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Conserved domains on  [gi|1820367121|ref|WP_165458012|]
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5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase [Klebsiella quasipneumoniae]

Protein Classification

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase( domain architecture ID 10012466)

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose or ribosylhomocysteine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-230 5.35e-140

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


:

Pssm-ID: 180148  Cd Length: 230  Bit Score: 391.02  E-value: 5.35e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   1 MKIGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGL 80
Cdd:PRK05584    1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  81 ASTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:PRK05584   81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAEKVAA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 161 IRHNFPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENLVQNLA 230
Cdd:PRK05584  161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
 
Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-230 5.35e-140

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 391.02  E-value: 5.35e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   1 MKIGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGL 80
Cdd:PRK05584    1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  81 ASTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:PRK05584   81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAEKVAA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 161 IRHNFPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENLVQNLA 230
Cdd:PRK05584  161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
1-231 3.14e-106

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: 305.68  E-value: 3.14e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   1 MKIGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGL 80
Cdd:COG0775     1 MTIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  81 ASTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:COG0775    81 DPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRR 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820367121 161 IRHNFPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENLVQNLAR 231
Cdd:COG0775   161 LRERFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKLRS 231
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
3-225 2.26e-105

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: 303.26  E-value: 2.26e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   3 IGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLAS 82
Cdd:cd09008     1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  83 TLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAKIR 162
Cdd:cd09008    81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKEELR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820367121 163 HNFPqAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENL 225
Cdd:cd09008   161 ENFP-ALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
2-229 1.28e-82

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: 246.17  E-value: 1.28e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   2 KIGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLA 81
Cdd:TIGR01704   1 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  82 STLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAKI 161
Cdd:TIGR01704  81 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKI 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820367121 162 RHNFPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENLVQNL 229
Cdd:TIGR01704 161 RHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
2-226 5.08e-52

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: 168.29  E-value: 5.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   2 KIGIIGAMEEEVTLLRDKIENRQTI--TIGGTEIYTGQLHGVDVALLKSGIGKVAAA-MGATLLLERCQPDVIINTGSAG 78
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVgpPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAiLAAIRLLKEFGVDAIIRTGTAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  79 GLASTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGL 158
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820367121 159 AKIRHNFPqAIAVEMEATAIAHVCHNFKVPFVVVRAISDVA-----DQQSHLSFEEFLAVAARQSTLMVENLV 226
Cdd:pfam01048 161 IRLLRRLG-ADAVEMETAAEAQVAREAGIPFAAIRVVSDLAaggadGELTHEEVEEFAERAAERAAALLLALL 232
 
Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-230 5.35e-140

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 391.02  E-value: 5.35e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   1 MKIGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGL 80
Cdd:PRK05584    1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  81 ASTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:PRK05584   81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAEKVAA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 161 IRHNFPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENLVQNLA 230
Cdd:PRK05584  161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
1-231 3.14e-106

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: 305.68  E-value: 3.14e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   1 MKIGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGL 80
Cdd:COG0775     1 MTIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  81 ASTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:COG0775    81 DPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRR 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820367121 161 IRHNFPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENLVQNLAR 231
Cdd:COG0775   161 LRERFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKLRS 231
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
3-225 2.26e-105

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: 303.26  E-value: 2.26e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   3 IGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLAS 82
Cdd:cd09008     1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  83 TLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAKIR 162
Cdd:cd09008    81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKEELR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820367121 163 HNFPqAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENL 225
Cdd:cd09008   161 ENFP-ALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
2-229 1.28e-82

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: 246.17  E-value: 1.28e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   2 KIGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLA 81
Cdd:TIGR01704   1 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  82 STLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAKI 161
Cdd:TIGR01704  81 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKI 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820367121 162 RHNFPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENLVQNL 229
Cdd:TIGR01704 161 RHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
3-211 2.62e-73

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: 221.40  E-value: 2.62e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   3 IGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLAS 82
Cdd:cd17877     1 IGIIAAMPEEISPLLRRIEVLQKVRLGGFRFYRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  83 TLKVGDIVVSDEARYHDADVtafgyeygqlpgcPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAKIR 162
Cdd:cd17877    81 GLAVGDLVIADRVLYHDGDV-------------PAGLEADEKLVALAEELAAGLNLKVHRGTIITVDAIVRKSAEKAALA 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1820367121 163 HNFPqAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFL 211
Cdd:cd17877   148 ARFP-ALAVDMESAAIAQVAAARGIPFLAIRAISDPADEELPFSIEEFL 195
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
2-226 5.08e-52

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: 168.29  E-value: 5.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   2 KIGIIGAMEEEVTLLRDKIENRQTI--TIGGTEIYTGQLHGVDVALLKSGIGKVAAA-MGATLLLERCQPDVIINTGSAG 78
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVgpPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAiLAAIRLLKEFGVDAIIRTGTAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  79 GLASTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGL 158
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820367121 159 AKIRHNFPqAIAVEMEATAIAHVCHNFKVPFVVVRAISDVA-----DQQSHLSFEEFLAVAARQSTLMVENLV 226
Cdd:pfam01048 161 IRLLRRLG-ADAVEMETAAEAQVAREAGIPFAAIRVVSDLAaggadGELTHEEVEEFAERAAERAAALLLALL 232
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
3-225 4.72e-50

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: 162.46  E-value: 4.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   3 IGIIGAMEEEVTLLRDKIENRQTITIG-GTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLErCQPDVIINTGSAGGLA 81
Cdd:cd09005     1 YAIIPGDPERVDVIDSKLENPQKVSSFrGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCA-LGVDTIIRVGSCGALR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  82 STLKVGDIVVSDEARYHDADVTAFGyeygqlPGCPAGFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGS-VGLAK 160
Cdd:cd09005    80 EDIKVGDLVIADGAIRGDGVTPYYV------VGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETrEESEK 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820367121 161 IRHNFpqAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENL 225
Cdd:cd09005   154 LRKLG--ALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEFLSEAEKKAIEIALDA 216
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
2-230 6.97e-42

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 142.07  E-value: 6.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   2 KIGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLA 81
Cdd:PRK14697    3 RIGIIGAMQIEIDLLLEKLVVQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  82 STLKVGDIVVSDEARYHDADVTafgyEYGQLPGCPAGFKADEKLVAAAESCINALDLN--AVRGLIVSGDAFINGSVGLA 159
Cdd:PRK14697   83 PDVKVGDIVISTNVTHHDVSKT----QMKNLFPFQEEFIASKELVELARKACNSSSLHieIHEGRIVSGECFVEDSKLKA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820367121 160 KIRHNF-PQaiAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENLVQNLA 230
Cdd:PRK14697  159 KLIDEYaPH--CTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAKTAANYCSEIIVEMLKNIS 228
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
2-230 4.86e-38

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 137.45  E-value: 4.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   2 KIGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLA 81
Cdd:PRK06698    3 RIGIIGAMQIEIDLLLEKLIMQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  82 STLKVGDIVVSDEARYHDADVTafgyEYGQLPGCPAGFKADEKLVAAAESCIN--ALDLNAVRGLIVSGDAFINGSVGLA 159
Cdd:PRK06698   83 PDVKVGDIVISTNVTHHDVSKT----QMKNLFPFQEEFIASKELVELARKACNssSLHMEIHEGRIVSGECFVEDSKLKA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820367121 160 KIRHNFpQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENLVQNLA 230
Cdd:PRK06698  159 KLIDEY-APHCTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAKTAANYCSEIIVEMLKTIS 228
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
2-196 5.90e-25

futalosine nucleosidase which catalyzes the hydrolysis of futalosine to dehypoxanthinylfutalosine and a hypoxanthine base; similar to Thermus thermophiles MqnB; Futalosine nucleosidase (MqnB, EC 3.2.2.26, also known as futalosine hydrolase) functions in an alternative menaquinone biosynthetic pathway (the futalosine pathway) which operates in some bacteria, including Streptomyces coelicolor and Thermus thermophiles. This domain model 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), homohexomeric (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: 350166  Cd Length: 217  Bit Score: 97.61  E-value: 5.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   2 KIGIIGAMEEEvtllrdkiENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLA 81
Cdd:cd17766     1 MILIVTAVPLE--------TNLERVEAEREAVLRGLLGDQRVDVLVAGVGPVNAAAATALLLERHPPDLVINAGIAGAFP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  82 -STLKVGDIVVSDEARYHDADVtafgyeygqlpGCPAGFK-------------ADEKLVAA-AESCINALDLNAVRGLIV 146
Cdd:cd17766    73 gSGLSVGDLVVASEEIAADLGV-----------ETPEGFLsldelgfgllrigTDPYLNRFpLSALLLAAGLQVKTGPFL 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1820367121 147 SGDAfINGSVGLAK-IRHNFPqAIAVEMEATAIAHVCHNFKVPFVVVRAIS 196
Cdd:cd17766   142 TVST-VTGTAERAAeLQRRFP-AIAENMEGAAVAHAALLYGVPFLEIRGIS 190
PRK06714 PRK06714
S-adenosylhomocysteine nucleosidase; Validated
2-203 1.37e-20

S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 168652  Cd Length: 236  Bit Score: 86.51  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   2 KIGIIGAMEEEVTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLA 81
Cdd:PRK06714    3 RIAIVAAWEPELTYLHQSYPSERIEKRAAWEFHFHTINDLEIISVITGVGKVSCASCVQLLISEFQPDELFMTGICGSLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  82 STLKVGDIVVSDEARYHDadVTAFGY---EYGQLPGCPAGFKADEKLVAAAESCINALDLNavRGLIVSGDAFINGSVgL 158
Cdd:PRK06714   83 NKVKNGHIVVALNAIQHD--VTAAGSgedVFNLYNGRTAPIETTKSLVRRIKKIRSYDPIH--FGTFLSGDQRIRSSE-M 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1820367121 159 AKIRHNFPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQS 203
Cdd:PRK06714  158 RYLLHTVYGALAVDQEVAAFAYVCQINKKPFLCLKAASDQANDKT 202
PRK07164 PRK07164
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional
1-203 1.10e-19

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional


Pssm-ID: 235950  Cd Length: 218  Bit Score: 83.68  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   1 MKIGIIGAMEEE-VTLLRDKIENRQTITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGG 79
Cdd:PRK07164    4 KIIAIIYADNNEfVNLENFEFILLKNIESFQKKIAIFRYKNYNILYINTGIGLINAALATQKLIEKYQIEIIINYGAVGS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  80 LAStLKVGDIVVSDEARYHDAdVTAFgYEYGQLPGCPAGFKADEKlvaaaESCINALDLNavrglivSGDAFINGSVGLa 159
Cdd:PRK07164   84 NIN-IDLGQVVYPEKFYLLDA-ITPW-YPPGQTPGEKEFYENNKI-----NKNFNKIHLG-------SSNSFIFDLDKL- 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1820367121 160 KIRHNFPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQS 203
Cdd:PRK07164  148 KIIKDFIFVSFFDMEAFALAQVCFKNKVKFYCIKYVSDFIENNS 191
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
2-215 1.05e-16

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 76.20  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   2 KIGIIGAMEEEVTLLRDKI---ENRQTITIGGT--EIYTGQLHGVDVALLKSG---------IGKVAAAMGATLLLERCQ 67
Cdd:PLN02584   10 TVLIVIAMQAEAMPLVNALglvEDVDSPFPKGVpwVRYSGTHKGLRVHVVCPGkdkalgvdsVGTVPASLVTYAAIQALK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  68 PDVIINTGSAGGL-ASTLKVGDIVVSDEARYHDADVTAFGYE-YGqlpgcpagfkadeklVAAAESCIN---ALDLNAVR 142
Cdd:PLN02584   90 PDLIINAGTAGGFkAKGAAIGDVFLATAVANHDRRIPIPVFDkYG---------------VGTRDAFPTpnlIKALGLKE 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820367121 143 GLIVSGDAFINGSVGLAKIRHNfpQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVAD--QQSHLSFEEFLAVAA 215
Cdd:PLN02584  155 GVLSTGNSLDMTEQDEESIKAN--DATVKDMEGAAVAYVADLLKVPAIFVKAVTDIVDgdKPTAEEFLENLSAAA 227
HpnG TIGR03468
hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 ...
43-201 4.64e-16

hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 family of phosphorylases typically acting on nucleotide-sugar substrates. The genes of the family modeled here are generally in the same locus with genes involved in the biosynthesis and elaboration of hopene, the cyclization product of the polyisoprenoid squalene. This gene is adjacent to the genes PhnA-E and squalene-hopene cyclase (which would be HpnF) in Zymomonas mobilis and their association with hopene biosynthesis has been noted in the literature. Extending the gene symbol sequence, we suggest the symbol HpnG for the product of this gene. Hopanoids are known to be components of the plasma membrane and to have polar sugar head groups in Z. mobilis and other species.


Pssm-ID: 274594  Cd Length: 212  Bit Score: 73.91  E-value: 4.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  43 VALLKSGIGKVAAAMGATLLLERcQPDVIINTGSAGGLASTLKVGDIVVSDEARyhdadvtafgyeygqLPGCpaGFKAD 122
Cdd:TIGR03468  22 LLVCLSGGGPERARAAAARLMAA-GAAGLVSFGTAGALDPALQPGDLVVPEEVR---------------ADGD--RFPTD 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820367121 123 EKLVAAAESCINALdLNAVRGLIVSGDAfINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQ 201
Cdd:TIGR03468  84 PAWRRRLLEALPAG-LRVHRGVLAASDT-VVSTAAAKAALARATGAAAVDMESGAVAAVAAAAGLPFAVIRVISDPADR 160
adenosylhopane_nucleosidase_HpnG-like cd17768
adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; ...
25-201 1.32e-14

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: 69.49  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  25 TITIGGTEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCqPDVIINTGSAGGLASTLKVGDIVVSDEAryHDADVTa 104
Cdd:cd17768     5 CLTVTGLKFEARIAIGDGLLVILSGAGPERARRAAERLLAAG-ARALISFGVAGGLDPALKPGDLVLPEAV--VADGER- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 105 fgyeygqlpgcpagFKADEKLVAAAESCINAlDLNAVRGLIVSGDAFINGSVGLAKIRHNfPQAIAVEMEATAIAHVCHN 184
Cdd:cd17768    81 --------------YPTDPAWRRRLLRALPA-GLRVVAGPLAGSDAPVLSVADKAALHAA-TGAVAVDMESGAVAAVAAE 144
                         170
                  ....*....|....*..
gi 1820367121 185 FKVPFVVVRAISDVADQ 201
Cdd:cd17768   145 AGLPFAAIRAIADPADR 161
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
34-223 1.05e-13

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: 67.81  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  34 YTGQLHGVDVALLKSGIGkvAAAMG--ATLLLERCQPDVIINTGSAGGLASTLKVGDIVVSDEArYHDadvTAFGYEYGq 111
Cdd:cd09006    45 YTGTYKGKRVSVMGSGMG--MPSIGiyAYELFKFYGVKNIIRIGTCGAYQPDLKLRDVVLAMGA-STD---SNYNRLRF- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 112 LPGCPAgFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAKIRHNFpQAIAVEMEATAIAHVCHNFKVPFVV 191
Cdd:cd09006   118 GGGDFA-PIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDDPELWKKLKKY-GVLAVEMEAAALYTNAARLGKKALA 195
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1820367121 192 VRAISDvadqqsHLSFEEFLAVAARQSTL--MVE 223
Cdd:cd09006   196 ILTVSD------SLVTGEELSAEERETSFtnMIE 223
PRK05634 PRK05634
nucleosidase; Provisional
42-217 1.26e-13

nucleosidase; Provisional


Pssm-ID: 235538  Cd Length: 185  Bit Score: 66.63  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  42 DVALLKSGIGKVAAAMGAT--LLLERCQPDVIINTGSAGGLASTLkvGDIVVSDEARYHDADVTAFGyeygQLPGcpagf 119
Cdd:PRK05634   22 GLPLLITGIGKVAAAVALTraLARRGVLPPRVVNIGTAGALRDGL--SGVFEPSHVINHDFSSDLIR----ALTG----- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 120 kadeklvaaaESCINALDLNAVRG-LIVSGDAFINGSVGLAKIRHnfpQAIAVEMEATAIAHVCHNFKVPFVVVRAISDV 198
Cdd:PRK05634   91 ----------HPVANRLELPTGDGaVLATGDAFISDTATRDRLAQ---RADLVDMEGYAVAAVAAEFGVPCRLVKHVSDS 157
                         170
                  ....*....|....*....
gi 1820367121 199 ADQQSHLSFEEFLAVAARQ 217
Cdd:PRK05634  158 ADESALGSWPEAVDASARE 176
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
34-197 2.51e-13

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 67.11  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  34 YTGQLHGVDVALLKSGIGkvaAAMGATLL--LERCQPDVIINTGSAGGLASTLKVGDIVVSDEARYHDAdVTAF--GYEY 109
Cdd:COG2820    56 YTGTYKGKRITVISTGIG---GPSAAIAVeeLAALGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDG-TSNFyaPAEY 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 110 gqlpgcPAgfKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAKIRHNFPQ---------AIAVEMEATAIAH 180
Cdd:COG2820   132 ------PA--VADFELTRALVEAAEELGVDYHVGITASTDGFYAEQGRELRVDPDLDEkleawrklgVLNVEMETAALFT 203
                         170
                  ....*....|....*..
gi 1820367121 181 VCHNFKVPFVVVRAISD 197
Cdd:COG2820   204 LARLRGHRAGSVLAVSA 220
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
2-197 2.68e-13

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: 66.35  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121   2 KIGIIGAMEEEVTLLRDKIENR---QTITIGGTEIYTGQLHGVDVALLKSGIGkvAAAmgATLLLER-----CQpdVIIN 73
Cdd:cd09007     3 EKCVLVFSGDLLEYLLEEYGAEkigELSSAGHTPLYRLEYDGEEVGVVGPPVG--APA--AVLVLEElialgAK--KFIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  74 TGSAGGLASTLKVGDIVVSDEA-R-----YHdadvtafgYeygqLPgcPAGF-KADEKLVAAAESCINALDLNAVRGLIV 146
Cdd:cd09007    77 VGSCGSLDPDLAVGDIILPTSAlRdegtsYH--------Y----LP--PSRYiEPDPELLDALEEALEKAGIPYVRGKTW 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1820367121 147 SGDAFINGSVGLAKIRHNfpQ-AIAVEMEATAIAHVCHNFKVPFVVVRAISD 197
Cdd:cd09007   143 TTDAPYRETRAKVARRRA--EgCLAVEMEAAALFAVAQFRGVELAQLLYVSD 192
PRK06026 PRK06026
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated
46-232 7.73e-13

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 180353  Cd Length: 212  Bit Score: 65.07  E-value: 7.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  46 LKSGIGKVAAAMGATLLLERCQ-----PDVIINTGSAGglASTLKVGDIVVSDEARYHDADVTAFGYEYGQLP--GCPAG 118
Cdd:PRK06026   34 LMTGVGPVEAAVNLTAALARLKaagdlPDLVVSLGSAG--SAKLEQTEVYQVSSVSYRDMDASPLGFEKGVTPflDLPAT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 119 FKADEKLVAAAESCInaldlnAVRGLIVSGDAFingsvglakirhnfpQAIA---VEMEATAIAHVCHNFKVPFVVVRAI 195
Cdd:PRK06026  112 VELPLRIPGIPEASL------STGGNIVSGAAY---------------DAIDadmVDMETYAVLRACQAFGVPLIGLRGI 170
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1820367121 196 SDVADQQSHLS-FEEFLAVAARQSTLMVENLVQNLARG 232
Cdd:PRK06026  171 SDGAAELKHVGdWTEYLHVIDEKLAGAVDRLERALEDG 208
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
34-223 3.02e-11

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: 60.90  E-value: 3.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  34 YTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLASTLKVGDIVVSDEArYHD---ADVTAFGYEYg 110
Cdd:COG0813    49 YTGTYKGKRVSVMGSGMGIPSISIYAYELITEYGVKNIIRVGTCGALQEDVKVRDVVIAMGA-STDsnvNRQRFGGGDF- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 111 qLPGcpAGFKADEKLVAAAEscinALDLNAVRGLIVSGDAFINGSVGLAKIRHNFpQAIAVEMEATAIAHVCHNFKVPFV 190
Cdd:COG0813   127 -API--ADFELLRKAVEAAK----ELGIKVHVGNVFSSDLFYREDPDLLEKLAKY-GVLAVEMEAAALYTLAAKYGKRAL 198
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1820367121 191 VVRAISDvadqqsHLSFEEFLAVAARQSTL--MVE 223
Cdd:COG0813   199 AILTVSD------HLVTGEETTAEERQTTFndMME 227
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
34-178 4.22e-10

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: 57.70  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  34 YTGQLHGVDVALLKSGIGKVAAAMgatLLLERCQPDV--IINTGSAGGLASTLKVGDIVVSDEAryHDADVTAFGYEYGQ 111
Cdd:cd17765    48 YTGTYKGKPVSVQTTGMGCPSAAI---VVEELAQLGVkrLIRVGTCGGLSSGLQLGDLIVATAA--VPADGTTRALLGGE 122
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820367121 112 lPGCPAgfkADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAKIRHNFPqAIAVEMEATAI 178
Cdd:cd17765   123 -PYAPA---ADFELVEALYRAARAAGMPVHVGPVATSDLFYDPTPDGVKRWRRRG-VLAVEMEASAL 184
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
21-175 1.13e-09

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: 56.46  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  21 ENRqtitigGTEIYTGQLHGVDVALLKSGIGKVAAA--------MGAtlllercqpDVIINTGSAGGLASTLKVGDIVVS 92
Cdd:cd17764    27 ENR------GLLVYTGKYKGEEVTIATHGIGGPSAAivfeelimLGA---------KVIIRLGTAGGLVPELRVGDIVVA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  93 DEARYHDadvtafGYEYGQ-LPG-CPAGfKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAKIRHNFpQAIA 170
Cdd:cd17764    92 TGASYYP------GGGLGQyFPDvCPPA-SPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEFAERWSSL-GFIA 163

                  ....*
gi 1820367121 171 VEMEA 175
Cdd:cd17764   164 VEMEC 168
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
34-223 8.89e-09

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 54.09  E-value: 8.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  34 YTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLASTLKVGDIVVSDEA---------RYHDADVTA 104
Cdd:PRK05819   48 FTGTYKGKRVSVMGTGMGIPSISIYANELITDYGVKKLIRVGSCGALQEDVKVRDVVIAMGAstdsnvnriRFKGHDFAP 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 105 FgyeygqlpgcpagfkADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAKIRHNFpQAIAVEMEATAIAHVCHN 184
Cdd:PRK05819  128 I---------------ADFDLLRKAYDAAKEKGITVHVGNVFSADLFYNPDPEMFDVLEKY-GVLGVEMEAAALYGLAAK 191
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1820367121 185 FKVPFVVVRAISDvadqqsHLSFEEFLAVAARQSTL--MVE 223
Cdd:PRK05819  192 YGVKALTILTVSD------HIVTGEATTAEERQTTFndMIE 226
PRK07077 PRK07077
phosphorylase;
71-200 1.38e-07

phosphorylase;


Pssm-ID: 235926  Cd Length: 238  Bit Score: 50.42  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  71 IINTGSAGGLASTLKVGDIVVSDEaryhdadVTAFGYEYGQLPGCPAGFKADEKLVAAAEScinaldlnAVRGLIVSGDA 150
Cdd:PRK07077   57 IVSFGVAGGLDPDLAPGDLVVATA-------VDAPFGRVDTDARWSARLAAALELTPVARR--------VVRGGLAGVEA 121
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1820367121 151 FINGSVGLAKIRHNfPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVAD 200
Cdd:PRK07077  122 PVVGAAAKAALHRA-TGALAVDMESHIAAAFAAARGLPFAACRVIVDPAW 170
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
34-178 3.40e-07

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: 49.36  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  34 YTGQLHGVDVALLKSGIGkvaaAMGATLLLE---RCQPDVIINTGSAGGLASTLKVGDIVVSDEARYHDAdvTAFGY--- 107
Cdd:cd17767    45 YTGTYKGVPVSVCSTGIG----GPSAAIAVEelaQLGAKTFIRVGTCGALQPDIKLGDLVIATGAVRDEG--TSKHYvpp 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 108 EYgqlpgcPAgfKADEKLVAAAESCINALDLNAVRGLIVSGDAF----INGSVGLAKIRHNFPQ------AIAVEMEATA 177
Cdd:cd17767   119 EY------PA--VADPEVVLALVEAAEELGVPYHVGITASKDSFyggqGRPGPGLPPELPELLEewqragVLNSEMESAA 190

                  .
gi 1820367121 178 I 178
Cdd:cd17767   191 L 191
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
34-194 8.28e-07

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: 48.34  E-value: 8.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  34 YTGQLHGVDVALlksgigkVAAAMGATL-------LLERCQ-PDVIINTGSAGGLASTLKVGDIVVSDEA-----RYHDA 100
Cdd:cd17769    37 ITGRYKGVPVSI-------VAIGMGAPMmdffvreARAVVDgPMAIIRLGSCGSLDPDVPVGSVVVPSASvavtrNYDDD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 101 DvTAFGYEYGQLP---GCPagFKADEKLVAAAESCI--NALDLNAVRGLIVSGDAFInGSVG-------------LAKIR 162
Cdd:cd17769   110 D-FAGPSTSSEKPyliSKP--VPADPELSELLESELkaSLGGEVVVEGLNASADSFY-SSQGrqdpnfpdhnenlIDKLL 185
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1820367121 163 HNFPQAIAVEMEATAIAHVCHNFKVPFVVVRA 194
Cdd:cd17769   186 KRYPGAASLEMETFHLFHLARCSRPAQGKIRA 217
PRK08236 PRK08236
hypothetical protein; Provisional
39-196 3.46e-05

hypothetical protein; Provisional


Pssm-ID: 236194  Cd Length: 212  Bit Score: 43.51  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121  39 HGVDValLKSGIGKV-AAAMGATLLLERCQP-DVIINTGSAGGLASTLKVGDIVVSDEARYHD---------ADVTAFGY 107
Cdd:PRK08236   25 SRFDV--LAAGVGPAaAAASTARALAAAAAPyDLVVSAGIAGGFPGKAEVGSLVVADEIIAADlgaetpdgfLPVDELGF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820367121 108 eygqlpGCPAgFKADEKLVAAAESCINALDLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFKV 187
Cdd:PRK08236  103 ------GTTT-IQVDPALVRQLTEALLAAALGATAGPVLTVSTVTGTAETAAALAARHPDAVAEAMEGFGVAEAAAAAGL 175

                  ....*....
gi 1820367121 188 PFVVVRAIS 196
Cdd:PRK08236  176 PVLELRAIS 184
 
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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