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Conserved domains on  [gi|1232339293|gb|OYW15564|]
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hypoxanthine-guanine phosphoribosyltransferase [Hydrogenophilales bacterium 12-64-6]

Protein Classification

hypoxanthine-guanine phosphoribosyltransferase( domain architecture ID 10793154)

hypoxanthine-guanine phosphoribosyltransferase converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 1-179 1.46e-106

hypoxanthine-guanine phosphoribosyltransferase; Provisional


:

Pssm-ID: 181675  Cd Length: 181  Bit Score: 302.55  E-value: 1.46e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293   1 MTSLDAQQLLDHAECIASEDEVQAVLDRLAGEIALGLRDAFPLVLAVMGGAVVFAGQLLPRLRFPLEFDYLHVTRYRGKT 80
Cdd:PRK09162    1 MSLEEIRQVLAEADCLVSAAEVEAAIDRMADEITADLADENPLVLCVMGGGLVFTGQLLPRLDFPLEFDYLHATRYRNET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  81 EGGEVEWRVLPGQNVVGRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNG-LAKPIRADFVGLDVPNRYVF 159
Cdd:PRK09162   81 TGGELVWKVKPRESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDrKAKPLKADFVGLEVPDRYVF 160

                         170       180
                  ....*....|....*....|
gi 1232339293 160 GCGMDAYGLWRNLPAIYALK 179
Cdd:PRK09162  161 GYGMDYKGYWRNLPGIYAVK 180
 
Name Accession Description Interval E-value
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 1-179 1.46e-106

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 302.55  E-value: 1.46e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293   1 MTSLDAQQLLDHAECIASEDEVQAVLDRLAGEIALGLRDAFPLVLAVMGGAVVFAGQLLPRLRFPLEFDYLHVTRYRGKT 80
Cdd:PRK09162    1 MSLEEIRQVLAEADCLVSAAEVEAAIDRMADEITADLADENPLVLCVMGGGLVFTGQLLPRLDFPLEFDYLHATRYRNET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  81 EGGEVEWRVLPGQNVVGRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNG-LAKPIRADFVGLDVPNRYVF 159
Cdd:PRK09162   81 TGGELVWKVKPRESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDrKAKPLKADFVGLEVPDRYVF 160

                         170       180
                  ....*....|....*....|
gi 1232339293 160 GCGMDAYGLWRNLPAIYALK 179
Cdd:PRK09162  161 GYGMDYKGYWRNLPGIYAVK 180
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 11-180 4.98e-74

Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; Hypoxanthine-guanine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440399  Cd Length: 176  Bit Score: 219.90  E-value: 4.98e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  11 DHAECIASEDEVQAVLDRLAGEIALGLRDAFPLVLAVMGGAVVFAGQLLPRLRFPLEFDYLHVTRYRGKTEG-GEVEWRV 89
Cdd:COG0634     4 DIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESsGEVRILK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  90 LPGQNVVGRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNGLAKPIRADFVGLDVPNRYVFGCGMDAYGLW 169
Cdd:COG0634    84 DLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYAEYY 163

                         170
                  ....*....|.
gi 1232339293 170 RNLPAIYALKD 180
Cdd:COG0634   164 RNLPYIYALKP 174
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 18-179 1.11e-24

hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine phosphoribosyltransferase. Sequence differences as small as a single residue can affect whether members of this family act on hypoxanthine and guanine or hypoxanthine only. The designation of this model as equivalog reflects hypoxanthine specificity and does not reflect whether or not guanine can replace hypoxanthine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273497  Cd Length: 166  Bit Score: 93.85  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  18 SEDEVQAVLDRLAGEIALGLRDAFPLVLAVMGGAVVFAGQLLPRLRFPLEFDYLHVTRY-RGKTEGGEVewRVLPG--QN 94
Cdd:TIGR01203   4 PEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYgNGMQSSGDV--KILKDldLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  95 VVGRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNGLAKPIRADFVGLDVPNRYVFGCGMDAYGLWRNLPA 174
Cdd:TIGR01203  82 IKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNLPY 161


                  ....*
gi 1232339293 175 IYALK 179
Cdd:TIGR01203 162 IGVLE 166
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 25-151 6.27e-16

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: 70.50  E-value: 6.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  25 VLDRLAGEIAlGLRDAFPLVLAVMGGAVVFAGQLlpRLRFPLEFDYLHVTRYR-GKTEGGEVEWRVLPGQNVVGRNVLVL 103
Cdd:cd06223     1 AGRLLAEEIR-EDLLEPDVVVGILRGGLPLAAAL--ARALGLPLAFIRKERKGpGRTPSEPYGLELPLGGDVKGKRVLLV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1232339293 104 DDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNG----LAKPIRADFVGL 151
Cdd:cd06223    78 DDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGgareLASPGDPVYSLF 129
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 24-165 5.11e-13

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: 63.15  E-value: 5.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  24 AVLDRLAGEIALGLRDAFPLVLAVMGGAVVFAGQLLPRLrfPLEFDYLHVTRYRGKTEGGEVEWRVLPgqNVVGRNVLVL 103
Cdd:pfam00156  13 KAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRL--DVPLAFVRKVSYNPDTSEVMKTSSALP--DLKGKTVLIV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232339293 104 DDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKdNGLAKPIRADFVGLDVPNRYVFGCGMDA 165
Cdd:pfam00156  89 DDILDTGGTLLKVLELLKNVGPKEVKIAVLIDK-PAGTEPKDKYDKRVDDWIVFVVGFGLDE 149
 
Name Accession Description Interval E-value
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 1-179 1.46e-106

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 302.55  E-value: 1.46e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293   1 MTSLDAQQLLDHAECIASEDEVQAVLDRLAGEIALGLRDAFPLVLAVMGGAVVFAGQLLPRLRFPLEFDYLHVTRYRGKT 80
Cdd:PRK09162    1 MSLEEIRQVLAEADCLVSAAEVEAAIDRMADEITADLADENPLVLCVMGGGLVFTGQLLPRLDFPLEFDYLHATRYRNET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  81 EGGEVEWRVLPGQNVVGRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNG-LAKPIRADFVGLDVPNRYVF 159
Cdd:PRK09162   81 TGGELVWKVKPRESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDrKAKPLKADFVGLEVPDRYVF 160

                         170       180
                  ....*....|....*....|
gi 1232339293 160 GCGMDAYGLWRNLPAIYALK 179
Cdd:PRK09162  161 GYGMDYKGYWRNLPGIYAVK 180
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 11-180 4.98e-74

Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; Hypoxanthine-guanine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440399  Cd Length: 176  Bit Score: 219.90  E-value: 4.98e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  11 DHAECIASEDEVQAVLDRLAGEIALGLRDAFPLVLAVMGGAVVFAGQLLPRLRFPLEFDYLHVTRYRGKTEG-GEVEWRV 89
Cdd:COG0634     4 DIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESsGEVRILK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  90 LPGQNVVGRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNGLAKPIRADFVGLDVPNRYVFGCGMDAYGLW 169
Cdd:COG0634    84 DLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYAEYY 163

                         170
                  ....*....|.
gi 1232339293 170 RNLPAIYALKD 180
Cdd:COG0634   164 RNLPYIYALKP 174
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 11-180 7.92e-25

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 95.10  E-value: 7.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  11 DHAEC-IASEDEVQAVLDRLAGEIALGLRDAFPLVLAVMGGAVVFAGQLLPRLRF---PLEFDYLHVTRYRGKTEG-GEV 85
Cdd:PLN02238    5 VDIEKvLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQPlprGLTVDFIRASSYGGGTESsGVA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  86 EWRVLPGQ-NVVGRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNGLAKPIR-----ADFVGLDVPNRYVF 159
Cdd:PLN02238   85 KVSGADLKiDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYElvgdgKEYVGFECPDEFVV 164

                         170       180
                  ....*....|....*....|.
gi 1232339293 160 GCGMDAYGLWRNLPAIYALKD 180
Cdd:PLN02238  165 GYGLDFAEKYRNLPYVGVLKP 185
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 18-179 1.11e-24

hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine phosphoribosyltransferase. Sequence differences as small as a single residue can affect whether members of this family act on hypoxanthine and guanine or hypoxanthine only. The designation of this model as equivalog reflects hypoxanthine specificity and does not reflect whether or not guanine can replace hypoxanthine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273497  Cd Length: 166  Bit Score: 93.85  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  18 SEDEVQAVLDRLAGEIALGLRDAFPLVLAVMGGAVVFAGQLLPRLRFPLEFDYLHVTRY-RGKTEGGEVewRVLPG--QN 94
Cdd:TIGR01203   4 PEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYgNGMQSSGDV--KILKDldLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  95 VVGRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNGLAKPIRADFVGLDVPNRYVFGCGMDAYGLWRNLPA 174
Cdd:TIGR01203  82 IKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNLPY 161


                  ....*
gi 1232339293 175 IYALK 179
Cdd:TIGR01203 162 IGVLE 166
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 25-151 6.27e-16

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: 70.50  E-value: 6.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  25 VLDRLAGEIAlGLRDAFPLVLAVMGGAVVFAGQLlpRLRFPLEFDYLHVTRYR-GKTEGGEVEWRVLPGQNVVGRNVLVL 103
Cdd:cd06223     1 AGRLLAEEIR-EDLLEPDVVVGILRGGLPLAAAL--ARALGLPLAFIRKERKGpGRTPSEPYGLELPLGGDVKGKRVLLV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1232339293 104 DDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNG----LAKPIRADFVGL 151
Cdd:cd06223    78 DDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGgareLASPGDPVYSLF 129
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 24-165 5.11e-13

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: 63.15  E-value: 5.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  24 AVLDRLAGEIALGLRDAFPLVLAVMGGAVVFAGQLLPRLrfPLEFDYLHVTRYRGKTEGGEVEWRVLPgqNVVGRNVLVL 103
Cdd:pfam00156  13 KAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRL--DVPLAFVRKVSYNPDTSEVMKTSSALP--DLKGKTVLIV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232339293 104 DDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKdNGLAKPIRADFVGLDVPNRYVFGCGMDA 165
Cdd:pfam00156  89 DDILDTGGTLLKVLELLKNVGPKEVKIAVLIDK-PAGTEPKDKYDKRVDDWIVFVVGFGLDE 149
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 18-159 1.59e-11

Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 441837 [Multi-domain]  Cd Length: 153  Bit Score: 59.09  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  18 SEDEVQAVLDRLAGEIalgLRDAFP--LVLAVMGGAVVFAGQLLPRLRFPlEFDYLHVTRYRG-KTEGGEVEWRVLPGQN 94
Cdd:COG2236    10 SWDEIHELSRRLAEQI---LESGFRpdVIVAIARGGLVPARILADALGVP-DLASIRVSSYTGtAKRLEEPVVKGPLDED 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232339293  95 VVGRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNGLAKPiraDFVGLDVPNRYVF 159
Cdd:COG2236    86 LAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSKFKP---DYYAEETDAWIVF 147
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 14-175 3.13e-11

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 58.88  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  14 ECIASEDEVQAVLDRLAGEIALGLRDAFP--LVLAVMGGAVVFAGQLLPRLRFPLEFDYLHVTRY-RGKTEGGEVEWRVL 90
Cdd:PRK15423    6 EVMIPEAEIKARIAELGRQITERYKDSGSdmVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYgSGMSTTRDVKILKD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  91 PGQNVVGRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNGLAKPIRADFVGLDVPNRYVFGCGMDAYGLWR 170
Cdd:PRK15423   86 LDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYR 165


                  ....*
gi 1232339293 171 NLPAI 175
Cdd:PRK15423  166 HLPYI 170
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 97-180 8.43e-10

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 55.93  E-value: 8.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  97 GRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNGLAKPIRADFVGLDVPNRYVFGCGMDAYGLWRNLPAIY 176
Cdd:PTZ00149  150 DKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGFKGDFVGFSIPDHFVVGYCLDYNEHFRDLDHVA 229


                  ....
gi 1232339293 177 ALKD 180
Cdd:PTZ00149  230 VLND 233
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 13-179 8.04e-08

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 50.02  E-value: 8.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  13 AECIASEDEVQAVLDRLAGEIA-----LGLRDAFPL-VLAVMGGAVVFAGQLLprlRF------PLEFDYLHVTRY-RGK 79
Cdd:PTZ00271   24 AHTLVTQEQVWAATAKCAKKIAedyrsFKLTTENPLyLLCVLKGSFIFTADLA---RFladegvPVKVEFICASSYgTGV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  80 TEGGEVEWRVLPGQNVVGRNVLVLDDILDEGETLAAIRDKLVDMGAAHVWSAVLTNKDNGLAKPIRADFVGLDVPNRYVF 159
Cdd:PTZ00271  101 ETSGQVRMLLDVRDSVENRHILIVEDIVDSAITLQYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVI 180

                         170       180
                  ....*....|....*....|
gi 1232339293 160 GCGMDAYGLWRNLPAIYALK 179
Cdd:PTZ00271  181 GYGMDYAESYRELRDICVLK 200
PyrR COG2065
Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide ...
 15-154 2.79e-07

Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 441668  Cd Length: 178  Bit Score: 48.13  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  15 CIASEDEVQAVLDRLAGEIALGLRDAFPLVLavMG---GAVVFAGQLLPRLR----FPLEFDYLHVTRYRGkteggevEW 87
Cdd:COG2065     5 EILDAADIDRALTRIAHEIIERNKGLEDLVL--VGiqtRGVPLAERLAERIEeiegVKVPVGSLDITLYRD-------DL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  88 RVLPGQNVV----------GRNVLVLDDILDEGETL-AAIrDKLVDMG-AAHVWSAVLTnkDNG---LakPIRADFVGLD 152
Cdd:COG2065    76 RRRPPRPVVneteipfdidGKTVVLVDDVLYTGRTVrAAL-DALMDFGrPAKIQLAVLV--DRGhreL--PIRADYVGKN 150


                  ..
gi 1232339293 153 VP 154
Cdd:COG2065   151 VP 152
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 42-132 1.11e-05

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: 44.58  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  42 PLVLAVMGGAVVFAGQLLPRLRfpLEFDYLHVTRYRGKTEggeVEWRVLPGqNVVGRNVLVLDDILDEGETLAAIRDKLV 121
Cdd:TIGR01251 161 PVVVSPDAGGVERAKKVADALG--CPLAIIDKRRISATNE---VEVMNLVG-DVEGKDVVIVDDIIDTGGTIAKAAEILK 234

                          90
                  ....*....|.
gi 1232339293 122 DMGAAHVWSAV 132
Cdd:TIGR01251 235 SAGAKRVIAAA 245
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 29-135 2.53e-05

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 43.36  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  29 LAGEIALGLRDafPLVLAVMGGAVVFAGQLLPRLRfpLEFDYLHVTRYRGKteggEVEWRVlPGQNVVGRNVLVLDDILD 108
Cdd:PRK00934  145 IAEYIGDKLDD--PLVLAPDKGALELAKEAAEILG--CEYDYLEKTRISPT----EVEIAP-KNLDVKGKDVLIVDDIIS 215

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232339293 109 EGETLA-AIRdKLVDMGAAHVWSA----VLTN 135
Cdd:PRK00934  216 TGGTMAtAIK-ILKEQGAKKVYVAcvhpVLVG 246
PRK05205 PRK05205
bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;
94-154 6.08e-03

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;


Pssm-ID: 235365  Cd Length: 176  Bit Score: 35.87  E-value: 6.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1232339293  94 NVVGRNVLVLDDILDEGETL-AAIrDKLVDMG-AAHVWSAVLTnkDNG---LakPIRADFVGLDVP 154
Cdd:PRK05205   92 DIEGKRVILVDDVLYTGRTIrAAL-DALFDYGrPARVQLAVLV--DRGhreL--PIRADYVGKNIP 152
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 48-132 7.40e-03

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 36.08  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232339293  48 MGGAVVFAGQL-LPRLRFPLEFDYLHVTRYRGKTeggeVEWRVLpGQNVVGRNVLVLDDILDEGETLAAIRDKLVDMGAA 126
Cdd:PRK06827  219 MDRAKYYASVLgVDLGLFYKRRDYSRVVNGRNPI----VAHEFL-GRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAK 293


                  ....*.
gi 1232339293 127 HVWSAV 132
Cdd:PRK06827  294 KIIVAA 299
 
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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