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Conserved domains on  [gi|1207174942|ref|XP_021331665|]
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ribose-phosphate pyrophosphokinase 1 isoform X4 [Danio rerio]

Protein Classification

ribose-phosphate pyrophosphokinase( domain architecture ID 11421473)

ribose-phosphate pyrophosphokinase catalyzes the transfer of the pyrophosphoryl group from ATP to the 1-hydroxyl of ribose-5-phosphate to form the the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP)

CATH:  3.40.50.2020
EC:  2.7.6.1
Gene Ontology:  GO:0005524|GO:0002189|GO:0016301|GO:0016310|GO:0004749
PubMed:  11751055

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 1-203 3.10e-96

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


:

Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 282.33  E-value: 3.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENinEWKNCTIVSPDAGGAKRcggVTSIADRLNVDFAL 80
Cdd:COG0462   115 LLEAAGADRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKSK--DLEDLVVVSPDVGGVKR---ARAFAKRLGAPLAI 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVVV 160
Cdd:COG0462   190 IDKRRPGANEVEVMNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAAATHGVLSGPAVERLENSPIDELVV 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207174942 161 TNTIPQEDKiKHCSKIQVIDISMILAEAIRRTHNGESVSYLFS 203
Cdd:COG0462   270 TDTIPLPEE-KRCDKIKVLSVAPLLAEAIRRIHEGESVSSLFD 311
 
Name Accession Description Interval E-value
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 1-203 3.10e-96

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 282.33  E-value: 3.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENinEWKNCTIVSPDAGGAKRcggVTSIADRLNVDFAL 80
Cdd:COG0462   115 LLEAAGADRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKSK--DLEDLVVVSPDVGGVKR---ARAFAKRLGAPLAI 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVVV 160
Cdd:COG0462   190 IDKRRPGANEVEVMNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAAATHGVLSGPAVERLENSPIDELVV 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207174942 161 TNTIPQEDKiKHCSKIQVIDISMILAEAIRRTHNGESVSYLFS 203
Cdd:COG0462   270 TDTIPLPEE-KRCDKIKVLSVAPLLAEAIRRIHEGESVSSLFD 311
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
1-202 2.65e-92

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 272.38  E-value: 2.65e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENinEWKNCTIVSPDAGGAKRcggVTSIADRLNVDFAL 80
Cdd:PRK01259  112 LLETAGADRVLTMDLHADQIQGFFDIPVDNLYGSPILLEDIKQK--NLENLVVVSPDVGGVVR---ARALAKRLDADLAI 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVVV 160
Cdd:PRK01259  187 IDKRRPRANVSEVMNIIGDVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSVYAYATHPVLSGGAIERIENSVIDELVV 266

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1207174942 161 TNTIPQEDKIKHCSKIQVIDISMILAEAIRRTHNGESVSYLF 202
Cdd:PRK01259  267 TDSIPLSEEAKKCDKIRVLSVAPLLAEAIRRISNEESVSSLF 308
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 1-203 1.26e-87

ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273523 [Multi-domain]  Cd Length: 308  Bit Score: 260.29  E-value: 1.26e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENIneWKNCTIVSPDAGGAKRcggVTSIADRLNVDFAL 80
Cdd:TIGR01251 113 LLETAGADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYLKKKI--LDNPVVVSPDAGGVER---AKKVADALGCPLAI 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERK-KANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVV 159
Cdd:TIGR01251 188 IDKRRIsATNEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIAAATHGVFSGPAIERIANAGVEEVI 267

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1207174942 160 VTNTIPQEdkiKHCSKIQVIDISMILAEAIRRTHNGESVSYLFS 203
Cdd:TIGR01251 268 VTNTIPHE---KHKPKVSVISVAPLIAEAIRRIHNNESVSSLFD 308
Pribosyl_synth pfam14572
Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes ...
 47-202 1.04e-44

Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes from class EC:2.7.6.1, phosphoribosyl-pyrophosphate transferase.


Pssm-ID: 434046  Cd Length: 184  Bit Score: 146.89  E-value: 1.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  47 EWKNCTIVSPDAGGAKRcggVTSIADRLNVDFALIHKERKKA--NEVDR----------------------------MVL 96
Cdd:pfam14572   1 DYRNAVIVARSPGSAKR---ATSFAERLRLGIAVIHGEQKEAesDEVDGrqspppyrsrtvsrslglpeiipkekppMTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  97 VGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVVVTNTIPQEDKIKHCSKI 176
Cdd:pfam14572  78 VGDVGGRIAIIVDDMIDDVDSFVAAAELLKERGAYKIYVMATHGLLSSDAPRLLEASPIDEVVVTNTIPHEIQKMQCHKI 157

                         170       180
                  ....*....|....*....|....*.
gi 1207174942 177 QVIDISMILAEAIRRTHNGESVSYLF 202
Cdd:pfam14572 158 KTIDISQLIAEAIRRIHNGESMSYLF 183
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 33-163 1.88e-21

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 85.53  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  33 AEPAVLKWIKENIneWKNCTIVSPDAGGAKRcggVTSIADRLNVDFALIHKERKKANEVDRM------VLVGDVKDRVAI 106
Cdd:cd06223     1 AGRLLAEEIREDL--LEPDVVVGILRGGLPL---AAALARALGLPLAFIRKERKGPGRTPSEpyglelPLGGDVKGKRVL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207174942 107 LVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAisRINNANFEAVVVTNT 163
Cdd:cd06223    76 LVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA--RELASPGDPVYSLFT 130
 
Name Accession Description Interval E-value
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 1-203 3.10e-96

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 282.33  E-value: 3.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENinEWKNCTIVSPDAGGAKRcggVTSIADRLNVDFAL 80
Cdd:COG0462   115 LLEAAGADRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKSK--DLEDLVVVSPDVGGVKR---ARAFAKRLGAPLAI 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVVV 160
Cdd:COG0462   190 IDKRRPGANEVEVMNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAAATHGVLSGPAVERLENSPIDELVV 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207174942 161 TNTIPQEDKiKHCSKIQVIDISMILAEAIRRTHNGESVSYLFS 203
Cdd:COG0462   270 TDTIPLPEE-KRCDKIKVLSVAPLLAEAIRRIHEGESVSSLFD 311
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
1-202 2.65e-92

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 272.38  E-value: 2.65e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENinEWKNCTIVSPDAGGAKRcggVTSIADRLNVDFAL 80
Cdd:PRK01259  112 LLETAGADRVLTMDLHADQIQGFFDIPVDNLYGSPILLEDIKQK--NLENLVVVSPDVGGVVR---ARALAKRLDADLAI 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVVV 160
Cdd:PRK01259  187 IDKRRPRANVSEVMNIIGDVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSVYAYATHPVLSGGAIERIENSVIDELVV 266

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1207174942 161 TNTIPQEDKIKHCSKIQVIDISMILAEAIRRTHNGESVSYLF 202
Cdd:PRK01259  267 TDSIPLSEEAKKCDKIRVLSVAPLLAEAIRRISNEESVSSLF 308
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 1-203 1.26e-87

ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273523 [Multi-domain]  Cd Length: 308  Bit Score: 260.29  E-value: 1.26e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENIneWKNCTIVSPDAGGAKRcggVTSIADRLNVDFAL 80
Cdd:TIGR01251 113 LLETAGADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYLKKKI--LDNPVVVSPDAGGVER---AKKVADALGCPLAI 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERK-KANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVV 159
Cdd:TIGR01251 188 IDKRRIsATNEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIAAATHGVFSGPAIERIANAGVEEVI 267

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1207174942 160 VTNTIPQEdkiKHCSKIQVIDISMILAEAIRRTHNGESVSYLFS 203
Cdd:TIGR01251 268 VTNTIPHE---KHKPKVSVISVAPLIAEAIRRIHNNESVSSLFD 308
PRK04923 PRK04923
ribose-phosphate diphosphokinase;
1-202 9.99e-63

ribose-phosphate diphosphokinase;


Pssm-ID: 179893 [Multi-domain]  Cd Length: 319  Bit Score: 197.46  E-value: 9.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIkenineWK-----NCTIVSPDAGGAKRcggVTSIADRL- 74
Cdd:PRK04923  119 MISAMGADRVLTVDLHADQIQGFFDVPVDNVYASPLLLADI------WRaygtdNLIVVSPDVGGVVR---ARAVAKRLd 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  75 NVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNAN 154
Cdd:PRK04923  190 DADLAIIDKRRPRANVATVMNIIGDVQGKTCVLVDDLVDTAGTLCAAAAALKQRGALKVVAYITHPVLSGPAVDNINNSQ 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1207174942 155 FEAVVVTNTIPQEDKIKHCSKIQVIDISMILAEAIRRTHNGESVSYLF 202
Cdd:PRK04923  270 LDELVVTDTIPLSEAARACAKIRQLSVAELLAETIRRIAFGESVSSLY 317
PLN02369 PLN02369
ribose-phosphate pyrophosphokinase
 1-202 7.87e-60

ribose-phosphate pyrophosphokinase


Pssm-ID: 215209 [Multi-domain]  Cd Length: 302  Bit Score: 189.52  E-value: 7.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENINEWKNCTIVSPDAGGAKRcggVTSIADRL-NVDFA 79
Cdd:PLN02369  103 LITEAGADRVLACDLHSGQSMGYFDIPVDHVYGQPVILDYLASKTISSPDLVVVSPDVGGVAR---ARAFAKKLsDAPLA 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  80 LIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVV 159
Cdd:PLN02369  180 IVDKRRQGHNVAEVMNLIGDVKGKVAIMVDDMIDTAGTITKGAALLHQEGAREVYACATHAVFSPPAIERLSSGLFQEVI 259

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207174942 160 VTNTIPQEDKiKHCSKIQVIDISMILAEAIRRTHNGESVSYLF 202
Cdd:PLN02369  260 VTNTIPVSEK-NYFPQLTVLSVANLLGETIWRVHDDCSVSSIF 301
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
1-202 1.06e-59

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 189.00  E-value: 1.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENINEwKNCTIVSPDAGGAKrcggVTSI-ADRL-NVDF 78
Cdd:PRK03092  101 LFKTAGADRIMTVDLHTAQIQGFFDGPVDHLFAMPLLADYVRDKYDL-DNVTVVSPDAGRVR----VAEQwADRLgGAPL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  79 ALIHKER--KKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFE 156
Cdd:PRK03092  176 AFIHKTRdpTVPNQVVANRVVGDVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVIIAATHGVLSGPAAERLKNCGAR 255

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1207174942 157 AVVVTNTIPQEDKiKHCSKIQVIDISMILAEAIRRTHNGESVSYLF 202
Cdd:PRK03092  256 EVVVTDTLPIPEE-KRFDKLTVLSIAPLLARAIREVFEDGSVTSLF 300
PRK02269 PRK02269
ribose-phosphate diphosphokinase;
1-202 1.73e-57

ribose-phosphate diphosphokinase;


Pssm-ID: 167353 [Multi-domain]  Cd Length: 320  Bit Score: 183.84  E-value: 1.73e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENINEWKNCTIVSPDAGGAKRcggVTSIADRLNVDFAL 80
Cdd:PRK02269  117 MLEVAGVDRLLTVDLHAAQIQGFFDIPVDHLMGAPLIADYFDRRGLVGDDVVVVSPDHGGVTR---ARKLAQFLKTPIAI 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERK--KANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAV 158
Cdd:PRK02269  194 IDKRRSvdKMNTSEVMNIIGNVKGKKCILIDDMIDTAGTICHAADALAEAGATEVYASCTHPVLSGPALDNIQKSAIEKL 273

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1207174942 159 VVTNTI--PQEdkiKHCSKIQVIDISMILAEAIRRTHNGESVSYLF 202
Cdd:PRK02269  274 VVLDTIylPEE---RLIDKIEQISIADLLGEAIIRIHEKRPLSPLF 316
PRK02812 PRK02812
ribose-phosphate pyrophosphokinase; Provisional
 1-202 2.88e-57

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235072 [Multi-domain]  Cd Length: 330  Bit Score: 183.79  E-value: 2.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENinEWKNCTIVSPDAGGAKRcggVTSIADRLN-VDFA 79
Cdd:PRK02812  133 LITKAGADRVLAMDLHSAQIQGYFDIPCDHVYGSPVLLDYLASK--NLEDIVVVSPDVGGVAR---ARAFAKKLNdAPLA 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  80 LIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVV 159
Cdd:PRK02812  208 IIDKRRQAHNVAEVLNVIGDVKGKTAILVDDMIDTGGTICEGARLLRKEGAKQVYACATHAVFSPPAIERLSSGLFEEVI 287

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207174942 160 VTNTIPQEDKiKHCSKIQVIDISMILAEAIRRTHNGESVSYLF 202
Cdd:PRK02812  288 VTNTIPVPEE-RRFPQLKVLSVANMLGEAIWRIHEESSVSSMF 329
PTZ00145 PTZ00145
phosphoribosylpyrophosphate synthetase; Provisional
 1-202 2.04e-56

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 240290 [Multi-domain]  Cd Length: 439  Bit Score: 184.31  E-value: 2.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFD--IPVDNLYAEPAVLKWIKENinEWKNCTIVSPDAGGAKRcggVTSIADRLN--- 75
Cdd:PTZ00145  231 MIEAMGVDRVVAIDLHSGQIQGFFGprVPVDNLEAQLIGLDYFTKK--DLYKPVIVSPDAGGVYR---ARKFQDGLNhrg 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  76 ---VDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINN 152
Cdd:PTZ00145  306 isdCGIAMLIKQRTKPNEIEKMDLVGNVYDSDVIIVDDMIDTSGTLCEAAKQLKKHGARRVFAFATHGLFSGPAIERIEA 385

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207174942 153 ANFEAVVVTNTIPQEDKIKHCSKIQVIDISMILAEAIRRTHNGESVSYLF 202
Cdd:PTZ00145  386 SPLEEVVVTDTVKSNKNIDSCKKITKLSVSVLVADAIRRIHQKESLNDLF 435
Pribosyl_synth pfam14572
Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes ...
 47-202 1.04e-44

Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes from class EC:2.7.6.1, phosphoribosyl-pyrophosphate transferase.


Pssm-ID: 434046  Cd Length: 184  Bit Score: 146.89  E-value: 1.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  47 EWKNCTIVSPDAGGAKRcggVTSIADRLNVDFALIHKERKKA--NEVDR----------------------------MVL 96
Cdd:pfam14572   1 DYRNAVIVARSPGSAKR---ATSFAERLRLGIAVIHGEQKEAesDEVDGrqspppyrsrtvsrslglpeiipkekppMTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  97 VGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVVVTNTIPQEDKIKHCSKI 176
Cdd:pfam14572  78 VGDVGGRIAIIVDDMIDDVDSFVAAAELLKERGAYKIYVMATHGLLSSDAPRLLEASPIDEVVVTNTIPHEIQKMQCHKI 157

                         170       180
                  ....*....|....*....|....*.
gi 1207174942 177 QVIDISMILAEAIRRTHNGESVSYLF 202
Cdd:pfam14572 158 KTIDISQLIAEAIRRIHNGESMSYLF 183
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 1-206 2.12e-39

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 137.18  E-value: 2.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENINEWKNCTIVSPDAGGAKRcggVTSIADRLNVDFAL 80
Cdd:PRK02458  121 MLVKAGVDRVLTLDLHAVQVQGFFDIPVDNLFTVPLFAKHYCKKGLSGSDVVVVSPKNSGIKR---ARSLAEYLDAPIAI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERKKANEVDRMVlVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVVV 160
Cdd:PRK02458  198 IDYAQDDSEREEGYI-IGDVAGKKAILIDDILNTGKTFAEAAKIVEREGATEIYAVASHGLFAGGAAEVLENAPIKEILV 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1207174942 161 TNTIPQEDKIKhcSKIQVIDISMILAEAIRRTHNGESVSYLFSHVP 206
Cdd:PRK02458  277 TDSVATKERVP--KNVTYLSASELIADAIIRIHERKPLSPLFAYNK 320
PRK00553 PRK00553
ribose-phosphate pyrophosphokinase; Provisional
 1-203 7.90e-39

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 179062 [Multi-domain]  Cd Length: 332  Bit Score: 136.20  E-value: 7.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   1 MLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKEnINEWKNCTIVSPDAGGAKRcggVTSIADRLNVDFAL 80
Cdd:PRK00553  121 LLTKAGVTRVTLTDIHSDQTQGFFDIPVDILRTYHVFLSRVLE-LLGKKDLVVVSPDYGGVKR---ARLIAESLELPLAI 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVV- 159
Cdd:PRK00553  197 IDKRRPKHNVAESINVLGEVKNKNCLIVDDMIDTGGTVIAAAKLLKKQKAKKVCVMATHGLFNKNAIQLFDEAFKKKLId 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1207174942 160 ---VTNTIPQEdKIKHCSKIQVIDISMILAEAIRRTHNGESVSYLFS 203
Cdd:PRK00553  277 klfVSNSIPQT-KFEKKPQFKVVDLAHLYEEVLLCYANGGSISAIYT 322
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 5-191 3.69e-31

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 115.01  E-value: 3.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   5 AGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIKENINewkNCTIVSPDAGGAKRcggVTSIADRLNVDFALIHKE 84
Cdd:PRK00934  113 AYYDRIITINIHEPSILEFFPIPFINLDAAPLIAEYIGDKLD---DPLVLAPDKGALEL---AKEAAEILGCEYDYLEKT 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  85 RKKANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVVVTNTI 164
Cdd:PRK00934  187 RISPTEVEIAPKNLDVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACVHPVLVGDAILKLYNAGVDEIIVTDTL 266

                         170       180
                  ....*....|....*....|....*..
gi 1207174942 165 PqedkikhcSKIQVIDISMILAEAIRR 191
Cdd:PRK00934  267 E--------SEVSKISVAPLIADLLKK 285
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
8-191 3.82e-25

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 99.24  E-value: 3.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   8 DHIITMDLH---ASQIQGFFDIPVDNLYAEPAVLKWIKENINEWkncTIVSPDAGGAKRcggVTSIADRLNVDFALIHKE 84
Cdd:PRK07199  119 DRLVTVDPHlhrYPSLSEVYPIPAVVLSAAPAIAAWIRAHVPRP---LLIGPDEESEQW---VAAVAERAGAPHAVLRKT 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  85 RKKANEVDrmVLVGDV---KDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISRINNANFEAVVVT 161
Cdd:PRK07199  193 RHGDRDVE--ISLPDAapwAGRTPVLVDDIVSTGRTLIEAARQLRAAGAASPDCVVVHALFAGDAYSALAAAGIARVVST 270

                         170       180       190
                  ....*....|....*....|....*....|
gi 1207174942 162 NTIPqedkikHCSkiQVIDISMILAEAIRR 191
Cdd:PRK07199  271 DTVP------HPS--NAISLAPLLAEALRR 292
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 33-163 1.88e-21

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 85.53  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  33 AEPAVLKWIKENIneWKNCTIVSPDAGGAKRcggVTSIADRLNVDFALIHKERKKANEVDRM------VLVGDVKDRVAI 106
Cdd:cd06223     1 AGRLLAEEIREDL--LEPDVVVGILRGGLPL---AAALARALGLPLAFIRKERKGPGRTPSEpyglelPLGGDVKGKRVL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207174942 107 LVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAisRINNANFEAVVVTNT 163
Cdd:cd06223    76 LVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA--RELASPGDPVYSLFT 130
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 6-201 1.90e-17

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 79.23  E-value: 1.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   6 GADHIITMDLHASQIQGFFDIP-VDNLYAEPAVLKWIKENINE----WKNCTIVSPDAGGAKRcggVTSIADRLNVDFAL 80
Cdd:PRK06827  159 GVDNIITFDAHDPRIENAIPLMgFENLYPSYQIIKALLKNEKDleidKDHLMVISPDTGAMDR---AKYYASVLGVDLGL 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERK-------KANEVDRMVLVGDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGpAISRINNA 153
Cdd:PRK06827  236 FYKRRDysrvvngRNPIVAHEFLGRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAATFGFFTN-GLEKFDKA 314

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207174942 154 N----FEAVVVTNTIPQEDKIKHCSKIQVIDISMILAEAIRRTHNGESVSYL 201
Cdd:PRK06827  315 YeegyFDRIIGTNLVYHPEELLSKPWYIEVDMSKLIARIIDALNHDVSLSKL 366
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 3-166 5.82e-07

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 48.92  E-value: 5.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942   3 SVAGADHIITMDLHASQIQGFFDIPVDNLYAE--PAVLKWIKEnINEWKNCTIVSPDAGGAKRcggvtsiadrlnvdfal 80
Cdd:PLN02297  136 SRGGPTSLVIFDIHALQERFYFGDNVLPCFESgiPLLKKRLQQ-LPDSDNIVIAFPDDGAWKR----------------- 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  81 IHKERKKANEV---------DRMVLV--GDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKVYAILTHGIFSGPAISR 149
Cdd:PLN02297  198 FHKQFEHFPMVvctkvregdKRIVRIkeGNPAGRHVVIVDDLVQSGGTLIECQKVLAAHGAAKVSAYVTHGVFPNESWER 277

                         170       180
                  ....*....|....*....|...
gi 1207174942 150 INNAN------FEAVVVTNTIPQ 166
Cdd:PLN02297  278 FTHDNggpeagFAYFWITDSCPQ 300
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 27-133 3.19e-06

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 45.05  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  27 PVDNLYAEPAVLKWIKE---NINE---WKNCTIVSPDAGGAKRcggVTSIADRLNVDFALIHKERKKAN---EVDRMVLV 97
Cdd:pfam00156   1 SVDEILDNPAILKAVARlaaQINEdygGKPDVVVGILRGGLPF---AGILARRLDVPLAFVRKVSYNPDtseVMKTSSAL 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1207174942  98 GDVKDRVAILVDDMADTCGTVCHAADKLVSAGAIKV 133
Cdd:pfam00156  78 PDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEV 113
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 67-162 4.09e-03

Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440229  Cd Length: 201  Bit Score: 36.67  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207174942  67 VTSIADRLNVDFALIhkeRKKANEVDRM-VLVGDVK--DRVAIlVDDMADTCGTVCHAADKLVSAGA--IKVYAILTHGi 141
Cdd:COG0461    78 AAAVARALGLPAIFV---RKEAKDHGTGgQIEGGLLpgERVLV-VEDVITTGGSVLEAVEALREAGAevVGVAVIVDRE- 152

                          90       100
                  ....*....|....*....|.
gi 1207174942 142 fsGPAISRINNANFEAVVVTN 162
Cdd:COG0461   153 --EGAAENLEEAGVPLHSLLT 171
 
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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