cdd:PRK07077 126 --AAAKAALHRATGALAVDME 144
 
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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