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Conserved domains on  [gi|297820126|ref|XP_002877946|]
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uracil phosphoribosyltransferase, chloroplastic [Arabidopsis lyrata subsp. lyrata]

Protein Classification

type I phosphoribosyltransferase; uracil phosphoribosyltransferase( domain architecture ID 10010821)

type I phosphoribosyltransferase similar to phosphoribosyltransferases with specificities for hypoxanthine, guanine, and/or xanthine| uracil phosphoribosyltransferase catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02541 PLN02541
uracil phosphoribosyltransferase
 47-289 2.90e-160

uracil phosphoribosyltransferase


:

Pssm-ID: 215297  Cd Length: 244  Bit Score: 445.77  E-value: 2.90e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126  47 LGASSSSVSRRTIRVRAKMAASEGSINGSNRMLVFVPPHPLIKHWISVLRNDQTPCPIFRNAIAELGRLLMYEAAREWLP 126
Cdd:PLN02541   1 VAPSRSSRLTRTVRASADAAASEPSPKAPQQMLVFVPPHPLIKHWLSVLRNEQTPPPIFRSAMAELGRLLIYEASRDWLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 127 TVVGEIMSPMGPASVEFIDPREPIAVVPILRAGLALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFPKNSRV 206
Cdd:PLN02541  81 TMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSMYLNKLPDKFPEGSRV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 207 FLVDPVLATGGTIMAAMDLLKERGLSVQQIKVICAIAAPPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRS 286
Cdd:PLN02541 161 LVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNEKGYIVPGLGDAGDRS 240


                 ...
gi 297820126 287 FGT 289
Cdd:PLN02541 241 FGT 243
 
Name Accession Description Interval E-value
PLN02541 PLN02541
uracil phosphoribosyltransferase
 47-289 2.90e-160

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 445.77  E-value: 2.90e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126  47 LGASSSSVSRRTIRVRAKMAASEGSINGSNRMLVFVPPHPLIKHWISVLRNDQTPCPIFRNAIAELGRLLMYEAAREWLP 126
Cdd:PLN02541   1 VAPSRSSRLTRTVRASADAAASEPSPKAPQQMLVFVPPHPLIKHWLSVLRNEQTPPPIFRSAMAELGRLLIYEASRDWLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 127 TVVGEIMSPMGPASVEFIDPREPIAVVPILRAGLALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFPKNSRV 206
Cdd:PLN02541  81 TMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSMYLNKLPDKFPEGSRV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 207 FLVDPVLATGGTIMAAMDLLKERGLSVQQIKVICAIAAPPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRS 286
Cdd:PLN02541 161 LVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNEKGYIVPGLGDAGDRS 240


                 ...
gi 297820126 287 FGT 289
Cdd:PLN02541 241 FGT 243
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 80-290 7.87e-97

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


Pssm-ID: 439805  Cd Length: 209  Bit Score: 283.88  E-value: 7.87e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126  80 VFVPPHPLIKHWISVLRNDQTPCPIFRNAIAELGRLLMYEAAREwLPTVVGEIMSPMGPASVEFIDpREPIAVVPILRAG 159
Cdd:COG0035    4 VHVVDHPLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRD-LPLEEVEVETPLGKTTGKVLA-GKKLVIVPILRAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 160 LALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFpKNSRVFLVDPVLATGGTIMAAMDLLKERGlsVQQIKVI 239
Cdd:COG0035   82 LGMLDGVLDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDL-EGRTVIVLDPMLATGGSLVAAIDLLKKRG--AKDIKIV 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 297820126 240 CAIAAPPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRSFGTD 290
Cdd:COG0035  159 CLIAAPEGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 84-289 1.11e-87

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


Pssm-ID: 434124  Cd Length: 204  Bit Score: 260.12  E-value: 1.11e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126   84 PHPLIKHWISVLRNDQTPCPIFRNAIAELGRLLMYEAAREwLPTVVGEIMSPMGPASVEFIDPREPIAVVPILRAGLALA 163
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRD-LPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGME 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126  164 EHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFPkNSRVFLVDPVLATGGTIMAAMDLLKERGLSVQQIKVICAIA 243
Cdd:pfam14681  80 DGLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDIS-DRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 297820126  244 APPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRSFGT 289
Cdd:pfam14681 159 APEGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 80-289 1.42e-83

uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees separates this mostly prokaryotic set of uracil phosphoribosyltransferases from a mostly eukaryotic set that includes uracil phosphoribosyltransferase, uridine kinases, and other, uncharacterized proteins. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273438  Cd Length: 207  Bit Score: 249.85  E-value: 1.42e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126   80 VFVPPHPLIKHWISVLRNDQTPCPIFRNAIAELGRLLMYEAAReWLPTVVGEIMSPMGPASVEFIDPREpIAVVPILRAG 159
Cdd:TIGR01091   2 VVVVDHPLIKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATR-DLELEEVEVETPLGETEGGRILGKK-IVLVPILRAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126  160 LALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFPKnSRVFLVDPVLATGGTIMAAMDLLKERGlsVQQIKVI 239
Cdd:TIGR01091  80 LGMVDGVLKLIPEAKVGHVGAYRNEETLKPVPYYSKLPEDIDE-RTVIVLDPMLATGGTMIAALDLLKKRG--PKKIKVL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 297820126  240 CAIAAPPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRSFGT 289
Cdd:TIGR01091 157 SIVAAPEGIEAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 145-265 4.59e-20

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: 83.98  E-value: 4.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 145 DPREPIAVVPILRAGLALAEHASSVLPAnKIYHLGVSRDEKTLLPSVYLNKL--PDEFPKNSRVFLVDPVLATGGTIMAA 222
Cdd:cd06223   12 DLLEPDVVVGILRGGLPLAAALARALGL-PLAFIRKERKGPGRTPSEPYGLElpLGGDVKGKRVLLVDDVIATGGTLLAA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 297820126 223 MDLLKERGLSVqqIKVICAIAAPPALsKLNEKFPGLHVYAGII 265
Cdd:cd06223   91 IELLKEAGAKV--VGVAVLLDKPEGG-ARELASPGDPVYSLFT 130
 
Name Accession Description Interval E-value
PLN02541 PLN02541
uracil phosphoribosyltransferase
 47-289 2.90e-160

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 445.77  E-value: 2.90e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126  47 LGASSSSVSRRTIRVRAKMAASEGSINGSNRMLVFVPPHPLIKHWISVLRNDQTPCPIFRNAIAELGRLLMYEAAREWLP 126
Cdd:PLN02541   1 VAPSRSSRLTRTVRASADAAASEPSPKAPQQMLVFVPPHPLIKHWLSVLRNEQTPPPIFRSAMAELGRLLIYEASRDWLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 127 TVVGEIMSPMGPASVEFIDPREPIAVVPILRAGLALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFPKNSRV 206
Cdd:PLN02541  81 TMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSMYLNKLPDKFPEGSRV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 207 FLVDPVLATGGTIMAAMDLLKERGLSVQQIKVICAIAAPPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRS 286
Cdd:PLN02541 161 LVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNEKGYIVPGLGDAGDRS 240


                 ...
gi 297820126 287 FGT 289
Cdd:PLN02541 241 FGT 243
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 80-290 7.87e-97

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


Pssm-ID: 439805  Cd Length: 209  Bit Score: 283.88  E-value: 7.87e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126  80 VFVPPHPLIKHWISVLRNDQTPCPIFRNAIAELGRLLMYEAAREwLPTVVGEIMSPMGPASVEFIDpREPIAVVPILRAG 159
Cdd:COG0035    4 VHVVDHPLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRD-LPLEEVEVETPLGKTTGKVLA-GKKLVIVPILRAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 160 LALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFpKNSRVFLVDPVLATGGTIMAAMDLLKERGlsVQQIKVI 239
Cdd:COG0035   82 LGMLDGVLDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDL-EGRTVIVLDPMLATGGSLVAAIDLLKKRG--AKDIKIV 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 297820126 240 CAIAAPPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRSFGTD 290
Cdd:COG0035  159 CLIAAPEGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 77-289 3.40e-95

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 279.67  E-value: 3.40e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126  77 RMLVFVPPHPLIKHWISVLRNDQTPCPIFRNAIAELGRLLMYEAAREwLPTVVGEIMSPMGPASVEFIDpREPIAVVPIL 156
Cdd:PRK00129   1 MMKVHVVDHPLIQHKLTLLRDKNTSTKRFRELLEELGRLLAYEATRD-LPLEEVEIETPLGKTTGKRIA-GKKLVIVPIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 157 RAGLALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFpKNSRVFLVDPVLATGGTIMAAMDLLKERGlsVQQI 236
Cdd:PRK00129  79 RAGLGMVDGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDI-DERTVIVVDPMLATGGSAIAAIDLLKKRG--AKNI 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 297820126 237 KVICAIAAPPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRSFGT 289
Cdd:PRK00129 156 KVLCLVAAPEGIKALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 84-289 1.11e-87

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


Pssm-ID: 434124  Cd Length: 204  Bit Score: 260.12  E-value: 1.11e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126   84 PHPLIKHWISVLRNDQTPCPIFRNAIAELGRLLMYEAAREwLPTVVGEIMSPMGPASVEFIDPREPIAVVPILRAGLALA 163
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRD-LPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGME 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126  164 EHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFPkNSRVFLVDPVLATGGTIMAAMDLLKERGLSVQQIKVICAIA 243
Cdd:pfam14681  80 DGLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDIS-DRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 297820126  244 APPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRSFGT 289
Cdd:pfam14681 159 APEGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 80-289 1.42e-83

uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees separates this mostly prokaryotic set of uracil phosphoribosyltransferases from a mostly eukaryotic set that includes uracil phosphoribosyltransferase, uridine kinases, and other, uncharacterized proteins. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273438  Cd Length: 207  Bit Score: 249.85  E-value: 1.42e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126   80 VFVPPHPLIKHWISVLRNDQTPCPIFRNAIAELGRLLMYEAAReWLPTVVGEIMSPMGPASVEFIDPREpIAVVPILRAG 159
Cdd:TIGR01091   2 VVVVDHPLIKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATR-DLELEEVEVETPLGETEGGRILGKK-IVLVPILRAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126  160 LALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDEFPKnSRVFLVDPVLATGGTIMAAMDLLKERGlsVQQIKVI 239
Cdd:TIGR01091  80 LGMVDGVLKLIPEAKVGHVGAYRNEETLKPVPYYSKLPEDIDE-RTVIVLDPMLATGGTMIAALDLLKKRG--PKKIKVL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 297820126  240 CAIAAPPALSKLNEKFPGLHVYAGIIDPEVNEKGYIIPGLGDAGDRSFGT 289
Cdd:TIGR01091 157 SIVAAPEGIEAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 145-265 4.59e-20

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: 83.98  E-value: 4.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 145 DPREPIAVVPILRAGLALAEHASSVLPAnKIYHLGVSRDEKTLLPSVYLNKL--PDEFPKNSRVFLVDPVLATGGTIMAA 222
Cdd:cd06223   12 DLLEPDVVVGILRGGLPLAAALARALGL-PLAFIRKERKGPGRTPSEPYGLElpLGGDVKGKRVLLVDDVIATGGTLLAA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 297820126 223 MDLLKERGLSVqqIKVICAIAAPPALsKLNEKFPGLHVYAGII 265
Cdd:cd06223   91 IELLKEAGAKV--VGVAVLLDKPEGG-ARELASPGDPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 145-245 1.32e-15

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: 72.40  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126  145 DPREPIAVVPILRAGLALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKLPDefPKNSRVFLVDPVLATGGTIMAAMD 224
Cdd:pfam00156  26 YGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTSSALPD--LKGKTVLIVDDILDTGGTLLKVLE 103

                          90       100
                  ....*....|....*....|.
gi 297820126  225 LLKERGlsVQQIKVICAIAAP 245
Cdd:pfam00156 104 LLKNVG--PKEVKIAVLIDKP 122
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 176-262 4.56e-08

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 52.00  E-value: 4.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 176 YHLGVSRDEktllpsVYLNKlpDEFPKNSRVFLVDPVLATGGTIMAAMDLLKERGlsvqqiKVICAIAAPPALSKLN--E 253
Cdd:PRK02304  95 YELEYGTDT------LEIHK--DAIKPGDRVLIVDDLLATGGTLEAAIKLLERLG------AEVVGAAFVIELPDLGgrE 160


                 ....*....
gi 297820126 254 KFPGLHVYA 262
Cdd:PRK02304 161 KLEGYPVKS 169
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 197-254 6.37e-07

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: 48.53  E-value: 6.37e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 297820126 197 PDEFPKNSRVFLVDPVLATGGTIMAAMDLLKERGLSVQQIKVICAIAAPPALSKLNEK 254
Cdd:COG0503  106 KDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKLRDY 163
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 206-253 1.10e-05

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: 46.12  E-value: 1.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 297820126  206 VFLVDPVLATGGTIMAAMDLLKERGLSvqqiKVICAIAAP----PALSKLNE 253
Cdd:TIGR01251 213 VVIVDDIIDTGGTIAKAAEILKSAGAK----RVIAAATHGvfsgPAIERIAN 260
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 205-253 3.52e-04

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: 41.58  E-value: 3.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 297820126 205 RVFLVDPVLATGGTIMAAMDLLKERGLSvqqiKVICAIA----APPALSKLNE 253
Cdd:COG0462  213 TCIIVDDMIDTGGTLVEAAEALKEAGAK----SVYAAAThgvlSGPAVERLEN 261
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 138-240 4.59e-04

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 41.05  E-value: 4.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 138 PASVEFI--DPREPIAVVPIlRAGLALAEHASSVLPAnKIYHLgvsrdEKTLL-PSVYLNKLPDEFPKNSRVFLVDPVLA 214
Cdd:PRK00934 143 PLIAEYIgdKLDDPLVLAPD-KGALELAKEAAEILGC-EYDYL-----EKTRIsPTEVEIAPKNLDVKGKDVLIVDDIIS 215

                         90       100
                 ....*....|....*....|....*.
gi 297820126 215 TGGTIMAAMDLLKERGLSvqQIKVIC 240
Cdd:PRK00934 216 TGGTMATAIKILKEQGAK--KVYVAC 239
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
161-251 5.03e-04

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 441529  Cd Length: 209  Bit Score: 40.44  E-value: 5.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 161 ALAEHASSVLPANKIYHLGVSRDEKTLLPSVYLNKL-----------PDEFPKNSRVFLVDPVLATGGTIMAAMDLLKER 229
Cdd:COG1926   68 AVAEDGVVVLNEDLIRRLGISEEYIEAEKAREREELerrrrryrggrPPPDLKGRTVILVDDGIATGATMRAALRALRRQ 147

                         90       100
                 ....*....|....*....|....
gi 297820126 230 GLSvqqiKVICAI--AAPPALSKL 251
Cdd:COG1926  148 GPA----RIVVAVpvAPPDTLEEL 167
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 206-289 9.27e-04

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 40.32  E-value: 9.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297820126 206 VFLVDPVLATGGTIMAAMDLLKERGLSvqqiKVICAIAAP---PALSKLNEKFpglhvyagiidpevnEKGYIipglgda 282
Cdd:PRK06827 267 VLIVDDMIASGGSMIDAAKELKSRGAK----KIIVAATFGfftNGLEKFDKAY---------------EEGYF------- 320


                 ....*..
gi 297820126 283 gDRSFGT 289
Cdd:PRK06827 321 -DRIIGT 326
PLN02293 PLN02293
adenine phosphoribosyltransferase
 202-245 1.14e-03

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 39.27  E-value: 1.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 297820126 202 KNSRVFLVDPVLATGGTIMAAMDLLKERGLSVqqIKVICAIAAP 245
Cdd:PLN02293 124 PGERALVIDDLIATGGTLCAAINLLERAGAEV--VECACVIELP 165
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 200-242 4.45e-03

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 37.44  E-value: 4.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 297820126 200 FPKNSRVFLVDPVLATGGTIMAAMDLLKERGLSVqqIKVICAI 242
Cdd:COG0461  109 LLPGERVLVVEDVITTGGSVLEAVEALREAGAEV--VGVAVIV 149
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 202-242 8.36e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 36.69  E-value: 8.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 297820126 202 KNSRVFLVDPVLATGGTIMAAMDLLKERGLSVQqiKVICAI 242
Cdd:PRK12560 113 KGDRVAIIDDTLSTGGTVIALIKAIENSGGIVS--DVICVI 151
 
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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