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Conserved domains on  [gi|1820375325|ref|WP_165465110|]
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5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase [Enterobacter cloacae]

Protein Classification

nucleoside phosphorylase-I family protein( domain architecture ID 762)

nucleoside phosphorylase-I family protein

CATH:  3.40.50.1580
PubMed:  11743878
SCOP:  4000573

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-230 6.78e-132

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


:

Pssm-ID: 180148  Cd Length: 230  Bit Score: 370.61  E-value: 6.78e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   1 MKIGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGL 80
Cdd:PRK05584    1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  81 AATLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:PRK05584   81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAEKVAA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325 161 IRHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQSTVMVETLVQKLA 230
Cdd:PRK05584  161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
 
Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-230 6.78e-132

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 370.61  E-value: 6.78e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   1 MKIGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGL 80
Cdd:PRK05584    1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  81 AATLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:PRK05584   81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAEKVAA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325 161 IRHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQSTVMVETLVQKLA 230
Cdd:PRK05584  161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 1-231 4.12e-97

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: 282.57  E-value: 4.12e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   1 MKIGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGL 80
Cdd:COG0775     1 MTIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  81 AATLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:COG0775    81 DPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820375325 161 IRHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQSTVMVETLVQKLAR 231
Cdd:COG0775   161 LRERFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKLRS 231
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 3-225 1.07e-93

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: 273.60  E-value: 1.07e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   3 IGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGLAA 82
Cdd:cd09008     1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  83 TLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGLAKIR 162
Cdd:cd09008    81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKEELR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820375325 163 HNFPqAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQSTVMVETL 225
Cdd:cd09008   161 ENFP-ALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 2-229 1.67e-79

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: 238.08  E-value: 1.67e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   2 KIGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGLA 81
Cdd:TIGR01704   1 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  82 ATLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGLAKI 161
Cdd:TIGR01704  81 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820375325 162 RHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQSTVMVETLVQKL 229
Cdd:TIGR01704 161 RHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 2-226 1.17e-48

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: 159.43  E-value: 1.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   2 KIGIIGAMEEEVTLLRDKIENRQTL--SLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLL-ERCKPDVIINTGSAG 78
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVgpPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIRLlKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  79 GLAATLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGL 158
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820375325 159 AKIRHNFPqAVAVEMEATAIAHVCHNFNVPFVVVRAISDVA-----DQQSHISFDEFLAVAAKQSTVMVETLV 226
Cdd:pfam01048 161 IRLLRRLG-ADAVEMETAAEAQVAREAGIPFAAIRVVSDLAaggadGELTHEEVEEFAERAAERAAALLLALL 232
 
Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-230 6.78e-132

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 370.61  E-value: 6.78e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   1 MKIGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGL 80
Cdd:PRK05584    1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  81 AATLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:PRK05584   81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAEKVAA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325 161 IRHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQSTVMVETLVQKLA 230
Cdd:PRK05584  161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 1-231 4.12e-97

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: 282.57  E-value: 4.12e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   1 MKIGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGL 80
Cdd:COG0775     1 MTIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  81 AATLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:COG0775    81 DPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820375325 161 IRHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQSTVMVETLVQKLAR 231
Cdd:COG0775   161 LRERFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKLRS 231
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 3-225 1.07e-93

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: 273.60  E-value: 1.07e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   3 IGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGLAA 82
Cdd:cd09008     1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  83 TLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGLAKIR 162
Cdd:cd09008    81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKEELR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820375325 163 HNFPqAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQSTVMVETL 225
Cdd:cd09008   161 ENFP-ALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 2-229 1.67e-79

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: 238.08  E-value: 1.67e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   2 KIGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGLA 81
Cdd:TIGR01704   1 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  82 ATLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGLAKI 161
Cdd:TIGR01704  81 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820375325 162 RHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQSTVMVETLVQKL 229
Cdd:TIGR01704 161 RHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 3-211 2.39e-69

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: 211.38  E-value: 2.39e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   3 IGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGLAA 82
Cdd:cd17877     1 IGIIAAMPEEISPLLRRIEVLQKVRLGGFRFYRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  83 TLKVGDIVVSDEARYHDADVtafgyeygqlpgcPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGLAKIR 162
Cdd:cd17877    81 GLAVGDLVIADRVLYHDGDV-------------PAGLEADEKLVALAEELAAGLNLKVHRGTIITVDAIVRKSAEKAALA 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1820375325 163 HNFPqAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFL 211
Cdd:cd17877   148 ARFP-ALAVDMESAAIAQVAAARGIPFLAIRAISDPADEELPFSIEEFL 195
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 3-218 7.08e-49

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: 159.38  E-value: 7.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   3 IGIIGAMEEEVTLLRDKIENRQTLSLG-GCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLErCKPDVIINTGSAGGLA 81
Cdd:cd09005     1 YAIIPGDPERVDVIDSKLENPQKVSSFrGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCA-LGVDTIIRVGSCGALR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  82 ATLKVGDIVVSDEARYHDADVTAFGyeygqlPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGS-VGLAK 160
Cdd:cd09005    80 EDIKVGDLVIADGAIRGDGVTPYYV------VGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETrEESEK 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820375325 161 IRHNFpqAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQS 218
Cdd:cd09005   154 LRKLG--ALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEFLSEAEKKA 209
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 2-226 1.17e-48

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: 159.43  E-value: 1.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   2 KIGIIGAMEEEVTLLRDKIENRQTL--SLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLL-ERCKPDVIINTGSAG 78
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVgpPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIRLlKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  79 GLAATLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGL 158
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820375325 159 AKIRHNFPqAVAVEMEATAIAHVCHNFNVPFVVVRAISDVA-----DQQSHISFDEFLAVAAKQSTVMVETLV 226
Cdd:pfam01048 161 IRLLRRLG-ADAVEMETAAEAQVAREAGIPFAAIRVVSDLAaggadGELTHEEVEEFAERAAERAAALLLALL 232
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 2-225 1.65e-38

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 133.60  E-value: 1.65e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   2 KIGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGLA 81
Cdd:PRK14697    3 RIGIIGAMQIEIDLLLEKLVVQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  82 ATLKVGDIVVSDEARYHDADVTafgyEYGQLPGCPAGFKADDKLIAAAESCINE--LNLNAVRGLIVSGDAFINGSVGLA 159
Cdd:PRK14697   83 PDVKVGDIVISTNVTHHDVSKT----QMKNLFPFQEEFIASKELVELARKACNSssLHIEIHEGRIVSGECFVEDSKLKA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820375325 160 KIRHNF-PQavAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQ-STVMVETL 225
Cdd:PRK14697  159 KLIDEYaPH--CTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAKTAANYcSEIIVEML 224
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 2-225 1.13e-34

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 128.59  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   2 KIGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGLA 81
Cdd:PRK06698    3 RIGIIGAMQIEIDLLLEKLIMQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  82 ATLKVGDIVVSDEARYHDADVTafgyEYGQLPGCPAGFKADDKLIAAAESCIN--ELNLNAVRGLIVSGDAFINGSVGLA 159
Cdd:PRK06698   83 PDVKVGDIVISTNVTHHDVSKT----QMKNLFPFQEEFIASKELVELARKACNssSLHMEIHEGRIVSGECFVEDSKLKA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820375325 160 KIRHNFpQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHISFDEFLAVAAKQ-STVMVETL 225
Cdd:PRK06698  159 KLIDEY-APHCTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAKTAANYcSEIIVEML 224
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
 2-196 2.63e-18

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: 79.89  E-value: 2.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   2 KIGIIGAMEEEvtllrdkiENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGLA 81
Cdd:cd17766     1 MILIVTAVPLE--------TNLERVEAEREAVLRGLLGDQRVDVLVAGVGPVNAAAATALLLERHPPDLVINAGIAGAFP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  82 AT-LKVGDIVVSDEARYHDADV-TAFGYEYGQLPGCPAGFKADDKLI--AAAESCINELNLNAVRGLIVSGDAfINGSVG 157
Cdd:cd17766    73 GSgLSVGDLVVASEEIAADLGVeTPEGFLSLDELGFGLLRIGTDPYLnrFPLSALLLAAGLQVKTGPFLTVST-VTGTAE 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1820375325 158 LAK-IRHNFPqAVAVEMEATAIAHVCHNFNVPFVVVRAIS 196
Cdd:cd17766   152 RAAeLQRRFP-AIAENMEGAAVAHAALLYGVPFLEIRGIS 190
PRK06714 PRK06714
S-adenosylhomocysteine nucleosidase; Validated
 2-203 6.66e-16

S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 168652  Cd Length: 236  Bit Score: 74.19  E-value: 6.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   2 KIGIIGAMEEEVTLLRDKIENRQTLSLGGCEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGLA 81
Cdd:PRK06714    3 RIAIVAAWEPELTYLHQSYPSERIEKRAAWEFHFHTINDLEIISVITGVGKVSCASCVQLLISEFQPDELFMTGICGSLS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  82 ATLKVGDIVVSDEARYHdaDVTAFGY---EYGQLPGCPAGFKADDKLIAAAESCINELNLNavRGLIVSGDAFINGSVgL 158
Cdd:PRK06714   83 NKVKNGHIVVALNAIQH--DVTAAGSgedVFNLYNGRTAPIETTKSLVRRIKKIRSYDPIH--FGTFLSGDQRIRSSE-M 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1820375325 159 AKIRHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQS 203
Cdd:PRK06714  158 RYLLHTVYGALAVDQEVAAFAYVCQINKKPFLCLKAASDQANDKT 202
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
 2-216 1.95e-15

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 72.73  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   2 KIGIIGAMEEEVTLLRDKIENRQTLS--LGG---CEIYSGQLNGVDVALLKSG---------IGKVAAALGATLLLERCK 67
Cdd:PLN02584   10 TVLIVIAMQAEAMPLVNALGLVEDVDspFPKgvpWVRYSGTHKGLRVHVVCPGkdkalgvdsVGTVPASLVTYAAIQALK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  68 PDVIINTGSAGGLAAT-LKVGDIVVSDEARYHDADVTAFGYE-YGqlpgcpagfkaddklIAAAESC-----INELNLNA 140
Cdd:PLN02584   90 PDLIINAGTAGGFKAKgAAIGDVFLATAVANHDRRIPIPVFDkYG---------------VGTRDAFptpnlIKALGLKE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820375325 141 vrGLIVSGDAFINGSVGLAKIRHNfpQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVAD--QQSHISFDEFLAVAAK 216
Cdd:PLN02584  155 --GVLSTGNSLDMTEQDEESIKAN--DATVKDMEGAAVAYVADLLKVPAIFVKAVTDIVDgdKPTAEEFLENLSAAAA 228
HpnG TIGR03468
hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 ...
 69-201 2.26e-14

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: 69.29  E-value: 2.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  69 DVIINTGSAGGLAATLKVGDIVVSDEARyhdadvtafgyeygqLPGCpaGFKADDKLIAAAESCInELNLNAVRGLIVSG 148
Cdd:TIGR03468  47 AGLVSFGTAGALDPALQPGDLVVPEEVR---------------ADGD--RFPTDPAWRRRLLEAL-PAGLRVHRGVLAAS 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1820375325 149 DAfINGSVGLAKIRHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQ 201
Cdd:TIGR03468 109 DT-VVSTAAAKAALARATGAAAVDMESGAVAAVAAAAGLPFAVIRVISDPADR 160
PRK07164 PRK07164
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional
 1-205 3.34e-14

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional


Pssm-ID: 235950  Cd Length: 218  Bit Score: 69.04  E-value: 3.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   1 MKIGIIGAMEEEVTLLRD----KIENRQTLSLggcEIYSGQLNGVDVALLKSGIGKVAAALGATLLLERCKPDVIINTGS 76
Cdd:PRK07164    4 KIIAIIYADNNEFVNLENfefiLLKNIESFQK---KIAIFRYKNYNILYINTGIGLINAALATQKLIEKYQIEIIINYGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  77 AGGLAaTLKVGDIVVSDEARYHDAdVTAFgYEYGQLPGCPAGFKaddkliaaaescINELNLNAVRGLIVSGDAFINGSV 156
Cdd:PRK07164   81 VGSNI-NIDLGQVVYPEKFYLLDA-ITPW-YPPGQTPGEKEFYE------------NNKINKNFNKIHLGSSNSFIFDLD 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1820375325 157 GLaKIRHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHI 205
Cdd:PRK07164  146 KL-KIIKDFIFVSFFDMEAFALAQVCFKNKVKFYCIKYVSDFIENNSDI 193
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 69-223 1.06e-11

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: 62.03  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  69 DVIINTGSAGGLAATLKVGDIVVSDEArYHDadvTAFGYEYGqLPGCPAgFKADDKLIAAAESCINELNLNAVRGLIVSG 148
Cdd:cd09006    80 KNIIRIGTCGAYQPDLKLRDVVLAMGA-STD---SNYNRLRF-GGGDFA-PIADFELLRKAVETAKELGIPVHVGNVFSS 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820375325 149 DAFINGSVGLAKIRHNFpQAVAVEMEATAIAHVCHNFNVPFVVVRAISDvadqqsHISFDEFLAVAAKQSTV--MVE 223
Cdd:cd09006   154 DVFYDDDPELWKKLKKY-GVLAVEMEAAALYTNAARLGKKALAILTVSD------SLVTGEELSAEERETSFtnMIE 223
adenosylhopane_nucleosidase_HpnG-like cd17768
adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; ...
 65-201 1.53e-10

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: 58.32  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  65 RCKPDVIINTGSAGGLAATLKVGDIVVSDEAryHDADVTafgyeygqlpgcpagFKAD----DKLIAAAEScinelNLNA 140
Cdd:cd17768    44 AAGARALISFGVAGGLDPALKPGDLVLPEAV--VADGER---------------YPTDpawrRRLLRALPA-----GLRV 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820375325 141 VRGLIVSGDAFInGSVGlAKIR-HNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQ 201
Cdd:cd17768   102 VAGPLAGSDAPV-LSVA-DKAAlHAATGAVAVDMESGAVAAVAAEAGLPFAAIRAIADPADR 161
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 65-197 2.88e-10

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 58.25  E-value: 2.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  65 RCKPDVIINTGSAGGLAATLKVGDIVVSDEARYHDAdVTAF--GYEYgqlpgcPAgfKADDKLIAAAESCINELNLNAVR 142
Cdd:COG2820    86 ALGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDG-TSNFyaPAEY------PA--VADFELTRALVEAAEELGVDYHV 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820375325 143 GLIVSGDAFINGSVGLAKIRHNFPQ---------AVAVEMEATAIAHVCHNFNVPFVVVRAISD 197
Cdd:COG2820   157 GITASTDGFYAEQGRELRVDPDLDEkleawrklgVLNVEMETAALFTLARLRGHRAGSVLAVSA 220
PRK06026 PRK06026
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated
 68-232 7.75e-10

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 180353  Cd Length: 212  Bit Score: 56.59  E-value: 7.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  68 PDVIINTGSAGglAATLKVGDIVVSDEARYHDADVTAFGYEYGQLP--GCPAGFKADDKLIAAAESCInelnlnAVRGLI 145
Cdd:PRK06026   61 PDLVVSLGSAG--SAKLEQTEVYQVSSVSYRDMDASPLGFEKGVTPflDLPATVELPLRIPGIPEASL------STGGNI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325 146 VSGDAFingsvglAKIrhnfpQAVAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHIS-FDEFLAVAAKQSTVMVET 224
Cdd:PRK06026  133 VSGAAY-------DAI-----DADMVDMETYAVLRACQAFGVPLIGLRGISDGAAELKHVGdWTEYLHVIDEKLAGAVDR 200


                  ....*...
gi 1820375325 225 LVQKLARG 232
Cdd:PRK06026  201 LERALEDG 208
PRK05634 PRK05634
nucleosidase; Provisional
 42-217 1.56e-09

nucleosidase; Provisional


Pssm-ID: 235538  Cd Length: 185  Bit Score: 55.46  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  42 DVALLKSGIGKVAAALGATLL--LERCKPDVIINTGSAGGLAATLkvGDIVVSDEARYHDADVTAF----GYEYGQLPGC 115
Cdd:PRK05634   22 GLPLLITGIGKVAAAVALTRAlaRRGVLPPRVVNIGTAGALRDGL--SGVFEPSHVINHDFSSDLIraltGHPVANRLEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325 116 PAGfkaDDKLIAaaescinelnlnavrglivSGDAFINGSVGLAKIRHnfpQAVAVEMEATAIAHVCHNFNVPFVVVRAI 195
Cdd:PRK05634  100 PTG---DGAVLA-------------------TGDAFISDTATRDRLAQ---RADLVDMEGYAVAAVAAEFGVPCRLVKHV 154

                         170       180
                  ....*....|....*....|..
gi 1820375325 196 SDVADQQSHISFDEFLAVAAKQ 217
Cdd:PRK05634  155 SDSADESALGSWPEAVDASARE 176
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 71-226 5.53e-09

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: 54.62  E-value: 5.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  71 IINTGSAGGLAATLKVGDIVVSDEAryHDADVTAFGYEYGQlPGCPAgfkADDKLIAAAESCINELNLNAVRGLIVSGDA 150
Cdd:cd17765    84 LIRVGTCGGLSSGLQLGDLIVATAA--VPADGTTRALLGGE-PYAPA---ADFELVEALYRAARAAGMPVHVGPVATSDL 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820375325 151 FINGSVGLAKIRHNFPqAVAVEMEATAIAHVCHNFNVPFVVVRAISD-VADQQSHISFDEFLAVAAKQSTVMVETLV 226
Cdd:cd17765   158 FYDPTPDGVKRWRRRG-VLAVEMEASALFTLAALRGLRAGCILTVSDlIGDPERRIDDEELRAGVDRMTEVALEAVV 233
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 69-223 6.78e-09

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: 54.35  E-value: 6.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  69 DVIINTGSAGGLAATLKVGDIVVSDEArYHD---ADVTAFGYEYgqLPGcpAGFKADDKLIAAAEscinELNLNAVRGLI 145
Cdd:COG0813    84 KNIIRVGTCGALQEDVKVRDVVIAMGA-STDsnvNRQRFGGGDF--API--ADFELLRKAVEAAK----ELGIKVHVGNV 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325 146 VSGDAFINGSVGLAKIRHNFpQAVAVEMEATAIAHVCHNFNVPFVVVRAISDvadqqsHISFDEFLAVAAKQSTV--MVE 223
Cdd:COG0813   155 FSSDLFYREDPDLLEKLAKY-GVLAVEMEAAALYTLAAKYGKRALAILTVSD------HLVTGEETTAEERQTTFndMME 227
PRK07077 PRK07077
phosphorylase;
71-200 2.11e-08

phosphorylase;


Pssm-ID: 235926  Cd Length: 238  Bit Score: 53.12  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  71 IINTGSAGGLAATLKVGDIVVSDEaryhdadVTAFGYEYGQLPGCPAGFKADDKLIAAAEScinelnlnAVRGLIVSGDA 150
Cdd:PRK07077   57 IVSFGVAGGLDPDLAPGDLVVATA-------VDAPFGRVDTDARWSARLAAALELTPVARR--------VVRGGLAGVEA 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1820375325 151 FINGSVGLAKIRHNfPQAVAVEME---ATAIAHVCHnfnVPFVVVRAISDVAD 200
Cdd:PRK07077  122 PVVGAAAKAALHRA-TGALAVDMEshiAAAFAAARG---LPFAACRVIVDPAW 170
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 2-197 2.72e-08

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: 52.49  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325   2 KIGIIGAMEEEVTLLRDKIENR---QTLSLGGCEIYSGQLNGVDVALLKSGIGkvaaALGATLLLER-----CKpdVIIN 73
Cdd:cd09007     3 EKCVLVFSGDLLEYLLEEYGAEkigELSSAGHTPLYRLEYDGEEVGVVGPPVG----APAAVLVLEElialgAK--KFIV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  74 TGSAGGLAATLKVGDIVVSDEA-R-----YHdadvtafgYeygqLPgcPAGF-KADDKLIAAAESCINELNLNAVRGLIV 146
Cdd:cd09007    77 VGSCGSLDPDLAVGDIILPTSAlRdegtsYH--------Y----LP--PSRYiEPDPELLDALEEALEKAGIPYVRGKTW 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1820375325 147 SGDAFINGSVGLAKIRHNfpQ-AVAVEMEATAIAHVCHNFNVPFVVVRAISD 197
Cdd:cd09007   143 TTDAPYRETRAKVARRRA--EgCLAVEMEAAALFAVAQFRGVELAQLLYVSD 192
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 70-194 1.73e-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: 50.27  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  70 VIINTGSAGGLAATLKVGDIVVSDEA-----RYHDADvTAFGYEYGQLP---GCPagFKADDKLIAAAESCI--NELNLN 139
Cdd:cd17769    74 AIIRLGSCGSLDPDVPVGSVVVPSASvavtrNYDDDD-FAGPSTSSEKPyliSKP--VPADPELSELLESELkaSLGGEV 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820375325 140 AVRGLIVSGDAFInGSVG-------------LAKIRHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRA 194
Cdd:cd17769   151 VVEGLNASADSFY-SSQGrqdpnfpdhnenlIDKLLKRYPGAASLEMETFHLFHLARCSRPAQGKIRA 217
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 21-175 7.10e-07

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: 48.38  E-value: 7.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  21 ENRqtlslgGCEIYSGQLNGVDVALLKSGIGkvaaALGATLLLE---RCKPDVIINTGSAGGLAATLKVGDIVVSDEARY 97
Cdd:cd17764    27 ENR------GLLVYTGKYKGEEVTIATHGIG----GPSAAIVFEeliMLGAKVIIRLGTAGGLVPELRVGDIVVATGASY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  98 HDadvtafGYEYGQ-LPG-CPAGfKADDKLIAAAESCINELNLNAVRGLIVSGDAFINGSVGLAKIRHNFpQAVAVEMEA 175
Cdd:cd17764    97 YP------GGGLGQyFPDvCPPA-SPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEFAERWSSL-GFIAVEMEC 168
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
71-223 9.07e-07

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 48.31  E-value: 9.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  71 IINTGSAGGLAATLKVGDIVVSDEA---------RYHDADVTAFgyeygqlpgcpagfkADDKLIAAAESCINELNLNAV 141
Cdd:PRK05819   85 LIRVGSCGALQEDVKVRDVVIAMGAstdsnvnriRFKGHDFAPI---------------ADFDLLRKAYDAAKEKGITVH 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325 142 RGLIVSGDAFINGSVGLAKI--RHNfpqAVAVEMEATAIAHVCHNFNVPFVVVRAISDvadqqsHISFDEFLAVAAKQST 219
Cdd:PRK05819  150 VGNVFSADLFYNPDPEMFDVleKYG---VLGVEMEAAALYGLAAKYGVKALTILTVSD------HIVTGEATTAEERQTT 220


                  ....*.
gi 1820375325 220 V--MVE 223
Cdd:PRK05819  221 FndMIE 226
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 34-178 2.56e-04

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: 40.89  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  34 YSGQLNGVDVALLKSGIG------KVaaalgatllLE--RCKPDVIINTGSAGGLAATLKVGDIVVSDEARYHDAdvTAF 105
Cdd:cd17767    45 YTGTYKGVPVSVCSTGIGgpsaaiAV---------EElaQLGAKTFIRVGTCGALQPDIKLGDLVIATGAVRDEG--TSK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325 106 GY---EYgqlpgcPAgfKADDKLIAAAESCINELNLNAVRGLIVSGDAF----INGSVGLAKIRHNFPQ------AVAVE 172
Cdd:cd17767   114 HYvppEY------PA--VADPEVVLALVEAAEELGVPYHVGITASKDSFyggqGRPGPGLPPELPELLEewqragVLNSE 185


                  ....*.
gi 1820375325 173 MEATAI 178
Cdd:cd17767   186 MESAAL 191
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 65-192 1.58e-03

uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine phosphorylases. Genes from human and mouse have been characterized. This enzyme is a member of the PHP/UDP subfamily (pfam01048) and is closely related to the bacterial uridine (TIGR01718) and inosine (TIGR00107) phosphorylase equivalogs. In addition to the eukaryotes, a gene from Mycobacterium leprae is included in this equivalog and may have resulted from lateral gene transfer. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130780 [Multi-domain]  Cd Length: 287  Bit Score: 38.97  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  65 RCKPDVIINTGSAGGLAatLKVGDIVVSDEAryHDADvtaFGYEYGQLPGC-----PAGFKAD--DKLIAAAESCINEln 137
Cdd:TIGR01719 107 RCKNPTFIRIGTSGGIG--VPPGTVVVSSEA--VDAC---LKPEYEQIVLGkrvirPTQLDEAlvQELLLCGAEGLDE-- 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820375325 138 LNAVRGLIVSGDAFINGSVGL--------AKIRHNFPQAVA------VEMEATAIAHVCHNFNVPFVVV 192
Cdd:TIGR01719 178 FTTVSGNTMCTDDFYEGQGRLdgafceytEKDKMAYLRKLYalgvrnIEMESSMFAAMTSRAGFKAAVV 246
PRK08236 PRK08236
hypothetical protein; Provisional
 69-196 2.48e-03

hypothetical protein; Provisional


Pssm-ID: 236194  Cd Length: 212  Bit Score: 37.73  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820375325  69 DVIINTGSAGGLAATLKVGDIVVSDEARYHD--AD-------VTAFGYeygqlpGCPAgFKADDKLIAAAESCINELNLN 139
Cdd:PRK08236   55 DLVVSAGIAGGFPGKAEVGSLVVADEIIAADlgAEtpdgflpVDELGF------GTTT-IQVDPALVRQLTEALLAAALG 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1820375325 140 AVRGLIVSGDAFINGSVGLAKIRHNFPQAVAVEMEATAIAHVCHNFNVPFVVVRAIS 196
Cdd:PRK08236  128 ATAGPVLTVSTVTGTAETAAALAARHPDAVAEAMEGFGVAEAAAAAGLPVLELRAIS 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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