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Conserved domains on  [gi|488286210|ref|WP_002357418|]
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MULTISPECIES: orotate phosphoribosyltransferase [Enterococcus]

Protein Classification

orotate phosphoribosyltransferase( domain architecture ID 10785483)

orotate phosphoribosyltransferase catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP)

CATH:  3.40.50.2020
EC:  2.4.2.-
Gene Ontology:  GO:0046132|GO:0004588|GO:0000287
PubMed:  11751055
SCOP:  4000253

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 5-206 2.26e-77

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


:

Pssm-ID: 440229  Cd Length: 201  Bit Score: 230.43  E-value: 2.26e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210   5 AKKIAKDLLDIEAVFLNPnepFTWASGIKSPIYCDNRITMSYPAVRKEIAEGLAAKIKETFPEVEVIAGTATAGIPHAAW 84
Cdd:COG0461    4 KEELAELLLEIGALLFGH---FTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  85 VADILGLPMVYIRSKAKDHGKGNQIEGRISEGQKMVVIEDLISTGGSVLEAAEAAEREGATVLGVAAIFTYElPKGTANF 164
Cdd:COG0461   81 VARALGLPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDRE-EGAAENL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488286210 165 ADKQMTLLTLTNYSTLIDAALEANYIEEKDVTLLQEWKKDPE 206
Cdd:COG0461  160 EEAGVPLHSLLTLDDLLELLKEKGYIDPEELEALEAYREKPG 201
 
Name Accession Description Interval E-value
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 5-206 2.26e-77

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 230.43  E-value: 2.26e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210   5 AKKIAKDLLDIEAVFLNPnepFTWASGIKSPIYCDNRITMSYPAVRKEIAEGLAAKIKETFPEVEVIAGTATAGIPHAAW 84
Cdd:COG0461    4 KEELAELLLEIGALLFGH---FTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  85 VADILGLPMVYIRSKAKDHGKGNQIEGRISEGQKMVVIEDLISTGGSVLEAAEAAEREGATVLGVAAIFTYElPKGTANF 164
Cdd:COG0461   81 VARALGLPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDRE-EGAAENL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488286210 165 ADKQMTLLTLTNYSTLIDAALEANYIEEKDVTLLQEWKKDPE 206
Cdd:COG0461  160 EEAGVPLHSLLTLDDLLELLKEKGYIDPEELEALEAYREKPG 201
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 1-207 1.94e-73

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 220.80  E-value: 1.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210   1 MTKVAKKIAKDLLDIEAVflnPNEPFTWASGIKSPIYCDNRITMSYPAVRKEIAEGLAAKIKETFPEVEVIAGTATAGIP 80
Cdd:PRK00455   1 MKMYAREFIEFLLEIGAL---LFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  81 HAAWVADILGLPMVYIRSKAKDHGKGNQIEGRISEGQKMVVIEDLISTGGSVLEAAEAAEREGATVLGVAAIFTYElPKG 160
Cdd:PRK00455  78 LAAAVARALDLPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ-SAA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488286210 161 TANFADKQMTLLTLTNYSTLIdAALEANYIEEKDVTLLQEWKKDPEN 207
Cdd:PRK00455 157 QEVFADAGVPLISLITLDDLL-EYAEEGPLCKEGLPAVKAYRRNYGV 202
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 12-180 4.12e-48

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: 155.28  E-value: 4.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210   12 LLDIEAVFLNPnepFTWASGIKSPIYCDNRITMSYPAVRKEIAEGLAAKIKETFpEVEVIAGTATAGIPHAAWVADIL-- 89
Cdd:TIGR00336   3 LLEVQALKFGE---FTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHL-EFDVIAGPALGGIPIATAVSVKLak 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210   90 ---GLPMVYIRSKAKDHGKGNQIEGRISEGQKMVVIEDLISTGGSVLEAAEAAEREGATVLGVAAIFTYELPKGTANFA- 165
Cdd:TIGR00336  79 pggDIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQERSAGQEFEk 158

                         170
                  ....*....|....*
gi 488286210  166 DKQMTLLTLTNYSTL 180
Cdd:TIGR00336 159 EYGLPVISLITLKDL 173
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 53-133 1.18e-15

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: 70.50  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  53 IAEGLAAKIKETFPEVEVIAGTATAGIPHAAWVADILGLPMVYIRSKAKDHGKGNQ-------IEGRISEGQKMVVIEDL 125
Cdd:cd06223    1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSepyglelPLGGDVKGKRVLLVDDV 80


                 ....*...
gi 488286210 126 ISTGGSVL 133
Cdd:cd06223   81 IATGGTLL 88
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 47-133 8.38e-08

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: 49.67  E-value: 8.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210   47 PAVRKEIAEgLAAKIKETFPEVE-VIAGTATAGIPHAAWVADILGLPMVYIRsKAKDHGKGNQIEGRIS-----EGQKMV 120
Cdd:pfam00156   9 PAILKAVAR-LAAQINEDYGGKPdVVVGILRGGLPFAGILARRLDVPLAFVR-KVSYNPDTSEVMKTSSalpdlKGKTVL 86

                          90
                  ....*....|...
gi 488286210  121 VIEDLISTGGSVL 133
Cdd:pfam00156  87 IVDDILDTGGTLL 99
 
Name Accession Description Interval E-value
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 5-206 2.26e-77

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 230.43  E-value: 2.26e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210   5 AKKIAKDLLDIEAVFLNPnepFTWASGIKSPIYCDNRITMSYPAVRKEIAEGLAAKIKETFPEVEVIAGTATAGIPHAAW 84
Cdd:COG0461    4 KEELAELLLEIGALLFGH---FTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  85 VADILGLPMVYIRSKAKDHGKGNQIEGRISEGQKMVVIEDLISTGGSVLEAAEAAEREGATVLGVAAIFTYElPKGTANF 164
Cdd:COG0461   81 VARALGLPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDRE-EGAAENL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488286210 165 ADKQMTLLTLTNYSTLIDAALEANYIEEKDVTLLQEWKKDPE 206
Cdd:COG0461  160 EEAGVPLHSLLTLDDLLELLKEKGYIDPEELEALEAYREKPG 201
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 1-207 1.94e-73

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 220.80  E-value: 1.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210   1 MTKVAKKIAKDLLDIEAVflnPNEPFTWASGIKSPIYCDNRITMSYPAVRKEIAEGLAAKIKETFPEVEVIAGTATAGIP 80
Cdd:PRK00455   1 MKMYAREFIEFLLEIGAL---LFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  81 HAAWVADILGLPMVYIRSKAKDHGKGNQIEGRISEGQKMVVIEDLISTGGSVLEAAEAAEREGATVLGVAAIFTYElPKG 160
Cdd:PRK00455  78 LAAAVARALDLPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ-SAA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488286210 161 TANFADKQMTLLTLTNYSTLIdAALEANYIEEKDVTLLQEWKKDPEN 207
Cdd:PRK00455 157 QEVFADAGVPLISLITLDDLL-EYAEEGPLCKEGLPAVKAYRRNYGV 202
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 12-180 4.12e-48

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: 155.28  E-value: 4.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210   12 LLDIEAVFLNPnepFTWASGIKSPIYCDNRITMSYPAVRKEIAEGLAAKIKETFpEVEVIAGTATAGIPHAAWVADIL-- 89
Cdd:TIGR00336   3 LLEVQALKFGE---FTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHL-EFDVIAGPALGGIPIATAVSVKLak 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210   90 ---GLPMVYIRSKAKDHGKGNQIEGRISEGQKMVVIEDLISTGGSVLEAAEAAEREGATVLGVAAIFTYELPKGTANFA- 165
Cdd:TIGR00336  79 pggDIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQERSAGQEFEk 158

                         170
                  ....*....|....*
gi 488286210  166 DKQMTLLTLTNYSTL 180
Cdd:TIGR00336 159 EYGLPVISLITLKDL 173
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 53-133 1.18e-15

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: 70.50  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  53 IAEGLAAKIKETFPEVEVIAGTATAGIPHAAWVADILGLPMVYIRSKAKDHGKGNQ-------IEGRISEGQKMVVIEDL 125
Cdd:cd06223    1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSepyglelPLGGDVKGKRVLLVDDV 80


                 ....*...
gi 488286210 126 ISTGGSVL 133
Cdd:cd06223   81 IATGGTLL 88
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
 26-133 1.02e-11

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 61.39  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  26 FTWASGIKSPIYCDNRITMSYPAVRKEIAEgLAAKIKETFPEvEVIAGTATAGIPHAAWVADILGLPMVYIRSKAKDHGK 105
Cdd:PRK13809  28 FILASGEETPIYVDMRLVISSPEVLQTIAT-LIWRLRPSFNS-SLLCGVPYTALTLATSISLKYNIPMVLRRKELKNVDP 105

                         90       100       110
                 ....*....|....*....|....*....|
gi 488286210 106 GNQI--EGRISEGQKMVVIEDLISTGGSVL 133
Cdd:PRK13809 106 SDAIkvEGLFTPGQTCLVINDMVSSGKSII 135
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
26-133 3.71e-11

bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 61.62  E-value: 3.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  26 FTWASGIKSPIYCDNRITMSYPAVRKEIAEGLAAKIKE-TFpevEVIAGTATAGIPHAAWVADILGLPMVYIRSKAKDHG 104
Cdd:PRK05500 305 YVQASGATFSYYIDLRKIISNPQLFHQVLSAYAEILKNlTF---DRIAGIPYGSLPTATGLALHLHHPMIFPRKEVKAHG 381

                         90       100
                 ....*....|....*....|....*....
gi 488286210 105 KGNQIEGRISEGQKMVVIEDLISTGGSVL 133
Cdd:PRK05500 382 TRRLIEGNFHPGETVVVVDDILITGKSVM 410
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 47-133 5.51e-11

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: 58.93  E-value: 5.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  47 PAVRKEIAEGLAAKIKETfpEVEVIAGTATAGIPHAAWVADILGLPMVYIRSKAK------------DHGKGNQIE---G 111
Cdd:COG0503   30 PELFRAAGDELAERFADK--GIDKVVGIEARGFILAAALAYALGVPFVPARKPGKlpgetvseeydlEYGTGDTLElhkD 107

                         90       100
                 ....*....|....*....|..
gi 488286210 112 RISEGQKMVVIEDLISTGGSVL 133
Cdd:COG0503  108 ALKPGDRVLIVDDLLATGGTAK 129
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 51-132 4.08e-09

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 54.10  E-value: 4.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  51 KEIAEGLAAKIKETFPEVEVIAGTATAGIPHAAWVADILGLPM-VYIRSKaKDHGKGNQIEGRIS------EGQKMVVIE 123
Cdd:PRK02277  69 RYIASAMADMLEKEDEEVDVVVGIAKSGVPLATLVADELGKDLaIYHPKK-WDHGEGEKKTGSFSrnfasvEGKRCVIVD 147


                 ....*....
gi 488286210 124 DLISTGGSV 132
Cdd:PRK02277 148 DVITSGTTM 156
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 51-154 3.55e-08

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 51.13  E-value: 3.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  51 KEIAEGLAAKIKetfPEVEVIAGTATAGIPHAAWVADILGLPMVYIRSKAKDH--------------GKGNQI--EGRIS 114
Cdd:PRK07322  39 EAAAEALAKRLP---TEVDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKPYmqdpiiqevvsittGKPQLLvlDGADA 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488286210 115 E---GQKMVVIEDLISTGGSVLEAAEAAEREGATVLGVAAIFT 154
Cdd:PRK07322 116 EklkGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAKAAIFA 158
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 47-133 8.38e-08

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: 49.67  E-value: 8.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210   47 PAVRKEIAEgLAAKIKETFPEVE-VIAGTATAGIPHAAWVADILGLPMVYIRsKAKDHGKGNQIEGRIS-----EGQKMV 120
Cdd:pfam00156   9 PAILKAVAR-LAAQINEDYGGKPdVVVGILRGGLPFAGILARRLDVPLAFVR-KVSYNPDTSEVMKTSSalpdlKGKTVL 86

                          90
                  ....*....|...
gi 488286210  121 VIEDLISTGGSVL 133
Cdd:pfam00156  87 IVDDILDTGGTLL 99
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 42-130 4.92e-06

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 45.07  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  42 IT--MSYPAVRKEIAEGLAAKIKETfpEVEVIAGTATAGIPHAAWVADILGLPMVYIRSKakdhGKG------------- 106
Cdd:PRK02304  26 ITplLADPEAFREVIDALVERYKDA--DIDKIVGIEARGFIFGAALAYKLGIGFVPVRKP----GKLpretisesyeley 99

                         90       100
                 ....*....|....*....|....*....
gi 488286210 107 --NQIE---GRISEGQKMVVIEDLISTGG 130
Cdd:PRK02304 100 gtDTLEihkDAIKPGDRVLIVDDLLATGG 128
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
 48-133 1.27e-04

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 41.66  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  48 AVRKEIAEGLAAKIKETfpEVEVIAGTATAGIPHAAWVADILG----LPMVYIRS--------------KAKDHGKGNQI 109
Cdd:PRK06031  67 EVLDALAEHLAEKARAF--DPDVVAGLPTLGLTLAAAVARKLGhtryVPLGTSRKfwyrdelsvplssiTTPDQGKRLYI 144

                         90       100
                 ....*....|....*....|....*..
gi 488286210 110 EGRIS---EGQKMVVIEDLISTGGSVL 133
Cdd:PRK06031 145 DPRMLpllEGRRVALIDDVISSGASIV 171
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 37-129 1.36e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 38.43  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286210  37 YCDNRITMSYPAVRKEIAEGLAakikETFP--EVEVIAGTATAGIPHAAWVADILGLPMVYIRsKAKDHGKGNQIEGR-- 112
Cdd:PRK08558  83 YVDNSSVVFDPSFLRLIAPVVA----ERFMglRVDVVLTAATDGIPLAVAIASYFGADLVYAK-KSKETGVEKFYEEYqr 157

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488286210 113 ---------------ISEGQKMVVIEDLISTG 129
Cdd:PRK08558 158 lasgievtlylpasaLKKGDRVLIVDDIIRSG 189
 
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.
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