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Conserved domains on  [gi|489523591|ref|WP_003428372|]
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purine-nucleoside phosphorylase [Clostridioides difficile]

Protein Classification

purine-nucleoside phosphorylase( domain architecture ID 12963719)

purine-nucleoside phosphorylase catalyzes the phosphorolysis of purine nucleoside to form the corresponding free purine base and pentose-1-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PNP-EcPNPII_like cd09009
purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); ...
3-267 1.83e-175

purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); Human PNP catalyzes the reversible phosphorolysis of the purine nucleosides and deoxynucleosides inosine, guanosine, deoxyinosine, and deoxyguanosine. Patients with PNP deficiency typically present with severe immunodeficiency, neurological dysfunction, and autoimmunity. Escherichia coli PNPII, product of the xapA/pndA gene, catalyzes the phosphorolysis of xanthosine, inosine and guanosine with equal efficiency and has been referred to as xanthosine phosphorylase and inosine-guanosine phosphorylase. E. coli PNPII is also capable of converting nicotinamide to nicotinamide riboside, and may be involved in the NAD+ salvage pathway. It is one of two purine nucleoside phosphorylases found in E. coli, which also contains PNPI, which displays a different substrate specificity and belongs to a different subgroup of the nucleoside phosphorylase-I (NP-I) family than PNPII. 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 (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: 350160  Cd Length: 265  Bit Score: 483.82  E-value: 1.83e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   3 EKIAQSSEFINSKINVKPKIGLILGSGLGDLANDIEDSVTIKYSEIPNFPVSTVAGHAGQLVIGKLEGKEVIAMQGRFHY 82
Cdd:cd09009    1 EKIEEAADYIRSRIGFKPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEGHAGRLVFGTLGGKPVLVMQGRFHY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  83 YEGYSQKEATFPVRVMKELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKNDDRFGARFPDMSDAYSSKY 162
Cdd:cd09009   81 YEGYSMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHINLTGDNPLIGPNDDEFGPRFPDMSDAYDPEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 163 VDVVKNCAKECNIDVKEGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQP 242
Cdd:cd09009  161 RELAKEAAKELGIPLHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNLAAGDSDEP 240
                        250       260
                 ....*....|....*....|....*
gi 489523591 243 LSHEEVIETTQKVKSEFMNLVKTTV 267
Cdd:cd09009  241 LSHEEVLEAAKKAAPKLSRLLREII 265
 
Name Accession Description Interval E-value
PNP-EcPNPII_like cd09009
purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); ...
3-267 1.83e-175

purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); Human PNP catalyzes the reversible phosphorolysis of the purine nucleosides and deoxynucleosides inosine, guanosine, deoxyinosine, and deoxyguanosine. Patients with PNP deficiency typically present with severe immunodeficiency, neurological dysfunction, and autoimmunity. Escherichia coli PNPII, product of the xapA/pndA gene, catalyzes the phosphorolysis of xanthosine, inosine and guanosine with equal efficiency and has been referred to as xanthosine phosphorylase and inosine-guanosine phosphorylase. E. coli PNPII is also capable of converting nicotinamide to nicotinamide riboside, and may be involved in the NAD+ salvage pathway. It is one of two purine nucleoside phosphorylases found in E. coli, which also contains PNPI, which displays a different substrate specificity and belongs to a different subgroup of the nucleoside phosphorylase-I (NP-I) family than PNPII. 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 (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: 350160  Cd Length: 265  Bit Score: 483.82  E-value: 1.83e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   3 EKIAQSSEFINSKINVKPKIGLILGSGLGDLANDIEDSVTIKYSEIPNFPVSTVAGHAGQLVIGKLEGKEVIAMQGRFHY 82
Cdd:cd09009    1 EKIEEAADYIRSRIGFKPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEGHAGRLVFGTLGGKPVLVMQGRFHY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  83 YEGYSQKEATFPVRVMKELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKNDDRFGARFPDMSDAYSSKY 162
Cdd:cd09009   81 YEGYSMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHINLTGDNPLIGPNDDEFGPRFPDMSDAYDPEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 163 VDVVKNCAKECNIDVKEGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQP 242
Cdd:cd09009  161 RELAKEAAKELGIPLHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNLAAGDSDEP 240
                        250       260
                 ....*....|....*....|....*
gi 489523591 243 LSHEEVIETTQKVKSEFMNLVKTTV 267
Cdd:cd09009  241 LSHEEVLEAAKKAAPKLSRLLREII 265
PRK08202 PRK08202
purine nucleoside phosphorylase; Provisional
1-270 8.47e-174

purine nucleoside phosphorylase; Provisional


Pssm-ID: 236183  Cd Length: 272  Bit Score: 480.07  E-value: 8.47e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   1 MFEKIAQSSEFINSKINV-KPKIGLILGSGLGDLANDIEDSVTIKYSEIPNFPVSTVAGHAGQLVIGKLEGKEVIAMQGR 79
Cdd:PRK08202   2 LLEKIEEAAAFIREKTGAfKPEIGLILGSGLGALADEIENAVVIPYADIPGFPVSTVEGHAGELVLGRLGGKPVLAMQGR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  80 FHYYEGYSQKEATFPVRVMKELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKNDDRFGARFPDMSDAYS 159
Cdd:PRK08202  82 FHYYEGYSMEAVTFPVRVMKALGVETLIVTNAAGGLNPDFGPGDLMLISDHINLTGRNPLIGPNDDEFGPRFPDMSDAYD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 160 SKYVDVVKNCAKECNIDVKEGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGIL 239
Cdd:PRK08202 162 PELRALAKKVAKELGIPLQEGVYVGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHCGLKVLGISCITNLAAGIS 241
                        250       260       270
                 ....*....|....*....|....*....|.
gi 489523591 240 NQPLSHEEVIETTQKVKSEFMNLVKTTVKNL 270
Cdd:PRK08202 242 DEPLSHEEVLEVAERAAPKFGRLVKAILARL 272
PNPH-PUNA-XAPA TIGR01697
inosine/guanosine/xanthosine phosphorylase family; This model is a subset of the subfamily ...
21-268 6.30e-137

inosine/guanosine/xanthosine phosphorylase family; This model is a subset of the subfamily represented by pfam00896 (phosphorylase family 2). This model excludes the methylthioadenosine phosphorylases (MTAP, TIGR01684) which are believed toplay a specific role in the recycling of methionine from methylthioadenosine. In this subfamily is found three clades of purine phosphorylases based on a neighbor-joining tree using the MTAP family as an outgroup. The highest-branching clade (TIGR01698) consists of a group of sequences from both gram positive and gram negative bacteria which have been annotated as purine nucleotide phosphorylases but have not been further characterized as to substrate specificity. Of the two remaining clades, one is xanthosine phosphorylase (XAPA, TIGR01699), is limited to certain gamma proteobacteria and constitutes a special purine phosphorylase found in a specialized operon for xanthosine catabolism. The enzyme also acts on the same purines (inosine and guanosine) as the other characterized members of this subfamily, but is only induced when xanthosine must be degraded. The remaining and largest clade consists of purine nucleotide phosphorylases (PNPH, TIGR01700) from metazoa and bacteria which act primarily on guanosine and inosine (and do not act on adenosine). Sequences from Clostridium (GP:15025051) and Thermotoga (OMNI:TM1596) fall between these last two clades and are uncharacterized with respect to substrate range and operon.


Pssm-ID: 130758  Cd Length: 248  Bit Score: 385.93  E-value: 6.30e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   21 KIGLILGSGLGDLANDIEDSVTIKYSEIPNFPVSTVAGHAGQLVIGKLEGKEVIAMQGRFHYYEGYSQKEATFPVRVMKE 100
Cdd:TIGR01697   1 DVAIILGSGLGALADQVEDAVIIPYEKIPGFPVSTVVGHAGELVFGRLGGKPVVCMQGRFHYYEGYDMATVTFPVRVMKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  101 LGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKNDDRFGARFPDMSDAYSSKYVDVVKNCAKECNIDVKEG 180
Cdd:TIGR01697  81 LGVEILVVTNAAGGLNPDFKPGDLMIIKDHINLPGLNPLVGPNDDRFGTRFPDLSNAYDRELRKLAQDVAKELGFPLTEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  181 VYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQPLSHEEVIETTQKVKSEFM 260
Cdd:TIGR01697 161 VYVMVSGPSYETPAEIRMLRILGADAVGMSTVPEVIVARHCGIKVLAVSLITNMAAGITDVPLSHEEVLAAAAAAAERFI 240

                  ....*...
gi 489523591  261 NLVKTTVK 268
Cdd:TIGR01697 241 SLLEDIIA 248
XapA COG0005
Purine nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine nucleoside ...
22-270 1.69e-122

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


Pssm-ID: 439776  Cd Length: 241  Bit Score: 348.97  E-value: 1.69e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  22 IGLILGSGLGDLANDI-EDSVTIKYSEipnfpvstvagHAGQLVIGKLEGKEVIAMQ--GRFHYYEGYsQKEATFPVRVM 98
Cdd:COG0005    1 IGIIGGSGLGDLLEDIeEVAVETPYGE-----------HSGELVIGTLGGKRVVFLPrhGRGHYYEPH-MINYRANIRAL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  99 KELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKNDDrfGARFPDMSDAYSSKYVDVVKNCAKECNIDVK 178
Cdd:COG0005   69 KALGVKRLIATNAVGSLNPDLKPGDLVLIDDHIDLTGGRPLTGFNGG--GVRFVDMTDPYDPELRELLLEAAKELGIPLD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 179 EGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQPLSHEEVIETTQKVKSE 258
Cdd:COG0005  147 EGVYVCTEGPRFETPAEIRMLRRLGADVVGMSTVPEAILAREAGLCYAGISLVTNYAAGISDEPLTHEEVLEVAAAAAEK 226
                        250
                 ....*....|..
gi 489523591 259 FMNLVKTTVKNL 270
Cdd:COG0005  227 LRRLLKELIARL 238
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
21-268 5.51e-62

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: 194.87  E-value: 5.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   21 KIGLILGSG--LGDLANDIEDsvtikysEIPNFPVStvagHAGQLVIGKLEGKEV-IAMQGrfhyyEGYSQKEATFPVRV 97
Cdd:pfam01048   1 KIAIIGGSPeeLALLAELLDD-------ETPVGPPS----RGGKFYTGTLGGVPVvLVRHG-----IGPPNAAILAAIRL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   98 MKELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKnddRFGARFPDMSDA-YSSKYVDVVKNCAKECNID 176
Cdd:pfam01048  65 LKEFGVDAIIRTGTAGGLNPDLKVGDVVIPTDAINHDGRSPLFGP---EGGPYFPDMAPApADPELRALAKEAAERLGIP 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  177 VKEGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQPLSHEEVIETTQKVK 256
Cdd:pfam01048 142 VHRGVYATGDGFYFETPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADGELTHEEVEEFAERAA 221
                         250
                  ....*....|..
gi 489523591  257 SEFMNLVKTTVK 268
Cdd:pfam01048 222 ERAAALLLALLA 233
 
Name Accession Description Interval E-value
PNP-EcPNPII_like cd09009
purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); ...
3-267 1.83e-175

purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); Human PNP catalyzes the reversible phosphorolysis of the purine nucleosides and deoxynucleosides inosine, guanosine, deoxyinosine, and deoxyguanosine. Patients with PNP deficiency typically present with severe immunodeficiency, neurological dysfunction, and autoimmunity. Escherichia coli PNPII, product of the xapA/pndA gene, catalyzes the phosphorolysis of xanthosine, inosine and guanosine with equal efficiency and has been referred to as xanthosine phosphorylase and inosine-guanosine phosphorylase. E. coli PNPII is also capable of converting nicotinamide to nicotinamide riboside, and may be involved in the NAD+ salvage pathway. It is one of two purine nucleoside phosphorylases found in E. coli, which also contains PNPI, which displays a different substrate specificity and belongs to a different subgroup of the nucleoside phosphorylase-I (NP-I) family than PNPII. 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 (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: 350160  Cd Length: 265  Bit Score: 483.82  E-value: 1.83e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   3 EKIAQSSEFINSKINVKPKIGLILGSGLGDLANDIEDSVTIKYSEIPNFPVSTVAGHAGQLVIGKLEGKEVIAMQGRFHY 82
Cdd:cd09009    1 EKIEEAADYIRSRIGFKPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEGHAGRLVFGTLGGKPVLVMQGRFHY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  83 YEGYSQKEATFPVRVMKELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKNDDRFGARFPDMSDAYSSKY 162
Cdd:cd09009   81 YEGYSMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHINLTGDNPLIGPNDDEFGPRFPDMSDAYDPEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 163 VDVVKNCAKECNIDVKEGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQP 242
Cdd:cd09009  161 RELAKEAAKELGIPLHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNLAAGDSDEP 240
                        250       260
                 ....*....|....*....|....*
gi 489523591 243 LSHEEVIETTQKVKSEFMNLVKTTV 267
Cdd:cd09009  241 LSHEEVLEAAKKAAPKLSRLLREII 265
PRK08202 PRK08202
purine nucleoside phosphorylase; Provisional
1-270 8.47e-174

purine nucleoside phosphorylase; Provisional


Pssm-ID: 236183  Cd Length: 272  Bit Score: 480.07  E-value: 8.47e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   1 MFEKIAQSSEFINSKINV-KPKIGLILGSGLGDLANDIEDSVTIKYSEIPNFPVSTVAGHAGQLVIGKLEGKEVIAMQGR 79
Cdd:PRK08202   2 LLEKIEEAAAFIREKTGAfKPEIGLILGSGLGALADEIENAVVIPYADIPGFPVSTVEGHAGELVLGRLGGKPVLAMQGR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  80 FHYYEGYSQKEATFPVRVMKELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKNDDRFGARFPDMSDAYS 159
Cdd:PRK08202  82 FHYYEGYSMEAVTFPVRVMKALGVETLIVTNAAGGLNPDFGPGDLMLISDHINLTGRNPLIGPNDDEFGPRFPDMSDAYD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 160 SKYVDVVKNCAKECNIDVKEGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGIL 239
Cdd:PRK08202 162 PELRALAKKVAKELGIPLQEGVYVGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHCGLKVLGISCITNLAAGIS 241
                        250       260       270
                 ....*....|....*....|....*....|.
gi 489523591 240 NQPLSHEEVIETTQKVKSEFMNLVKTTVKNL 270
Cdd:PRK08202 242 DEPLSHEEVLEVAERAAPKFGRLVKAILARL 272
PNPH-PUNA-XAPA TIGR01697
inosine/guanosine/xanthosine phosphorylase family; This model is a subset of the subfamily ...
21-268 6.30e-137

inosine/guanosine/xanthosine phosphorylase family; This model is a subset of the subfamily represented by pfam00896 (phosphorylase family 2). This model excludes the methylthioadenosine phosphorylases (MTAP, TIGR01684) which are believed toplay a specific role in the recycling of methionine from methylthioadenosine. In this subfamily is found three clades of purine phosphorylases based on a neighbor-joining tree using the MTAP family as an outgroup. The highest-branching clade (TIGR01698) consists of a group of sequences from both gram positive and gram negative bacteria which have been annotated as purine nucleotide phosphorylases but have not been further characterized as to substrate specificity. Of the two remaining clades, one is xanthosine phosphorylase (XAPA, TIGR01699), is limited to certain gamma proteobacteria and constitutes a special purine phosphorylase found in a specialized operon for xanthosine catabolism. The enzyme also acts on the same purines (inosine and guanosine) as the other characterized members of this subfamily, but is only induced when xanthosine must be degraded. The remaining and largest clade consists of purine nucleotide phosphorylases (PNPH, TIGR01700) from metazoa and bacteria which act primarily on guanosine and inosine (and do not act on adenosine). Sequences from Clostridium (GP:15025051) and Thermotoga (OMNI:TM1596) fall between these last two clades and are uncharacterized with respect to substrate range and operon.


Pssm-ID: 130758  Cd Length: 248  Bit Score: 385.93  E-value: 6.30e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   21 KIGLILGSGLGDLANDIEDSVTIKYSEIPNFPVSTVAGHAGQLVIGKLEGKEVIAMQGRFHYYEGYSQKEATFPVRVMKE 100
Cdd:TIGR01697   1 DVAIILGSGLGALADQVEDAVIIPYEKIPGFPVSTVVGHAGELVFGRLGGKPVVCMQGRFHYYEGYDMATVTFPVRVMKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  101 LGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKNDDRFGARFPDMSDAYSSKYVDVVKNCAKECNIDVKEG 180
Cdd:TIGR01697  81 LGVEILVVTNAAGGLNPDFKPGDLMIIKDHINLPGLNPLVGPNDDRFGTRFPDLSNAYDRELRKLAQDVAKELGFPLTEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  181 VYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQPLSHEEVIETTQKVKSEFM 260
Cdd:TIGR01697 161 VYVMVSGPSYETPAEIRMLRILGADAVGMSTVPEVIVARHCGIKVLAVSLITNMAAGITDVPLSHEEVLAAAAAAAERFI 240

                  ....*...
gi 489523591  261 NLVKTTVK 268
Cdd:TIGR01697 241 SLLEDIIA 248
PNPH TIGR01700
purine nucleoside phosphorylase I, inosine and guanosine-specific; This model represents a ...
21-267 2.18e-131

purine nucleoside phosphorylase I, inosine and guanosine-specific; This model represents a family of bacterial and metazoan purine phosphorylases acting primarily on inosine and guanosine and not acting on adenosine. PNP-I refers to the nomenclature from Bacillus stearothermophilus where PHP-II refers to the nucleotidase acting on adenosine as the primary substrate.The bacterial enzymes (PUNA) are typified by the Bacilus PupG protein, which is involved in the metabolism of nucleosides as a carbon source.Several metazoan enzymes (PNPH) are well characterized including the human and bovine enzymes which have been crystallized. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273764  Cd Length: 249  Bit Score: 371.80  E-value: 2.18e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   21 KIGLILGSGLGDLANDIEDSVTIKYSEIPNFPVSTVAGHAGQLVIGKLEGKEVIAMQGRFHYYEGYSQKEATFPVRVMKE 100
Cdd:TIGR01700   1 DIAIILGSGLGPLAEKVEDATIIDYSEIPHFPQSTVVGHAGNLVFGILGGKPVVAMQGRFHMYEGYDMAKVTFPVRVMKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  101 LGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKNDDRFGARFPDMSDAYSSKYVDVVKNCAKECNIDVKEG 180
Cdd:TIGR01700  81 LGVETLVVTNAAGGINPEFKVGDLMLIRDHINLPGFNPLRGPNEERFGVRFPDMSDAYDRDLRQKAHSIAKQLNIPLQEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  181 VYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQPLS-HEEVIETTQKVKSEF 259
Cdd:TIGR01700 161 VYVMLGGPSYETPAEVRLLRTLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKAAGILDYELSvHEEVMEAAKQAAEKL 240

                  ....*...
gi 489523591  260 MNLVKTTV 267
Cdd:TIGR01700 241 EKFVSLLI 248
XapA COG0005
Purine nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine nucleoside ...
22-270 1.69e-122

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


Pssm-ID: 439776  Cd Length: 241  Bit Score: 348.97  E-value: 1.69e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  22 IGLILGSGLGDLANDI-EDSVTIKYSEipnfpvstvagHAGQLVIGKLEGKEVIAMQ--GRFHYYEGYsQKEATFPVRVM 98
Cdd:COG0005    1 IGIIGGSGLGDLLEDIeEVAVETPYGE-----------HSGELVIGTLGGKRVVFLPrhGRGHYYEPH-MINYRANIRAL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  99 KELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKNDDrfGARFPDMSDAYSSKYVDVVKNCAKECNIDVK 178
Cdd:COG0005   69 KALGVKRLIATNAVGSLNPDLKPGDLVLIDDHIDLTGGRPLTGFNGG--GVRFVDMTDPYDPELRELLLEAAKELGIPLD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 179 EGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQPLSHEEVIETTQKVKSE 258
Cdd:COG0005  147 EGVYVCTEGPRFETPAEIRMLRRLGADVVGMSTVPEAILAREAGLCYAGISLVTNYAAGISDEPLTHEEVLEVAAAAAEK 226
                        250
                 ....*....|..
gi 489523591 259 FMNLVKTTVKNL 270
Cdd:COG0005  227 LRRLLKELIARL 238
PUNP TIGR01698
purine nucleotide phosphorylase; This clade of purine nucleotide phosphorylases has not been ...
22-268 5.86e-90

purine nucleotide phosphorylase; This clade of purine nucleotide phosphorylases has not been experimentally characterized but is assigned based on strong sequence homology. Closely related clades act on inosine and guanosine (PNPH, TIGR01700), and xanthosine, inosine and guanosine (XAPA, TIGR01699) neither of these will act on adenosine. A more distantly related clade (MTAP, TIGR01694) acts on methylthioadenosine.


Pssm-ID: 130759  Cd Length: 237  Bit Score: 266.31  E-value: 5.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   22 IGLILGSGLGDLANDIEDSVTIKYSEIPNFPVSTVAGHAGQLVIGKLEGKEVIAMQGRFHYYEGYSQKEATFPVRVMKEL 101
Cdd:TIGR01698   2 MAIVLGSGWGGAVEALGEPVELPYAEIPGFPAPTVSGHAGELIRVRIGDGPVLVLGGRTHAYEGGDARAVVHPVRTARAT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  102 GVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVgknddrfGARFPDMSDAYSSKyvdvVKNCAKECNIDVKEGV 181
Cdd:TIGR01698  82 GAETLILTNAAGGLRQDWGPGTPVLISDHINLTARSPLI-------GPRFVDLTDAYSPR----LRELAERVDPPLAEGV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  182 YMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQPLSHEEVIETTQKVKSEFMN 261
Cdd:TIGR01698 151 YAWFPGPHYETPAEIRMAGILGADLVGMSTVPETIAARFCGLEVLGVSLVTNLAAGITGTPLSHAEVKAAGAAAGTRLAA 230

                  ....*..
gi 489523591  262 LVKTTVK 268
Cdd:TIGR01698 231 LLADIIK 237
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
21-268 5.51e-62

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: 194.87  E-value: 5.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   21 KIGLILGSG--LGDLANDIEDsvtikysEIPNFPVStvagHAGQLVIGKLEGKEV-IAMQGrfhyyEGYSQKEATFPVRV 97
Cdd:pfam01048   1 KIAIIGGSPeeLALLAELLDD-------ETPVGPPS----RGGKFYTGTLGGVPVvLVRHG-----IGPPNAAILAAIRL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591   98 MKELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKnddRFGARFPDMSDA-YSSKYVDVVKNCAKECNID 176
Cdd:pfam01048  65 LKEFGVDAIIRTGTAGGLNPDLKVGDVVIPTDAINHDGRSPLFGP---EGGPYFPDMAPApADPELRALAKEAAERLGIP 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  177 VKEGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQPLSHEEVIETTQKVK 256
Cdd:pfam01048 142 VHRGVYATGDGFYFETPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADGELTHEEVEEFAERAA 221
                         250
                  ....*....|..
gi 489523591  257 SEFMNLVKTTVK 268
Cdd:pfam01048 222 ERAAALLLALLA 233
MTAP_SsMTAPII_like_MTIP cd09010
5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus ...
22-267 1.18e-39

5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus MTAPII and Pseudomonas aeruginosa PAO1 5'-methylthioinosine phosphorylase (MTIP); MTAP catalyzes the reversible phosphorolysis of 5'-deoxy-5'-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate. This subfamily includes human MTAP which is highly specific for MTA, and Sulfolobus solfataricus MTAPII which accepts adenosine in addition to MTA. Two MTAPs have been isolated from S. solfataricus: SsMTAP1 and SsMTAPII, SsMTAP1 belongs to a different subfamily of the nucleoside phosphorylase-I (NP-I) family. This group also includes Pseudomonas aeruginosa PAO1 MTI phosphorylase (MTIP) which uses 5'-methylthioinosine (MTI) as a preferred substrate, and does not use MTA. 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 (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: 350161  Cd Length: 238  Bit Score: 137.55  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  22 IGLILGSGLGDLaNDIEDSVTIKyseipnfpVSTVAGH-AGQLVIGKLEGKEV--IAMQGRFHyyegysqkeaTFP---- 94
Cdd:cd09010    1 IGIIGGSGLYDL-DGLEDVEEVT--------VETPYGKpSGPVTIGELGGREVafLPRHGRGH----------RIPphri 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  95 -----VRVMKELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGknDDRFGARFPDMSDAYSSKYVDVVKNC 169
Cdd:cd09010   62 nyranIWALKELGVTRIIAVSAVGSLREEIKPGDLVIPDQFIDFTKGRPSTF--FDGGGVVHVDFAEPFCPELRELLIEA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 170 AKECNIDV-KEGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQPLSHEEV 248
Cdd:cd09010  140 AKELGIPVhDGGTYVCTEGPRFETRAEIRMFRRLGGDVVGMTGVPEAVLARELGICYASIALVTNYAAGLEDEPVTVEEV 219
                        250
                 ....*....|....*....
gi 489523591 249 IETTQKVKSEFMNLVKTTV 267
Cdd:cd09010  220 LEVLKENAEKVKRLLLAAI 238
PRK08666 PRK08666
5'-methylthioadenosine phosphorylase; Validated
19-270 2.50e-37

5'-methylthioadenosine phosphorylase; Validated


Pssm-ID: 169548  Cd Length: 261  Bit Score: 132.52  E-value: 2.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  19 KPKIGLILGSGLGD---LANDIEDSVTIKYSEIpnfpvstvaghagQLVIGKLEGKEV--IAMQGRFHyyegysqkeaTF 93
Cdd:PRK08666   1 MVRIAIIGGSGVYDpkiLENIREETVETPYGEV-------------KVKIGTYAGEEVafLARHGEGH----------SV 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  94 P---------VRVMKELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGKNDDRFGARFPDMSDAYSSKYVD 164
Cdd:PRK08666  58 PphkinyranIWALKELGVERILATSAVGSLNPNMKPGDFVILDQFLDFTKNRHYTFYDGGESGVVHVDFTDPYCPELRK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 165 VVKNCAKECNIDVKE-GVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGILNQPL 243
Cdd:PRK08666 138 ALITAARELGLTYHPgGTYVCTEGPRFETAAEIRMFRILGGDLVGMTQVPEAVLARELEMCYATVAIVTNYAAGISPTKL 217
                        250       260
                 ....*....|....*....|....*..
gi 489523591 244 SHEEVIETTQKVKSEFMNLVKTTVKNL 270
Cdd:PRK08666 218 THSEVVELMAQNSENIKKLIMKAIELI 244
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
22-233 2.70e-24

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: 96.98  E-value: 2.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  22 IGLILGSGLGDLANDIEDSVTIKYSEIPNFPVSTvaghagqlviGKLEGKEVIAMQGrfhyyeGYSQKEATFPVRVMKEL 101
Cdd:cd09005    1 YAIIPGDPERVDVIDSKLENPQKVSSFRGYTMYT----------GKYNGKRVTVVNG------GMGSPSAAIVVEELCAL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 102 GVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVGknddrfgaRFPDMSDAYSSKYVDVVKNCAKECNIDVKEGV 181
Cdd:cd09005   65 GVDTIIRVGSCGALREDIKVGDLVIADGAIRGDGVTPYYV--------VGPPFAPEADPELTAALEEAAKELGLTVHVGT 136
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489523591 182 YMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITN 233
Cdd:cd09005  137 VWTTDAFYRETREESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSD 188
PRK08564 PRK08564
S-methyl-5'-thioadenosine phosphorylase;
17-256 5.71e-20

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 236290  Cd Length: 267  Bit Score: 86.62  E-value: 5.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  17 NVKPKIGLILGSGLGDLaNDIEDSVTIKyseipnfpVSTVAGH-AGQLVIGKLEGKEV--IAMQGRFHYYEgysqkeatf 93
Cdd:PRK08564   5 NEKASIGIIGGSGLYDP-GIFENSKEVK--------VYTPYGEpSDNIIIGEIEGVEVafLPRHGRGHRIP--------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  94 PVRV--------MKELGVEILIVTNAAGGVNKEFKAGDLMLIRDHINFSGSNPLVgknddrfgarFPD--------MSDA 157
Cdd:PRK08564  67 PHKInyraniwaLKELGVEWVIAVSAVGSLREDYKPGDFVIPDQFIDMTKKREYT----------FYDgpvvahvsMADP 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 158 YSSKYVDVVKNCAKECNIDVKE-GVYMFFSGPNYETPAEVRM-AQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMA 235
Cdd:PRK08564 137 FCPELRKIIIETAKELGIRTHEkGTYICIEGPRFSTRAESRMwREVFKADIIGMTLVPEVNLACELGMCYATIAMVTDYD 216
                        250       260
                 ....*....|....*....|....*
gi 489523591 236 AgILNQPLSHEEVI----ETTQKVK 256
Cdd:PRK08564 217 V-WAEKPVTAEEVTrvmaENTEKAK 240
PRK07432 PRK07432
S-methyl-5'-thioadenosine phosphorylase;
18-233 2.90e-09

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 180977  Cd Length: 290  Bit Score: 56.33  E-value: 2.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  18 VKPKIGLILGSGLGDLAnDIEDSVTIKYsEIPNFPVSTVaghagqLVIGKLEGKEV--IAMQGRFHYYegySQKEATFPV 95
Cdd:PRK07432   2 TQAKIGIIGGSGLYKME-ALKDVEEVQL-ETPFGSPSDA------LIVGTLDGTRVafLARHGRNHTL---LPTELPFRA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  96 RV--MKELGVEILIVTNAAGGVNKEFKAGDlMLIRDHinfsgsnpLVGKNDDRFGARFPD-------MSDAYSSKYVDVV 166
Cdd:PRK07432  71 NIyaMKQLGVEYLISASAVGSLKEEAKPLD-MVVPDQ--------FIDRTKNRISTFFGEgivahigFGDPICPALAGVL 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489523591 167 KNCAKECNI-DV---KEGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITN 233
Cdd:PRK07432 142 ADAIASLNLpDVtlhRGGTYVCMEGPAFSTKAESNLYRSWGATVIGMTNLPEAKLAREAEIAYATLALVTD 212
PRK09136 PRK09136
S-methyl-5'-thioinosine phosphorylase;
22-237 3.75e-09

S-methyl-5'-thioinosine phosphorylase;


Pssm-ID: 236390  Cd Length: 245  Bit Score: 55.73  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  22 IGLILGSGLGDLANdiedsVTIKYSEipnfPVSTVAGH-AGQLVIGKLEGKEVI--AMQGRFHyyegysqkeaTFP---- 94
Cdd:PRK09136   2 LAIIGGTGLTQLAG-----LDIVQRQ----VVRTPYGApSGPLTFGTLAGREVVflARHGHGH----------TIPphkv 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  95 -----VRVMKELGVEILIVTNAAGGVNKEFKAGDLM----LI-----RDHINFSGSNPLVgknddrfgaRFPDMSDAYSS 160
Cdd:PRK09136  63 nyranIWALKQAGATRVLAVNTVGGIHADMGPGTLVvpdqIIdytwgRKSTFFEGDGEEV---------THIDFTHPYSP 133
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489523591 161 KYVDVVKNCAKECNIDVKE-GVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAG 237
Cdd:PRK09136 134 MLRQRLLAAARAAGVSLVDgGVYAATQGPRLETAAEIARLERDGCDLVGMTGMPEAALARELGLPYACLALVANWAAG 211
PRK08931 PRK08931
S-methyl-5'-thioadenosine phosphorylase;
18-218 1.10e-08

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 181584  Cd Length: 289  Bit Score: 54.63  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  18 VKPKIGLILGSGLGDLANdIEDsVTIKYSEIPNFPVSTvaghagQLVIGKLEGKEVI--AMQGRFHYYEgysqkEATFPV 95
Cdd:PRK08931   2 TKAVLGIIGGSGVYDIDG-LED-ARWERVESPWGEPSD------ALLFGRLGGVPMVflPRHGRGHRLS-----PSDINY 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  96 R----VMKELGVEILIVTNAAGGVNKEFKAGDLMLIRDHInfsgsnplvgkndDRFGAR----FPD-------MSDAYSS 160
Cdd:PRK08931  69 RanidALKRAGVTDIVSLSACGSFREELPPGTFVIVDQFI-------------DRTFAReksfFGTgcvahvsMAHPVCP 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489523591 161 KYVDVVKNCAKECNIDVKE-GVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVA 218
Cdd:PRK08931 136 RLGDRLAAAARAEGITVHRgGTYLCMEGPQFSTLAESKLYRSWGCDVIGMTNMPEAKLA 194
PRK07823 PRK07823
S-methyl-5'-thioadenosine phosphorylase;
17-270 4.68e-05

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 236107  Cd Length: 264  Bit Score: 43.92  E-value: 4.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  17 NVKPKIGLILGSGLGDLANDIEDSVTIkysEIPNFPVStvaghaGQLVIGKLEGKEV--IAMQGRFHYYEGYsqkeaTFP 94
Cdd:PRK07823   3 NNGAMLGVIGGSGFYSFFGSDAREVNV---DTPYGPPS------APITIGEVGGRRVafLPRHGRDHEFSPH-----TVP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591  95 VRV----MKELGVEILIVTNAAGGVNKEFKAGDlMLIRDHinfsgsnpLVgkndDRFGARFPDMSD------AYSSKYVD 164
Cdd:PRK07823  69 YRAnmwaLRALGVRRVFAPCAVGSLRPELGPGT-VVVPDQ--------LV----DRTSGRAQTYFDsggvhvSFADPYCP 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523591 165 VVKNCAKECNIDVKEGVYMFFSGPNYETPAEVRMAQILGADAVGMSTVPEVIVASHSNIGVIGISCITNMAAGI-LNQPL 243
Cdd:PRK07823 136 TLRAAALGLPGVVDGGTMVVVQGPRFSTRAESRWFAAQGWSLVNMTGYPEAVLARELELCYAAIALVTDLDAGVeAGEGV 215
                        250       260
                 ....*....|....*....|....*..
gi 489523591 244 SHEEVIETTQKVKSEFMNLVKTTVKNL 270
Cdd:PRK07823 216 KAVDVFAEFGRNIERLKRLVRDAIAAV 242
 
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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