NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1831512073|ref|NP_001368342|]
View 

Purine nucleoside phosphorylase [Caenorhabditis elegans]

Protein Classification

purine-nucleoside phosphorylase( domain architecture ID 10019816)

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
PNPH TIGR01700
purine nucleoside phosphorylase I, inosine and guanosine-specific; This model represents a ...
61-314 1.54e-154

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: 432.66  E-value: 1.54e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  61 DLGIICGSGLGPIGDTVQDATILPYSKIPGFPTTHVVGHKGNMIFGKLGGKKVVCLQGRFHPYEHnMDLALCTLPVRVMH 140
Cdd:TIGR01700   1 DIAIILGSGLGPLAEKVEDATIIDYSEIPHFPQSTVVGHAGNLVFGILGGKPVVAMQGRFHMYEG-YDMAKVTFPVRVMK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 141 QLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLPalaGFSPLVGCNDPRFGARFVSVHDAYDKQLRQLAIDVGRRSDMT 220
Cdd:TIGR01700  80 LLGVETLVVTNAAGGINPEFKVGDLMLIRDHINLP---GFNPLRGPNEERFGVRFPDMSDAYDRDLRQKAHSIAKQLNIP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 221 LYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIANLDADASVEVsHEEVMDIAQQ 300
Cdd:TIGR01700 157 LQEGVYVMLGGPSYETPAEVRLLRTLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKAAGILDYELSV-HEEVMEAAKQ 235
                         250
                  ....*....|....
gi 1831512073 301 AGERASRFVSDIIT 314
Cdd:TIGR01700 236 AAEKLEKFVSLLIA 249
 
Name Accession Description Interval E-value
PNPH TIGR01700
purine nucleoside phosphorylase I, inosine and guanosine-specific; This model represents a ...
61-314 1.54e-154

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: 432.66  E-value: 1.54e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  61 DLGIICGSGLGPIGDTVQDATILPYSKIPGFPTTHVVGHKGNMIFGKLGGKKVVCLQGRFHPYEHnMDLALCTLPVRVMH 140
Cdd:TIGR01700   1 DIAIILGSGLGPLAEKVEDATIIDYSEIPHFPQSTVVGHAGNLVFGILGGKPVVAMQGRFHMYEG-YDMAKVTFPVRVMK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 141 QLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLPalaGFSPLVGCNDPRFGARFVSVHDAYDKQLRQLAIDVGRRSDMT 220
Cdd:TIGR01700  80 LLGVETLVVTNAAGGINPEFKVGDLMLIRDHINLP---GFNPLRGPNEERFGVRFPDMSDAYDRDLRQKAHSIAKQLNIP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 221 LYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIANLDADASVEVsHEEVMDIAQQ 300
Cdd:TIGR01700 157 LQEGVYVMLGGPSYETPAEVRLLRTLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKAAGILDYELSV-HEEVMEAAKQ 235
                         250
                  ....*....|....
gi 1831512073 301 AGERASRFVSDIIT 314
Cdd:TIGR01700 236 AAEKLEKFVSLLIA 249
PNP-EcPNPII_like cd09009
purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); ...
40-313 1.38e-133

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: 379.82  E-value: 1.38e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  40 DDVLSVAASIREQVGEdvaRADLGIICGSGLGPIGDTVQDATILPYSKIPGFPTTHVVGHKGNMIFGKLGGKKVVCLQGR 119
Cdd:cd09009     1 EKIEEAADYIRSRIGF---KPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEGHAGRLVFGTLGGKPVLVMQGR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 120 FHPYEHNmDLALCTLPVRVMHQLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLPalaGFSPLVGCNDPRFGARFVSVH 199
Cdd:cd09009    78 FHYYEGY-SMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHINLT---GDNPLIGPNDDEFGPRFPDMS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 200 DAYDKQLRQLAIDVGRRSDMTLYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIA 279
Cdd:cd09009   154 DAYDPELRELAKEAAKELGIPLHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNLA 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1831512073 280 NLDADAsvEVSHEEVMDIAQQAGERASRFVSDII 313
Cdd:cd09009   234 AGDSDE--PLSHEEVLEAAKKAAPKLSRLLREII 265
PRK08202 PRK08202
purine nucleoside phosphorylase; Provisional
38-316 5.29e-122

purine nucleoside phosphorylase; Provisional


Pssm-ID: 236183  Cd Length: 272  Bit Score: 351.03  E-value: 5.29e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  38 NYDDVLSVAASIREQVGedVARADLGIICGSGLGPIGDTVQDATILPYSKIPGFPTTHVVGHKGNMIFGKLGGKKVVCLQ 117
Cdd:PRK08202    2 LLEKIEEAAAFIREKTG--AFKPEIGLILGSGLGALADEIENAVVIPYADIPGFPVSTVEGHAGELVLGRLGGKPVLAMQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 118 GRFHPYEHNmDLALCTLPVRVMHQLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIflpALAGFSPLVGCNDPRFGARFVS 197
Cdd:PRK08202   80 GRFHYYEGY-SMEAVTFPVRVMKALGVETLIVTNAAGGLNPDFGPGDLMLISDHI---NLTGRNPLIGPNDDEFGPRFPD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 198 VHDAYDKQLRQLAIDVGRRSDMTLYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITN 277
Cdd:PRK08202  156 MSDAYDPELRALAKKVAKELGIPLQEGVYVGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHCGLKVLGISCITN 235
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1831512073 278 IANLDADasVEVSHEEVMDIAQQAGERASRFVSDIITEI 316
Cdd:PRK08202  236 LAAGISD--EPLSHEEVLEVAERAAPKFGRLVKAILARL 272
XapA COG0005
Purine nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine nucleoside ...
62-316 5.00e-85

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: 255.75  E-value: 5.00e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  62 LGIICGSGLGPIGDTVQDATI-LPYSKipgfptthvvgHKGNMIFGKLGGKKVVCLQ--GRFHPYEHNMdlALCTLPVRV 138
Cdd:COG0005     1 IGIIGGSGLGDLLEDIEEVAVeTPYGE-----------HSGELVIGTLGGKRVVFLPrhGRGHYYEPHM--INYRANIRA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 139 MHQLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLpalAGFSPLVGCNDPrfGARFVSVHDAYDKQLRQLAIDVGRRSD 218
Cdd:COG0005    68 LKALGVKRLIATNAVGSLNPDLKPGDLVLIDDHIDL---TGGRPLTGFNGG--GVRFVDMTDPYDPELRELLLEAAKELG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 219 MTLYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIANLDADAsvEVSHEEVMDIA 298
Cdd:COG0005   143 IPLDEGVYVCTEGPRFETPAEIRMLRRLGADVVGMSTVPEAILAREAGLCYAGISLVTNYAAGISDE--PLTHEEVLEVA 220
                         250
                  ....*....|....*...
gi 1831512073 299 QQAGERASRFVSDIITEI 316
Cdd:COG0005   221 AAAAEKLRRLLKELIARL 238
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
61-313 6.06e-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: 173.68  E-value: 6.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  61 DLGIICGSG--LGPIGDTVQDatilpysKIPGFPTTHvvghKGNMIFGKLGGKKVVCLQGRFHPyeHNMDlalCTLPVRV 138
Cdd:pfam01048   1 KIAIIGGSPeeLALLAELLDD-------ETPVGPPSR----GGKFYTGTLGGVPVVLVRHGIGP--PNAA---ILAAIRL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 139 MHQLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLpalAGFSPLVGcndPRFGARFVSVHDA-YDKQLRQLAIDVGRRS 217
Cdd:pfam01048  65 LKEFGVDAIIRTGTAGGLNPDLKVGDVVIPTDAINH---DGRSPLFG---PEGGPYFPDMAPApADPELRALAKEAAERL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 218 DMTLYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIANLDADAsvEVSHEEVMDI 297
Cdd:pfam01048 139 GIPVHRGVYATGDGFYFETPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADG--ELTHEEVEEF 216
                         250
                  ....*....|....*.
gi 1831512073 298 AQQAGERASRFVSDII 313
Cdd:pfam01048 217 AERAAERAAALLLALL 232
 
Name Accession Description Interval E-value
PNPH TIGR01700
purine nucleoside phosphorylase I, inosine and guanosine-specific; This model represents a ...
61-314 1.54e-154

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: 432.66  E-value: 1.54e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  61 DLGIICGSGLGPIGDTVQDATILPYSKIPGFPTTHVVGHKGNMIFGKLGGKKVVCLQGRFHPYEHnMDLALCTLPVRVMH 140
Cdd:TIGR01700   1 DIAIILGSGLGPLAEKVEDATIIDYSEIPHFPQSTVVGHAGNLVFGILGGKPVVAMQGRFHMYEG-YDMAKVTFPVRVMK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 141 QLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLPalaGFSPLVGCNDPRFGARFVSVHDAYDKQLRQLAIDVGRRSDMT 220
Cdd:TIGR01700  80 LLGVETLVVTNAAGGINPEFKVGDLMLIRDHINLP---GFNPLRGPNEERFGVRFPDMSDAYDRDLRQKAHSIAKQLNIP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 221 LYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIANLDADASVEVsHEEVMDIAQQ 300
Cdd:TIGR01700 157 LQEGVYVMLGGPSYETPAEVRLLRTLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKAAGILDYELSV-HEEVMEAAKQ 235
                         250
                  ....*....|....
gi 1831512073 301 AGERASRFVSDIIT 314
Cdd:TIGR01700 236 AAEKLEKFVSLLIA 249
PNPH-PUNA-XAPA TIGR01697
inosine/guanosine/xanthosine phosphorylase family; This model is a subset of the subfamily ...
61-314 1.76e-142

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: 401.73  E-value: 1.76e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  61 DLGIICGSGLGPIGDTVQDATILPYSKIPGFPTTHVVGHKGNMIFGKLGGKKVVCLQGRFHPYEHnMDLALCTLPVRVMH 140
Cdd:TIGR01697   1 DVAIILGSGLGALADQVEDAVIIPYEKIPGFPVSTVVGHAGELVFGRLGGKPVVCMQGRFHYYEG-YDMATVTFPVRVMK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 141 QLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLPALagfSPLVGCNDPRFGARFVSVHDAYDKQLRQLAIDVGRRSDMT 220
Cdd:TIGR01697  80 LLGVEILVVTNAAGGLNPDFKPGDLMIIKDHINLPGL---NPLVGPNDDRFGTRFPDLSNAYDRELRKLAQDVAKELGFP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 221 LYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIANLDADAsvEVSHEEVMDIAQQ 300
Cdd:TIGR01697 157 LTEGVYVMVSGPSYETPAEIRMLRILGADAVGMSTVPEVIVARHCGIKVLAVSLITNMAAGITDV--PLSHEEVLAAAAA 234
                         250
                  ....*....|....
gi 1831512073 301 AGERASRFVSDIIT 314
Cdd:TIGR01697 235 AAERFISLLEDIIA 248
PNP-EcPNPII_like cd09009
purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); ...
40-313 1.38e-133

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: 379.82  E-value: 1.38e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  40 DDVLSVAASIREQVGEdvaRADLGIICGSGLGPIGDTVQDATILPYSKIPGFPTTHVVGHKGNMIFGKLGGKKVVCLQGR 119
Cdd:cd09009     1 EKIEEAADYIRSRIGF---KPKIGIILGSGLGGLADEIEDPVEIPYSDIPGFPVSTVEGHAGRLVFGTLGGKPVLVMQGR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 120 FHPYEHNmDLALCTLPVRVMHQLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLPalaGFSPLVGCNDPRFGARFVSVH 199
Cdd:cd09009    78 FHYYEGY-SMQEVTFPVRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHINLT---GDNPLIGPNDDEFGPRFPDMS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 200 DAYDKQLRQLAIDVGRRSDMTLYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIA 279
Cdd:cd09009   154 DAYDPELRELAKEAAKELGIPLHEGVYAGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNLA 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1831512073 280 NLDADAsvEVSHEEVMDIAQQAGERASRFVSDII 313
Cdd:cd09009   234 AGDSDE--PLSHEEVLEAAKKAAPKLSRLLREII 265
PRK08202 PRK08202
purine nucleoside phosphorylase; Provisional
38-316 5.29e-122

purine nucleoside phosphorylase; Provisional


Pssm-ID: 236183  Cd Length: 272  Bit Score: 351.03  E-value: 5.29e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  38 NYDDVLSVAASIREQVGedVARADLGIICGSGLGPIGDTVQDATILPYSKIPGFPTTHVVGHKGNMIFGKLGGKKVVCLQ 117
Cdd:PRK08202    2 LLEKIEEAAAFIREKTG--AFKPEIGLILGSGLGALADEIENAVVIPYADIPGFPVSTVEGHAGELVLGRLGGKPVLAMQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 118 GRFHPYEHNmDLALCTLPVRVMHQLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIflpALAGFSPLVGCNDPRFGARFVS 197
Cdd:PRK08202   80 GRFHYYEGY-SMEAVTFPVRVMKALGVETLIVTNAAGGLNPDFGPGDLMLISDHI---NLTGRNPLIGPNDDEFGPRFPD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 198 VHDAYDKQLRQLAIDVGRRSDMTLYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITN 277
Cdd:PRK08202  156 MSDAYDPELRALAKKVAKELGIPLQEGVYVGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHCGLKVLGISCITN 235
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1831512073 278 IANLDADasVEVSHEEVMDIAQQAGERASRFVSDIITEI 316
Cdd:PRK08202  236 LAAGISD--EPLSHEEVLEVAERAAPKFGRLVKAILARL 272
XapA COG0005
Purine nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine nucleoside ...
62-316 5.00e-85

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: 255.75  E-value: 5.00e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  62 LGIICGSGLGPIGDTVQDATI-LPYSKipgfptthvvgHKGNMIFGKLGGKKVVCLQ--GRFHPYEHNMdlALCTLPVRV 138
Cdd:COG0005     1 IGIIGGSGLGDLLEDIEEVAVeTPYGE-----------HSGELVIGTLGGKRVVFLPrhGRGHYYEPHM--INYRANIRA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 139 MHQLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLpalAGFSPLVGCNDPrfGARFVSVHDAYDKQLRQLAIDVGRRSD 218
Cdd:COG0005    68 LKALGVKRLIATNAVGSLNPDLKPGDLVLIDDHIDL---TGGRPLTGFNGG--GVRFVDMTDPYDPELRELLLEAAKELG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 219 MTLYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIANLDADAsvEVSHEEVMDIA 298
Cdd:COG0005   143 IPLDEGVYVCTEGPRFETPAEIRMLRRLGADVVGMSTVPEAILAREAGLCYAGISLVTNYAAGISDE--PLTHEEVLEVA 220
                         250
                  ....*....|....*...
gi 1831512073 299 QQAGERASRFVSDIITEI 316
Cdd:COG0005   221 AAAAEKLRRLLKELIARL 238
PUNP TIGR01698
purine nucleotide phosphorylase; This clade of purine nucleotide phosphorylases has not been ...
61-313 4.19e-71

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: 220.08  E-value: 4.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  61 DLGIICGSGLGPIGDTVQDATILPYSKIPGFPTTHVVGHKGNMIFGKLGGKKVVCLQGRFHPYEHNmDLALCTLPVRVMH 140
Cdd:TIGR01698   1 DMAIVLGSGWGGAVEALGEPVELPYAEIPGFPAPTVSGHAGELIRVRIGDGPVLVLGGRTHAYEGG-DARAVVHPVRTAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 141 QLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIflpALAGFSPLVGcndprfgARFVSVHDAYDKQLRQLAidvgRRSDMT 220
Cdd:TIGR01698  80 ATGAETLILTNAAGGLRQDWGPGTPVLISDHI---NLTARSPLIG-------PRFVDLTDAYSPRLRELA----ERVDPP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 221 LYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIANldADASVEVSHEEVMDIAQQ 300
Cdd:TIGR01698 146 LAEGVYAWFPGPHYETPAEIRMAGILGADLVGMSTVPETIAARFCGLEVLGVSLVTNLAA--GITGTPLSHAEVKAAGAA 223
                         250
                  ....*....|...
gi 1831512073 301 AGERASRFVSDII 313
Cdd:TIGR01698 224 AGTRLAALLADII 236
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
61-313 6.06e-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: 173.68  E-value: 6.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  61 DLGIICGSG--LGPIGDTVQDatilpysKIPGFPTTHvvghKGNMIFGKLGGKKVVCLQGRFHPyeHNMDlalCTLPVRV 138
Cdd:pfam01048   1 KIAIIGGSPeeLALLAELLDD-------ETPVGPPSR----GGKFYTGTLGGVPVVLVRHGIGP--PNAA---ILAAIRL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 139 MHQLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLpalAGFSPLVGcndPRFGARFVSVHDA-YDKQLRQLAIDVGRRS 217
Cdd:pfam01048  65 LKEFGVDAIIRTGTAGGLNPDLKVGDVVIPTDAINH---DGRSPLFG---PEGGPYFPDMAPApADPELRALAKEAAERL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 218 DMTLYEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIANLDADAsvEVSHEEVMDI 297
Cdd:pfam01048 139 GIPVHRGVYATGDGFYFETPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADG--ELTHEEVEEF 216
                         250
                  ....*....|....*.
gi 1831512073 298 AQQAGERASRFVSDII 313
Cdd:pfam01048 217 AERAAERAAALLLALL 232
MTAP_SsMTAPII_like_MTIP cd09010
5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus ...
62-313 5.28e-29

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: 111.36  E-value: 5.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  62 LGIICGSGL-GPIGDTVQDATIL--PYskipGFPTthvvghkGNMIFGKLGGKKVVCLQgRfHPYEHNmdlalcTLPVRV 138
Cdd:cd09010     1 IGIIGGSGLyDLDGLEDVEEVTVetPY----GKPS-------GPVTIGELGGREVAFLP-R-HGRGHR------IPPHRI 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 139 --------MHQLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLpalAGFSPLVGCNDPrfGARFVSVHDAYDKQLRQLA 210
Cdd:cd09010    62 nyraniwaLKELGVTRIIAVSAVGSLREEIKPGDLVIPDQFIDF---TKGRPSTFFDGG--GVVHVDFAEPFCPELRELL 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 211 IDVGRRSDMTLYE-GVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIAN-LDADasvE 288
Cdd:cd09010   137 IEAAKELGIPVHDgGTYVCTEGPRFETRAEIRMFRRLGGDVVGMTGVPEAVLARELGICYASIALVTNYAAgLEDE---P 213
                         250       260
                  ....*....|....*....|....*
gi 1831512073 289 VSHEEVMDIAQQAGERASRFVSDII 313
Cdd:cd09010   214 VTVEEVLEVLKENAEKVKRLLLAAI 238
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
62-311 2.61e-20

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: 87.35  E-value: 2.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  62 LGIICGSGLGpigdtvQDATILPYSKipgfPTTHVVGHKGNMIFGKLGGKKVVCLQGRFHPyehnmdlALCTLPVRVMHQ 141
Cdd:cd09005     1 YAIIPGDPER------VDVIDSKLEN----PQKVSSFRGYTMYTGKYNGKRVTVVNGGMGS-------PSAAIVVEELCA 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 142 LGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLPalaGFSPLVGCNDPRFgarfvsvhDAYDKQLRQLAIDVGRRSDMTL 221
Cdd:cd09005    64 LGVDTIIRVGSCGALREDIKVGDLVIADGAIRGD---GVTPYYVVGPPFA--------PEADPELTAALEEAAKELGLTV 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 222 YEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITnianldaDASVEVSHEEVMDIAQQA 301
Cdd:cd09005   133 HVGTVWTTDAFYRETREESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVS-------DNLITGEIGFVDEFLSEA 205
                         250
                  ....*....|
gi 1831512073 302 GERASRFVSD 311
Cdd:cd09005   206 EKKAIEIALD 215
PRK08564 PRK08564
S-methyl-5'-thioadenosine phosphorylase;
59-316 9.76e-18

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 236290  Cd Length: 267  Bit Score: 81.23  E-value: 9.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  59 RADLGIICGSGLGPIG-----DTVQDATilPYskipGFPTthvvghkGNMIFGKLGGKKVVCL--QGRFH-------PYE 124
Cdd:PRK08564    7 KASIGIIGGSGLYDPGifensKEVKVYT--PY----GEPS-------DNIIIGEIEGVEVAFLprHGRGHripphkiNYR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 125 HNMdLALctlpvrvmHQLGIKIMIVSNAAGGINAVLRHGDLMLIKDHIFLPALAGFSPLVGcndPRFGarFVSVHDAYDK 204
Cdd:PRK08564   74 ANI-WAL--------KELGVEWVIAVSAVGSLREDYKPGDFVIPDQFIDMTKKREYTFYDG---PVVA--HVSMADPFCP 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 205 QLRQLAIDVGRRSDMTLYE-GVYVMSGGPQYESPAEVSLFKTV-GADALGMSTCHEVTVARQCGikvLGFSLITNIANLD 282
Cdd:PRK08564  140 ELRKIIIETAKELGIRTHEkGTYICIEGPRFSTRAESRMWREVfKADIIGMTLVPEVNLACELG---MCYATIAMVTDYD 216
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1831512073 283 ADASVEVSHEEVMDIAQQAGERASRFVSDIITEI 316
Cdd:PRK08564  217 VWAEKPVTAEEVTRVMAENTEKAKKLLYEAIPRI 250
PRK08666 PRK08666
5'-methylthioadenosine phosphorylase; Validated
62-317 4.03e-17

5'-methylthioadenosine phosphorylase; Validated


Pssm-ID: 169548  Cd Length: 261  Bit Score: 79.37  E-value: 4.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  62 LGIICGSGL--GPIGDTVQDATI-LPYSKIpgfptthvvghkgNMIFGKLGGKKVVCL--QGRFH---PYEHNMDLALCT 133
Cdd:PRK08666    4 IAIIGGSGVydPKILENIREETVeTPYGEV-------------KVKIGTYAGEEVAFLarHGEGHsvpPHKINYRANIWA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 134 LpvrvmHQLGIKIMIVSNAAGGINAVLRHGDLMLIKD---------HIFLPAlaGFSPLVGCNdprfgarfvsVHDAYDK 204
Cdd:PRK08666   71 L-----KELGVERILATSAVGSLNPNMKPGDFVILDQfldftknrhYTFYDG--GESGVVHVD----------FTDPYCP 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 205 QLRQLAIDVGRRSDMTLYE-GVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIAnldA 283
Cdd:PRK08666  134 ELRKALITAARELGLTYHPgGTYVCTEGPRFETAAEIRMFRILGGDLVGMTQVPEAVLARELEMCYATVAIVTNYA---A 210
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1831512073 284 DASVE-VSHEEVMDIAQQAGERASRFVSDIITEIT 317
Cdd:PRK08666  211 GISPTkLTHSEVVELMAQNSENIKKLIMKAIELIP 245
PRK09136 PRK09136
S-methyl-5'-thioinosine phosphorylase;
62-316 7.25e-09

S-methyl-5'-thioinosine phosphorylase;


Pssm-ID: 236390  Cd Length: 245  Bit Score: 55.35  E-value: 7.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  62 LGIICGSG---LGPIGDTVQDATILPYskipGFPTthvvghkGNMIFGKLGGKKVVCLqGRfHPYEHnmdlalcTLP--- 135
Cdd:PRK09136    2 LAIIGGTGltqLAGLDIVQRQVVRTPY----GAPS-------GPLTFGTLAGREVVFL-AR-HGHGH-------TIPphk 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 136 ------VRVMHQLGIKIMIVSNAAGGINAVLRHGDLML---IKD------HIFlpalagfsplvgCNDPRFGARFVSVHD 200
Cdd:PRK09136   62 vnyranIWALKQAGATRVLAVNTVGGIHADMGPGTLVVpdqIIDytwgrkSTF------------FEGDGEEVTHIDFTH 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 201 AYDKQLRQLAIDVGRRSDMTLYE-GVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITNIA 279
Cdd:PRK09136  130 PYSPMLRQRLLAAARAAGVSLVDgGVYAATQGPRLETAAEIARLERDGCDLVGMTGMPEAALARELGLPYACLALVANWA 209
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1831512073 280 nldadASVEVSHEEVMDIAQQAGERASRFVSDIITEI 316
Cdd:PRK09136  210 -----AGRGDSAEITMAEIEAALDAAMGRVRELLERL 241
PRK07432 PRK07432
S-methyl-5'-thioadenosine phosphorylase;
58-277 1.30e-08

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 180977  Cd Length: 290  Bit Score: 55.17  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  58 ARADLGIICGSGLGPIgDTVQDATILPYSKIPGFPTThvvghkgNMIFGKLGGKKVVCL--QGRFH---PYEhnmdlalc 132
Cdd:PRK07432    2 TQAKIGIIGGSGLYKM-EALKDVEEVQLETPFGSPSD-------ALIVGTLDGTRVAFLarHGRNHtllPTE-------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 133 tLPVRV----MHQLGIKIMIVSNAAGGINAVLRHGDlMLIKDHIFLPALAGFSPLvgcndprFGARFVSvHDAYD----K 204
Cdd:PRK07432   66 -LPFRAniyaMKQLGVEYLISASAVGSLKEEAKPLD-MVVPDQFIDRTKNRISTF-------FGEGIVA-HIGFGdpicP 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831512073 205 QLRQLAIDVGRR---SDMTLYE-GVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITN 277
Cdd:PRK07432  136 ALAGVLADAIASlnlPDVTLHRgGTYVCMEGPAFSTKAESNLYRSWGATVIGMTNLPEAKLAREAEIAYATLALVTD 212
PRK07823 PRK07823
S-methyl-5'-thioadenosine phosphorylase;
58-314 6.48e-08

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 236107  Cd Length: 264  Bit Score: 52.78  E-value: 6.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  58 ARADLGIICGSG----LGPIGDTVQDATilPYSKiPGFPTThvvghkgnmiFGKLGGKKVVCL--QGRFH-------PYE 124
Cdd:PRK07823    4 NGAMLGVIGGSGfysfFGSDAREVNVDT--PYGP-PSAPIT----------IGEVGGRRVAFLprHGRDHefsphtvPYR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 125 HNMdLALctlpvrvmHQLGIKIMIVSNAAGGINAVLRHGDlMLIKDHiflpalagfspLV----GCNDPRF--GARFVSV 198
Cdd:PRK07823   71 ANM-WAL--------RALGVRRVFAPCAVGSLRPELGPGT-VVVPDQ-----------LVdrtsGRAQTYFdsGGVHVSF 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 199 HDAYDKQLRQLAIDVGRRSDmtlyEGVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITni 278
Cdd:PRK07823  130 ADPYCPTLRAAALGLPGVVD----GGTMVVVQGPRFSTRAESRWFAAQGWSLVNMTGYPEAVLARELELCYAAIALVT-- 203
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1831512073 279 anlDADASVE----VSHEEVMDIAQQAGERASRFVSDIIT 314
Cdd:PRK07823  204 ---DLDAGVEagegVKAVDVFAEFGRNIERLKRLVRDAIA 240
PRK08931 PRK08931
S-methyl-5'-thioadenosine phosphorylase;
58-313 1.49e-06

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 181584  Cd Length: 289  Bit Score: 48.85  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073  58 ARADLGIICGSGLGPIgDTVQDATILPYSKIPGFPTTHVvghkgnmIFGKLGGKKVVCL--QGRFH-------PYEHNMD 128
Cdd:PRK08931    2 TKAVLGIIGGSGVYDI-DGLEDARWERVESPWGEPSDAL-------LFGRLGGVPMVFLprHGRGHrlspsdiNYRANID 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 129 lalctlpvrVMHQLGIKIMIVSNAAGGINAVLRHGDLMLIK---DHIFLPALAGFSPlvGCndprfgARFVSVHDAYDKQ 205
Cdd:PRK08931   74 ---------ALKRAGVTDIVSLSACGSFREELPPGTFVIVDqfiDRTFAREKSFFGT--GC------VAHVSMAHPVCPR 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512073 206 LRQLAIDVGRRSDMTLYE-GVYVMSGGPQYESPAEVSLFKTVGADALGMSTCHEVTVARQCGIKVLGFSLITnianlDAD 284
Cdd:PRK08931  137 LGDRLAAAARAEGITVHRgGTYLCMEGPQFSTLAESKLYRSWGCDVIGMTNMPEAKLAREAEICYATVAMVT-----DYD 211
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1831512073 285 A------SVEVshEEVMDIAQQAGERASRFVSDII 313
Cdd:PRK08931  212 CwhpdhdAVTV--DAVIAVLLANADKARALVARLA 244
 
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