|
Name |
Accession |
Description |
Interval |
E-value |
| pyrE |
PRK00455 |
orotate phosphoribosyltransferase; Validated |
1-213 |
4.37e-99 |
|
orotate phosphoribosyltransferase; Validated
Pssm-ID: 234771 Cd Length: 202 Bit Score: 285.90 E-value: 4.37e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 1 MKPYQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAG-LFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIAT 79
Cdd:PRK00455 1 MKMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRkLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 80 TTAVAmaehhdLDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQe 158
Cdd:PRK00455 81 AVARA------LDLPAIFVRKEAKDHGEGGQIEGRRLFGkRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 534751287 159 rgrgeiSAIQEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYREEFGV 213
Cdd:PRK00455 154 ------SAAQEVFADAGVPLISLITLDDLLEYAEEGPLCKEGLPAVKAYRRNYGV 202
|
|
| pyrE |
TIGR00336 |
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ... |
10-187 |
5.20e-86 |
|
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: 251.58 E-value: 5.20e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 10 EFALSKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTAVAMAEHH 89
Cdd:TIGR00336 1 ELLLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIATAVSVKLAKPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 90 DlDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERgrgeiSAIQ 168
Cdd:TIGR00336 81 G-DIPLCFNRKEAKDHGEGGNIEGELLEGdKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQER-----SAGQ 154
|
170
....*....|....*....
gi 534751287 169 EVERDYNCKVISIITLKDL 187
Cdd:TIGR00336 155 EFEKEYGLPVISLITLKDL 173
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
4-212 |
1.70e-78 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 233.51 E-value: 1.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 4 YQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAGLFNT-GRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTA 82
Cdd:COG0461 3 YKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSyPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 83 VAmaehhdLDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQErgr 161
Cdd:COG0461 83 RA------LGLPAIFVRKEAKDHGTGGQIEGGLLPGeRVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREE--- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 534751287 162 geiSAIQEVErDYNCKVISIITLKDLIAYLEEKPEMAE-HLAAVKAYREEFG 212
Cdd:COG0461 154 ---GAAENLE-EAGVPLHSLLTLDDLLELLKEKGYIDPeELEALEAYREKPG 201
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
49-166 |
1.78e-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: 72.43 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 49 LGRFYAEALVDSGIEFDLLFGPAYKGIPIATttavAMAEHhdLDLPYCFNRKEAKDHGEGG-------NLVGSALQG-RV 120
Cdd:cd06223 1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAA----ALARA--LGLPLAFIRKERKGPGRTPsepygleLPLGGDVKGkRV 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 534751287 121 MLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISA 166
Cdd:cd06223 75 LLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELAS 120
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
39-175 |
2.86e-06 |
|
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: 45.43 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 39 LFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTAvamaehHDLDLPYCFNRKEAKDHGEGGNLVGSALQG 118
Cdd:pfam00156 5 ILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILA------RRLDVPLAFVRKVSYNPDTSEVMKTSSALP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 534751287 119 -----RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQE----------RGRGEISAIQEVERDYN 175
Cdd:pfam00156 79 dlkgkTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAgtepkdkydkRVDDWIVFVVGFGLDER 150
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| pyrE |
PRK00455 |
orotate phosphoribosyltransferase; Validated |
1-213 |
4.37e-99 |
|
orotate phosphoribosyltransferase; Validated
Pssm-ID: 234771 Cd Length: 202 Bit Score: 285.90 E-value: 4.37e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 1 MKPYQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAG-LFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIAT 79
Cdd:PRK00455 1 MKMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRkLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 80 TTAVAmaehhdLDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQe 158
Cdd:PRK00455 81 AVARA------LDLPAIFVRKEAKDHGEGGQIEGRRLFGkRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 534751287 159 rgrgeiSAIQEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYREEFGV 213
Cdd:PRK00455 154 ------SAAQEVFADAGVPLISLITLDDLLEYAEEGPLCKEGLPAVKAYRRNYGV 202
|
|
| pyrE |
TIGR00336 |
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ... |
10-187 |
5.20e-86 |
|
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: 251.58 E-value: 5.20e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 10 EFALSKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTAVAMAEHH 89
Cdd:TIGR00336 1 ELLLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIATAVSVKLAKPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 90 DlDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERgrgeiSAIQ 168
Cdd:TIGR00336 81 G-DIPLCFNRKEAKDHGEGGNIEGELLEGdKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQER-----SAGQ 154
|
170
....*....|....*....
gi 534751287 169 EVERDYNCKVISIITLKDL 187
Cdd:TIGR00336 155 EFEKEYGLPVISLITLKDL 173
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
4-212 |
1.70e-78 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 233.51 E-value: 1.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 4 YQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAGLFNT-GRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTA 82
Cdd:COG0461 3 YKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSyPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 83 VAmaehhdLDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQErgr 161
Cdd:COG0461 83 RA------LGLPAIFVRKEAKDHGTGGQIEGGLLPGeRVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREE--- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 534751287 162 geiSAIQEVErDYNCKVISIITLKDLIAYLEEKPEMAE-HLAAVKAYREEFG 212
Cdd:COG0461 154 ---GAAENLE-EAGVPLHSLLTLDDLLELLKEKGYIDPeELEALEAYREKPG 201
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
49-166 |
1.78e-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: 72.43 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 49 LGRFYAEALVDSGIEFDLLFGPAYKGIPIATttavAMAEHhdLDLPYCFNRKEAKDHGEGG-------NLVGSALQG-RV 120
Cdd:cd06223 1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAA----ALARA--LGLPLAFIRKERKGPGRTPsepygleLPLGGDVKGkRV 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 534751287 121 MLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISA 166
Cdd:cd06223 75 LLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELAS 120
|
|
| PRK13809 |
PRK13809 |
orotate phosphoribosyltransferase; Provisional |
18-204 |
1.79e-11 |
|
orotate phosphoribosyltransferase; Provisional
Pssm-ID: 184340 Cd Length: 206 Bit Score: 61.01 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 18 LKFGEFTLKSGRKSPYFFNAGLFNTGRDL-----ALLGRfyaeaLVDSgIEFDLLFGPAYKGIPIATTTAVAMaehhdlD 92
Cdd:PRK13809 23 IKFGKFILASGEETPIYVDMRLVISSPEVlqtiaTLIWR-----LRPS-FNSSLLCGVPYTALTLATSISLKY------N 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 93 LPYCFNRKEAKDHGEGGNLVGSALQG---RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGrgeisaiQE 169
Cdd:PRK13809 91 IPMVLRRKELKNVDPSDAIKVEGLFTpgqTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKGA-------CQ 163
|
170 180 190
....*....|....*....|....*....|....*
gi 534751287 170 VERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAV 204
Cdd:PRK13809 164 PLGPQGIKLSSVFTVPDLIKSLISYGKLSSGDLTL 198
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
54-165 |
2.48e-10 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 57.57 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 54 AEALVD----SGIEFDLLFGPAYKGIPIATTtavaMAEHHDLDLPYCFNRKEakDHGEGGNLVGS------ALQG-RVML 122
Cdd:PRK02277 72 ASAMADmlekEDEEVDVVVGIAKSGVPLATL----VADELGKDLAIYHPKKW--DHGEGEKKTGSfsrnfaSVEGkRCVI 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 534751287 123 VDDVITAGTAIRESMEIIQANGAT--LAGVLISldrqERGRGEIS 165
Cdd:PRK02277 146 VDDVITSGTTMKETIEYLKEHGGKpvAVVVLID----KSGIDEID 186
|
|
| PRK05500 |
PRK05500 |
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase; |
18-159 |
6.20e-08 |
|
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
Pssm-ID: 180119 [Multi-domain] Cd Length: 477 Bit Score: 51.99 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 18 LKFGEFTLKSGRKSPYFF-------NAGLFNTgrdlALLGrfYAEALvdSGIEFDLLFGPAYKGIPiaTTTAVAMAEHHd 90
Cdd:PRK05500 300 LLFGEYVQASGATFSYYIdlrkiisNPQLFHQ----VLSA--YAEIL--KNLTFDRIAGIPYGSLP--TATGLALHLHH- 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 91 ldlPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQER 159
Cdd:PRK05500 369 ---PMIFPRKEVKAHGTRRLIEGNFHPGeTVVVVDDILITGKSVMEGAEKLKSAGLNVRDIVVFIDHEQG 435
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
39-175 |
2.86e-06 |
|
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: 45.43 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 39 LFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTAvamaehHDLDLPYCFNRKEAKDHGEGGNLVGSALQG 118
Cdd:pfam00156 5 ILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILA------RRLDVPLAFVRKVSYNPDTSEVMKTSSALP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 534751287 119 -----RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQE----------RGRGEISAIQEVERDYN 175
Cdd:pfam00156 79 dlkgkTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAgtepkdkydkRVDDWIVFVVGFGLDER 150
|
|
| Apt |
COG0503 |
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ... |
54-184 |
5.31e-06 |
|
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: 45.07 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 54 AEALVD--SGIEFDLLFGPAYKGIPIATTTAVAmaehhdLDLPYCFNRKEAK------------DHGEGGNLV--GSALQ 117
Cdd:COG0503 37 GDELAErfADKGIDKVVGIEARGFILAAALAYA------LGVPFVPARKPGKlpgetvseeydlEYGTGDTLElhKDALK 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534751287 118 G--RVMLVDDVITAGTAIRESMEIIQANGATLAG--VLISLDRQErGRGEIsaiqeveRDYNckVISIITL 184
Cdd:COG0503 111 PgdRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGiaFLIELGFLG-GREKL-------RDYP--VESLLTL 171
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
63-169 |
4.56e-05 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 42.27 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 63 EFDLLFGPAYKGIPIATttavAMAEHhdLDLPYCFNRKEAKDH--------------GEGGNLV-----GSALQG-RVML 122
Cdd:PRK07322 52 EVDVLVTPETKGIPLAH----ALSRR--LGKPYVVARKSRKPYmqdpiiqevvsittGKPQLLVldgadAEKLKGkRVAI 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 534751287 123 VDDVITAGTAIRESMEIIQANGATLAGVL-ISLDRQERGRGEISAIQE 169
Cdd:PRK07322 126 VDDVVSTGGTLTALERLVERAGGQVVAKAaIFAEGDASNRLDVIYLAH 173
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
33-184 |
1.86e-04 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 33 YFFNAGLFNTGRDLALLGRFYAEALvdSGIEFDLLFGPAYKGIPIAtttaVAMAEHHDLDLPYCFNRKE--------AKD 104
Cdd:PRK08558 83 YVDNSSVVFDPSFLRLIAPVVAERF--MGLRVDVVLTAATDGIPLA----VAIASYFGADLVYAKKSKEtgvekfyeEYQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534751287 105 HGEGGN-----LVGSALQ--GRVMLVDDVITAGTAIRESMEIIQANGATLAGV--LISldrqergRGEISaIQEVERDYN 175
Cdd:PRK08558 157 RLASGIevtlyLPASALKkgDRVLIVDDIIRSGETQRALLDLARQAGADVVGVffLIA-------VGEVG-IDRAREETD 228
|
....*....
gi 534751287 176 CKVISIITL 184
Cdd:PRK08558 229 APVDALYTL 237
|
|
| PRK06031 |
PRK06031 |
phosphoribosyltransferase; Provisional |
116-166 |
1.62e-03 |
|
phosphoribosyltransferase; Provisional
Pssm-ID: 235678 Cd Length: 233 Bit Score: 38.20 E-value: 1.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 534751287 116 LQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISA 166
Cdd:PRK06031 152 LEGrRVALIDDVISSGASIVAGLRLLAACGIEPAGIGAAMLQSERWRESLAA 203
|
|
| |
