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Conserved domains on  [gi|24762376|ref|NP_611822|]
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uncharacterized protein Dmel_CG18128 [Drosophila melanogaster]

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

CATH:  3.40.50.1580
EC:  2.4.2.1
Gene Ontology:  GO:0004731|GO:0006139|GO:0001882|GO:0042802|GO:0047975|GO:0002060|GO:0042301
SCOP:  4000573

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); ...
 48-290 2.86e-93

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: 278.51  E-value: 2.86e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  48 EEVEAMAKYIVNVSHIRPKYGLICGSFLSDMVSLVEQPVVIPYEDIPNFPDGIEP--DCSFVLGTVMGAPIIALVHSFHS 125
Cdd:cd09009   1 EKIEEAADYIRSRIGFKPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEghAGRLVFGTLGGKPVLVMQGRFHY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376 126 CDGYNLATCALPVRVMQLCGVRTIMLTSEAAAVDHGFALGDIMLVQDHINvvgMMHQTPLEGPSDPRFGSRRFSMVNAYD 205
Cdd:cd09009  81 YEGYSMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHIN---LTGDNPLIGPNDDEFGPRFPDMSDAYD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376 206 KDLLEKALEIGKRMGIQkfLHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVISRAASD 285
Cdd:cd09009 158 PELRELAKEAAKELGIP--LHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNLAAG 235


                ....*
gi 24762376 286 KESEE 290
Cdd:cd09009 236 DSDEP 240
 
Name Accession Description Interval E-value
PNP-EcPNPII_like cd09009
purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); ...
 48-290 2.86e-93

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: 278.51  E-value: 2.86e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  48 EEVEAMAKYIVNVSHIRPKYGLICGSFLSDMVSLVEQPVVIPYEDIPNFPDGIEP--DCSFVLGTVMGAPIIALVHSFHS 125
Cdd:cd09009   1 EKIEEAADYIRSRIGFKPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEghAGRLVFGTLGGKPVLVMQGRFHY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376 126 CDGYNLATCALPVRVMQLCGVRTIMLTSEAAAVDHGFALGDIMLVQDHINvvgMMHQTPLEGPSDPRFGSRRFSMVNAYD 205
Cdd:cd09009  81 YEGYSMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHIN---LTGDNPLIGPNDDEFGPRFPDMSDAYD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376 206 KDLLEKALEIGKRMGIQkfLHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVISRAASD 285
Cdd:cd09009 158 PELRELAKEAAKELGIP--LHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNLAAG 235


                ....*
gi 24762376 286 KESEE 290
Cdd:cd09009 236 DSDEP 240
PRK08202 PRK08202
purine nucleoside phosphorylase; Provisional
 46-280 8.36e-73

purine nucleoside phosphorylase; Provisional


Pssm-ID: 236183  Cd Length: 272  Bit Score: 226.61  E-value: 8.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376   46 PFEEVEAMAKYIVN-VSHIRPKYGLICGSFLSDMVSLVEQPVVIPYEDIPNFP----DGIEPdcSFVLGTVMGAPIIALV 120
Cdd:PRK08202   2 LLEKIEEAAAFIREkTGAFKPEIGLILGSGLGALADEIENAVVIPYADIPGFPvstvEGHAG--ELVLGRLGGKPVLAMQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  121 HSFHSCDGYNLATCALPVRVMQLCGVRTIMLTSEAAAVDHGFALGDIMLVQDHINvvgMMHQTPLEGPSDPRFGSRRFSM 200
Cdd:PRK08202  80 GRFHYYEGYSMEAVTFPVRVMKALGVETLIVTNAAGGLNPDFGPGDLMLISDHIN---LTGRNPLIGPNDDEFGPRFPDM 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  201 VNAYDKDLLEKALEIGKRMGIQkfLHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVIS 280
Cdd:PRK08202 157 SDAYDPELRALAKKVAKELGIP--LQEGVYVGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHCGLKVLGISCIT 234
PNPH-PUNA-XAPA TIGR01697
inosine/guanosine/xanthosine phosphorylase family; This model is a subset of the subfamily ...
 66-283 2.05e-64

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: 204.12  E-value: 2.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376    66 KYGLICGSFLSDMVSLVEQPVVIPYEDIPNFPDGIEPDCS--FVLGTVMGAPIIALVHSFHSCDGYNLATCALPVRVMQL 143
Cdd:TIGR01697   1 DVAIILGSGLGALADQVEDAVIIPYEKIPGFPVSTVVGHAgeLVFGRLGGKPVVCMQGRFHYYEGYDMATVTFPVRVMKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376   144 CGVRTIMLTSEAAAVDHGFALGDIMLVQDHINVVGMmhqTPLEGPSDPRFGSRRFSMVNAYDKDLLEKALEIGKRMGIQk 223
Cdd:TIGR01697  81 LGVEILVVTNAAGGLNPDFKPGDLMIIKDHINLPGL---NPLVGPNDDRFGTRFPDLSNAYDRELRKLAQDVAKELGFP- 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376   224 fLHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVISRAA 283
Cdd:TIGR01697 157 -LTEGVYVMVSGPSYETPAEIRMLRILGADAVGMSTVPEVIVARHCGIKVLAVSLITNMA 215
XapA COG0005
Purine nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine nucleoside ...
 68-280 2.06e-46

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: 157.53  E-value: 2.06e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  68 GLICGSFLSDMVSLV-EQPVVIPYEdipnfpdgiEPDCSFVLGTVMGAPIIAL-VHS-FHSCDGYnLATCALPVRVMQLC 144
Cdd:COG0005   2 GIIGGSGLGDLLEDIeEVAVETPYG---------EHSGELVIGTLGGKRVVFLpRHGrGHYYEPH-MINYRANIRALKAL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376 145 GVRTIMLTSEAAAVDHGFALGDIMLVQDHINvvgMMHQTPLEGPSDPrfGSRRFSMVNAYDKDLLEKALEIGKRMGIQkf 224
Cdd:COG0005  72 GVKRLIATNAVGSLNPDLKPGDLVLIDDHID---LTGGRPLTGFNGG--GVRFVDMTDPYDPELRELLLEAAKELGIP-- 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24762376 225 LHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVIS 280
Cdd:COG0005 145 LDEGVYVCTEGPRFETPAEIRMLRRLGADVVGMSTVPEAILAREAGLCYAGISLVT 200
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 66-301 3.05e-31

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: 117.45  E-value: 3.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376    66 KYGLICGS--FLSDMVSLVEqpvvipyEDIPNFPdgIEPDCSFVLGTVMGAPIIALVHSFhscdGYNLATCALPVRVMQL 143
Cdd:pfam01048   1 KIAIIGGSpeELALLAELLD-------DETPVGP--PSRGGKFYTGTLGGVPVVLVRHGI----GPPNAAILAAIRLLKE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376   144 CGVRTIMLTSEAAAVDHGFALGDIMLVQDHINvvgMMHQTPLEGPsdpRFGSRRFSMVNA-YDKDLLEKALEIGKRMGIQ 222
Cdd:pfam01048  68 FGVDAIIRTGTAGGLNPDLKVGDVVIPTDAIN---HDGRSPLFGP---EGGPYFPDMAPApADPELRALAKEAAERLGIP 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376   223 kfLHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVIS-RAASDKESEESDKDKEKDTDR 301
Cdd:pfam01048 142 --VHRGVYATGDGFYFETPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSdLAAGGADGELTHEEVEEFAER 219
 
Name Accession Description Interval E-value
PNP-EcPNPII_like cd09009
purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); ...
 48-290 2.86e-93

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: 278.51  E-value: 2.86e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  48 EEVEAMAKYIVNVSHIRPKYGLICGSFLSDMVSLVEQPVVIPYEDIPNFPDGIEP--DCSFVLGTVMGAPIIALVHSFHS 125
Cdd:cd09009   1 EKIEEAADYIRSRIGFKPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEghAGRLVFGTLGGKPVLVMQGRFHY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376 126 CDGYNLATCALPVRVMQLCGVRTIMLTSEAAAVDHGFALGDIMLVQDHINvvgMMHQTPLEGPSDPRFGSRRFSMVNAYD 205
Cdd:cd09009  81 YEGYSMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHIN---LTGDNPLIGPNDDEFGPRFPDMSDAYD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376 206 KDLLEKALEIGKRMGIQkfLHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVISRAASD 285
Cdd:cd09009 158 PELRELAKEAAKELGIP--LHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNLAAG 235


                ....*
gi 24762376 286 KESEE 290
Cdd:cd09009 236 DSDEP 240
PRK08202 PRK08202
purine nucleoside phosphorylase; Provisional
 46-280 8.36e-73

purine nucleoside phosphorylase; Provisional


Pssm-ID: 236183  Cd Length: 272  Bit Score: 226.61  E-value: 8.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376   46 PFEEVEAMAKYIVN-VSHIRPKYGLICGSFLSDMVSLVEQPVVIPYEDIPNFP----DGIEPdcSFVLGTVMGAPIIALV 120
Cdd:PRK08202   2 LLEKIEEAAAFIREkTGAFKPEIGLILGSGLGALADEIENAVVIPYADIPGFPvstvEGHAG--ELVLGRLGGKPVLAMQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  121 HSFHSCDGYNLATCALPVRVMQLCGVRTIMLTSEAAAVDHGFALGDIMLVQDHINvvgMMHQTPLEGPSDPRFGSRRFSM 200
Cdd:PRK08202  80 GRFHYYEGYSMEAVTFPVRVMKALGVETLIVTNAAGGLNPDFGPGDLMLISDHIN---LTGRNPLIGPNDDEFGPRFPDM 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  201 VNAYDKDLLEKALEIGKRMGIQkfLHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVIS 280
Cdd:PRK08202 157 SDAYDPELRALAKKVAKELGIP--LQEGVYVGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHCGLKVLGISCIT 234
PNPH-PUNA-XAPA TIGR01697
inosine/guanosine/xanthosine phosphorylase family; This model is a subset of the subfamily ...
 66-283 2.05e-64

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: 204.12  E-value: 2.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376    66 KYGLICGSFLSDMVSLVEQPVVIPYEDIPNFPDGIEPDCS--FVLGTVMGAPIIALVHSFHSCDGYNLATCALPVRVMQL 143
Cdd:TIGR01697   1 DVAIILGSGLGALADQVEDAVIIPYEKIPGFPVSTVVGHAgeLVFGRLGGKPVVCMQGRFHYYEGYDMATVTFPVRVMKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376   144 CGVRTIMLTSEAAAVDHGFALGDIMLVQDHINVVGMmhqTPLEGPSDPRFGSRRFSMVNAYDKDLLEKALEIGKRMGIQk 223
Cdd:TIGR01697  81 LGVEILVVTNAAGGLNPDFKPGDLMIIKDHINLPGL---NPLVGPNDDRFGTRFPDLSNAYDRELRKLAQDVAKELGFP- 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376   224 fLHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVISRAA 283
Cdd:TIGR01697 157 -LTEGVYVMVSGPSYETPAEIRMLRILGADAVGMSTVPEVIVARHCGIKVLAVSLITNMA 215
XapA COG0005
Purine nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine nucleoside ...
 68-280 2.06e-46

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: 157.53  E-value: 2.06e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  68 GLICGSFLSDMVSLV-EQPVVIPYEdipnfpdgiEPDCSFVLGTVMGAPIIAL-VHS-FHSCDGYnLATCALPVRVMQLC 144
Cdd:COG0005   2 GIIGGSGLGDLLEDIeEVAVETPYG---------EHSGELVIGTLGGKRVVFLpRHGrGHYYEPH-MINYRANIRALKAL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376 145 GVRTIMLTSEAAAVDHGFALGDIMLVQDHINvvgMMHQTPLEGPSDPrfGSRRFSMVNAYDKDLLEKALEIGKRMGIQkf 224
Cdd:COG0005  72 GVKRLIATNAVGSLNPDLKPGDLVLIDDHID---LTGGRPLTGFNGG--GVRFVDMTDPYDPELRELLLEAAKELGIP-- 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24762376 225 LHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVIS 280
Cdd:COG0005 145 LDEGVYVCTEGPRFETPAEIRMLRRLGADVVGMSTVPEAILAREAGLCYAGISLVT 200
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 66-301 3.05e-31

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: 117.45  E-value: 3.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376    66 KYGLICGS--FLSDMVSLVEqpvvipyEDIPNFPdgIEPDCSFVLGTVMGAPIIALVHSFhscdGYNLATCALPVRVMQL 143
Cdd:pfam01048   1 KIAIIGGSpeELALLAELLD-------DETPVGP--PSRGGKFYTGTLGGVPVVLVRHGI----GPPNAAILAAIRLLKE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376   144 CGVRTIMLTSEAAAVDHGFALGDIMLVQDHINvvgMMHQTPLEGPsdpRFGSRRFSMVNA-YDKDLLEKALEIGKRMGIQ 222
Cdd:pfam01048  68 FGVDAIIRTGTAGGLNPDLKVGDVVIPTDAIN---HDGRSPLFGP---EGGPYFPDMAPApADPELRALAKEAAERLGIP 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376   223 kfLHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVIS-RAASDKESEESDKDKEKDTDR 301
Cdd:pfam01048 142 --VHRGVYATGDGFYFETPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSdLAAGGADGELTHEEVEEFAER 219
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 135-301 3.79e-15

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: 73.48  E-value: 3.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376 135 ALPVRVMQLCGVRTIMLTSEAAAVDHGFALGDIMLVQDHINVVGMmhqTPLEGPSDPrfgsrrfsMVNAYDKDLLEKALE 214
Cdd:cd09005  55 AIVVEELCALGVDTIIRVGSCGALREDIKVGDLVIADGAIRGDGV---TPYYVVGPP--------FAPEADPELTAALEE 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376 215 IGKRMGIQkfLHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGLKVLAFVVISRAASDKESEESDKD 294
Cdd:cd09005 124 AAKELGLT--VHVGTVWTTDAFYRETREESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEF 201


                ....*..
gi 24762376 295 KEKDTDR 301
Cdd:cd09005 202 LSEAEKK 208
MTAP_SsMTAPII_like_MTIP cd09010
5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus ...
 68-266 1.11e-10

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: 60.90  E-value: 1.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  68 GLICGSFLSDMVSL-VEQPVVI--PYEdipnfpdgiEPDCSFVLGTVMGAPIIALvhSFHScDGYNLatcaLPVRV---- 140
Cdd:cd09010   2 GIIGGSGLYDLDGLeDVEEVTVetPYG---------KPSGPVTIGELGGREVAFL--PRHG-RGHRI----PPHRInyra 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376 141 ----MQLCGVRTIMLTSEAAAVDHGFALGDIMLVQDHINVVGMMHQTPLEGPsdprfGSRRFSMVNAYDKDLLEKALEIG 216
Cdd:cd09010  66 niwaLKELGVTRIIAVSAVGSLREEIKPGDLVIPDQFIDFTKGRPSTFFDGG-----GVVHVDFAEPFCPELRELLIEAA 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24762376 217 KRMGIqKFLHSGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAA 266
Cdd:cd09010 141 KELGI-PVHDGGTYVCTEGPRFETRAEIRMFRRLGGDVVGMTGVPEAVLA 189
PRK08666 PRK08666
5'-methylthioadenosine phosphorylase; Validated
 145-271 1.56e-07

5'-methylthioadenosine phosphorylase; Validated


Pssm-ID: 169548  Cd Length: 261  Bit Score: 51.63  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  145 GVRTIMLTSEAAAVDHGFALGDIMLVQDHINVVGMMHQTPLEGPSDPrfgSRRFSMVNAYDKDLLEKALEIGKRMGIQkf 224
Cdd:PRK08666  75 GVERILATSAVGSLNPNMKPGDFVILDQFLDFTKNRHYTFYDGGESG---VVHVDFTDPYCPELRKALITAARELGLT-- 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 24762376  225 LH-SGVLACMGGPILGTVAEERMLRTMEVSAVGMSLVPEVIAAHHGGL 271
Cdd:PRK08666 150 YHpGGTYVCTEGPRFETAAEIRMFRILGGDLVGMTQVPEAVLARELEM 197
PRK08564 PRK08564
S-methyl-5'-thioadenosine phosphorylase;
145-263 6.66e-06

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 236290  Cd Length: 267  Bit Score: 46.95  E-value: 6.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762376  145 GVRTIMLTSEAAAVDHGFALGDIMLVQDHINVVGMMHQTPLEGPSdprfgSRRFSMVNAYDKDLLEKALEIGKRMGIQkf 224
Cdd:PRK08564  83 GVEWVIAVSAVGSLREDYKPGDFVIPDQFIDMTKKREYTFYDGPV-----VAHVSMADPFCPELRKIIIETAKELGIR-- 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 24762376  225 LH-SGVLACMGGPILGTVAEERMLRtmEVSA---VGMSLVPEV 263
Cdd:PRK08564 156 THeKGTYICIEGPRFSTRAESRMWR--EVFKadiIGMTLVPEV 196
 
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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