NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|56119114|ref|NP_001007819|]
View 

purine nucleoside phosphorylase [Bos taurus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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); ...
8-276 1.82e-162

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: 451.85  E-value: 1.82e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   8 EDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHM 87
Cdd:cd09009   1 EKIEEAADYIRSRIGFKPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEGHAGRLVFGTLGGKPVLVMQGRFHY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  88 YEGYPFWKVTFPVRVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPgfsGENPLRGPNEERFGVRFPAMSDAYD 167
Cdd:cd09009  81 YEGYSMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHINLT---GDNPLIGPNDDEFGPRFPDMSDAYD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114 168 RDMRQKAHSTWKQMGeqRELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNKVIM 247
Cdd:cd09009 158 PELRELAKEAAKELG--IPLHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNLAAG 235
                       250       260
                ....*....|....*....|....*....
gi 56119114 248 DyeSQGKANHEEVLEAGKQAAQKLEQFVS 276
Cdd:cd09009 236 D--SDEPLSHEEVLEAAKKAAPKLSRLLR 262
 
Name Accession Description Interval E-value
PNP-EcPNPII_like cd09009
purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); ...
8-276 1.82e-162

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: 451.85  E-value: 1.82e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   8 EDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHM 87
Cdd:cd09009   1 EKIEEAADYIRSRIGFKPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEGHAGRLVFGTLGGKPVLVMQGRFHY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  88 YEGYPFWKVTFPVRVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPgfsGENPLRGPNEERFGVRFPAMSDAYD 167
Cdd:cd09009  81 YEGYSMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHINLT---GDNPLIGPNDDEFGPRFPDMSDAYD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114 168 RDMRQKAHSTWKQMGeqRELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNKVIM 247
Cdd:cd09009 158 PELRELAKEAAKELG--IPLHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNLAAG 235
                       250       260
                ....*....|....*....|....*....
gi 56119114 248 DyeSQGKANHEEVLEAGKQAAQKLEQFVS 276
Cdd:cd09009 236 D--SDEPLSHEEVLEAAKKAAPKLSRLLR 262
PNPH TIGR01700
purine nucleoside phosphorylase I, inosine and guanosine-specific; This model represents a ...
26-280 1.89e-161

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: 448.84  E-value: 1.89e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114    26 QVAVICGSGLGGLVNKLTQAQTFDYSEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRVFRL 105
Cdd:TIGR01700   1 DIAIILGSGLGPLAEKVEDATIIDYSEIPHFPQSTVVGHAGNLVFGILGGKPVVAMQGRFHMYEGYDMAKVTFPVRVMKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   106 LGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFsgeNPLRGPNEERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQr 185
Cdd:TIGR01700  81 LGVETLVVTNAAGGINPEFKVGDLMLIRDHINLPGF---NPLRGPNEERFGVRFPDMSDAYDRDLRQKAHSIAKQLNIP- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   186 eLQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNKV--IMDYESQgkaNHEEVLEA 263
Cdd:TIGR01700 157 -LQEGVYVMLGGPSYETPAEVRLLRTLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKAagILDYELS---VHEEVMEA 232
                         250
                  ....*....|....*..
gi 56119114   264 GKQAAQKLEQFVSLLMA 280
Cdd:TIGR01700 233 AKQAAEKLEKFVSLLIA 249
PRK08202 PRK08202
purine nucleoside phosphorylase; Provisional
7-282 8.04e-145

purine nucleoside phosphorylase; Provisional


Pssm-ID: 236183  Cd Length: 272  Bit Score: 407.65  E-value: 8.04e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114    7 YEDYQDTAKWLLSHTE-QRPQVAVICGSGLGGLVNKLTQAQTFDYSEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRF 85
Cdd:PRK08202   3 LEKIEEAAAFIREKTGaFKPEIGLILGSGLGALADEIENAVVIPYADIPGFPVSTVEGHAGELVLGRLGGKPVLAMQGRF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   86 HMYEGYPFWKVTFPVRVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINlpgFSGENPLRGPNEERFGVRFPAMSDA 165
Cdd:PRK08202  83 HYYEGYSMEAVTFPVRVMKALGVETLIVTNAAGGLNPDFGPGDLMLISDHIN---LTGRNPLIGPNDDEFGPRFPDMSDA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  166 YDRDMRQKAHSTWKQMGEqrELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNKV 245
Cdd:PRK08202 160 YDPELRALAKKVAKELGI--PLQEGVYVGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHCGLKVLGISCITNLA 237
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 56119114  246 IMDyeSQGKANHEEVLEAGKQAAQKLEQFVSLLMASI 282
Cdd:PRK08202 238 AGI--SDEPLSHEEVLEVAERAAPKFGRLVKAILARL 272
XapA COG0005
Purine nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine nucleoside ...
27-283 1.68e-97

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: 286.18  E-value: 1.68e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  27 VAVICGSGLGGLVNKL-TQAQTFDYSEipnfpestvpgHAGRLVFGILNGRACVMMQ--GRFHMYEGYPfWKVTFPVRVF 103
Cdd:COG0005   1 IGIIGGSGLGDLLEDIeEVAVETPYGE-----------HSGELVIGTLGGKRVVFLPrhGRGHYYEPHM-INYRANIRAL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114 104 RLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINlpgFSGENPLRGPNEErfGVRFPAMSDAYDRDMRQKAHSTWKQMGE 183
Cdd:COG0005  69 KALGVKRLIATNAVGSLNPDLKPGDLVLIDDHID---LTGGRPLTGFNGG--GVRFVDMTDPYDPELRELLLEAAKELGI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114 184 qrELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNkviMDY-ESQGKANHEEVLE 262
Cdd:COG0005 144 --PLDEGVYVCTEGPRFETPAEIRMLRRLGADVVGMSTVPEAILAREAGLCYAGISLVTN---YAAgISDEPLTHEEVLE 218
                       250       260
                ....*....|....*....|.
gi 56119114 263 AGKQAAQKLEQFVSLLMASIP 283
Cdd:COG0005 219 VAAAAAEKLRRLLKELIARLP 239
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
27-275 3.49e-53

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: 173.30  E-value: 3.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114    27 VAVICGSG--LGGLVNKLTQaqtfdysEIPNFPEStvpgHAGRLVFGILNG-RACVMMQGrfhmyEGYPFWKVTFPVRVF 103
Cdd:pfam01048   2 IAIIGGSPeeLALLAELLDD-------ETPVGPPS----RGGKFYTGTLGGvPVVLVRHG-----IGPPNAAILAAIRLL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   104 RLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINlpgFSGENPLRGPneeRFGVRFPAMSDA-YDRDMRQKAHSTWKQMG 182
Cdd:pfam01048  66 KEFGVDAIIRTGTAGGLNPDLKVGDVVIPTDAIN---HDGRSPLFGP---EGGPYFPDMAPApADPELRALAKEAAERLG 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   183 eqRELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNkvIMDYESQGKANHEEVLE 262
Cdd:pfam01048 140 --IPVHRGVYATGDGFYFETPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSD--LAAGGADGELTHEEVEE 215
                         250
                  ....*....|...
gi 56119114   263 AGKQAAQKLEQFV 275
Cdd:pfam01048 216 FAERAAERAAALL 228
 
Name Accession Description Interval E-value
PNP-EcPNPII_like cd09009
purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); ...
8-276 1.82e-162

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: 451.85  E-value: 1.82e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   8 EDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHM 87
Cdd:cd09009   1 EKIEEAADYIRSRIGFKPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEGHAGRLVFGTLGGKPVLVMQGRFHY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  88 YEGYPFWKVTFPVRVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPgfsGENPLRGPNEERFGVRFPAMSDAYD 167
Cdd:cd09009  81 YEGYSMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHINLT---GDNPLIGPNDDEFGPRFPDMSDAYD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114 168 RDMRQKAHSTWKQMGeqRELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNKVIM 247
Cdd:cd09009 158 PELRELAKEAAKELG--IPLHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNLAAG 235
                       250       260
                ....*....|....*....|....*....
gi 56119114 248 DyeSQGKANHEEVLEAGKQAAQKLEQFVS 276
Cdd:cd09009 236 D--SDEPLSHEEVLEAAKKAAPKLSRLLR 262
PNPH TIGR01700
purine nucleoside phosphorylase I, inosine and guanosine-specific; This model represents a ...
26-280 1.89e-161

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: 448.84  E-value: 1.89e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114    26 QVAVICGSGLGGLVNKLTQAQTFDYSEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRVFRL 105
Cdd:TIGR01700   1 DIAIILGSGLGPLAEKVEDATIIDYSEIPHFPQSTVVGHAGNLVFGILGGKPVVAMQGRFHMYEGYDMAKVTFPVRVMKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   106 LGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFsgeNPLRGPNEERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQr 185
Cdd:TIGR01700  81 LGVETLVVTNAAGGINPEFKVGDLMLIRDHINLPGF---NPLRGPNEERFGVRFPDMSDAYDRDLRQKAHSIAKQLNIP- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   186 eLQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNKV--IMDYESQgkaNHEEVLEA 263
Cdd:TIGR01700 157 -LQEGVYVMLGGPSYETPAEVRLLRTLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKAagILDYELS---VHEEVMEA 232
                         250
                  ....*....|....*..
gi 56119114   264 GKQAAQKLEQFVSLLMA 280
Cdd:TIGR01700 233 AKQAAEKLEKFVSLLIA 249
PRK08202 PRK08202
purine nucleoside phosphorylase; Provisional
7-282 8.04e-145

purine nucleoside phosphorylase; Provisional


Pssm-ID: 236183  Cd Length: 272  Bit Score: 407.65  E-value: 8.04e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114    7 YEDYQDTAKWLLSHTE-QRPQVAVICGSGLGGLVNKLTQAQTFDYSEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRF 85
Cdd:PRK08202   3 LEKIEEAAAFIREKTGaFKPEIGLILGSGLGALADEIENAVVIPYADIPGFPVSTVEGHAGELVLGRLGGKPVLAMQGRF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   86 HMYEGYPFWKVTFPVRVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINlpgFSGENPLRGPNEERFGVRFPAMSDA 165
Cdd:PRK08202  83 HYYEGYSMEAVTFPVRVMKALGVETLIVTNAAGGLNPDFGPGDLMLISDHIN---LTGRNPLIGPNDDEFGPRFPDMSDA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  166 YDRDMRQKAHSTWKQMGEqrELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNKV 245
Cdd:PRK08202 160 YDPELRALAKKVAKELGI--PLQEGVYVGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHCGLKVLGISCITNLA 237
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 56119114  246 IMDyeSQGKANHEEVLEAGKQAAQKLEQFVSLLMASI 282
Cdd:PRK08202 238 AGI--SDEPLSHEEVLEVAERAAPKFGRLVKAILARL 272
PNPH-PUNA-XAPA TIGR01697
inosine/guanosine/xanthosine phosphorylase family; This model is a subset of the subfamily ...
27-280 2.27e-124

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: 354.73  E-value: 2.27e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114    27 VAVICGSGLGGLVNKLTQAQTFDYSEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRVFRLL 106
Cdd:TIGR01697   2 VAIILGSGLGALADQVEDAVIIPYEKIPGFPVSTVVGHAGELVFGRLGGKPVVCMQGRFHYYEGYDMATVTFPVRVMKLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   107 GVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFsgeNPLRGPNEERFGVRFPAMSDAYDRDMRQKAHSTWKQMGeqRE 186
Cdd:TIGR01697  82 GVEILVVTNAAGGLNPDFKPGDLMIIKDHINLPGL---NPLVGPNDDRFGTRFPDLSNAYDRELRKLAQDVAKELG--FP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   187 LQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYEsqGKANHEEVLEAGKQ 266
Cdd:TIGR01697 157 LTEGVYVMVSGPSYETPAEIRMLRILGADAVGMSTVPEVIVARHCGIKVLAVSLITNMAAGITD--VPLSHEEVLAAAAA 234
                         250
                  ....*....|....
gi 56119114   267 AAQKLEQFVSLLMA 280
Cdd:TIGR01697 235 AAERFISLLEDIIA 248
XapA COG0005
Purine nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine nucleoside ...
27-283 1.68e-97

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: 286.18  E-value: 1.68e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  27 VAVICGSGLGGLVNKL-TQAQTFDYSEipnfpestvpgHAGRLVFGILNGRACVMMQ--GRFHMYEGYPfWKVTFPVRVF 103
Cdd:COG0005   1 IGIIGGSGLGDLLEDIeEVAVETPYGE-----------HSGELVIGTLGGKRVVFLPrhGRGHYYEPHM-INYRANIRAL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114 104 RLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINlpgFSGENPLRGPNEErfGVRFPAMSDAYDRDMRQKAHSTWKQMGE 183
Cdd:COG0005  69 KALGVKRLIATNAVGSLNPDLKPGDLVLIDDHID---LTGGRPLTGFNGG--GVRFVDMTDPYDPELRELLLEAAKELGI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114 184 qrELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNkviMDY-ESQGKANHEEVLE 262
Cdd:COG0005 144 --PLDEGVYVCTEGPRFETPAEIRMLRRLGADVVGMSTVPEAILAREAGLCYAGISLVTN---YAAgISDEPLTHEEVLE 218
                       250       260
                ....*....|....*....|.
gi 56119114 263 AGKQAAQKLEQFVSLLMASIP 283
Cdd:COG0005 219 VAAAAAEKLRRLLKELIARLP 239
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
27-275 3.49e-53

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: 173.30  E-value: 3.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114    27 VAVICGSG--LGGLVNKLTQaqtfdysEIPNFPEStvpgHAGRLVFGILNG-RACVMMQGrfhmyEGYPFWKVTFPVRVF 103
Cdd:pfam01048   2 IAIIGGSPeeLALLAELLDD-------ETPVGPPS----RGGKFYTGTLGGvPVVLVRHG-----IGPPNAAILAAIRLL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   104 RLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINlpgFSGENPLRGPneeRFGVRFPAMSDA-YDRDMRQKAHSTWKQMG 182
Cdd:pfam01048  66 KEFGVDAIIRTGTAGGLNPDLKVGDVVIPTDAIN---HDGRSPLFGP---EGGPYFPDMAPApADPELRALAKEAAERLG 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   183 eqRELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNkvIMDYESQGKANHEEVLE 262
Cdd:pfam01048 140 --IPVHRGVYATGDGFYFETPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSD--LAAGGADGELTHEEVEE 215
                         250
                  ....*....|...
gi 56119114   263 AGKQAAQKLEQFV 275
Cdd:pfam01048 216 FAERAAERAAALL 228
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
27-278 1.31e-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: 163.23  E-value: 1.31e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  27 VAVICGSGLGG--LVNKLTQAQTFDYSeipnfpestvpgHAGRLVFGILNGRACVMMQGrfhmyeGYPFWKVTFPVRVFR 104
Cdd:cd09005   1 YAIIPGDPERVdvIDSKLENPQKVSSF------------RGYTMYTGKYNGKRVTVVNG------GMGSPSAAIVVEELC 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114 105 LLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENplrgpneerfgVRFPAMSDAYDRDMRQKAHSTWKQMGeq 184
Cdd:cd09005  63 ALGVDTIIRVGSCGALREDIKVGDLVIADGAIRGDGVTPYY-----------VVGPPFAPEADPELTAALEEAAKELG-- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114 185 RELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYesqgkanHEEVLEAG 264
Cdd:cd09005 130 LTVHVGTVWTTDAFYRETREESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGE-------IGFVDEFL 202
                       250
                ....*....|....
gi 56119114 265 KQAAQKLEQFVSLL 278
Cdd:cd09005 203 SEAEKKAIEIALDA 216
MTAP_SsMTAPII_like_MTIP cd09010
5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus ...
27-275 1.05e-24

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: 99.03  E-value: 1.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  27 VAVICGSGLGGLvNKLTQAQTFDYsEIPnFPESTVPghagrLVFGILNGRACVMMQ--GRFHmyegypfwkvTFP----- 99
Cdd:cd09010   1 IGIIGGSGLYDL-DGLEDVEEVTV-ETP-YGKPSGP-----VTIGELGGREVAFLPrhGRGH----------RIPphrin 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114 100 ----VRVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINL-----PGFSGEnplrgpneerFGVRFPAMSDAYDRDM 170
Cdd:cd09010  63 yranIWALKELGVTRIIAVSAVGSLREEIKPGDLVIPDQFIDFtkgrpSTFFDG----------GGVVHVDFAEPFCPEL 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114 171 RQKAHSTWKQMGEqRELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNkvimdYE 250
Cdd:cd09010 133 RELLIEAAKELGI-PVHDGGTYVCTEGPRFETRAEIRMFRRLGGDVVGMTGVPEAVLARELGICYASIALVTN-----YA 206
                       250       260
                ....*....|....*....|....*...
gi 56119114 251 ---SQGKANHEEVLEAGKQAAQKLEQFV 275
Cdd:cd09010 207 aglEDEPVTVEEVLEVLKENAEKVKRLL 234
PRK08666 PRK08666
5'-methylthioadenosine phosphorylase; Validated
25-283 1.45e-24

5'-methylthioadenosine phosphorylase; Validated


Pssm-ID: 169548  Cd Length: 261  Bit Score: 99.40  E-value: 1.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   25 PQVAVICGSGLgglvnkltqaqtFDYSEIPNFPESTV--PGHAGRLVFGILNGRACVMM--QGRFHmyeGYPFWKVTFPV 100
Cdd:PRK08666   2 VRIAIIGGSGV------------YDPKILENIREETVetPYGEVKVKIGTYAGEEVAFLarHGEGH---SVPPHKINYRA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  101 RVFRL--LGVETLVVTNAAGGLNPNFEVGDIMLIRDHINlpgFSGENPLRGPNEERFGVRFPAMSDAYDRDMRQKAHSTW 178
Cdd:PRK08666  67 NIWALkeLGVERILATSAVGSLNPNMKPGDFVILDQFLD---FTKNRHYTFYDGGESGVVHVDFTDPYCPELRKALITAA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  179 KQMGEQRElQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNkvimdYE---SQGKA 255
Cdd:PRK08666 144 RELGLTYH-PGGTYVCTEGPRFETAAEIRMFRILGGDLVGMTQVPEAVLARELEMCYATVAIVTN-----YAagiSPTKL 217
                        250       260
                 ....*....|....*....|....*...
gi 56119114  256 NHEEVLEAgkqAAQKLEQFVSLLMASIP 283
Cdd:PRK08666 218 THSEVVEL---MAQNSENIKKLIMKAIE 242
PRK08564 PRK08564
S-methyl-5'-thioadenosine phosphorylase;
21-283 1.58e-15

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 236290  Cd Length: 267  Bit Score: 74.68  E-value: 1.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   21 TEQRPQVAVICGSGL---GGLVNKLTQAQTFDYSEipnfPESTVpghagrlVFGILNGR--ACVMMQGRFHMYegyPFWK 95
Cdd:PRK08564   4 PNEKASIGIIGGSGLydpGIFENSKEVKVYTPYGE----PSDNI-------IIGEIEGVevAFLPRHGRGHRI---PPHK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   96 VTFPVRVFRL--LGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGPNeerfgVRFPAMSDAYDRDMRQK 173
Cdd:PRK08564  70 INYRANIWALkeLGVEWVIAVSAVGSLREDYKPGDFVIPDQFIDMTKKREYTFYDGPV-----VAHVSMADPFCPELRKI 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  174 AHSTWKQMGeQRELQEGTYVMLGGPNFETVAECRLLRNL-GADAEGMSTVPEVIVARHCGLRVFGFSLITnkvimDYE-- 250
Cdd:PRK08564 145 IIETAKELG-IRTHEKGTYICIEGPRFSTRAESRMWREVfKADIIGMTLVPEVNLACELGMCYATIAMVT-----DYDvw 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 56119114  251 SQGKANHEEVLeagKQAAQKLEQFVSLLMASIP 283
Cdd:PRK08564 219 AEKPVTAEEVT---RVMAENTEKAKKLLYEAIP 248
PRK09136 PRK09136
S-methyl-5'-thioinosine phosphorylase;
28-233 2.17e-07

S-methyl-5'-thioinosine phosphorylase;


Pssm-ID: 236390  Cd Length: 245  Bit Score: 50.72  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   28 AVICGSGLGGLVN-KLTQAQTFD--YSEipnfpestvPghAGRLVFGILNGRACVmmqgrFHMYEGYPFwkvTFP----- 99
Cdd:PRK09136   3 AIIGGTGLTQLAGlDIVQRQVVRtpYGA---------P--SGPLTFGTLAGREVV-----FLARHGHGH---TIPphkvn 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  100 ----VRVFRLLGVETLVVTNAAGGLNPNFEVGDImLIRDHINLPGFSGENPL-RGPNEERFGVRFpamSDAYDRDMRQKA 174
Cdd:PRK09136  64 yranIWALKQAGATRVLAVNTVGGIHADMGPGTL-VVPDQIIDYTWGRKSTFfEGDGEEVTHIDF---THPYSPMLRQRL 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 56119114  175 HSTWKQMGEQReLQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGL 233
Cdd:PRK09136 140 LAAARAAGVSL-VDGGVYAATQGPRLETAAEIARLERDGCDLVGMTGMPEAALARELGL 197
PRK07432 PRK07432
S-methyl-5'-thioadenosine phosphorylase;
188-285 2.79e-06

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 180977  Cd Length: 290  Bit Score: 47.85  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  188 QEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITnkvimDYESQgKANHEEV------- 260
Cdd:PRK07432 157 RGGTYVCMEGPAFSTKAESNLYRSWGATVIGMTNLPEAKLAREAEIAYATLALVT-----DYDCW-HPDHDSVtvemvig 230
                         90       100
                 ....*....|....*....|....*..
gi 56119114  261 -LEAGKQAAQK-LEQFVSLLMASIPVS 285
Cdd:PRK07432 231 nLHKNAVNAQKvIQETVRRLSANPPVS 257
PRK08931 PRK08931
S-methyl-5'-thioadenosine phosphorylase;
190-229 6.78e-06

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 181584  Cd Length: 289  Bit Score: 46.54  E-value: 6.78e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 56119114  190 GTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVAR 229
Cdd:PRK08931 156 GTYLCMEGPQFSTLAESKLYRSWGCDVIGMTNMPEAKLAR 195
PRK07823 PRK07823
S-methyl-5'-thioadenosine phosphorylase;
24-282 9.31e-06

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 236107  Cd Length: 264  Bit Score: 46.23  E-value: 9.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114   24 RPQVAVICGSGLGGLVNKLTQAQTFDyseIPNFPES---TVPGHAGRLVfgilngrACVMMQGRFHMYEGYpfwkvTFPV 100
Cdd:PRK07823   5 GAMLGVIGGSGFYSFFGSDAREVNVD---TPYGPPSapiTIGEVGGRRV-------AFLPRHGRDHEFSPH-----TVPY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  101 RV----FRLLGVETLVVTNAAGGLNPNFEVGDiMLIRDHInlpgfsgENPLRGPNEERF--GVRFPAMSDAYDRDMRQKA 174
Cdd:PRK07823  70 RAnmwaLRALGVRRVFAPCAVGSLRPELGPGT-VVVPDQL-------VDRTSGRAQTYFdsGGVHVSFADPYCPTLRAAA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56119114  175 hstwkqMGEQRELQEGTYVMLGGPNFETVAECRLLRNLGADAEGMSTVPEVIVARHCGLRVFGFSLITNkVIMDYESQGK 254
Cdd:PRK07823 142 ------LGLPGVVDGGTMVVVQGPRFSTRAESRWFAAQGWSLVNMTGYPEAVLARELELCYAAIALVTD-LDAGVEAGEG 214
                        250       260
                 ....*....|....*....|....*...
gi 56119114  255 ANHEEVLeagKQAAQKLEQFVSLLMASI 282
Cdd:PRK07823 215 VKAVDVF---AEFGRNIERLKRLVRDAI 239
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH