NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|47085697|ref|NP_998151|]
View 

hypoxanthine-guanine phosphoribosyltransferase [Danio rerio]

Protein Classification

type I phosphoribosyltransferase( domain architecture ID 27)

type I phosphoribosyltransferase similar to phosphoribosyltransferases with specificities for hypoxanthine, guanine, and/or xanthine

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRTases_typeI super family cl00309
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 6-218 4.40e-96

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.


The actual alignment was detected with superfamily member PTZ00149:

Pssm-ID: 444823  Cd Length: 241  Bit Score: 280.12  E-value: 4.40e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697    6 PCVVISDEeqGYDLDLFCIPKHYAADLERVYIPHGLIMDRTERLARDIMKDMGGHHIVALCVLKGGYKFFADLLDYIKAL 85
Cdd:PTZ00149  29 PIYIKDDD--FYDLDSFLIPPHYKNYLTKILLPNGLIKDRVEKLAYDIKQVYGNEELHILCILKGSRGFFSALVDYLNRI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697   86 NRNSDRSIPMTV---DFIRLKSYQNDQSTGDIKVIGgDDLSTLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVAS 162
Cdd:PTZ00149 107 HNYSSTESPKPPyqeHYVRVKSYCNDESTGKLEIVS-DDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIAT 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 47085697  163 LLVKRTPRSVGYRPDFVGFEVPDKFVVGYALDYNEYFRDLNHICVISETGKEKYKA 218
Cdd:PTZ00149 186 LFEKRTPLSNGFKGDFVGFSIPDHFVVGYCLDYNEHFRDLDHVAVLNDEGIKKYKK 241
 
Name Accession Description Interval E-value
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 6-218 4.40e-96

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 280.12  E-value: 4.40e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697    6 PCVVISDEeqGYDLDLFCIPKHYAADLERVYIPHGLIMDRTERLARDIMKDMGGHHIVALCVLKGGYKFFADLLDYIKAL 85
Cdd:PTZ00149  29 PIYIKDDD--FYDLDSFLIPPHYKNYLTKILLPNGLIKDRVEKLAYDIKQVYGNEELHILCILKGSRGFFSALVDYLNRI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697   86 NRNSDRSIPMTV---DFIRLKSYQNDQSTGDIKVIGgDDLSTLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVAS 162
Cdd:PTZ00149 107 HNYSSTESPKPPyqeHYVRVKSYCNDESTGKLEIVS-DDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIAT 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 47085697  163 LLVKRTPRSVGYRPDFVGFEVPDKFVVGYALDYNEYFRDLNHICVISETGKEKYKA 218
Cdd:PTZ00149 186 LFEKRTPLSNGFKGDFVGFSIPDHFVVGYCLDYNEHFRDLDHVAVLNDEGIKKYKK 241
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 35-209 1.17e-78

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: 232.90  E-value: 1.17e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697    35 VYIPHGLIMDRTERLARDIMKDMGGHHIVALCVLKGGYKFFADLLDYIKalnrnsdrsIPMTVDFIRLKSYQND-QSTGD 113
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIA---------VPVQVDFMAVSSYGNGmQSSGD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697   114 IKVIGGDDLSTLtGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEVPDKFVVGYAL 193
Cdd:TIGR01203  72 VKILKDLDLDIK-GKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGL 150

                         170
                  ....*....|....*.
gi 47085697   194 DYNEYFRDLNHICVIS 209
Cdd:TIGR01203 151 DYAERYRNLPYIGVLE 166
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 31-210 2.51e-62

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: 191.78  E-value: 2.51e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697  31 DLERVYIPHGLIMDRTERLARDIMKDMGGHHIVALCVLKGGYKFFADLldyIKALNrnsdrsIPMTVDFIRLKSYQN-DQ 109
Cdd:COG0634   4 DIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADL---LRALD------FPLEIDFMHVSSYGGgTE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697 110 STGDIKVIGGDDLStLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEVPDKFVV 189
Cdd:COG0634  75 SSGEVRILKDLDED-IEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVV 153

                       170       180
                ....*....|....*....|.
gi 47085697 190 GYALDYNEYFRDLNHICVISE 210
Cdd:COG0634 154 GYGLDYAEYYRNLPYIYALKP 174
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 39-196 2.24e-21

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: 86.26  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697    39 HGLIMDRTERLARDIMKDMGGHHIVALCVLKGGYKFFADLLDYIKalnrnsdrsIPMTvdFIRLKSYQNDQSTGdikVIG 118
Cdd:pfam00156   8 NPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLD---------VPLA--FVRKVSYNPDTSEV---MKT 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47085697   119 GDDLSTLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEvPDKFVVGYALDYN 196
Cdd:pfam00156  74 SSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDER 150
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 47-182 2.88e-20

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: 82.83  E-value: 2.88e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697  47 ERLARDImKDMGGHHIVALCVLKGGYKFFADLLDYIKAlnrnsdrsipmTVDFIRLKSYQNDQSTGDIKVIGGDDLSTLT 126
Cdd:cd06223   3 RLLAEEI-REDLLEPDVVVGILRGGLPLAAALARALGL-----------PLAFIRKERKGPGRTPSEPYGLELPLGGDVK 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697 127 GKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKRTPRSVGYR----PDFVGFE 182
Cdd:cd06223  71 GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELAspgdPVYSLFT 130
 
Name Accession Description Interval E-value
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 6-218 4.40e-96

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 280.12  E-value: 4.40e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697    6 PCVVISDEeqGYDLDLFCIPKHYAADLERVYIPHGLIMDRTERLARDIMKDMGGHHIVALCVLKGGYKFFADLLDYIKAL 85
Cdd:PTZ00149  29 PIYIKDDD--FYDLDSFLIPPHYKNYLTKILLPNGLIKDRVEKLAYDIKQVYGNEELHILCILKGSRGFFSALVDYLNRI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697   86 NRNSDRSIPMTV---DFIRLKSYQNDQSTGDIKVIGgDDLSTLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVAS 162
Cdd:PTZ00149 107 HNYSSTESPKPPyqeHYVRVKSYCNDESTGKLEIVS-DDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIAT 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 47085697  163 LLVKRTPRSVGYRPDFVGFEVPDKFVVGYALDYNEYFRDLNHICVISETGKEKYKA 218
Cdd:PTZ00149 186 LFEKRTPLSNGFKGDFVGFSIPDHFVVGYCLDYNEHFRDLDHVAVLNDEGIKKYKK 241
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 35-209 1.17e-78

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: 232.90  E-value: 1.17e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697    35 VYIPHGLIMDRTERLARDIMKDMGGHHIVALCVLKGGYKFFADLLDYIKalnrnsdrsIPMTVDFIRLKSYQND-QSTGD 113
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIA---------VPVQVDFMAVSSYGNGmQSSGD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697   114 IKVIGGDDLSTLtGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEVPDKFVVGYAL 193
Cdd:TIGR01203  72 VKILKDLDLDIK-GKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGL 150

                         170
                  ....*....|....*.
gi 47085697   194 DYNEYFRDLNHICVIS 209
Cdd:TIGR01203 151 DYAERYRNLPYIGVLE 166
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 31-210 2.51e-62

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: 191.78  E-value: 2.51e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697  31 DLERVYIPHGLIMDRTERLARDIMKDMGGHHIVALCVLKGGYKFFADLldyIKALNrnsdrsIPMTVDFIRLKSYQN-DQ 109
Cdd:COG0634   4 DIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADL---LRALD------FPLEIDFMHVSSYGGgTE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697 110 STGDIKVIGGDDLStLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEVPDKFVV 189
Cdd:COG0634  75 SSGEVRILKDLDED-IEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVV 153

                       170       180
                ....*....|....*....|.
gi 47085697 190 GYALDYNEYFRDLNHICVISE 210
Cdd:COG0634 154 GYGLDYAEYYRNLPYIYALKP 174
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 28-210 1.43e-44

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 147.11  E-value: 1.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697   28 YAADLERVYIPHGLIMDRTERLARDIMKDMGGHHIVALCVLKGGYKFFADLLDYIKALNRnsdrsiPMTVDFIRLKSY-Q 106
Cdd:PLN02238   3 YEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQPLPR------GLTVDFIRASSYgG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697  107 NDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKRTPRSVGYR-----PDFVGF 181
Cdd:PLN02238  77 GTESSGVAKVSGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYElvgdgKEYVGF 156

                        170       180
                 ....*....|....*....|....*....
gi 47085697  182 EVPDKFVVGYALDYNEYFRDLNHICVISE 210
Cdd:PLN02238 157 ECPDEFVVGYGLDFAEKYRNLPYVGVLKP 185
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 47-205 1.90e-27

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 102.63  E-value: 1.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697   47 ERLARDIMKDMGGHHIVALCVLKGGYKFFADLLDYIKAlnrnsdrsiPMTVDFIRLKSYQNDQSTGDI--KVIGGDDLSt 124
Cdd:PRK09162  27 DRMADEITADLADENPLVLCVMGGGLVFTGQLLPRLDF---------PLEFDYLHATRYRNETTGGELvwKVKPRESLK- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697  125 ltGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKRTPRSV-GYRPDFVGFEVPDKFVVGYALDYNEYFRDLN 203
Cdd:PRK09162  97 --GRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAkPLKADFVGLEVPDRYVFGYGMDYKGYWRNLP 174


                 ..
gi 47085697  204 HI 205
Cdd:PRK09162 175 GI 176
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 35-205 1.73e-25

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 97.78  E-value: 1.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697   35 VYIPHGLIMDRTERLARDIMKDM--GGHHIVALCVLKGGYKFFADLLDYIKalnrnsdrsIPMTVDFIRLKSYQNDQSTG 112
Cdd:PRK15423   7 VMIPEAEIKARIAELGRQITERYkdSGSDMVLVGLLRGSFMFMADLCREVQ---------VSHEVDFMTASSYGSGMSTT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697  113 -DIKVIGGDDlSTLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEVPDKFVVGY 191
Cdd:PRK15423  78 rDVKILKDLD-EDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGY 156

                        170
                 ....*....|....
gi 47085697  192 ALDYNEYFRDLNHI 205
Cdd:PRK15423 157 GIDYAQRYRHLPYI 170
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 65-215 2.00e-23

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 93.16  E-value: 2.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697   65 LCVLKGGYKFFADLLDYIkalnrnSDRSIPMTVDFIRLKSY-QNDQSTGDIKVIGgDDLSTLTGKNVLIVEDIIDTGKTM 143
Cdd:PTZ00271  62 LCVLKGSFIFTADLARFL------ADEGVPVKVEFICASSYgTGVETSGQVRMLL-DVRDSVENRHILIVEDIVDSAITL 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47085697  144 KTLLELLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEVPDKFVVGYALDYNEYFRDLNHICVISETGKEK 215
Cdd:PTZ00271 135 QYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGMDYAESYRELRDICVLKKEYYEK 206
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 33-185 2.64e-22

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: 88.75  E-value: 2.64e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697  33 ERVYIPHGLIMDRTERLARDIMKDmGGHHIVALCVLKGGYkFFADLLDYikALNrnsdrsIPMtVDFIRLKSYQNDQSTG 112
Cdd:COG2236   5 KKEYLSWDEIHELSRRLAEQILES-GFRPDVIVAIARGGL-VPARILAD--ALG------VPD-LASIRVSSYTGTAKRL 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47085697 113 DIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKrtPRSVgYRPDFVGFEVPD 185
Cdd:COG2236  74 EEPVVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYK--PSSK-FKPDYYAEETDA 143
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 39-196 2.24e-21

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: 86.26  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697    39 HGLIMDRTERLARDIMKDMGGHHIVALCVLKGGYKFFADLLDYIKalnrnsdrsIPMTvdFIRLKSYQNDQSTGdikVIG 118
Cdd:pfam00156   8 NPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLD---------VPLA--FVRKVSYNPDTSEV---MKT 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47085697   119 GDDLSTLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEvPDKFVVGYALDYN 196
Cdd:pfam00156  74 SSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDER 150
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 47-182 2.88e-20

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: 82.83  E-value: 2.88e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697  47 ERLARDImKDMGGHHIVALCVLKGGYKFFADLLDYIKAlnrnsdrsipmTVDFIRLKSYQNDQSTGDIKVIGGDDLSTLT 126
Cdd:cd06223   3 RLLAEEI-REDLLEPDVVVGILRGGLPLAAALARALGL-----------PLAFIRKERKGPGRTPSEPYGLELPLGGDVK 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085697 127 GKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKRTPRSVGYR----PDFVGFE 182
Cdd:cd06223  71 GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELAspgdPVYSLFT 130
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 116-164 2.75e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 43.04  E-value: 2.75e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 47085697  116 VIGGDDLSTLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLL 164
Cdd:PRK07322 109 VLDGADAEKLKGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAKAAIF 157
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 125-161 5.49e-05

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 42.98  E-value: 5.49e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 47085697  125 LTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVA 161
Cdd:PRK00934 202 VKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVA 238
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
 97-150 2.32e-04

xanthine-guanine phosphoribosyltransferase; Validated


Pssm-ID: 236395  Cd Length: 156  Bit Score: 40.23  E-value: 2.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 47085697   97 VDFIRLKSYQNDQStGDIKV---IGGDdlstltGKNVLIVEDIIDTGKTMKTLLELL 150
Cdd:PRK09177  58 VDTVCISSYDHDNQ-GELKVlkrAEGD------GEGFLVVDDLVDTGGTARAVREMY 107
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 123-167 5.34e-04

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 39.47  E-value: 5.34e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 47085697  123 STLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLLVKR 167
Cdd:PRK02277 136 ASVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDKS 180
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 127-163 5.37e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 39.98  E-value: 5.37e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 47085697  127 GKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASL 163
Cdd:PRK08558 176 GDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFL 212
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 127-161 6.83e-04

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: 39.57  E-value: 6.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 47085697   127 GKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVA 161
Cdd:TIGR01251 210 GKDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIAA 244
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 104-164 1.19e-03

Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440269  Cd Length: 171  Bit Score: 38.13  E-value: 1.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47085697 104 SYQNDQSTGDIKVIGGDDLSTltGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLL 164
Cdd:COG0503  91 EYDLEYGTGDTLELHKDALKP--GDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLI 149
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 125-164 1.65e-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: 38.21  E-value: 1.65e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 47085697 125 LTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLL 164
Cdd:COG0461 110 LPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIV 149
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 127-161 4.05e-03

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: 37.35  E-value: 4.05e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 47085697 127 GKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVA 161
Cdd:COG0462 211 GKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAA 245
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 122-164 4.18e-03

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 37.06  E-value: 4.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 47085697  122 LSTLTGKNVLIVEDIIDTGKTMKTLLELLKQYNPKMVKVASLL 164
Cdd:PRK00455 108 GRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIV 150
 
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