NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|506339935|ref|WP_015859654|]
View 

ribose-phosphate diphosphokinase [Thermococcus gammatolerans]

Protein Classification

ribose-phosphate pyrophosphokinase( domain architecture ID 11479357)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 1-279 3.46e-151

ribose-phosphate pyrophosphokinase; Provisional


:

Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 423.56  E-value: 3.46e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935   1 MFVIGSGGKHLEDEL-RELGGEVIEIELRKFPDGEKYVRVLGFGR-EATVISSTFAPQDEKILELLLIGDALREKGFEKL 78
Cdd:PRK00934   1 MIIGGSASQLLASEVaRLLNTELALVETKRFPDGELYVRILGEIDgEDVVIISTTYPQDENLVELLLLIDALRDEGAKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  79 RAVVPYFAYSRQDRVTKEGEPISVRAVMRALGLYYDELYIFDLHNPETIKYFPGKGINVSPARIIADYFREKLGEGIVLA 158
Cdd:PRK00934  81 TLVIPYLGYARQDKRFKPGEPISARAIAKIISAYYDRIITINIHEPSILEFFPIPFINLDAAPLIAEYIGDKLDDPLVLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 159 PDRGALGRARAVAMELGLEYSHFEKRRISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGVT 238
Cdd:PRK00934 161 PDKGALELAKEAAEILGCEYDYLEKTRISPTEVEIAPKNLDVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACV 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 506339935 239 HGVFAEGAVERVSKA-VDELAVTNTIPTPVSKISIVPEILRL 279
Cdd:PRK00934 241 HPVLVGDAILKLYNAgVDEIIVTDTLESEVSKISVAPLIADL 282
 
Name Accession Description Interval E-value
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 1-279 3.46e-151

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 423.56  E-value: 3.46e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935   1 MFVIGSGGKHLEDEL-RELGGEVIEIELRKFPDGEKYVRVLGFGR-EATVISSTFAPQDEKILELLLIGDALREKGFEKL 78
Cdd:PRK00934   1 MIIGGSASQLLASEVaRLLNTELALVETKRFPDGELYVRILGEIDgEDVVIISTTYPQDENLVELLLLIDALRDEGAKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  79 RAVVPYFAYSRQDRVTKEGEPISVRAVMRALGLYYDELYIFDLHNPETIKYFPGKGINVSPARIIADYFREKLGEGIVLA 158
Cdd:PRK00934  81 TLVIPYLGYARQDKRFKPGEPISARAIAKIISAYYDRIITINIHEPSILEFFPIPFINLDAAPLIAEYIGDKLDDPLVLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 159 PDRGALGRARAVAMELGLEYSHFEKRRISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGVT 238
Cdd:PRK00934 161 PDKGALELAKEAAEILGCEYDYLEKTRISPTEVEIAPKNLDVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACV 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 506339935 239 HGVFAEGAVERVSKA-VDELAVTNTIPTPVSKISIVPEILRL 279
Cdd:PRK00934 241 HPVLVGDAILKLYNAgVDEIIVTDTLESEVSKISVAPLIADL 282
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 1-276 4.00e-103

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: 302.66  E-value: 4.00e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935    1 MFVIGSGGKHLEDELRE-LGGEVIEIELRKFPDGEKYVRVLGFGR---EATVISSTFAPQDEKILELLLIGDALREKGFE 76
Cdd:TIGR01251   2 KIFSGSSNQELAQKVAKnLGLPLGDVEVKRFPDGELYVRINESVRgkdVFIIQQSTSAPVNDNLMELLIMIDALKRASAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935   77 KLRAVVPYFAYSRQDRVTKEGEPISVRAVMRALGLY-YDELYIFDLHNPETIKYFPGKGINVSPARIIADYFREKLGE-G 154
Cdd:TIGR01251  82 SITAVIPYYGYARQDKKFKSREPISAKLVANLLETAgADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYLKKKILDnP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  155 IVLAPDRGALGRARAVAMELGLEYSHFEKRRISPT-EVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKI 233
Cdd:TIGR01251 162 VVVSPDAGGVERAKKVADALGCPLAIIDKRRISATnEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKRV 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 506339935  234 FVGVTHGVFAEGAVERVSKA-VDELAVTNTIPT-----PVSKISIVPEI 276
Cdd:TIGR01251 242 IAAATHGVFSGPAIERIANAgVEEVIVTNTIPHekhkpKVSVISVAPLI 290
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 5-274 7.95e-88

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: 263.84  E-value: 7.95e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935   5 GSGGKHLEDEL-RELGGEVIEIELRKFPDGEKYVRVLG--FGREATVISSTFAPQDEKILELLLIGDALREKGFEKLRAV 81
Cdd:COG0462    9 GNANPELAEEIaEYLGVPLGKAEVRRFSDGEIYVRIEEsvRGRDVFVIQSTSPPVNDNLMELLIMIDALKRASARRITAV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  82 VPYFAYSRQDRVTKEGEPISVRAV---MRALGLyyDELYIFDLHNPETIKYFPGKGINVSPARIIADYFREKLGEGIVL- 157
Cdd:COG0462   89 IPYYGYARQDRKFRPREPITAKLVadlLEAAGA--DRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKSKDLEDLVVv 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 158 APDRGALGRARAVAMELGLEYSHFEKRRISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGV 237
Cdd:COG0462  167 SPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVMNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAAA 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 506339935 238 THGVFAEGAVERVSKA-VDELAVTNTIPTP----VSKISIVP 274
Cdd:COG0462  247 THGVLSGPAVERLENSpIDELVVTDTIPLPeekrCDKIKVLS 288
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 140-262 1.19e-25

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: 98.24  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 140 ARIIADYFREKLGEG-IVLAPDRGALGRARAVAMELGLEYSHFEKRRISPTEVEIR------PVDIDVRGKNVLIVDDII 212
Cdd:cd06223    2 GRLLAEEIREDLLEPdVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEpyglelPLGGDVKGKRVLLVDDVI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 506339935 213 STGGTMVKAARILRKLGAEKIFVGVTHGVFaEGAVERVSKAVDELAVTNT 262
Cdd:cd06223   82 ATGGTLLAAIELLKEAGAKVVGVAVLLDKP-EGGARELASPGDPVYSLFT 130
Pribosyltran_N pfam13793
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ...
 5-105 4.93e-23

N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found N-terminal to the Pribosyltran, pfam00156.


Pssm-ID: 433483 [Multi-domain]  Cd Length: 117  Bit Score: 90.94  E-value: 4.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935    5 GSGGKHLEDEL-RELGGEVIEIELRKFPDGEKYVRVLG--FGREATVISSTFAPQDEKILELLLIGDALREKGFEKLRAV 81
Cdd:pfam13793   6 GNSNPELAEKIaKRLGIPLGKATVSRFSDGEIYVRIEEsvRGKDVFIIQSTCPPVNDNLMELLIMIDALKRASAKRITAV 85

                          90       100
                  ....*....|....*....|....
gi 506339935   82 VPYFAYSRQDRVTKEGEPISVRAV 105
Cdd:pfam13793  86 IPYFGYARQDRKDKPREPITAKLV 109
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
201-231 4.50e-04

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 40.29  E-value: 4.50e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 506339935 201 RGKNVLIVDDIISTGGTMVKAARILRKLGAE 231
Cdd:NF040646 113 KGDRVLIVDDVISTGGTLIAVIKALEKAGAE 143
 
Name Accession Description Interval E-value
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 1-279 3.46e-151

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 423.56  E-value: 3.46e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935   1 MFVIGSGGKHLEDEL-RELGGEVIEIELRKFPDGEKYVRVLGFGR-EATVISSTFAPQDEKILELLLIGDALREKGFEKL 78
Cdd:PRK00934   1 MIIGGSASQLLASEVaRLLNTELALVETKRFPDGELYVRILGEIDgEDVVIISTTYPQDENLVELLLLIDALRDEGAKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  79 RAVVPYFAYSRQDRVTKEGEPISVRAVMRALGLYYDELYIFDLHNPETIKYFPGKGINVSPARIIADYFREKLGEGIVLA 158
Cdd:PRK00934  81 TLVIPYLGYARQDKRFKPGEPISARAIAKIISAYYDRIITINIHEPSILEFFPIPFINLDAAPLIAEYIGDKLDDPLVLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 159 PDRGALGRARAVAMELGLEYSHFEKRRISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGVT 238
Cdd:PRK00934 161 PDKGALELAKEAAEILGCEYDYLEKTRISPTEVEIAPKNLDVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACV 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 506339935 239 HGVFAEGAVERVSKA-VDELAVTNTIPTPVSKISIVPEILRL 279
Cdd:PRK00934 241 HPVLVGDAILKLYNAgVDEIIVTDTLESEVSKISVAPLIADL 282
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 1-276 4.00e-103

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: 302.66  E-value: 4.00e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935    1 MFVIGSGGKHLEDELRE-LGGEVIEIELRKFPDGEKYVRVLGFGR---EATVISSTFAPQDEKILELLLIGDALREKGFE 76
Cdd:TIGR01251   2 KIFSGSSNQELAQKVAKnLGLPLGDVEVKRFPDGELYVRINESVRgkdVFIIQQSTSAPVNDNLMELLIMIDALKRASAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935   77 KLRAVVPYFAYSRQDRVTKEGEPISVRAVMRALGLY-YDELYIFDLHNPETIKYFPGKGINVSPARIIADYFREKLGE-G 154
Cdd:TIGR01251  82 SITAVIPYYGYARQDKKFKSREPISAKLVANLLETAgADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYLKKKILDnP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  155 IVLAPDRGALGRARAVAMELGLEYSHFEKRRISPT-EVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKI 233
Cdd:TIGR01251 162 VVVSPDAGGVERAKKVADALGCPLAIIDKRRISATnEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKRV 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 506339935  234 FVGVTHGVFAEGAVERVSKA-VDELAVTNTIPT-----PVSKISIVPEI 276
Cdd:TIGR01251 242 IAAATHGVFSGPAIERIANAgVEEVIVTNTIPHekhkpKVSVISVAPLI 290
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 5-274 7.95e-88

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: 263.84  E-value: 7.95e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935   5 GSGGKHLEDEL-RELGGEVIEIELRKFPDGEKYVRVLG--FGREATVISSTFAPQDEKILELLLIGDALREKGFEKLRAV 81
Cdd:COG0462    9 GNANPELAEEIaEYLGVPLGKAEVRRFSDGEIYVRIEEsvRGRDVFVIQSTSPPVNDNLMELLIMIDALKRASARRITAV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  82 VPYFAYSRQDRVTKEGEPISVRAV---MRALGLyyDELYIFDLHNPETIKYFPGKGINVSPARIIADYFREKLGEGIVL- 157
Cdd:COG0462   89 IPYYGYARQDRKFRPREPITAKLVadlLEAAGA--DRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKSKDLEDLVVv 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 158 APDRGALGRARAVAMELGLEYSHFEKRRISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGV 237
Cdd:COG0462  167 SPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVMNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAAA 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 506339935 238 THGVFAEGAVERVSKA-VDELAVTNTIPTP----VSKISIVP 274
Cdd:COG0462  247 THGVLSGPAVERLENSpIDELVVTDTIPLPeekrCDKIKVLS 288
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
16-274 1.54e-55

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 180.90  E-value: 1.54e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  16 RELGGEVIEIELRKFPDGEKYVRVLG--FGREaTVISSTFAPQDEKILELLLIGDALREKGFEKLRAVVPYFAYSRQDRV 93
Cdd:PRK07199  20 AALGVEVGRIELHRFPDGESYVRLDSpvAGRT-VVLVCSLDRPDEKLLPLLFAAEAARELGARRVGLVAPYLAYMRQDIA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  94 TKEGEPISVRAVMRALGLYYDELYIFD--LHNPETI-KYFPGKGINVSPARIIADYFREKLGEGIVLAPDRGALGRARAV 170
Cdd:PRK07199  99 FHPGEAISQRHFARLLSGSFDRLVTVDphLHRYPSLsEVYPIPAVVLSAAPAIAAWIRAHVPRPLLIGPDEESEQWVAAV 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 171 AMELGLEYSHFEKRRISPTEVEIR-PVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGVTHGVFAEGAVER 249
Cdd:PRK07199 179 AERAGAPHAVLRKTRHGDRDVEISlPDAAPWAGRTPVLVDDIVSTGRTLIEAARQLRAAGAASPDCVVVHALFAGDAYSA 258

                        250       260
                 ....*....|....*....|....*.
gi 506339935 250 VSKA-VDELAVTNTIPTPVSKISIVP 274
Cdd:PRK07199 259 LAAAgIARVVSTDTVPHPSNAISLAP 284
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
16-273 5.35e-52

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 172.22  E-value: 5.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  16 RELGGEVIEIELRKFPDGE---KY---VRvlgfGREATVISSTFAPQDEKILELLLIGDALREKGFEKLRAVVPYFAYSR 89
Cdd:PRK01259  18 KYLGIPLGKASVGRFSDGEisvEInenVR----GKDVFIIQSTCAPTNDNLMELLIMIDALKRASAGRITAVIPYFGYAR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  90 QDRVTKEGEPISVRAV---MRALGLyyDELYIFDLHNPETIKYF--PGKGINVSParIIADYFREK-LGEGIVLAPDRGA 163
Cdd:PRK01259  94 QDRKARSRVPITAKLVanlLETAGA--DRVLTMDLHADQIQGFFdiPVDNLYGSP--ILLEDIKQKnLENLVVVSPDVGG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 164 LGRARAVAMELGLEYSHFEKRRISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGVTHGVFA 243
Cdd:PRK01259 170 VVRARALAKRLDADLAIIDKRRPRANVSEVMNIIGDVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSVYAYATHPVLS 249

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 506339935 244 EGAVERVSKAV-DELAVTNTIPTP-----VSKISIV 273
Cdd:PRK01259 250 GGAIERIENSViDELVVTDSIPLSeeakkCDKIRVL 285
PLN02369 PLN02369
ribose-phosphate pyrophosphokinase
 18-266 5.89e-49

ribose-phosphate pyrophosphokinase


Pssm-ID: 215209 [Multi-domain]  Cd Length: 302  Bit Score: 164.10  E-value: 5.89e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  18 LGGEVIEIELRKFPDGEKYVRVLGF--GREATVISSTFAPQDEKILELLLIGDALREKGFEKLRAVVPYFAYSRQDRVTK 95
Cdd:PLN02369  11 LGLELGKITIKRFADGEIYVQLQESvrGCDVFLVQPTCPPANENLMELLIMIDACRRASAKRITAVIPYFGYARADRKTQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  96 EGEPISVRAVMRAL---GLyyDELYIFDLHNPETIKYFPGKGINVSPARIIADYFREKL---GEGIVLAPDRGALGRARA 169
Cdd:PLN02369  91 GRESIAAKLVANLIteaGA--DRVLACDLHSGQSMGYFDIPVDHVYGQPVILDYLASKTissPDLVVVSPDVGGVARARA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 170 VAMELG-LEYSHFEKRRISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGVTHGVFAEGAVE 248
Cdd:PLN02369 169 FAKKLSdAPLAIVDKRRQGHNVAEVMNLIGDVKGKVAIMVDDMIDTAGTITKGAALLHQEGAREVYACATHAVFSPPAIE 248

                        250
                 ....*....|....*....
gi 506339935 249 RVSKAV-DELAVTNTIPTP 266
Cdd:PLN02369 249 RLSSGLfQEVIVTNTIPVS 267
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
16-278 1.27e-44

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 152.79  E-value: 1.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  16 RELGGEVIEIELRKFPDGEKYVRvlgF-----GREATVISSTFAPQDEKILELLLIGDALREKGFEKLRAVVPYFAYSRQ 90
Cdd:PRK03092   7 KELGVEVTPTTAYDFANGEIYVR---FeesvrGCDAFVLQSHTAPINKWLMEQLIMIDALKRASAKRITVVLPFYPYARQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  91 DRVTKEGEPISVRAV---MRALGLyyDELYIFDLHNPETIKYFPGKGINVSPARIIADYFREKLGEG--IVLAPDRGALG 165
Cdd:PRK03092  84 DKKHRGREPISARLVadlFKTAGA--DRIMTVDLHTAQIQGFFDGPVDHLFAMPLLADYVRDKYDLDnvTVVSPDAGRVR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 166 RARAVAMELG---LEYSHfeKRR--ISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGVTHG 240
Cdd:PRK03092 162 VAEQWADRLGgapLAFIH--KTRdpTVPNQVVANRVVGDVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVIIAATHG 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 506339935 241 VFAEGAVERVSKA-VDELAVTNTIPTPVSK-------ISIVPEILR 278
Cdd:PRK03092 240 VLSGPAAERLKNCgAREVVVTDTLPIPEEKrfdkltvLSIAPLLAR 285
PRK02812 PRK02812
ribose-phosphate pyrophosphokinase; Provisional
 5-269 3.15e-44

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235072 [Multi-domain]  Cd Length: 330  Bit Score: 152.59  E-value: 3.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935   5 GSGGKHLEDEL-RELGGEVIEIELRKFPDGEKYVRVLGFGREATV--ISSTFAPQDEKILELLLIGDALREKGFEKLRAV 81
Cdd:PRK02812  27 GSSNPALAQEVaRYLGMDLGPMIRKRFADGELYVQIQESIRGCDVylIQPTCAPVNDHLMELLIMVDACRRASARQITAV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  82 VPYFAYSRQDRVTKEGEPISVRAVMRAL---GLyyDELYIFDLHNPETIKYF--PGKGINVSParIIADYFREK-LGEGI 155
Cdd:PRK02812 107 IPYYGYARADRKTAGRESITAKLVANLItkaGA--DRVLAMDLHSAQIQGYFdiPCDHVYGSP--VLLDYLASKnLEDIV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 156 VLAPDRGALGRARAVAMEL-GLEYSHFEKRRISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIF 234
Cdd:PRK02812 183 VVSPDVGGVARARAFAKKLnDAPLAIIDKRRQAHNVAEVLNVIGDVKGKTAILVDDMIDTGGTICEGARLLRKEGAKQVY 262

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 506339935 235 VGVTHGVFAEGAVERVSKAV-DELAVTNTIPTPVSK 269
Cdd:PRK02812 263 ACATHAVFSPPAIERLSSGLfEEVIVTNTIPVPEER 298
PRK00553 PRK00553
ribose-phosphate pyrophosphokinase; Provisional
 24-264 1.11e-40

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 179062 [Multi-domain]  Cd Length: 332  Bit Score: 143.52  E-value: 1.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  24 EIELRKFPDGEKYVRVLGFGREATV--ISSTFAPQDEKILELLLIGDALREKGFEKLRAVVPYFAYSRQDRVTKEGEPIS 101
Cdd:PRK00553  35 EIVIQKFADGETYIRFDESVRNKDVviFQSTCSPVNDSLMELLIAIDALKRGSAKSITAILPYYGYARQDRKTAGREPIT 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 102 VRAVMRAL---GLyyDELYIFDLHNPETIKYF-----PGKGINVSPARIIADYFREKLgegIVLAPDRGALGRARAVAME 173
Cdd:PRK00553 115 SKLVADLLtkaGV--TRVTLTDIHSDQTQGFFdipvdILRTYHVFLSRVLELLGKKDL---VVVSPDYGGVKRARLIAES 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 174 LGLEYSHFEKRRISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGVTHGVFAEGAVERVSKA 253
Cdd:PRK00553 190 LELPLAIIDKRRPKHNVAESINVLGEVKNKNCLIVDDMIDTGGTVIAAAKLLKKQKAKKVCVMATHGLFNKNAIQLFDEA 269

                        250
                 ....*....|....*.
gi 506339935 254 -----VDELAVTNTIP 264
Cdd:PRK00553 270 fkkklIDKLFVSNSIP 285
PRK04923 PRK04923
ribose-phosphate diphosphokinase;
1-264 3.72e-40

ribose-phosphate diphosphokinase;


Pssm-ID: 179893 [Multi-domain]  Cd Length: 319  Bit Score: 141.60  E-value: 3.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935   1 MFVIGSGGKHLEDEL-RELGGEVIEIELRKFPDGEKYVRVLGF--GREATVISSTFAPQDEKILELLLIGDALREKGFEK 77
Cdd:PRK04923   8 LVFSGNANKPLAQSIcKELGVRMGKALVTRFSDGEVQVEIEESvrRQEVFVIQPTCAPSAENLMELLVLIDALKRASAAS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  78 LRAVVPYFAYSRQDRVTKEGE-PISVRAVMRAL-GLYYDELYIFDLHNPETIKYF--PGKGINVSPArIIADYFRE-KLG 152
Cdd:PRK04923  88 VTAVIPYFGYSRQDRRMRSSRvPITAKVAAKMIsAMGADRVLTVDLHADQIQGFFdvPVDNVYASPL-LLADIWRAyGTD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 153 EGIVLAPDRGALGRARAVAMELG-LEYSHFEKRRISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAE 231
Cdd:PRK04923 167 NLIVVSPDVGGVVRARAVAKRLDdADLAIIDKRRPRANVATVMNIIGDVQGKTCVLVDDLVDTAGTLCAAAAALKQRGAL 246

                        250       260       270
                 ....*....|....*....|....*....|....
gi 506339935 232 KIFVGVTHGVFAEGAVERVSKAV-DELAVTNTIP 264
Cdd:PRK04923 247 KVVAYITHPVLSGPAVDNINNSQlDELVVTDTIP 280
PRK02269 PRK02269
ribose-phosphate diphosphokinase;
1-276 6.82e-39

ribose-phosphate diphosphokinase;


Pssm-ID: 167353 [Multi-domain]  Cd Length: 320  Bit Score: 138.39  E-value: 6.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935   1 MFVIGSGGKHLEDELRELGGEVIEIELRKFPDGEKYVRVLGF--GREATVISSTFAPQDEKILELLLIGDALREKGFEKL 78
Cdd:PRK02269   8 LFALSSNKELAEKVAQEIGIELGKSSVRQFSDGEIQVNIEESirGHHVFILQSTSSPVNDNLMEILIMVDALKRASAESI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  79 RAVVPYFAYSRQDRVTKEGEPISVRAVMRALGLY-YDELYIFDLHNPETIKYFPGKGINVSPARIIADYFREKLGEG--- 154
Cdd:PRK02269  88 NVVMPYYGYARQDRKARSREPITSKLVANMLEVAgVDRLLTVDLHAAQIQGFFDIPVDHLMGAPLIADYFDRRGLVGddv 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 155 IVLAPDRGALGRARAVAMELGLEYSHFEKRRISPTE--VEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEK 232
Cdd:PRK02269 168 VVVSPDHGGVTRARKLAQFLKTPIAIIDKRRSVDKMntSEVMNIIGNVKGKKCILIDDMIDTAGTICHAADALAEAGATE 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 506339935 233 IFVGVTHGVFAEGAVERVSK-AVDELAVTNTIPTPVSK-------ISIVPEI 276
Cdd:PRK02269 248 VYASCTHPVLSGPALDNIQKsAIEKLVVLDTIYLPEERlidkieqISIADLL 299
PTZ00145 PTZ00145
phosphoribosylpyrophosphate synthetase; Provisional
 18-263 8.69e-37

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 240290 [Multi-domain]  Cd Length: 439  Bit Score: 135.38  E-value: 8.69e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  18 LGGEVIEIELRKFPDGEKYVRVLGF--GREATVISSTFAPQDEKILELLLIGDALREKGFEKLRAVVPYFAYSRQDRVTK 95
Cdd:PTZ00145 139 LGTILGRVHLKRFADGEVSMQFLESirGKDVYIIQPTCPPVNENLIELLLMISTCRRASAKKITAVIPYYGYARQDRKLS 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  96 EGEPISVRAVMR---ALGLyyDELYIFDLHNPETIKYF-PGKGINVSPARIIA-DYFREK-LGEGIVLAPDRGALGRARA 169
Cdd:PTZ00145 219 SRVPISAADVARmieAMGV--DRVVAIDLHSGQIQGFFgPRVPVDNLEAQLIGlDYFTKKdLYKPVIVSPDAGGVYRARK 296

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 170 vaMELGLEYSHFE--------KRRISPTEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGVTHGV 241
Cdd:PTZ00145 297 --FQDGLNHRGISdcgiamliKQRTKPNEIEKMDLVGNVYDSDVIIVDDMIDTSGTLCEAAKQLKKHGARRVFAFATHGL 374

                        250       260
                 ....*....|....*....|...
gi 506339935 242 FAEGAVERVSKA-VDELAVTNTI 263
Cdd:PTZ00145 375 FSGPAIERIEASpLEEVVVTDTV 397
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 28-265 6.92e-30

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 114.45  E-value: 6.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  28 RKFPDGE------KYVRvlgfGREATVISSTFAPQDEKILELLLIGDALREKGFEKLRAVVPYFAYSRQDRVTKEGEPIS 101
Cdd:PRK02458  39 RQFSDGEiminieESVR----GDDIYIIQSTSFPVNDHLWELLIMIDACKRASANTVNVVLPYFGYARQDRIAKPREPIT 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 102 VRAVMRAL-GLYYDELYIFDLHNPETIKYFPGKGINVSPARIIADYFREK--LGEGIVL-APDRGALGRARAVAMELG-- 175
Cdd:PRK02458 115 AKLVANMLvKAGVDRVLTLDLHAVQVQGFFDIPVDNLFTVPLFAKHYCKKglSGSDVVVvSPKNSGIKRARSLAEYLDap 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 176 ---LEYSHFEKRRisptevEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGVTHGVFAEGAVERVSK 252
Cdd:PRK02458 195 iaiIDYAQDDSER------EEGYIIGDVAGKKAILIDDILNTGKTFAEAAKIVEREGATEIYAVASHGLFAGGAAEVLEN 268

                        250
                 ....*....|....
gi 506339935 253 A-VDELAVTNTIPT 265
Cdd:PRK02458 269 ApIKEILVTDSVAT 282
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 81-256 6.77e-26

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 105.03  E-value: 6.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  81 VVPYFAYSRQDRVTKEgEPISVRAVMRAL-GLYYDELYIFDLHNPETIKYFPGKGI-NVSPARIIADYFREKLGE----- 153
Cdd:PRK06827 128 IMPFLYESRQHKRKGR-ESLDCALALQELeELGVDNIITFDAHDPRIENAIPLMGFeNLYPSYQIIKALLKNEKDleidk 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 154 --GIVLAPDRGALGRARAVAMELGLEYSHFEKRR--------ISPTeVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAAR 223
Cdd:PRK06827 207 dhLMVISPDTGAMDRAKYYASVLGVDLGLFYKRRdysrvvngRNPI-VAHEFLGRDVEGKDVLIVDDMIASGGSMIDAAK 285

                        170       180       190
                 ....*....|....*....|....*....|...
gi 506339935 224 ILRKLGAEKIFVGVTHGVFAEGaVERVSKAVDE 256
Cdd:PRK06827 286 ELKSRGAKKIIVAATFGFFTNG-LEKFDKAYEE 317
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 140-262 1.19e-25

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: 98.24  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 140 ARIIADYFREKLGEG-IVLAPDRGALGRARAVAMELGLEYSHFEKRRISPTEVEIR------PVDIDVRGKNVLIVDDII 212
Cdd:cd06223    2 GRLLAEEIREDLLEPdVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEpyglelPLGGDVKGKRVLLVDDVI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 506339935 213 STGGTMVKAARILRKLGAEKIFVGVTHGVFaEGAVERVSKAVDELAVTNT 262
Cdd:cd06223   82 ATGGTLLAAIELLKEAGAKVVGVAVLLDKP-EGGARELASPGDPVYSLFT 130
Pribosyltran_N pfam13793
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ...
 5-105 4.93e-23

N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found N-terminal to the Pribosyltran, pfam00156.


Pssm-ID: 433483 [Multi-domain]  Cd Length: 117  Bit Score: 90.94  E-value: 4.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935    5 GSGGKHLEDEL-RELGGEVIEIELRKFPDGEKYVRVLG--FGREATVISSTFAPQDEKILELLLIGDALREKGFEKLRAV 81
Cdd:pfam13793   6 GNSNPELAEKIaKRLGIPLGKATVSRFSDGEIYVRIEEsvRGKDVFIIQSTCPPVNDNLMELLIMIDALKRASAKRITAV 85

                          90       100
                  ....*....|....*....|....
gi 506339935   82 VPYFAYSRQDRVTKEGEPISVRAV 105
Cdd:pfam13793  86 IPYFGYARQDRKDKPREPITAKLV 109
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 12-279 1.63e-16

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 77.81  E-value: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  12 EDELRELGgeviEIELRKFPDGEKYVRVLGF----GREATVISSTFAPqdEKILELLLIGDALREKGFEKLRAVVPYFAY 87
Cdd:PLN02297  35 ESDAIELG----SINWRKFPDGFPNLFINNAhgirGQHVAFLASFSSP--AVIFEQLSVIYALPKLFVASFTLVLPFFPT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  88 SRQDRVTKEGE--------------PISVRAVMRalglyydeLYIFDLHNPETIKYFpgkGINVSP----------ARII 143
Cdd:PLN02297 109 GTSERVEREGDvataftlarilsniPISRGGPTS--------LVIFDIHALQERFYF---GDNVLPcfesgipllkKRLQ 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 144 ADYFREKlgegIVLA-PDRGALGRaravameLGLEYSHFE-----KRRisptEVEIRPVDI---DVRGKNVLIVDDIIST 214
Cdd:PLN02297 178 QLPDSDN----IVIAfPDDGAWKR-------FHKQFEHFPmvvctKVR----EGDKRIVRIkegNPAGRHVVIVDDLVQS 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506339935 215 GGTMVKAARILRKLGAEKIFVGVTHGVFAEGAVERV-------SKAVDELAVTNTIPTPVSKISIVP--EILRL 279
Cdd:PLN02297 243 GGTLIECQKVLAAHGAAKVSAYVTHGVFPNESWERFthdnggpEAGFAYFWITDSCPQTVKAVRGKApfEVLSL 316
Pribosyl_synth pfam14572
Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes ...
 155-270 1.11e-14

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


Pssm-ID: 434046  Cd Length: 184  Bit Score: 70.62  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  155 IVLAPDRGALGRARAVA--MELGLEYSHFEKR---------RISPTEVEIRPVDI-------------------DVRGKN 204
Cdd:pfam14572   6 VIVARSPGSAKRATSFAerLRLGIAVIHGEQKeaesdevdgRQSPPPYRSRTVSRslglpeiipkekppmtvvgDVGGRI 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506339935  205 VLIVDDIISTGGTMVKAARILRKLGAEKIFVGVTHGVFAEGAVERV-SKAVDELAVTNTIPTPVSKI 270
Cdd:pfam14572  86 AIIVDDMIDDVDSFVAAAELLKERGAYKIYVMATHGLLSSDAPRLLeASPIDEVVVTNTIPHEIQKM 152
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 140-233 4.28e-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: 65.46  E-value: 4.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  140 ARIIADYFREKLGEGIVL-APDRGALGRARAVAMELGLEYSHFEKRRISP---TEVEIRPVDIDVRGKNVLIVDDIISTG 215
Cdd:pfam00156  16 ARLAAQINEDYGGKPDVVvGILRGGLPFAGILARRLDVPLAFVRKVSYNPdtsEVMKTSSALPDLKGKTVLIVDDILDTG 95

                          90
                  ....*....|....*...
gi 506339935  216 GTMVKAARILRKLGAEKI 233
Cdd:pfam00156  96 GTLLKVLELLKNVGPKEV 113
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 155-237 1.15e-10

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: 58.70  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 155 IVLAPDRGALGRARAVAMELGLE---------YSHFEKRRispTEVEIR-PVDIDVRGKNVLIVDDIISTGGTMVKAARI 224
Cdd:COG2236   34 VIVAIARGGLVPARILADALGVPdlasirvssYTGTAKRL---EEPVVKgPLDEDLAGKRVLIVDDVADTGRTLEAVRDL 110

                         90
                 ....*....|...
gi 506339935 225 LRKLGAEKIFVGV 237
Cdd:COG2236  111 LKEAGPAEVRTAV 123
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 167-235 3.98e-09

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 55.21  E-value: 3.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 167 ARAVAMELGLEYSHFEKRRISPTE-----------------VEIRPvDIDVRGKNVLIVDDIISTGGTMVKAARILRKLG 229
Cdd:COG1040  104 ARALARALGIPVLPDLLRRVRATPsqaglsraerrrnlrgaFAVRP-PARLAGKHVLLVDDVLTTGATLAEAARALKAAG 182


                 ....*.
gi 506339935 230 AEKIFV 235
Cdd:COG1040  183 AARVDV 188
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 140-253 9.08e-09

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 54.00  E-value: 9.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 140 ARIIADYFREKLGE-GIVLAPDRGALGRARAVAMELGLEY--------SHFEKRRIspteveIRPVdidVRGKNVLIVDD 210
Cdd:COG0461   50 GEALAELIKELGPEfDAVAGPATGGIPLAAAVARALGLPAifvrkeakDHGTGGQI------EGGL---LPGERVLVVED 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 506339935 211 IISTGGTMVKAARILRKLGAE--KIFVGVTHGvfaEGAVERVSKA 253
Cdd:COG0461  121 VITTGGSVLEAVEALREAGAEvvGVAVIVDRE---EGAAENLEEA 162
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 167-233 3.11e-08

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: 52.34  E-value: 3.11e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506339935 167 ARAVAMELGLEY---SHFEKRRISPTEVEIR-PVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKI 233
Cdd:COG0634   52 LRALDFPLEIDFmhvSSYGGGTESSGEVRILkDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASV 122
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 150-231 3.77e-08

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 52.00  E-value: 3.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 150 KLGEGIVLAPDRGALGRArAVAMELGLEYSHfekrrispTEVEIRPVDIdVRGKNVLIVDDIISTGGTMVKAARILRKLG 229
Cdd:PRK02304  72 KLGIGFVPVRKPGKLPRE-TISESYELEYGT--------DTLEIHKDAI-KPGDRVLIVDDLLATGGTLEAAIKLLERLG 141


                 ..
gi 506339935 230 AE 231
Cdd:PRK02304 142 AE 143
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 150-231 5.34e-08

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: 51.23  E-value: 5.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 150 KLGEGIVLAPDRGALGRArAVAMELGLEYShfekrriSPTEVEIRPVDIDvRGKNVLIVDDIISTGGTMVKAARILRKLG 229
Cdd:COG0503   69 ALGVPFVPARKPGKLPGE-TVSEEYDLEYG-------TGDTLELHKDALK-PGDRVLIVDDLLATGGTAKAAIKLVEEAG 139


                 ..
gi 506339935 230 AE 231
Cdd:COG0503  140 AE 141
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 140-231 5.77e-08

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 51.70  E-value: 5.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 140 ARIIADYFREKLGE-GIVLAPDRGALGRARAVAMELGLEY--------SHFEKRRIsptevEIRPVDidvrGKNVLIVDD 210
Cdd:PRK00455  51 GRFLAEAIKDSGIEfDVVAGPATGGIPLAAAVARALDLPAifvrkeakDHGEGGQI-----EGRRLF----GKRVLVVED 121

                         90       100
                 ....*....|....*....|.
gi 506339935 211 IISTGGTMVKAARILRKLGAE 231
Cdd:PRK00455 122 VITTGGSVLEAVEAIRAAGAE 142
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 150-231 1.68e-07

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: 49.97  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935  150 KLGEGIVLAPDRGALGRaRAVAMELGLEYSHfekrrispTEVEIRpVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLG 229
Cdd:TIGR01090  67 KLGVGFVPVRKPGKLPG-ETISASYDLEYGK--------DVLEIH-KDAIKPGQRVLIVDDLLATGGTAAATDELIKKLG 136


                  ..
gi 506339935  230 AE 231
Cdd:TIGR01090 137 GE 138
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 200-249 2.69e-06

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 46.51  E-value: 2.69e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 506339935 200 VRGKNVLIVDDIISTGGTMVKAARILRKLGAEkifVGVTHGVFAEG-AVER 249
Cdd:PRK07322 118 LKGKRVAIVDDVVSTGGTLTALERLVERAGGQ---VVAKAAIFAEGdASNR 165
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
 134-233 1.61e-05

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 45.80  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 134 GINVSPARIIA--DYFRE-KLGEGIVLA-PDRG---ALGRARA--VAMELGLEYSHFEKRR-ISPTE--------VEIRP 195
Cdd:PRK05793 267 GISVYESRVRAgrQLYKEyPVDADIVIGvPDSGipaAIGYAEAsgIPYGIGFIKNKYVGRTfIAPSQelreravrVKLNP 346

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 506339935 196 VDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKI 233
Cdd:PRK05793 347 LKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEV 384
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 199-237 2.62e-05

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 44.09  E-value: 2.62e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 506339935 199 DVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGV 237
Cdd:PRK02277 137 SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVV 175
PLN02440 PLN02440
amidophosphoribosyltransferase
 147-234 3.30e-05

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 44.67  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 147 FREKLGE----------GIVLA-PDRG---ALGRARA--VAMELGLEYSHFEKRR-ISPTEvEIR---------PVDIDV 200
Cdd:PLN02440 260 SRLEFGEilateipvdcDVVIPvPDSGrvaALGYAAKlgVPFQQGLIRSHYVGRTfIEPSQ-KIRdfsvklklnPVRSVL 338

                         90       100       110
                 ....*....|....*....|....*....|....
gi 506339935 201 RGKNVLIVDDIISTGGTMVKAARILRKLGAEKIF 234
Cdd:PLN02440 339 EGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVH 372
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
 200-237 6.34e-05

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 43.20  E-value: 6.34e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 506339935 200 VRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFVGV 237
Cdd:PRK06031 152 LEGRRVALIDDVISSGASIVAGLRLLAACGIEPAGIGA 189
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
 159-238 9.38e-05

Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439804 [Multi-domain]  Cd Length: 464  Bit Score: 43.47  E-value: 9.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 159 PDRG---ALGraraVAMELGLEYSH-FEKRR------ISPT----EVEIR----PVDIDVRGKNVLIVDDIISTGGTMVK 220
Cdd:COG0034  288 PDSGrpaAIG----YAEESGIPYEEgLIKNRyvgrtfIQPTqelrELGVRlklnPIREVVKGKRVVLVDDSIVRGTTSRR 363

                         90
                 ....*....|....*...
gi 506339935 221 AARILRKLGAEKIFVGVT 238
Cdd:COG0034  364 IVKMLREAGAKEVHFRIA 381
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 200-235 1.43e-04

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 42.06  E-value: 1.43e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 506339935 200 VRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFV 235
Cdd:PTZ00149 148 LKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRI 183
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 189-235 2.39e-04

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 41.18  E-value: 2.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 506339935 189 TEVEIRPVDIDVRGKNVLIVDDIISTGGTMVKAARILRKLGAEKIFV 235
Cdd:PLN02238  84 AKVSGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSV 130
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 195-253 2.83e-04

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 41.23  E-value: 2.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 506339935 195 PVDIDvrGKNVLIVDDIISTGGTMVKAARILRKLGAEKI-FVGVthgVFAEGAVERVSKA 253
Cdd:PRK00129 119 PEDID--ERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIkVLCL---VAAPEGIKALEEA 173
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
201-231 4.50e-04

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 40.29  E-value: 4.50e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 506339935 201 RGKNVLIVDDIISTGGTMVKAARILRKLGAE 231
Cdd:NF040646 113 KGDRVLIVDDVISTGGTLIAVIKALEKAGAE 143
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 195-253 5.41e-04

Uracil phosphoribosyltransferase; This family includes the enzyme uracil phosphoribosyltransferase (EC:2.4.2.9). This enzyme catalyzes the first step of UMP biosynthesis.


Pssm-ID: 434124  Cd Length: 204  Bit Score: 40.17  E-value: 5.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506339935  195 PVDIDVRgkNVLIVDDIISTGGTMVKAARILRKLGA--EKI-FVGVthgVFAEGAVERVSKA 253
Cdd:pfam14681 113 PKDISDR--TVILLDPMLATGGSAIAAIQVLREHGVpeENIvVLSV---IAAPEGLHRLAAA 169
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 197-230 8.41e-04

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 39.64  E-value: 8.41e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 506339935 197 DIDVRGKNVLIVDDIISTGGTMVKAARILRKLGA 230
Cdd:PRK11595 182 ELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGA 215
PLN02293 PLN02293
adenine phosphoribosyltransferase
 202-231 1.42e-03

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 38.89  E-value: 1.42e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 506339935 202 GKNVLIVDDIISTGGTMVKAARILRKLGAE 231
Cdd:PLN02293 125 GERALVIDDLIATGGTLCAAINLLERAGAE 154
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 202-253 2.65e-03

orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 129436 [Multi-domain]  Cd Length: 173  Bit Score: 37.79  E-value: 2.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 506339935  202 GKNVLIVDDIISTGGTMVKAARILRKLGAE--KIFVGVTHGvfAEGAVERVSKA 253
Cdd:TIGR00336 108 GDKVVVVEDVITTGTSILEAVEIIQAAGGQvaGVIIAVDRQ--ERSAGQEFEKE 159
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 201-231 4.61e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 37.07  E-value: 4.61e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 506339935 201 RGKNVLIVDDIISTGGTMVKAARILRKLGAE 231
Cdd:PRK12560 113 KGDRVAIIDDTLSTGGTVIALIKAIENSGGI 143
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 193-225 9.54e-03

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 36.15  E-value: 9.54e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 506339935 193 IRPVDIDVRGKNVLIVDDIISTGGTMVKAARIL 225
Cdd:PRK15423  83 LKDLDEDIRGKDVLIVEDIIDSGNTLSKVREIL 115
 
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