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pur operon repressor [Streptococcus pyogenes]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
purR_Bsub super family cl31138
pur operon repressor, Bacillus subtilis type; This model represents the puring operon ...
 3-255 2.79e-131

pur operon repressor, Bacillus subtilis type; This model represents the puring operon repressor PurR of low-GC Gram-positive bacteria. This homodimeric repressor contains a large region homologous to phosphoribosyltransferases and is inhibited by 5-phosphoribosyl 1-pyrophosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis, Regulatory functions, DNA interactions]


The actual alignment was detected with superfamily member TIGR01743:

Pssm-ID: 130804 [Multi-domain]  Cd Length: 268  Bit Score: 372.58  E-value: 2.79e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147    3 LRRSERMVVISNYLINNPYKLTSLNTFATKYEAAKSSISEDIAIIKKAFEEANIGDIDTLTGASGGVIFTPSISETEART 82
Cdd:TIGR01743   1 LRRSGRLVDLTNYLITNPNKLIPLNFFSERYESAKSSISEDIVIIKETFEKFGIGKLLTVPGAAGGVKYIPKMSQAEAEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147   83 IVEDLCQRLSESDRILPGGYIYLSDLLSTPKILQNIGRIIANAFKGEKIDAVMTVATKGVPLANAVANILSVPFVIVRRD 162
Cdd:TIGR01743  81 FVEELCQSLSEPERILPGGYLYLTDILGKPSILSKIGKILASVFAEREIDAVMTVATKGIPLAYAVASVLNVPLVIVRKD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147  163 LKITEGSTVSVNYASASSDRIEKMFLSKRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAENAQSERE- 241
Cdd:TIGR01743 161 SKVTEGSTVSINYVSGSSNRIQTMSLAKRSLKTGSKVLIIDDFMKAGGTINGMINLLDEFDAEVAGIGVLIDNEGVDEKl 240

                         250
                  ....*....|....
gi 489082147  242 QMTFKSLLKVSEID 255
Cdd:TIGR01743 241 VDDYMSLLTLSNIN 254
 
Name Accession Description Interval E-value
purR_Bsub TIGR01743
pur operon repressor, Bacillus subtilis type; This model represents the puring operon ...
 3-255 2.79e-131

pur operon repressor, Bacillus subtilis type; This model represents the puring operon repressor PurR of low-GC Gram-positive bacteria. This homodimeric repressor contains a large region homologous to phosphoribosyltransferases and is inhibited by 5-phosphoribosyl 1-pyrophosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis, Regulatory functions, DNA interactions]


Pssm-ID: 130804 [Multi-domain]  Cd Length: 268  Bit Score: 372.58  E-value: 2.79e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147    3 LRRSERMVVISNYLINNPYKLTSLNTFATKYEAAKSSISEDIAIIKKAFEEANIGDIDTLTGASGGVIFTPSISETEART 82
Cdd:TIGR01743   1 LRRSGRLVDLTNYLITNPNKLIPLNFFSERYESAKSSISEDIVIIKETFEKFGIGKLLTVPGAAGGVKYIPKMSQAEAEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147   83 IVEDLCQRLSESDRILPGGYIYLSDLLSTPKILQNIGRIIANAFKGEKIDAVMTVATKGVPLANAVANILSVPFVIVRRD 162
Cdd:TIGR01743  81 FVEELCQSLSEPERILPGGYLYLTDILGKPSILSKIGKILASVFAEREIDAVMTVATKGIPLAYAVASVLNVPLVIVRKD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147  163 LKITEGSTVSVNYASASSDRIEKMFLSKRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAENAQSERE- 241
Cdd:TIGR01743 161 SKVTEGSTVSINYVSGSSNRIQTMSLAKRSLKTGSKVLIIDDFMKAGGTINGMINLLDEFDAEVAGIGVLIDNEGVDEKl 240

                         250
                  ....*....|....
gi 489082147  242 QMTFKSLLKVSEID 255
Cdd:TIGR01743 241 VDDYMSLLTLSNIN 254
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 85-234 3.08e-47

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: 155.23  E-value: 3.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147  85 EDLCQRLSESDRILPGG--YIYLSDLLSTPKILQNIGRIIANAFKGEKIDAVMTVATKGVPLANAVANILSVPFVIVRRD 162
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGilFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489082147 163 LKITeGSTVSVNYASASSdRIEKMFLSKRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAE 234
Cdd:COG0503   81 GKLP-GETVSEEYDLEYG-TGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIE 150
PuR_N pfam09182
Bacterial purine repressor, N-terminal; The N-terminal domain of the bacterial purine ...
 4-73 9.33e-32

Bacterial purine repressor, N-terminal; The N-terminal domain of the bacterial purine repressor PuR is a winged-helix domain, a subdivision of the HTH structural family. It consists of a canonical arrangement of secondary structures: a1-b1-a2-T-a3-b2-W-b3, where a2-T-a3 is the HTH motif, a3 is the recognition helix, and W is the wing. The domain allows for recognition of a conserved CGAA sequence in the centre of a DNA PurBox, resulting in binding to the major groove of DNA.


Pssm-ID: 430456  Cd Length: 70  Bit Score: 112.16  E-value: 9.33e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147    4 RRSERMVVISNYLINNPYKLTSLNTFATKYEAAKSSISEDIAIIKKAFEEANIGDIDTLTGASGGVIFTP 73
Cdd:pfam09182   1 KRSERLVAITKILLENPNKLISLTYFAERFGAAKSSISEDLVIIKEAFEKEGLGTIETIPGAAGGVKYIP 70
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 100-234 2.98e-16

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 74.34  E-value: 2.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 100 GGYIY--LSDLLSTPKILQNIGRIIANAFKGEKIDAVMTVATKGVPLANAVANILSVPFVIVRRDLKITEGsTVSVNYAS 177
Cdd:PRK02304  19 PGILFrdITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPGKLPRE-TISESYEL 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489082147 178 A-SSDRIEkmfLSKRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAE 234
Cdd:PRK02304  98 EyGTDTLE---IHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIE 152
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 118-234 1.00e-12

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: 63.57  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 118 IGRIIANAFK--GEKIDAVMTVATKGVPLANAVANILSVPFVIVRRDLKITEGSTVSVNyasassdrieKMFLSKRSLKP 195
Cdd:cd06223    1 AGRLLAEEIRedLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPY----------GLELPLGGDVK 70

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489082147 196 NSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAE 234
Cdd:cd06223   71 GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLD 109
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
112-255 3.18e-05

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 43.76  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 112 PKILQNIG-RIIANAfkGEKIDAVMTVATKGVPLANAVANILSVPFVIVRRDLKITEGStVSVNYASASSDriEKMFLSk 190
Cdd:NF040646  36 PELLREIAdRIIKIA--DLDVDKIVTVEAMGIPIATALSLKTDIPLVIIRKRKYGLPGE-VEVHQSTGYSK--GELYIN- 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 191 rSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAE--NAQSEREQMT---FKSLLKVSEID 255
Cdd:NF040646 110 -GINKGDRVLIVDDVISTGGTLIAVIKALEKAGAEIKDVVVVIErgEGKKIVEEKTgykVKTLVKIDVVD 178
 
Name Accession Description Interval E-value
purR_Bsub TIGR01743
pur operon repressor, Bacillus subtilis type; This model represents the puring operon ...
 3-255 2.79e-131

pur operon repressor, Bacillus subtilis type; This model represents the puring operon repressor PurR of low-GC Gram-positive bacteria. This homodimeric repressor contains a large region homologous to phosphoribosyltransferases and is inhibited by 5-phosphoribosyl 1-pyrophosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis, Regulatory functions, DNA interactions]


Pssm-ID: 130804 [Multi-domain]  Cd Length: 268  Bit Score: 372.58  E-value: 2.79e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147    3 LRRSERMVVISNYLINNPYKLTSLNTFATKYEAAKSSISEDIAIIKKAFEEANIGDIDTLTGASGGVIFTPSISETEART 82
Cdd:TIGR01743   1 LRRSGRLVDLTNYLITNPNKLIPLNFFSERYESAKSSISEDIVIIKETFEKFGIGKLLTVPGAAGGVKYIPKMSQAEAEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147   83 IVEDLCQRLSESDRILPGGYIYLSDLLSTPKILQNIGRIIANAFKGEKIDAVMTVATKGVPLANAVANILSVPFVIVRRD 162
Cdd:TIGR01743  81 FVEELCQSLSEPERILPGGYLYLTDILGKPSILSKIGKILASVFAEREIDAVMTVATKGIPLAYAVASVLNVPLVIVRKD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147  163 LKITEGSTVSVNYASASSDRIEKMFLSKRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAENAQSERE- 241
Cdd:TIGR01743 161 SKVTEGSTVSINYVSGSSNRIQTMSLAKRSLKTGSKVLIIDDFMKAGGTINGMINLLDEFDAEVAGIGVLIDNEGVDEKl 240

                         250
                  ....*....|....
gi 489082147  242 QMTFKSLLKVSEID 255
Cdd:TIGR01743 241 VDDYMSLLTLSNIN 254
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 85-234 3.08e-47

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: 155.23  E-value: 3.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147  85 EDLCQRLSESDRILPGG--YIYLSDLLSTPKILQNIGRIIANAFKGEKIDAVMTVATKGVPLANAVANILSVPFVIVRRD 162
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGilFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489082147 163 LKITeGSTVSVNYASASSdRIEKMFLSKRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAE 234
Cdd:COG0503   81 GKLP-GETVSEEYDLEYG-TGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIE 150
PuR_N pfam09182
Bacterial purine repressor, N-terminal; The N-terminal domain of the bacterial purine ...
 4-73 9.33e-32

Bacterial purine repressor, N-terminal; The N-terminal domain of the bacterial purine repressor PuR is a winged-helix domain, a subdivision of the HTH structural family. It consists of a canonical arrangement of secondary structures: a1-b1-a2-T-a3-b2-W-b3, where a2-T-a3 is the HTH motif, a3 is the recognition helix, and W is the wing. The domain allows for recognition of a conserved CGAA sequence in the centre of a DNA PurBox, resulting in binding to the major groove of DNA.


Pssm-ID: 430456  Cd Length: 70  Bit Score: 112.16  E-value: 9.33e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147    4 RRSERMVVISNYLINNPYKLTSLNTFATKYEAAKSSISEDIAIIKKAFEEANIGDIDTLTGASGGVIFTP 73
Cdd:pfam09182   1 KRSERLVAITKILLENPNKLISLTYFAERFGAAKSSISEDLVIIKEAFEKEGLGTIETIPGAAGGVKYIP 70
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 106-241 1.33e-20

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: 85.49  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147  106 SDLLSTPKILQNIGRIIANAF--KGEKIDAVMTVATKGVPLANAVANILSVPFVIVRRDLKITEGSTVSVNYasassdri 183
Cdd:pfam00156   3 DEILDNPAILKAVARLAAQINedYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTS-------- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489082147  184 ekmflSKRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAENAQSERE 241
Cdd:pfam00156  75 -----SALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEP 127
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 100-234 2.98e-16

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 74.34  E-value: 2.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 100 GGYIY--LSDLLSTPKILQNIGRIIANAFKGEKIDAVMTVATKGVPLANAVANILSVPFVIVRRDLKITEGsTVSVNYAS 177
Cdd:PRK02304  19 PGILFrdITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPGKLPRE-TISESYEL 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489082147 178 A-SSDRIEkmfLSKRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAE 234
Cdd:PRK02304  98 EyGTDTLE---IHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIE 152
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 76-242 1.97e-14

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 70.79  E-value: 1.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147  76 SETEARTIVEDLCQRLSESD------RILPGGYIYLSDLLSTPKILQNIGRIIANAFKGEKIDAVMTVATKGVPLANAVA 149
Cdd:PRK08558  51 SVERAREIVEKLGPYYNLEEevkariKVDDEGYVDNSSVVFDPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 150 NILSVPFVIVRRDlKITEGSTVSVNYASASSDRIEKMFLSKRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVG- 228
Cdd:PRK08558 131 SYFGADLVYAKKS-KETGVEKFYEEYQRLASGIEVTLYLPASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGv 209

                        170
                 ....*....|....*..
gi 489082147 229 ---VAVFAENAQSEREQ 242
Cdd:PRK08558 210 fflIAVGEVGIDRAREE 226
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 96-245 2.14e-14

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 69.62  E-value: 2.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147  96 RILPGGYIYLSDLLSTPKILQNIGRIIANAFKGEkIDAVMTVATKGVPLANAVANILSVPFVIVRRDLKITEGSTVSVNY 175
Cdd:PRK07322  19 RVGPDLAIALFVILGDTELTEAAAEALAKRLPTE-VDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKPYMQDPIIQEV 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489082147 176 ASASSDRIEKMFLSKR---SLKpNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGV-AVFAENAQSEREQMTF 245
Cdd:PRK07322  98 VSITTGKPQLLVLDGAdaeKLK-GKRVAIVDDVVSTGGTLTALERLVERAGGQVVAKaAIFAEGDASNRLDVIY 170
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 108-254 3.36e-14

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 69.41  E-value: 3.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 108 LLSTPKILQNIGRIIANAFK--GEKIDAVMTVATKGVPLANAVANILSVPFVIVRRDLKiTEGSTVsvnyasassdRIEk 185
Cdd:COG0461   39 VLSYPEALELLGEALAELIKelGPEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAK-DHGTGG----------QIE- 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489082147 186 mflskRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFA---ENAQS--EREQMTFKSLLKVSEI 254
Cdd:COG0461  107 -----GGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVdreEGAAEnlEEAGVPLHSLLTLDDL 175
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 85-229 2.73e-13

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 66.73  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147  85 EDLCQRLSESDRILPGGYIYLSDLLS---TPKILQNIGRIIANAFKGEKIDAVMTVATKGVPLANAVANILSVPFVIVR- 160
Cdd:PRK09219   2 KLLEERILKDGKVLSGNILKVDSFLNhqvDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAKk 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 161 -RDLKITEGSTVSVNYaSASSDRIEKMFLSKRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGV 229
Cdd:PRK09219  82 kKSLTLTDDVYTATVY-SFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGI 150
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 108-254 7.11e-13

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 65.95  E-value: 7.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 108 LLSTPKILQNIGRIIANAFK--GEKIDAVMTVATKGVPLANAVANILSVPFVIVRRDLKI--TEGstvsvnyasassdRI 183
Cdd:PRK00455  40 LLSYPEALALLGRFLAEAIKdsGIEFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAKDhgEGG-------------QI 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489082147 184 EkmflskRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFA--ENAQSEREQ---MTFKSLLKVSEI 254
Cdd:PRK00455 107 E------GRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVdrQSAAQEVFAdagVPLISLITLDDL 176
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 118-234 1.00e-12

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: 63.57  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 118 IGRIIANAFK--GEKIDAVMTVATKGVPLANAVANILSVPFVIVRRDLKITEGSTVSVNyasassdrieKMFLSKRSLKP 195
Cdd:cd06223    1 AGRLLAEEIRedLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPY----------GLELPLGGDVK 70

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489082147 196 NSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAE 234
Cdd:cd06223   71 GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLD 109
PLN02293 PLN02293
adenine phosphoribosyltransferase
 89-230 1.75e-09

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 55.84  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147  89 QRLSESDRILP-----GGYIY-LSDLLSTPKILQNIGRIIANAFKGEKIDAVMTVATKGVPLANAVANILSVPFVIVRRD 162
Cdd:PLN02293  15 QGISSAIRVVPdfpkpGIMFQdITTLLLDPKAFKDTIDLFVERYRDMGISVVAGIEARGFIFGPPIALAIGAKFVPLRKP 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489082147 163 LKITeGSTVSVNYASA-SSDRIEkmfLSKRSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVA 230
Cdd:PLN02293  95 GKLP-GEVISEEYVLEyGTDCLE---MHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECA 159
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 115-255 1.82e-07

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 50.25  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 115 LQNIGRIIANAF--KGEKIDAVMTVATKGVPLANAVANILSVPFVIVR------RDLKITEGStVSVNYASASsdriekm 186
Cdd:PRK02277  68 LRYIASAMADMLekEDEEVDVVVGIAKSGVPLATLVADELGKDLAIYHpkkwdhGEGEKKTGS-FSRNFASVE------- 139

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 187 flskrslkpNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAE-NAQSEREQMTFKSLLKVSEID 255
Cdd:PRK02277 140 ---------GKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDkSGIDEIDGVPVYSLIRVVRVD 200
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 130-221 1.58e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 44.39  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 130 KIDAVMTVATKGVPLANAVANILSVPFVIVRR-DLKITEGSTVSVNYasaSSDRIE-KMFLSkrSLKPNSRVLIVDDFLK 207
Cdd:PRK12560  51 DIDKIVTEEDKGAPLATPVSLLSGKPLAMARWyPYSLSELNYNVVEI---GSEYFEgVVYLN--GIEKGDRVAIIDDTLS 125

                         90
                 ....*....|....
gi 489082147 208 GGGTITGMISLLTE 221
Cdd:PRK12560 126 TGGTVIALIKAIEN 139
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
112-255 3.18e-05

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 43.76  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 112 PKILQNIG-RIIANAfkGEKIDAVMTVATKGVPLANAVANILSVPFVIVRRDLKITEGStVSVNYASASSDriEKMFLSk 190
Cdd:NF040646  36 PELLREIAdRIIKIA--DLDVDKIVTVEAMGIPIATALSLKTDIPLVIIRKRKYGLPGE-VEVHQSTGYSK--GELYIN- 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 191 rSLKPNSRVLIVDDFLKGGGTITGMISLLTEFDSTLVGVAVFAE--NAQSEREQMT---FKSLLKVSEID 255
Cdd:NF040646 110 -GINKGDRVLIVDDVISTGGTLIAVIKALEKAGAEIKDVVVVIErgEGKKIVEEKTgykVKTLVKIDVVD 178
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
 130-240 5.71e-04

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 40.51  E-value: 5.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 130 KIDAVMTVATKGVPLANAVANILS----VPFVIVRrdlKITEGSTVSVNYASASSDRIEKM-FLSKR--SLKPNSRVLIV 202
Cdd:PRK06031  84 DPDVVAGLPTLGLTLAAAVARKLGhtryVPLGTSR---KFWYRDELSVPLSSITTPDQGKRlYIDPRmlPLLEGRRVALI 160

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489082147 203 DDFLKGGGTITGMISLLTEFDSTLVGVAVFAEnaQSER 240
Cdd:PRK06031 161 DDVISSGASIVAGLRLLAACGIEPAGIGAAML--QSER 196
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 128-238 3.94e-03

Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 441837 [Multi-domain]  Cd Length: 153  Bit Score: 37.13  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082147 128 GEKIDAVMTVATKGVPLANAVANILSVPFVIvrrdlkitegsTVSVNYASASSDRIEKMFLSK---RSLKpNSRVLIVDD 204
Cdd:COG2236   29 GFRPDVIVAIARGGLVPARILADALGVPDLA-----------SIRVSSYTGTAKRLEEPVVKGpldEDLA-GKRVLIVDD 96

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489082147 205 FLKGGGTITGMISLLTEFDSTLVGVAVFAENAQS 238
Cdd:COG2236   97 VADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSS 130
 
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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