|
Name |
Accession |
Description |
Interval |
E-value |
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
1-203 |
7.46e-86 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 252.00 E-value: 7.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 1 MKQAIAKHLLHIEAVFLRPnepFTWASGILSPIYCDNRLTLSYPKVRNDVADGLGKLLKEHFPEAEMIAGTATAGIPHAA 80
Cdd:COG0461 3 YKEELAELLLEIGALLFGH---FTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 81 LLADRTGAPMCYVRSKPKAHGKGNQIEGAIKKGQKTVVIEDLISTGGSVLEAAAALQREGAEVLGVISIFTYGlPKAKEA 160
Cdd:COG0461 80 AVARALGLPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDRE-EGAAEN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494885261 161 FKKAGLPYYSLTDYDTLIEVALENGTIHSADIEKLKSWKLNPE 203
Cdd:COG0461 159 LEEAGVPLHSLLTLDDLLELLKEKGYIDPEELEALEAYREKPG 201
|
|
| pyrE |
PRK00455 |
orotate phosphoribosyltransferase; Validated |
1-203 |
2.13e-81 |
|
orotate phosphoribosyltransferase; Validated
Pssm-ID: 234771 Cd Length: 202 Bit Score: 240.83 E-value: 2.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 1 MKQAIAKHLLHIEAVflrPNEPFTWASGILSPIYCDNRLTLSYPKVRNDVADGLGKLLKEHFPEAEMIAGTATAGIPHAA 80
Cdd:PRK00455 4 YAREFIEFLLEIGAL---LFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 81 LLADRTGAPMCYVRSKPKAHGKGNQIEGAIKKGQKTVVIEDLISTGGSVLEAAAALQREGAEVLGVISIFTYGlPKAKEA 160
Cdd:PRK00455 81 AVARALDLPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ-SAAQEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494885261 161 FKKAGLPYYSLTDYDTLIEVAlENGTIHSADIEKLKSWKLNPE 203
Cdd:PRK00455 160 FADAGVPLISLITLDDLLEYA-EEGPLCKEGLPAVKAYRRNYG 201
|
|
| pyrE |
TIGR00336 |
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ... |
7-177 |
4.69e-61 |
|
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: 188.41 E-value: 4.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 7 KHLLHIEAVFLrpNEpFTWASGILSPIYCDNRLTLSYPKVRNDVADGLGKLLKEHFpEAEMIAGTATAGIPHAALLAD-- 84
Cdd:TIGR00336 1 ELLLEVQALKF--GE-FTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHL-EFDVIAGPALGGIPIATAVSVkl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 85 ---RTGAPMCYVRSKPKAHGKGNQIEGAIKKGQKTVVIEDLISTGGSVLEAAAALQREGAEVLGVISIFTYGLPKAKEAF 161
Cdd:TIGR00336 77 akpGGDIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQERSAGQEF 156
|
170
....*....|....*..
gi 494885261 162 KKA-GLPYYSLTDYDTL 177
Cdd:TIGR00336 157 EKEyGLPVISLITLKDL 173
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
54-171 |
1.57e-21 |
|
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: 85.91 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 54 LGKLLKEHFPEAEMIAGTATAGIPHAALLADRTGAPMCYVRSKPKAHGKGNQ-------IEGAIKKGQKTVVIEDLISTG 126
Cdd:cd06223 5 LAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSepyglelPLGGDVKGKRVLLVDDVIATG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 494885261 127 GSVLEAAAALQREGAEVLGVISIFTYGLPKAKEAfKKAGLPYYSL 171
Cdd:cd06223 85 GTLLAAIELLKEAGAKVVGVAVLLDKPEGGAREL-ASPGDPVYSL 128
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
51-150 |
2.17e-09 |
|
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: 53.91 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 51 ADGLGKLLKEHFPEAE----MIAGTATAGIPHAALLADRTGAPMCYVRSKpKAHGKGNQIEGA-----IKKGQKTVVIED 121
Cdd:pfam00156 12 LKAVARLAAQINEDYGgkpdVVVGILRGGLPFAGILARRLDVPLAFVRKV-SYNPDTSEVMKTssalpDLKGKTVLIVDD 90
|
90 100
....*....|....*....|....*....
gi 494885261 122 LISTGGSVLEAAAALQREGAEVLGVISIF 150
Cdd:pfam00156 91 ILDTGGTLLKVLELLKNVGPKEVKIAVLI 119
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
1-203 |
7.46e-86 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 252.00 E-value: 7.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 1 MKQAIAKHLLHIEAVFLRPnepFTWASGILSPIYCDNRLTLSYPKVRNDVADGLGKLLKEHFPEAEMIAGTATAGIPHAA 80
Cdd:COG0461 3 YKEELAELLLEIGALLFGH---FTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 81 LLADRTGAPMCYVRSKPKAHGKGNQIEGAIKKGQKTVVIEDLISTGGSVLEAAAALQREGAEVLGVISIFTYGlPKAKEA 160
Cdd:COG0461 80 AVARALGLPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDRE-EGAAEN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494885261 161 FKKAGLPYYSLTDYDTLIEVALENGTIHSADIEKLKSWKLNPE 203
Cdd:COG0461 159 LEEAGVPLHSLLTLDDLLELLKEKGYIDPEELEALEAYREKPG 201
|
|
| pyrE |
PRK00455 |
orotate phosphoribosyltransferase; Validated |
1-203 |
2.13e-81 |
|
orotate phosphoribosyltransferase; Validated
Pssm-ID: 234771 Cd Length: 202 Bit Score: 240.83 E-value: 2.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 1 MKQAIAKHLLHIEAVflrPNEPFTWASGILSPIYCDNRLTLSYPKVRNDVADGLGKLLKEHFPEAEMIAGTATAGIPHAA 80
Cdd:PRK00455 4 YAREFIEFLLEIGAL---LFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 81 LLADRTGAPMCYVRSKPKAHGKGNQIEGAIKKGQKTVVIEDLISTGGSVLEAAAALQREGAEVLGVISIFTYGlPKAKEA 160
Cdd:PRK00455 81 AVARALDLPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ-SAAQEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494885261 161 FKKAGLPYYSLTDYDTLIEVAlENGTIHSADIEKLKSWKLNPE 203
Cdd:PRK00455 160 FADAGVPLISLITLDDLLEYA-EEGPLCKEGLPAVKAYRRNYG 201
|
|
| pyrE |
TIGR00336 |
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ... |
7-177 |
4.69e-61 |
|
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: 188.41 E-value: 4.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 7 KHLLHIEAVFLrpNEpFTWASGILSPIYCDNRLTLSYPKVRNDVADGLGKLLKEHFpEAEMIAGTATAGIPHAALLAD-- 84
Cdd:TIGR00336 1 ELLLEVQALKF--GE-FTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHL-EFDVIAGPALGGIPIATAVSVkl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 85 ---RTGAPMCYVRSKPKAHGKGNQIEGAIKKGQKTVVIEDLISTGGSVLEAAAALQREGAEVLGVISIFTYGLPKAKEAF 161
Cdd:TIGR00336 77 akpGGDIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQERSAGQEF 156
|
170
....*....|....*..
gi 494885261 162 KKA-GLPYYSLTDYDTL 177
Cdd:TIGR00336 157 EKEyGLPVISLITLKDL 173
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
54-171 |
1.57e-21 |
|
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: 85.91 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 54 LGKLLKEHFPEAEMIAGTATAGIPHAALLADRTGAPMCYVRSKPKAHGKGNQ-------IEGAIKKGQKTVVIEDLISTG 126
Cdd:cd06223 5 LAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSepyglelPLGGDVKGKRVLLVDDVIATG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 494885261 127 GSVLEAAAALQREGAEVLGVISIFTYGLPKAKEAfKKAGLPYYSL 171
Cdd:cd06223 85 GTLLAAIELLKEAGAKVVGVAVLLDKPEGGAREL-ASPGDPVYSL 128
|
|
| PRK13809 |
PRK13809 |
orotate phosphoribosyltransferase; Provisional |
23-192 |
1.82e-19 |
|
orotate phosphoribosyltransferase; Provisional
Pssm-ID: 184340 Cd Length: 206 Bit Score: 82.19 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 23 FTWASGILSPIYCDNRLTLSYPKVRNDVADGLGKLlKEHFPeAEMIAGTATAGIPHAALLADRTGAPMCYVRSKPKAHGK 102
Cdd:PRK13809 28 FILASGEETPIYVDMRLVISSPEVLQTIATLIWRL-RPSFN-SSLLCGVPYTALTLATSISLKYNIPMVLRRKELKNVDP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 103 GNQI--EGAIKKGQKTVVIEDLISTGGSVLEAAAALQREGAEVLGvISIFTYGLPKAKEAFKKAGLPYYSLTDYDTLIEV 180
Cdd:PRK13809 106 SDAIkvEGLFTPGQTCLVINDMVSSGKSIIETAVALEEEGLVVRE-ALVFLDRQKGACQPLGPQGIKLSSVFTVPDLIKS 184
|
170
....*....|..
gi 494885261 181 ALENGTIHSADI 192
Cdd:PRK13809 185 LISYGKLSSGDL 196
|
|
| PRK05500 |
PRK05500 |
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase; |
23-187 |
1.25e-18 |
|
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
Pssm-ID: 180119 [Multi-domain] Cd Length: 477 Bit Score: 83.19 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 23 FTWASGILSPIYCDNRLTLSYPKVRNDVADGLGKLLKEHfpEAEMIAGTATAGIPHAALLADRTGAPMCYVRSKPKAHGK 102
Cdd:PRK05500 305 YVQASGATFSYYIDLRKIISNPQLFHQVLSAYAEILKNL--TFDRIAGIPYGSLPTATGLALHLHHPMIFPRKEVKAHGT 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 103 GNQIEGAIKKGQKTVVIEDLISTGGSVLEAAAALQREGAEVLGVISIFTYGlPKAKEAFKKAGLPYYSLTDYDTLIEVAL 182
Cdd:PRK05500 383 RRLIEGNFHPGETVVVVDDILITGKSVMEGAEKLKSAGLNVRDIVVFIDHE-QGVKDKLQSHGYQAYSVLTISEITETLY 461
|
....*
gi 494885261 183 ENGTI 187
Cdd:PRK05500 462 QAGRI 466
|
|
| PRK02304 |
PRK02304 |
adenine phosphoribosyltransferase; Provisional |
41-175 |
1.21e-16 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 235028 Cd Length: 175 Bit Score: 73.96 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 41 LSYPKVRNDVADGLGKLLKEHfpEAEMIAGTATAGIPHAALLADRTGAPMCYVRsKPkahGKG---------------NQ 105
Cdd:PRK02304 30 LADPEAFREVIDALVERYKDA--DIDKIVGIEARGFIFGAALAYKLGIGFVPVR-KP---GKLpretisesyeleygtDT 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494885261 106 IE---GAIKKGQKTVVIEDLISTGGSVLEAAAALQREGAEVLGVISIFtyGLPKAKEAFKKAGLPYYSLTDYD 175
Cdd:PRK02304 104 LEihkDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVI--ELPDLGGREKLEGYPVKSLVKFD 174
|
|
| Apt |
COG0503 |
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ... |
54-174 |
3.47e-16 |
|
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: 72.80 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 54 LGKLLKEHFPEAE--MIAGTATAGIPHAALLADRTGAPMCYVRSKPKA------------HGKGNQIE---GAIKKGQKT 116
Cdd:COG0503 36 AGDELAERFADKGidKVVGIEARGFILAAALAYALGVPFVPARKPGKLpgetvseeydleYGTGDTLElhkDALKPGDRV 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 494885261 117 VVIEDLISTGGSvLEAAAALQRE-GAEVLGVISIFTYGLPKAKEAFKkaGLPYYSLTDY 174
Cdd:COG0503 116 LIVDDLLATGGT-AKAAIKLVEEaGAEVVGIAFLIELGFLGGREKLR--DYPVESLLTL 171
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
50-150 |
1.71e-11 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 60.65 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 50 VADGLGKLLKEHFPEAEMIAGTATAGIPHAALLADRTGAPMCYVRSKPKAHGKGNQIEGAIK------KGQKTVVIEDLI 123
Cdd:PRK02277 71 IASAMADMLEKEDEEVDVVVGIAKSGVPLATLVADELGKDLAIYHPKKWDHGEGEKKTGSFSrnfasvEGKRCVIVDDVI 150
|
90 100
....*....|....*....|....*..
gi 494885261 124 STGGSVLEAAAALQREGAEVLGVISIF 150
Cdd:PRK02277 151 TSGTTMKETIEYLKEHGGKPVAVVVLI 177
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
50-153 |
5.13e-10 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 56.14 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 50 VADGLGKLLKehfPEAEMIAGTATAGIPHAALLADRTGAPMCYVRSKPKAH--------------GKGNQI-----EGAI 110
Cdd:PRK07322 41 AAEALAKRLP---TEVDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKPYmqdpiiqevvsittGKPQLLvldgaDAEK 117
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 494885261 111 KKGQKTVVIEDLISTGGSVLEAAAALQREGAEVLGVISIFTYG 153
Cdd:PRK07322 118 LKGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAKAAIFAEG 160
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
51-150 |
2.17e-09 |
|
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: 53.91 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 51 ADGLGKLLKEHFPEAE----MIAGTATAGIPHAALLADRTGAPMCYVRSKpKAHGKGNQIEGA-----IKKGQKTVVIED 121
Cdd:pfam00156 12 LKAVARLAAQINEDYGgkpdVVVGILRGGLPFAGILARRLDVPLAFVRKV-SYNPDTSEVMKTssalpDLKGKTVLIVDD 90
|
90 100
....*....|....*....|....*....
gi 494885261 122 LISTGGSVLEAAAALQREGAEVLGVISIF 150
Cdd:pfam00156 91 ILDTGGTLLKVLELLKNVGPKEVKIAVLI 119
|
|
| PLN02293 |
PLN02293 |
adenine phosphoribosyltransferase |
108-177 |
3.73e-08 |
|
adenine phosphoribosyltransferase
Pssm-ID: 177930 Cd Length: 187 Bit Score: 51.21 E-value: 3.73e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494885261 108 GAIKKGQKTVVIEDLISTGGSVLEAAAALQREGAEVL---GVIsiftyGLPKAKEAFKKAGLPYYSLTDYDTL 177
Cdd:PLN02293 120 GAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVecaCVI-----ELPELKGREKLNGKPLFVLVESRGI 187
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
72-175 |
1.25e-05 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 44.60 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 72 ATAGIPHAALLADRTGAPMCYVRsKPKAHGKGNQIE-----------------GAIKKGQKTVVIEDLISTgGSVLEAAA 134
Cdd:PRK08558 119 ATDGIPLAVAIASYFGADLVYAK-KSKETGVEKFYEeyqrlasgievtlylpaSALKKGDRVLIVDDIIRS-GETQRALL 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 494885261 135 ALQRE-GAEVLGV---ISIFTYGLPKAKEafkKAGLPYYSLTDYD 175
Cdd:PRK08558 197 DLARQaGADVVGVfflIAVGEVGIDRARE---ETDAPVDALYTLE 238
|
|
| PRK12560 |
PRK12560 |
adenine phosphoribosyltransferase; Provisional |
44-147 |
2.29e-05 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 183595 Cd Length: 187 Bit Score: 43.23 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 44 PKVRNDVADGLGKLLKEHFpeaEMIAGTATAGIPHAALLADRTGAPMCYVRSKPKAHGKGNQI---------EG-----A 109
Cdd:PRK12560 34 PKVLKETAKEIIKYIDKDI---DKIVTEEDKGAPLATPVSLLSGKPLAMARWYPYSLSELNYNvveigseyfEGvvylnG 110
|
90 100 110
....*....|....*....|....*....|....*...
gi 494885261 110 IKKGQKTVVIEDLISTGGSVLEAAAALQREGAEVLGVI 147
Cdd:PRK12560 111 IEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVI 148
|
|
| PRK03092 |
PRK03092 |
ribose-phosphate diphosphokinase; |
83-173 |
7.50e-05 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 179535 [Multi-domain] Cd Length: 304 Bit Score: 42.63 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 83 ADRTG-APMCYV---RSKPKA-HGKGNQIEGAIKkGQKTVVIEDLISTGGSVLEAAAALQREGAEvlGVISIFTYGL--P 155
Cdd:PRK03092 167 ADRLGgAPLAFIhktRDPTVPnQVVANRVVGDVE-GRTCVLVDDMIDTGGTIAGAVRALKEAGAK--DVIIAATHGVlsG 243
|
90
....*....|....*...
gi 494885261 156 KAKEAFKKAGLPYYSLTD 173
Cdd:PRK03092 244 PAAERLKNCGAREVVVTD 261
|
|
| PRK01259 |
PRK01259 |
ribose-phosphate diphosphokinase; |
82-154 |
2.28e-04 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 234929 [Multi-domain] Cd Length: 309 Bit Score: 40.87 E-value: 2.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494885261 82 LADRTGAPMCYV-RSKPKAhgkgNQIE-----GAIKkGQKTVVIEDLISTGGSVLEAAAALQREGAEvlGVISIFTYGL 154
Cdd:PRK01259 176 LAKRLDADLAIIdKRRPRA----NVSEvmniiGDVE-GRDCILVDDMIDTAGTLCKAAEALKERGAK--SVYAYATHPV 247
|
|
| PRK00553 |
PRK00553 |
ribose-phosphate pyrophosphokinase; Provisional |
75-164 |
2.54e-04 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 179062 [Multi-domain] Cd Length: 332 Bit Score: 41.06 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494885261 75 GIPHAALLADRTGAPMCYVRSKPKAHGKGNQIE--GAIKKgQKTVVIEDLISTGGSVLEAAAALQREGAEVLGVISifTY 152
Cdd:PRK00553 179 GVKRARLIAESLELPLAIIDKRRPKHNVAESINvlGEVKN-KNCLIVDDMIDTGGTVIAAAKLLKKQKAKKVCVMA--TH 255
|
90
....*....|....
gi 494885261 153 GL--PKAKEAFKKA 164
Cdd:PRK00553 256 GLfnKNAIQLFDEA 269
|
|
| PRK07199 |
PRK07199 |
ribose-phosphate diphosphokinase; |
117-165 |
1.46e-03 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 235960 [Multi-domain] Cd Length: 301 Bit Score: 38.77 E-value: 1.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 494885261 117 VVIEDLISTGGSVLEAAAALQREGA---EVLGVISIFTyglPKAKEAFKKAG 165
Cdd:PRK07199 215 VLVDDIVSTGRTLIEAARQLRAAGAaspDCVVVHALFA---GDAYSALAAAG 263
|
|
| PLN02369 |
PLN02369 |
ribose-phosphate pyrophosphokinase |
88-142 |
4.14e-03 |
|
ribose-phosphate pyrophosphokinase
Pssm-ID: 215209 [Multi-domain] Cd Length: 302 Bit Score: 37.37 E-value: 4.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 494885261 88 APMCYVRSKPKAHGKGNQIE--GAIKkGQKTVVIEDLISTGGSVLEAAAALQREGAE 142
Cdd:PLN02369 176 APLAIVDKRRQGHNVAEVMNliGDVK-GKVAIMVDDMIDTAGTITKGAALLHQEGAR 231
|
|
|