|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
3-280 |
3.43e-99 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 291.82 E-value: 3.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 3 IISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFP-DEKIVELLLLLEAIHEAGAASVT 81
Cdd:PRK00934 2 IIGGSASQLLASEVARLLNTELALVETKRFPDGELYVRILGEIDGEDVVIISTTYPqDENLVELLLLIDALRDEGAKSIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 82 TVIPYMGYARQERIFQEGEAISAHAVARPIGMRSDRVLTVSVHTPEVLDFFGCPAEDIDGLREVVHYLK-GFSPGLVVAP 160
Cdd:PRK00934 82 LVIPYLGYARQDKRFKPGEPISARAIAKIISAYYDRIITINIHEPSILEFFPIPFINLDAAPLIAEYIGdKLDDPLVLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 161 DEGARERCGIAARELKAPLHVMSKKRLDDRTVETDSGKISVKGETVVILDDIIATGGTIASAALLLKDWGASQVLAACTH 240
Cdd:PRK00934 162 DKGALELAKEAAEILGCEYDYLEKTRISPTEVEIAPKNLDVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACVH 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1101729359 241 GLFIEDAANRLRV--CDDILSSDTLEGVYTRYSVAPAIAAVL 280
Cdd:PRK00934 242 PVLVGDAILKLYNagVDEIIVTDTLESEVSKISVAPLIADLL 283
|
|
| ribP_PPkin |
TIGR01251 |
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ... |
1-280 |
1.12e-84 |
|
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: 256.05 E-value: 1.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 1 MFIISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFP---DEKIVELLLLLEAIHEAGA 77
Cdd:TIGR01251 1 MKIFSGSSNQELAQKVAKNLGLPLGDVEVKRFPDGELYVRINESVRGKDVFIIQQSTSapvNDNLMELLIMIDALKRASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 78 ASVTTVIPYMGYARQERIFQEGEAISAHAVARPIGMR-SDRVLTVSVHTPEVLDFFGCPAEDIDGLREVVHYLKG--FSP 154
Cdd:TIGR01251 81 KSITAVIPYYGYARQDKKFKSREPISAKLVANLLETAgADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYLKKkiLDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 155 GLVVAPDEGARERCGIAARELKAPLHVMSKKRLD-DRTVETDSGKISVKGETVVILDDIIATGGTIASAALLLKDWGASQ 233
Cdd:TIGR01251 161 PVVVSPDAGGVERAKKVADALGCPLAIIDKRRISaTNEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1101729359 234 VLAACTHGLFIEDAANRLRVC--DDILSSDTLEGV-----YTRYSVAPAIAAVL 280
Cdd:TIGR01251 241 VIAAATHGVFSGPAIERIANAgvEEVIVTNTIPHEkhkpkVSVISVAPLIAEAI 294
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
1-280 |
3.97e-81 |
|
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: 246.89 E-value: 3.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 1 MFIISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFP--DEKIVELLLLLEAIHEAGAA 78
Cdd:COG0462 4 LKIFSGNANPELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPpvNDNLMELLIMIDALKRASAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 79 SVTTVIPYMGYARQERIFQEGEAISAHAVARPIGMRS-DRVLTVSVHTPEVLDFFGCPAEDIDGLREVVHYLK--GFSPG 155
Cdd:COG0462 84 RITAVIPYYGYARQDRKFRPREPITAKLVADLLEAAGaDRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKskDLEDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 156 LVVAPDEGARERCGIAARELKAPLHVMSKKRLDDRTVETDSGKISVKGETVVILDDIIATGGTIASAALLLKDWGASQVL 235
Cdd:COG0462 164 VVVSPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVMNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1101729359 236 AACTHGLFIEDAANRLR--VCDDILSSDTLE-------GVYTRYSVAPAIAAVL 280
Cdd:COG0462 244 AAATHGVLSGPAVERLEnsPIDELVVTDTIPlpeekrcDKIKVLSVAPLLAEAI 297
|
|
| Pribosyltran_N |
pfam13793 |
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ... |
1-109 |
5.65e-28 |
|
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: 104.04 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 1 MFIISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFPD--EKIVELLLLLEAIHEAGAA 78
Cdd:pfam13793 1 LKIFSGNSNPELAEKIAKRLGIPLGKATVSRFSDGEIYVRIEESVRGKDVFIIQSTCPPvnDNLMELLIMIDALKRASAK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1101729359 79 SVTTVIPYMGYARQERIFQEGEAISAHAVAR 109
Cdd:pfam13793 81 RITAVIPYFGYARQDRKDKPREPITAKLVAD 111
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
156-262 |
4.56e-16 |
|
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 72.81 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 156 LVVAPDEGARERCGIAARELKAPLHVMSKKRLDDRTVETDSGKI------SVKGETVVILDDIIATGGTIASAALLLKDW 229
Cdd:cd06223 18 VVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLelplggDVKGKRVLLVDDVIATGGTLLAAIELLKEA 97
|
90 100 110
....*....|....*....|....*....|...
gi 1101729359 230 GASQVLAACTHGLFIEDAANRLRVCDDILSSDT 262
Cdd:cd06223 98 GAKVVGVAVLLDKPEGGARELASPGDPVYSLFT 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
3-280 |
3.43e-99 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 291.82 E-value: 3.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 3 IISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFP-DEKIVELLLLLEAIHEAGAASVT 81
Cdd:PRK00934 2 IIGGSASQLLASEVARLLNTELALVETKRFPDGELYVRILGEIDGEDVVIISTTYPqDENLVELLLLIDALRDEGAKSIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 82 TVIPYMGYARQERIFQEGEAISAHAVARPIGMRSDRVLTVSVHTPEVLDFFGCPAEDIDGLREVVHYLK-GFSPGLVVAP 160
Cdd:PRK00934 82 LVIPYLGYARQDKRFKPGEPISARAIAKIISAYYDRIITINIHEPSILEFFPIPFINLDAAPLIAEYIGdKLDDPLVLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 161 DEGARERCGIAARELKAPLHVMSKKRLDDRTVETDSGKISVKGETVVILDDIIATGGTIASAALLLKDWGASQVLAACTH 240
Cdd:PRK00934 162 DKGALELAKEAAEILGCEYDYLEKTRISPTEVEIAPKNLDVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACVH 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1101729359 241 GLFIEDAANRLRV--CDDILSSDTLEGVYTRYSVAPAIAAVL 280
Cdd:PRK00934 242 PVLVGDAILKLYNagVDEIIVTDTLESEVSKISVAPLIADLL 283
|
|
| ribP_PPkin |
TIGR01251 |
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ... |
1-280 |
1.12e-84 |
|
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: 256.05 E-value: 1.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 1 MFIISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFP---DEKIVELLLLLEAIHEAGA 77
Cdd:TIGR01251 1 MKIFSGSSNQELAQKVAKNLGLPLGDVEVKRFPDGELYVRINESVRGKDVFIIQQSTSapvNDNLMELLIMIDALKRASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 78 ASVTTVIPYMGYARQERIFQEGEAISAHAVARPIGMR-SDRVLTVSVHTPEVLDFFGCPAEDIDGLREVVHYLKG--FSP 154
Cdd:TIGR01251 81 KSITAVIPYYGYARQDKKFKSREPISAKLVANLLETAgADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYLKKkiLDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 155 GLVVAPDEGARERCGIAARELKAPLHVMSKKRLD-DRTVETDSGKISVKGETVVILDDIIATGGTIASAALLLKDWGASQ 233
Cdd:TIGR01251 161 PVVVSPDAGGVERAKKVADALGCPLAIIDKRRISaTNEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1101729359 234 VLAACTHGLFIEDAANRLRVC--DDILSSDTLEGV-----YTRYSVAPAIAAVL 280
Cdd:TIGR01251 241 VIAAATHGVFSGPAIERIANAgvEEVIVTNTIPHEkhkpkVSVISVAPLIAEAI 294
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
1-280 |
3.97e-81 |
|
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: 246.89 E-value: 3.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 1 MFIISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFP--DEKIVELLLLLEAIHEAGAA 78
Cdd:COG0462 4 LKIFSGNANPELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPpvNDNLMELLIMIDALKRASAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 79 SVTTVIPYMGYARQERIFQEGEAISAHAVARPIGMRS-DRVLTVSVHTPEVLDFFGCPAEDIDGLREVVHYLK--GFSPG 155
Cdd:COG0462 84 RITAVIPYYGYARQDRKFRPREPITAKLVADLLEAAGaDRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKskDLEDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 156 LVVAPDEGARERCGIAARELKAPLHVMSKKRLDDRTVETDSGKISVKGETVVILDDIIATGGTIASAALLLKDWGASQVL 235
Cdd:COG0462 164 VVVSPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVMNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1101729359 236 AACTHGLFIEDAANRLR--VCDDILSSDTLE-------GVYTRYSVAPAIAAVL 280
Cdd:COG0462 244 AAATHGVLSGPAVERLEnsPIDELVVTDTIPlpeekrcDKIKVLSVAPLLAEAI 297
|
|
| PRK07199 |
PRK07199 |
ribose-phosphate diphosphokinase; |
10-280 |
6.59e-50 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 235960 [Multi-domain] Cd Length: 301 Bit Score: 166.65 E-value: 6.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 10 QRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQN-TFPDEKIVELLLLLEAIHEAGAASVTTVIPYMG 88
Cdd:PRK07199 12 EAAAGRLAAALGVEVGRIELHRFPDGESYVRLDSPVAGRTVVLVCSlDRPDEKLLPLLFAAEAARELGARRVGLVAPYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 89 YARQERIFQEGEAISAHAVARPIGMRSDRVLTVSVH---TPEVLDFFGCPAEDIDGLREVVHYLKGFSPG-LVVAPDEGA 164
Cdd:PRK07199 92 YMRQDIAFHPGEAISQRHFARLLSGSFDRLVTVDPHlhrYPSLSEVYPIPAVVLSAAPAIAAWIRAHVPRpLLIGPDEES 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 165 RERCGIAARELKAPLHVMSKKRLDDRTVETDSGKISV-KGETVVILDDIIATGGTIASAALLLKDWGASQVLAACTHGLF 243
Cdd:PRK07199 172 EQWVAAVAERAGAPHAVLRKTRHGDRDVEISLPDAAPwAGRTPVLVDDIVSTGRTLIEAARQLRAAGAASPDCVVVHALF 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 1101729359 244 IEDAANRLR--VCDDILSSDTLEGVYTRYSVAPAIAAVL 280
Cdd:PRK07199 252 AGDAYSALAaaGIARVVSTDTVPHPSNAISLAPLLAEAL 290
|
|
| PLN02369 |
PLN02369 |
ribose-phosphate pyrophosphokinase |
15-277 |
7.94e-49 |
|
ribose-phosphate pyrophosphokinase
Pssm-ID: 215209 [Multi-domain] Cd Length: 302 Bit Score: 163.71 E-value: 7.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 15 ALAQET----GAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFP--DEKIVELLLLLEAIHEAGAASVTTVIPYMG 88
Cdd:PLN02369 2 ALSQEIacylGLELGKITIKRFADGEIYVQLQESVRGCDVFLVQPTCPpaNENLMELLIMIDACRRASAKRITAVIPYFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 89 YARQERIFQEGEAISAHAVARPI-GMRSDRVLTVSVHTPEVLDFFGCPAEDIDGLREVVHYL--KGFSPG--LVVAPDEG 163
Cdd:PLN02369 82 YARADRKTQGRESIAAKLVANLItEAGADRVLACDLHSGQSMGYFDIPVDHVYGQPVILDYLasKTISSPdlVVVSPDVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 164 ARERCGIAARELK-APLHVMSKKRLDDRTVETDSGKISVKGETVVILDDIIATGGTIASAALLLKDWGASQVLAACTHGL 242
Cdd:PLN02369 162 GVARARAFAKKLSdAPLAIVDKRRQGHNVAEVMNLIGDVKGKVAIMVDDMIDTAGTITKGAALLHQEGAREVYACATHAV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1101729359 243 FIEDAANRL--RVCDDILSSDTLEGVYTRY-------SVAPAIA 277
Cdd:PLN02369 242 FSPPAIERLssGLFQEVIVTNTIPVSEKNYfpqltvlSVANLLG 285
|
|
| PRK01259 |
PRK01259 |
ribose-phosphate diphosphokinase; |
1-251 |
4.76e-43 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 234929 [Multi-domain] Cd Length: 309 Bit Score: 148.73 E-value: 4.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 1 MFIISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNT-FP-DEKIVELLLLLEAIHEAGAA 78
Cdd:PRK01259 1 MKLFAGNANPELAEKIAKYLGIPLGKASVGRFSDGEISVEINENVRGKDVFIIQSTcAPtNDNLMELLIMIDALKRASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 79 SVTTVIPYMGYARQERIFQEGEAISAHAVARPI---GmrSDRVLTVSVHTPEVLDFFGCPAEDIDGLREVVHYLK--GFS 153
Cdd:PRK01259 81 RITAVIPYFGYARQDRKARSRVPITAKLVANLLetaG--ADRVLTMDLHADQIQGFFDIPVDNLYGSPILLEDIKqkNLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 154 PGLVVAPDEGARERCGIAARELKAPLHVMSKKRldDRTVETDSGKI--SVKGETVVILDDIIATGGTIASAALLLKDWGA 231
Cdd:PRK01259 159 NLVVVSPDVGGVVRARALAKRLDADLAIIDKRR--PRANVSEVMNIigDVEGRDCILVDDMIDTAGTLCKAAEALKERGA 236
|
250 260
....*....|....*....|
gi 1101729359 232 SQVLAACTHGLFIEDAANRL 251
Cdd:PRK01259 237 KSVYAYATHPVLSGGAIERI 256
|
|
| PRK02812 |
PRK02812 |
ribose-phosphate pyrophosphokinase; Provisional |
3-266 |
5.39e-41 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 235072 [Multi-domain] Cd Length: 330 Bit Score: 144.11 E-value: 5.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 3 IISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFP--DEKIVELLLLLEAIHEAGAASV 80
Cdd:PRK02812 24 LFSGSSNPALAQEVARYLGMDLGPMIRKRFADGELYVQIQESIRGCDVYLIQPTCApvNDHLMELLIMVDACRRASARQI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 81 TTVIPYMGYARQERIFQEGEAISAHAVARPI-GMRSDRVLTVSVHTPEVLDFFGCPAEDIDGLREVVHYL--KGFSPGLV 157
Cdd:PRK02812 104 TAVIPYYGYARADRKTAGRESITAKLVANLItKAGADRVLAMDLHSAQIQGYFDIPCDHVYGSPVLLDYLasKNLEDIVV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 158 VAPDEGARERCGIAARELK-APLHVMSKKRLDDRTVETDSGKISVKGETVVILDDIIATGGTIASAALLLKDWGASQVLA 236
Cdd:PRK02812 184 VSPDVGGVARARAFAKKLNdAPLAIIDKRRQAHNVAEVLNVIGDVKGKTAILVDDMIDTGGTICEGARLLRKEGAKQVYA 263
|
250 260 270
....*....|....*....|....*....|
gi 1101729359 237 ACTHGLFIEDAANRlrvcddiLSSDTLEGV 266
Cdd:PRK02812 264 CATHAVFSPPAIER-------LSSGLFEEV 286
|
|
| PRK02269 |
PRK02269 |
ribose-phosphate diphosphokinase; |
7-277 |
1.45e-40 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 167353 [Multi-domain] Cd Length: 320 Bit Score: 143.01 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 7 STHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFP--DEKIVELLLLLEAIHEAGAASVTTVI 84
Cdd:PRK02269 12 SSNKELAEKVAQEIGIELGKSSVRQFSDGEIQVNIEESIRGHHVFILQSTSSpvNDNLMEILIMVDALKRASAESINVVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 85 PYMGYARQERIFQEGEAISAHAVARPIGM-RSDRVLTVSVHTPEVLDFFGCPAEDIDGLREVVHYLK--GFSPG--LVVA 159
Cdd:PRK02269 92 PYYGYARQDRKARSREPITSKLVANMLEVaGVDRLLTVDLHAAQIQGFFDIPVDHLMGAPLIADYFDrrGLVGDdvVVVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 160 PDEGARERCGIAARELKAPLHVMSKKRLDDRTVETDSGKI--SVKGETVVILDDIIATGGTIASAALLLKDWGASQVLAA 237
Cdd:PRK02269 172 PDHGGVTRARKLAQFLKTPIAIIDKRRSVDKMNTSEVMNIigNVKGKKCILIDDMIDTAGTICHAADALAEAGATEVYAS 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1101729359 238 CTHGLFIEDAANRLR--------VCDDI-LSSDTLEGVYTRYSVAPAIA 277
Cdd:PRK02269 252 CTHPVLSGPALDNIQksaieklvVLDTIyLPEERLIDKIEQISIADLLG 300
|
|
| PRK03092 |
PRK03092 |
ribose-phosphate diphosphokinase; |
12-278 |
3.06e-39 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 179535 [Multi-domain] Cd Length: 304 Bit Score: 138.93 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 12 LGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQ-NTFP-DEKIVELLLLLEAIHEAGAASVTTVIPYMGY 89
Cdd:PRK03092 1 LAEEVAKELGVEVTPTTAYDFANGEIYVRFEESVRGCDAFVLQsHTAPiNKWLMEQLIMIDALKRASAKRITVVLPFYPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 90 ARQERIFQEGEAISAHAVA---RPIGmrSDRVLTVSVHTPEVLDFFGCPAEDIDGLREVVHYLK---GFSPGLVVAPDEG 163
Cdd:PRK03092 81 ARQDKKHRGREPISARLVAdlfKTAG--ADRIMTVDLHTAQIQGFFDGPVDHLFAMPLLADYVRdkyDLDNVTVVSPDAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 164 aRERCG--IAARELKAPLHVMSKKRLDDRTVETDSGKI--SVKGETVVILDDIIATGGTIASAALLLKDWGASQVLAACT 239
Cdd:PRK03092 159 -RVRVAeqWADRLGGAPLAFIHKTRDPTVPNQVVANRVvgDVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVIIAAT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1101729359 240 HGLFIEDAANRLRVC--DDILSSDTL----EGVY---TRYSVAPAIAA 278
Cdd:PRK03092 238 HGVLSGPAAERLKNCgaREVVVTDTLpipeEKRFdklTVLSIAPLLAR 285
|
|
| PTZ00145 |
PTZ00145 |
phosphoribosylpyrophosphate synthetase; Provisional |
3-251 |
2.67e-38 |
|
phosphoribosylpyrophosphate synthetase; Provisional
Pssm-ID: 240290 [Multi-domain] Cd Length: 439 Bit Score: 139.62 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 3 IISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFP--DEKIVELLLLLEAIHEAGAASV 80
Cdd:PTZ00145 122 LFSGSSNPLLSKNIADHLGTILGRVHLKRFADGEVSMQFLESIRGKDVYIIQPTCPpvNENLIELLLMISTCRRASAKKI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 81 TTVIPYMGYARQERIFQEGEAISAHAVARPI-GMRSDRVLTVSVHTPEVLDFFGcPAEDIDGLREVVHYLKGFSPG---- 155
Cdd:PTZ00145 202 TAVIPYYGYARQDRKLSSRVPISAADVARMIeAMGVDRVVAIDLHSGQIQGFFG-PRVPVDNLEAQLIGLDYFTKKdlyk 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 156 -LVVAPDEG----AR-----------ERCGIAarelkaplhVMSKKRLDDRTVETDSGKISVKGETVVILDDIIATGGTI 219
Cdd:PTZ00145 281 pVIVSPDAGgvyrARkfqdglnhrgiSDCGIA---------MLIKQRTKPNEIEKMDLVGNVYDSDVIIVDDMIDTSGTL 351
|
250 260 270
....*....|....*....|....*....|..
gi 1101729359 220 ASAALLLKDWGASQVLAACTHGLFIEDAANRL 251
Cdd:PTZ00145 352 CEAAKQLKKHGARRVFAFATHGLFSGPAIERI 383
|
|
| PRK00553 |
PRK00553 |
ribose-phosphate pyrophosphokinase; Provisional |
27-254 |
3.20e-36 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 179062 [Multi-domain] Cd Length: 332 Bit Score: 131.58 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 27 VVNKAYPDGERYVRILRQVSGRDVVVIQNTFP--DEKIVELLLLLEAIHEAGAASVTTVIPYMGYARQERIFQEGEAISA 104
Cdd:PRK00553 36 IVIQKFADGETYIRFDESVRNKDVVIFQSTCSpvNDSLMELLIAIDALKRGSAKSITAILPYYGYARQDRKTAGREPITS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 105 HAVARPIGMRS-DRVLTVSVHTPEVLDFFGCPaedIDGLREV------VHYLKGFSPGLVVAPDEGARERCGIAARELKA 177
Cdd:PRK00553 116 KLVADLLTKAGvTRVTLTDIHSDQTQGFFDIP---VDILRTYhvflsrVLELLGKKDLVVVSPDYGGVKRARLIAESLEL 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1101729359 178 PLHVMSKKRLDDRTVETDSGKISVKGETVVILDDIIATGGTIASAALLLKDWGASQVLAACTHGLFIEDAANRLRVC 254
Cdd:PRK00553 193 PLAIIDKRRPKHNVAESINVLGEVKNKNCLIVDDMIDTGGTVIAAAKLLKKQKAKKVCVMATHGLFNKNAIQLFDEA 269
|
|
| PRK04923 |
PRK04923 |
ribose-phosphate diphosphokinase; |
1-263 |
3.79e-35 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 179893 [Multi-domain] Cd Length: 319 Bit Score: 128.51 E-value: 3.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 1 MFIISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFP--DEKIVELLLLLEAIHEAGAA 78
Cdd:PRK04923 7 LLVFSGNANKPLAQSICKELGVRMGKALVTRFSDGEVQVEIEESVRRQEVFVIQPTCApsAENLMELLVLIDALKRASAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 79 SVTTVIPYMGYARQERIFQEGEA-ISAHAVARPI-GMRSDRVLTVSVHTPEVLDFFGCPAEDIDG---LREVVHYLKGFS 153
Cdd:PRK04923 87 SVTAVIPYFGYSRQDRRMRSSRVpITAKVAAKMIsAMGADRVLTVDLHADQIQGFFDVPVDNVYAsplLLADIWRAYGTD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 154 PGLVVAPDEGARERCGIAAREL-KAPLHVMSKK--RLDDRTVETDSGkiSVKGETVVILDDIIATGGTIASAALLLKDWG 230
Cdd:PRK04923 167 NLIVVSPDVGGVVRARAVAKRLdDADLAIIDKRrpRANVATVMNIIG--DVQGKTCVLVDDLVDTAGTLCAAAAALKQRG 244
|
250 260 270
....*....|....*....|....*....|....*
gi 1101729359 231 ASQVLAACTHGLFIEDAANRLR--VCDDILSSDTL 263
Cdd:PRK04923 245 ALKVVAYITHPVLSGPAVDNINnsQLDELVVTDTI 279
|
|
| PRK02458 |
PRK02458 |
ribose-phosphate pyrophosphokinase; Provisional |
16-263 |
7.61e-33 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 235039 [Multi-domain] Cd Length: 323 Bit Score: 122.54 E-value: 7.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 16 LAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNT-FP-DEKIVELLLLLEAIHEAGAASVTTVIPYMGYARQE 93
Cdd:PRK02458 25 IAQAAGVPLGKLSSRQFSDGEIMINIEESVRGDDIYIIQSTsFPvNDHLWELLIMIDACKRASANTVNVVLPYFGYARQD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 94 RIFQEGEAISAHAVARPI-GMRSDRVLTVSVHTPEVLDFFGCPaedIDGLREVVHYLKGFSP-GL------VVAPDEGAR 165
Cdd:PRK02458 105 RIAKPREPITAKLVANMLvKAGVDRVLTLDLHAVQVQGFFDIP---VDNLFTVPLFAKHYCKkGLsgsdvvVVSPKNSGI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 166 ERCGIAARELKAPLHVMSKKRLDDrtvETDSGKI--SVKGETVVILDDIIATGGTIASAALLLKDWGASQVLAACTHGLF 243
Cdd:PRK02458 182 KRARSLAEYLDAPIAIIDYAQDDS---EREEGYIigDVAGKKAILIDDILNTGKTFAEAAKIVEREGATEIYAVASHGLF 258
|
250 260
....*....|....*....|..
gi 1101729359 244 IEDAANRLRVCD--DILSSDTL 263
Cdd:PRK02458 259 AGGAAEVLENAPikEILVTDSV 280
|
|
| Pribosyltran_N |
pfam13793 |
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ... |
1-109 |
5.65e-28 |
|
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: 104.04 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 1 MFIISGSTHQRLGVALAQETGAEFCGVVNKAYPDGERYVRILRQVSGRDVVVIQNTFPD--EKIVELLLLLEAIHEAGAA 78
Cdd:pfam13793 1 LKIFSGNSNPELAEKIAKRLGIPLGKATVSRFSDGEIYVRIEESVRGKDVFIIQSTCPPvnDNLMELLIMIDALKRASAK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1101729359 79 SVTTVIPYMGYARQERIFQEGEAISAHAVAR 109
Cdd:pfam13793 81 RITAVIPYFGYARQDRKDKPREPITAKLVAD 111
|
|
| PRK06827 |
PRK06827 |
phosphoribosylpyrophosphate synthetase; Provisional |
35-245 |
2.50e-21 |
|
phosphoribosylpyrophosphate synthetase; Provisional
Pssm-ID: 180714 [Multi-domain] Cd Length: 382 Bit Score: 92.32 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 35 GERYVRILRQVSGRDVVVIQ---------NTF-------PDEKIVELLLLLEAIhEAGAASVTTVIPYMGYARQER---- 94
Cdd:PRK06827 65 GEAKGEILESVRGKDIYILQdvgnysvtyNMFgeknhmsPDDHFQDLKRTIDAI-RGKARRITVIMPFLYESRQHKrkgr 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 95 -------IFQEGEaisahavarpiGMRSDRVLTVSVHTPEV--------LDFFGCPAEDIDGLREVVHYLKGFSPGL-VV 158
Cdd:PRK06827 144 esldcalALQELE-----------ELGVDNIITFDAHDPRIenaiplmgFENLYPSYQIIKALLKNEKDLEIDKDHLmVI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 159 APDEGARERCGIAARELKAPLHVMSKKRlDDRTVETDSGKI--------SVKGETVVILDDIIATGGTIASAALLLKDWG 230
Cdd:PRK06827 213 SPDTGAMDRAKYYASVLGVDLGLFYKRR-DYSRVVNGRNPIvaheflgrDVEGKDVLIVDDMIASGGSMIDAAKELKSRG 291
|
250
....*....|....*
gi 1101729359 231 ASQVLAACTHGLFIE 245
Cdd:PRK06827 292 AKKIIVAATFGFFTN 306
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
156-262 |
4.56e-16 |
|
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 72.81 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 156 LVVAPDEGARERCGIAARELKAPLHVMSKKRLDDRTVETDSGKI------SVKGETVVILDDIIATGGTIASAALLLKDW 229
Cdd:cd06223 18 VVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLelplggDVKGKRVLLVDDVIATGGTLLAAIELLKEA 97
|
90 100 110
....*....|....*....|....*....|...
gi 1101729359 230 GASQVLAACTHGLFIEDAANRLRVCDDILSSDT 262
Cdd:cd06223 98 GAKVVGVAVLLDKPEGGARELASPGDPVYSLFT 130
|
|
| PLN02297 |
PLN02297 |
ribose-phosphate pyrophosphokinase |
78-243 |
4.73e-11 |
|
ribose-phosphate pyrophosphokinase
Pssm-ID: 177934 [Multi-domain] Cd Length: 326 Bit Score: 62.01 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 78 ASVTTVIPYMGYARQERIFQEGEAISAHAVAR-----PIGM-RSDRVLTVSVHTPEVLDFFG-----CPAEDIDGLREVV 146
Cdd:PLN02297 97 ASFTLVLPFFPTGTSERVEREGDVATAFTLARilsniPISRgGPTSLVIFDIHALQERFYFGdnvlpCFESGIPLLKKRL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 147 HYLKGfSPGLVVA-PDEGARERCGiaaRELKA-PLHVMSKKRL-DDRTVETDSGKisVKGETVVILDDIIATGGTIASAA 223
Cdd:PLN02297 177 QQLPD-SDNIVIAfPDDGAWKRFH---KQFEHfPMVVCTKVREgDKRIVRIKEGN--PAGRHVVIVDDLVQSGGTLIECQ 250
|
170 180
....*....|....*....|
gi 1101729359 224 LLLKDWGASQVLAACTHGLF 243
Cdd:PLN02297 251 KVLAAHGAAKVSAYVTHGVF 270
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
151-240 |
2.36e-10 |
|
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: 57.76 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 151 GFSPGLVVAPDEGARERCGIAARELKAPLHVMSKKRLDDRTVE---TDSGKISVKGETVVILDDIIATGGTIASAALLLK 227
Cdd:pfam00156 27 GGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEvmkTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLK 106
|
90
....*....|...
gi 1101729359 228 DWGASQVLAACTH 240
Cdd:pfam00156 107 NVGPKEVKIAVLI 119
|
|
| PRK02304 |
PRK02304 |
adenine phosphoribosyltransferase; Provisional |
137-238 |
6.37e-06 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 235028 Cd Length: 175 Bit Score: 45.45 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 137 EDIDGLREV----VHYLKGFSPGLVVAPDegARercGI-----AARELKAPLHVMSKK-RLDDRTVE--------TDSGK 198
Cdd:PRK02304 31 ADPEAFREVidalVERYKDADIDKIVGIE--AR---GFifgaaLAYKLGIGFVPVRKPgKLPRETISesyeleygTDTLE 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1101729359 199 ISV----KGETVVILDDIIATGGTIASAALLLKDWGAsQVLAAC 238
Cdd:PRK02304 106 IHKdaikPGDRVLIVDDLLATGGTLEAAIKLLERLGA-EVVGAA 148
|
|
| PLN02293 |
PLN02293 |
adenine phosphoribosyltransferase |
202-242 |
6.55e-06 |
|
adenine phosphoribosyltransferase
Pssm-ID: 177930 Cd Length: 187 Bit Score: 45.82 E-value: 6.55e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1101729359 202 KGETVVILDDIIATGGTIASAALLLKDWGASQVLAACTHGL 242
Cdd:PLN02293 124 PGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIEL 164
|
|
| Pribosyl_synth |
pfam14572 |
Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes ... |
201-251 |
7.55e-05 |
|
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: 42.50 E-value: 7.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1101729359 201 VKGETVVILDDIIATGGTIASAALLLKDWGASQVLAACTHGLFIEDAANRL 251
Cdd:pfam14572 81 VGGRIAIIVDDMIDDVDSFVAAAELLKERGAYKIYVMATHGLLSSDAPRLL 131
|
|
| PRK11595 |
PRK11595 |
DNA utilization protein GntX; Provisional |
200-238 |
1.04e-04 |
|
DNA utilization protein GntX; Provisional
Pssm-ID: 183221 [Multi-domain] Cd Length: 227 Bit Score: 42.72 E-value: 1.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1101729359 200 SVKGETVVILDDIIATGGTIASAA-LLLKDWGAS-QVLAAC 238
Cdd:PRK11595 184 PVQGQHMAIVDDVVTTGSTVAEIAqLLLRNGAASvQVWCLC 224
|
|
| Apt |
COG0503 |
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ... |
138-238 |
1.22e-04 |
|
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: 41.60 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101729359 138 DIDGLREVV----HYLKGFSPGLVVAPDegARercGIA-----ARELKAPLhVMSKKR----LDDRTVETDSG-----KI 199
Cdd:COG0503 29 DPELFRAAGdelaERFADKGIDKVVGIE--AR---GFIlaaalAYALGVPF-VPARKPgklpGETVSEEYDLEygtgdTL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1101729359 200 SV------KGETVVILDDIIATGGTIASAALLLKDWGAsQVLAAC 238
Cdd:COG0503 103 ELhkdalkPGDRVLIVDDLLATGGTAKAAIKLVEEAGA-EVVGIA 146
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
201-253 |
1.92e-04 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 41.12 E-value: 1.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1101729359 201 VKGETVVILDDIIATGGTIASAALLLKDWGASQV--LAACTHGlfieDAANRLRV 253
Cdd:PRK07322 118 LKGKRVAIVDDVVSTGGTLTALERLVERAGGQVVakAAIFAEG----DASNRLDV 168
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
172-237 |
2.35e-04 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 41.39 E-value: 2.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1101729359 172 ARELKAPLHVMSKKRLDDRTVETDSGKIS-----VKGETVVILDDIIATGGTIASAALLLKDWGASQVLAA 237
Cdd:PRK02277 104 ADELGKDLAIYHPKKWDHGEGEKKTGSFSrnfasVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVV 174
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
205-238 |
5.59e-03 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 36.99 E-value: 5.59e-03
10 20 30
....*....|....*....|....*....|....
gi 1101729359 205 TVVILDDIIATGGTIASAALLLKDWGASQVLAAC 238
Cdd:PRK00129 126 TVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLC 159
|
|
| PLN02238 |
PLN02238 |
hypoxanthine phosphoribosyltransferase |
191-239 |
9.35e-03 |
|
hypoxanthine phosphoribosyltransferase
Pssm-ID: 215132 Cd Length: 189 Bit Score: 36.17 E-value: 9.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1101729359 191 TVETDSGKISVKGETVVILDDIIATGGTIASAALLLKDWGASQVlAACT 239
Cdd:PLN02238 85 KVSGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASV-SVCA 132
|
|
| |
