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Conserved domains on  [gi|96975138|ref|NP_038584.2|]
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hypoxanthine-guanine phosphoribosyltransferase

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List of domain hits

Name Accession Description Interval E-value
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
47-182 3.72e-17

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-pyrpphosphate (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  Cd Length: 130  Bit Score: 74.35  E-value: 3.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138  47 ERLARDVmKEMGGHHIVALCVLKGGYKFFADLLDYIKAlnrnsdrsipmTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLT 126
Cdd:cd06223   3 RLLAEEI-REDLLEPDVVVGILRGGLPLAAALARALGL-----------PLAFIRKERKGPGRTPSEPYGLELPLGGDVK 70
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138 127 GKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYR----PDFVGFE 182
Cdd:cd06223  71 GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELAspgdPVYSLFT 130
 
Name Accession Description Interval E-value
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
47-182 3.72e-17

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-pyrpphosphate (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  Cd Length: 130  Bit Score: 74.35  E-value: 3.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138  47 ERLARDVmKEMGGHHIVALCVLKGGYKFFADLLDYIKAlnrnsdrsipmTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLT 126
Cdd:cd06223   3 RLLAEEI-REDLLEPDVVVGILRGGLPLAAALARALGL-----------PLAFIRKERKGPGRTPSEPYGLELPLGGDVK 70
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138 127 GKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYR----PDFVGFE 182
Cdd:cd06223  71 GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELAspgdPVYSLFT 130
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
6-218 2.72e-92

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 273.18  E-value: 2.72e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138    6 PSVVISDDepGYDLDLFCIPNHYAEDLEKVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKAL 85
Cdd:PTZ00149  29 PIYIKDDD--FYDLDSFLIPPHYKNYLTKILLPNGLIKDRVEKLAYDIKQVYGNEELHILCILKGSRGFFSALVDYLNRI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138   86 NRNSDRSIPMTV---DFIRLKSYCNDQSTGDIKVIGgDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVAS 162
Cdd:PTZ00149 107 HNYSSTESPKPPyqeHYVRVKSYCNDESTGKLEIVS-DDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIAT 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 96975138  163 LLVKRTSRSVGYRPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA 218
Cdd:PTZ00149 186 LFEKRTPLSNGFKGDFVGFSIPDHFVVGYCLDYNEHFRDLDHVAVLNDEGIKKYKK 241
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
35-209 4.97e-75

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: 226.36  E-value: 4.97e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138    35 VFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKalnrnsdrsIPMTVDFIRLKSYCND-QSTGD 113
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIA---------VPVQVDFMAVSSYGNGmQSSGD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138   114 IKVIGGDDLSTLtGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYRPDFVGFEIPDKFVVGYAL 193
Cdd:TIGR01203  72 VKILKDLDLDIK-GKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGL 150
                         170
                  ....*....|....*.
gi 96975138   194 DYNEYFRDLNHVCVIS 209
Cdd:TIGR01203 151 DYAERYRNLPYIGVLE 166
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; linked ...
31-202 2.42e-43

Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; linked to 3D-structure


Pssm-ID: 223707  Cd Length: 178  Bit Score: 145.36  E-value: 2.42e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138  31 DLEKVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIkalnrnsdrSIPMTVDFIRLKSYCND-Q 109
Cdd:COG0634   6 HIKEVLISEEQIKARIKELAAQITEDYGGKDPLVVGVLKGSFPFMADLIRAI---------DFPLEVDFMHVSSYGGGtS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138 110 STGDIKVIGGDDLStLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYRPDFVGFEIPDKFVV 189
Cdd:COG0634  77 SSGEVKILKDLDED-IKGRDVLIVEDIIDSGLTLSKVRDLLKERGAKSVRIATLLDKPERRKVDIEADYVGFEVPDEFVV 155
                       170
                ....*....|...
gi 96975138 190 GYALDYNEYFRDL 202
Cdd:COG0634 156 GYGLDYAERYRNL 168
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
28-210 1.71e-42

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 143.64  E-value: 1.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138   28 YAEDLEKVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRnsdrsiPMTVDFIRLKSY-C 106
Cdd:PLN02238   3 YEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQPLPR------GLTVDFIRASSYgG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138  107 NDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYR-----PDFVGF 181
Cdd:PLN02238  77 GTESSGVAKVSGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYElvgdgKEYVGF 156
                        170       180
                 ....*....|....*....|....*....
gi 96975138  182 EIPDKFVVGYALDYNEYFRDLNHVCVISE 210
Cdd:PLN02238 157 ECPDEFVVGYGLDFAEKYRNLPYVGVLKP 185
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
34-205 1.83e-24

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 95.85  E-value: 1.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138   34 KVFIPHGLIMDRTERLARDVMKEM--GGHHIVALCVLKGGYKFFADLLDYIKalnrnsdrsIPMTVDFIRLKSYCNDQST 111
Cdd:PRK15423   6 EVMIPEAEIKARIAELGRQITERYkdSGSDMVLVGLLRGSFMFMADLCREVQ---------VSHEVDFMTASSYGSGMST 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138  112 G-DIKVIGGDDlSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYRPDFVGFEIPDKFVVG 190
Cdd:PRK15423  77 TrDVKILKDLD-EDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVG 155
                        170
                 ....*....|....*
gi 96975138  191 YALDYNEYFRDLNHV 205
Cdd:PRK15423 156 YGIDYAQRYRHLPYI 170
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
33-164 6.34e-14

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: 249637  Cd Length: 123  Bit Score: 65.09  E-value: 6.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138    33 EKVFIPHGLIMDRTERLARDVMKEMGGHHIVaLCVLKGGYKFFADLLDYIKalnrnsdrsIPMTVDFIRLKSYCNDQSTG 112
Cdd:pfam00156   1 SNLLLDPEELKELIEALAEKLREEGIDKDVI-VGIARGGIPLATALARELG---------IPLVLVRKRRSLPSSIKSRG 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 96975138   113 D-IKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLL 164
Cdd:pfam00156  71 GeSVTLLSRLPALLKGKRVLIVDDVLDTGGTLRAAVELLKKAGAKVVGVAVLV 123
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
125-161 1.06e-04

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 41.05  E-value: 1.06e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 96975138  125 LTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVA 161
Cdd:PRK00934 202 VKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVA 238
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism, Amino acid ...
114-172 2.02e-03

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism, Amino acid transport and metabolism]; linked to 3D-structure


Pssm-ID: 223538 [Multi-domain]  Cd Length: 314  Bit Score: 37.18  E-value: 2.02e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 96975138 114 IKVIGGDdlstLTGKNVLIVEDIIDTGKTmqtllslvkqyspkMVKVASLLVKRTSRSV 172
Cdd:COG0462 205 VMNLIGD----VEGKDVVIVDDIIDTGGT--------------IAKAAKALKERGAKKV 245
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
127-161 3.53e-03

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: 36.10  E-value: 3.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 96975138   127 GKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVA 161
Cdd:TIGR01251 210 GKDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIAA 244
 
Name Accession Description Interval E-value
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
47-182 3.72e-17

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-pyrpphosphate (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  Cd Length: 130  Bit Score: 74.35  E-value: 3.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138  47 ERLARDVmKEMGGHHIVALCVLKGGYKFFADLLDYIKAlnrnsdrsipmTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLT 126
Cdd:cd06223   3 RLLAEEI-REDLLEPDVVVGILRGGLPLAAALARALGL-----------PLAFIRKERKGPGRTPSEPYGLELPLGGDVK 70
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138 127 GKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYR----PDFVGFE 182
Cdd:cd06223  71 GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELAspgdPVYSLFT 130
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
6-218 2.72e-92

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 273.18  E-value: 2.72e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138    6 PSVVISDDepGYDLDLFCIPNHYAEDLEKVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKAL 85
Cdd:PTZ00149  29 PIYIKDDD--FYDLDSFLIPPHYKNYLTKILLPNGLIKDRVEKLAYDIKQVYGNEELHILCILKGSRGFFSALVDYLNRI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138   86 NRNSDRSIPMTV---DFIRLKSYCNDQSTGDIKVIGgDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVAS 162
Cdd:PTZ00149 107 HNYSSTESPKPPyqeHYVRVKSYCNDESTGKLEIVS-DDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIAT 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 96975138  163 LLVKRTSRSVGYRPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA 218
Cdd:PTZ00149 186 LFEKRTPLSNGFKGDFVGFSIPDHFVVGYCLDYNEHFRDLDHVAVLNDEGIKKYKK 241
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
35-209 4.97e-75

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: 226.36  E-value: 4.97e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138    35 VFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKalnrnsdrsIPMTVDFIRLKSYCND-QSTGD 113
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIA---------VPVQVDFMAVSSYGNGmQSSGD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138   114 IKVIGGDDLSTLtGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYRPDFVGFEIPDKFVVGYAL 193
Cdd:TIGR01203  72 VKILKDLDLDIK-GKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGL 150
                         170
                  ....*....|....*.
gi 96975138   194 DYNEYFRDLNHVCVIS 209
Cdd:TIGR01203 151 DYAERYRNLPYIGVLE 166
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; linked ...
31-202 2.42e-43

Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; linked to 3D-structure


Pssm-ID: 223707  Cd Length: 178  Bit Score: 145.36  E-value: 2.42e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138  31 DLEKVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIkalnrnsdrSIPMTVDFIRLKSYCND-Q 109
Cdd:COG0634   6 HIKEVLISEEQIKARIKELAAQITEDYGGKDPLVVGVLKGSFPFMADLIRAI---------DFPLEVDFMHVSSYGGGtS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138 110 STGDIKVIGGDDLStLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYRPDFVGFEIPDKFVV 189
Cdd:COG0634  77 SSGEVKILKDLDED-IKGRDVLIVEDIIDSGLTLSKVRDLLKERGAKSVRIATLLDKPERRKVDIEADYVGFEVPDEFVV 155
                       170
                ....*....|...
gi 96975138 190 GYALDYNEYFRDL 202
Cdd:COG0634 156 GYGLDYAERYRNL 168
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
28-210 1.71e-42

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 143.64  E-value: 1.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138   28 YAEDLEKVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRnsdrsiPMTVDFIRLKSY-C 106
Cdd:PLN02238   3 YEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQPLPR------GLTVDFIRASSYgG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138  107 NDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYR-----PDFVGF 181
Cdd:PLN02238  77 GTESSGVAKVSGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYElvgdgKEYVGF 156
                        170       180
                 ....*....|....*....|....*....
gi 96975138  182 EIPDKFVVGYALDYNEYFRDLNHVCVISE 210
Cdd:PLN02238 157 ECPDEFVVGYGLDFAEKYRNLPYVGVLKP 185
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
34-205 1.83e-24

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 95.85  E-value: 1.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138   34 KVFIPHGLIMDRTERLARDVMKEM--GGHHIVALCVLKGGYKFFADLLDYIKalnrnsdrsIPMTVDFIRLKSYCNDQST 111
Cdd:PRK15423   6 EVMIPEAEIKARIAELGRQITERYkdSGSDMVLVGLLRGSFMFMADLCREVQ---------VSHEVDFMTASSYGSGMST 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138  112 G-DIKVIGGDDlSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYRPDFVGFEIPDKFVVG 190
Cdd:PRK15423  77 TrDVKILKDLD-EDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVG 155
                        170
                 ....*....|....*
gi 96975138  191 YALDYNEYFRDLNHV 205
Cdd:PRK15423 156 YGIDYAQRYRHLPYI 170
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
65-210 3.03e-23

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 93.16  E-value: 3.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138   65 LCVLKGGYKFFADLLDYIkalnrnSDRSIPMTVDFIRLKSYCND-QSTGDIKVIGgDDLSTLTGKNVLIVEDIIDTGKTM 143
Cdd:PTZ00271  62 LCVLKGSFIFTADLARFL------ADEGVPVKVEFICASSYGTGvETSGQVRMLL-DVRDSVENRHILIVEDIVDSAITL 134
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 96975138  144 QTLLSLVKQYSPKMVKVASLLVKRTSRSVGYRPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISE 210
Cdd:PTZ00271 135 QYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGMDYAESYRELRDICVLKK 201
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
47-202 5.81e-23

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 91.85  E-value: 5.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138   47 ERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKAlnrnsdrsiPMTVDFIRLKSYCNDQSTGDI--KVIGGDDLSt 124
Cdd:PRK09162  27 DRMADEITADLADENPLVLCVMGGGLVFTGQLLPRLDF---------PLEFDYLHATRYRNETTGGELvwKVKPRESLK- 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 96975138  125 ltGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSV-GYRPDFVGFEIPDKFVVGYALDYNEYFRDL 202
Cdd:PRK09162  97 --GRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAkPLKADFVGLEVPDRYVFGYGMDYKGYWRNL 173
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
33-164 6.34e-14

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: 249637  Cd Length: 123  Bit Score: 65.09  E-value: 6.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138    33 EKVFIPHGLIMDRTERLARDVMKEMGGHHIVaLCVLKGGYKFFADLLDYIKalnrnsdrsIPMTVDFIRLKSYCNDQSTG 112
Cdd:pfam00156   1 SNLLLDPEELKELIEALAEKLREEGIDKDVI-VGIARGGIPLATALARELG---------IPLVLVRKRRSLPSSIKSRG 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 96975138   113 D-IKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLL 164
Cdd:pfam00156  71 GeSVTLLSRLPALLKGKRVLIVDDVLDTGGTLRAAVELLKKAGAKVVGVAVLV 123
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism];
31-203 3.43e-10

Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism];


Pssm-ID: 225145  Cd Length: 192  Bit Score: 55.83  E-value: 3.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138  31 DLEKVFIPHGLIMDRTERLARDVmKEMGGHHIVALCVLKGGYkFFADLL-DYIKAlnrnsdrsIPMTVdfIRLKSYCN-D 108
Cdd:COG2236   1 KFPKLYVSWEEIHRLCRALAEKI-RASGFKPDVIVAIARGGL-IPARILsDFLGV--------KPLYS--IKVEHYDEtA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138 109 QSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYRPDFVGFEI-PDKF 187
Cdd:COG2236  69 ERDGEAKVKYPITIDPLSGKKVLIVDDIVDTGETLELALEELKKLAPAEVRTAVLQYKKSPDYYGEEVTAWAWIIfPWNR 148
                       170
                ....*....|....*.
gi 96975138 188 VVGYALDYNEYFRDLN 203
Cdd:COG2236 149 KEDLADLILKILPEKG 164
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
116-164 2.40e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 42.27  E-value: 2.40e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 96975138  116 VIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLL 164
Cdd:PRK07322 109 VLDGADAEKLKGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAKAAIF 157
PyrR COG2065
Pyrimidine operon attenuation protein/uracil phosphoribosyltransferase [Nucleotide transport ...
125-184 3.70e-05

Pyrimidine operon attenuation protein/uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; linked to 3D-structure


Pssm-ID: 224976  Cd Length: 179  Bit Score: 41.50  E-value: 3.70e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 96975138 125 LTGKNVLIVEDIIDTGKTMQTLLSLVKQYS-PKMVKVAsLLVKRTSRSVGYRPDFVGFEIP 184
Cdd:COG2065  94 ITGKRVILVDDVLYTGRTIRAALDALVDYGrPAKIQLA-VLVDRGHRELPIRADYVGKNIP 153
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
97-156 5.66e-04

xanthine-guanine phosphoribosyltransferase; Validated


Pssm-ID: 236395  Cd Length: 156  Bit Score: 37.92  E-value: 5.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 96975138   97 VDFIRLKSYcNDQSTGDIKV---IGGDdlstltGKNVLIVEDIIDTGKTMQtllsLVKQYSPK 156
Cdd:PRK09177  58 VDTVCISSY-DHDNQGELKVlkrAEGD------GEGFLVVDDLVDTGGTAR----AVREMYPK 109
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
127-152 1.59e-03

Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; linked to 3D-structure


Pssm-ID: 223577  Cd Length: 179  Bit Score: 36.86  E-value: 1.59e-03
                        10        20
                ....*....|....*....|....*.
gi 96975138 127 GKNVLIVEDIIDTGKTMQTLLSLVKQ 152
Cdd:COG0503 116 GDRVLIVDDLLATGGTALALIELLEQ 141
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
118-202 1.71e-03

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 224837  Cd Length: 220  Bit Score: 36.90  E-value: 1.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138 118 GGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVAsllVKRTSRSV-----GYRPDFVGFEIPDKFV-VGy 191
Cdd:COG1926 115 GGRPVPSLKGRTVILVDDGIATGATMKAAVRALRAKGPKEIVIA---VPVAPEDAaaeleSEADEVVCLYMPAPFEaVG- 190
                        90
                ....*....|.
gi 96975138 192 aldynEYFRDL 202
Cdd:COG1926 191 -----EFYRDF 196
PRTase_3 pfam15610
PRTase ComF-like; This PRTase family is related to the ComF PRTases. These genes are found in ...
27-153 2.89e-03

PRTase ComF-like; This PRTase family is related to the ComF PRTases. These genes are found in the smaller biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo- nucleoside involved in stress response.


Pssm-ID: 259741  Cd Length: 275  Bit Score: 36.48  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96975138    27 HYAEDLEKVFIPHGLIMDRTERLArdVMKEMGGHHI-VALCVLKggYKFFADLLDYIKALNRNSdrsiPMTVDFIRLKSY 105
Cdd:pfam15610  37 QFGRELADGFIATFSNAILTDDQI--VVLPSPYRSIpTATNVLR--EHFVKYLNRHLAHNGANP----VLEAKIHRVITY 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 96975138   106 CNDQSTGD----IKVIGGD----DLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQY 153
Cdd:pfam15610 109 CQDYGNLSaedrESLIANDtyhiDKEFLEGKTLIFLDDIKITGSHEDKVRKSLKEY 164
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
123-172 3.67e-03

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023  Cd Length: 200  Bit Score: 36.00  E-value: 3.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 96975138  123 STLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSV 172
Cdd:PRK02277 136 ASVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDKSGIDEI 185
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
127-164 5.06e-03

adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the bi-directional best hit homologs from the spirochetes from the seed for this model and making only tentative predictions of adenine phosphoribosyltransferase function for this lineage. The trusted cutoff score is made high for this reason. Most proteins scoring between the trusted and noise cutoffs are likely to act as adenine phosphotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273437  Cd Length: 169  Bit Score: 35.33  E-value: 5.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 96975138   127 GKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLL 164
Cdd:TIGR01090 109 GQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLI 146
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
125-161 1.06e-04

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 41.05  E-value: 1.06e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 96975138  125 LTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVA 161
Cdd:PRK00934 202 VKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVA 238
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
127-152 5.39e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 38.43  E-value: 5.39e-04
                         10        20
                 ....*....|....*....|....*.
gi 96975138  127 GKNVLIVEDIIDTGKTMQTLLSLVKQ 152
Cdd:PRK08558 176 GDRVLIVDDIIRSGETQRALLDLARQ 201
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism, Amino acid ...
114-172 2.02e-03

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism, Amino acid transport and metabolism]; linked to 3D-structure


Pssm-ID: 223538 [Multi-domain]  Cd Length: 314  Bit Score: 37.18  E-value: 2.02e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 96975138 114 IKVIGGDdlstLTGKNVLIVEDIIDTGKTmqtllslvkqyspkMVKVASLLVKRTSRSV 172
Cdd:COG0462 205 VMNLIGD----VEGKDVVIVDDIIDTGGT--------------IAKAAKALKERGAKKV 245
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
127-161 3.53e-03

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: 36.10  E-value: 3.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 96975138   127 GKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVA 161
Cdd:TIGR01251 210 GKDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIAA 244
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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