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Conserved domains on  [gi|1799599438|gb|QHN26562|]
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bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR [Gordonia pseudamarae]

Protein Classification

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase( domain architecture ID 10788351)

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PyrR COG2065
Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide ...
11-185 6.21e-93

Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


:

Pssm-ID: 441668  Cd Length: 178  Bit Score: 268.46  E-value: 6.21e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  11 RVLLDAADVSRTIARVAHQVIEKTaldaPDAPHVVLIGIPTRGTALAKRLGAKISEFAGTDIPVGYLDITLYRDDLRDKP 90
Cdd:COG2065     4 KEILDAADIDRALTRIAHEIIERN----KGLEDLVLVGIQTRGVPLAERLAERIEEIEGVKVPVGSLDITLYRDDLRRRP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  91 HRP-LERTMVPAGgVDGAIVILVDDVLYSGRTVRAALDALRDLGRPAAVQLAVLVDRGHRELPLRADYVGKNIPTAREEN 169
Cdd:COG2065    80 PRPvVNETEIPFD-IDGKTVVLVDDVLYTGRTVRAALDALMDFGRPAKIQLAVLVDRGHRELPIRADYVGKNVPTSRSER 158
                         170
                  ....*....|....*.
gi 1799599438 170 VAVHLTEHDGVDEVVL 185
Cdd:COG2065   159 VEVRLKEIDGEDAVVI 174
 
Name Accession Description Interval E-value
PyrR COG2065
Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide ...
11-185 6.21e-93

Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 441668  Cd Length: 178  Bit Score: 268.46  E-value: 6.21e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  11 RVLLDAADVSRTIARVAHQVIEKTaldaPDAPHVVLIGIPTRGTALAKRLGAKISEFAGTDIPVGYLDITLYRDDLRDKP 90
Cdd:COG2065     4 KEILDAADIDRALTRIAHEIIERN----KGLEDLVLVGIQTRGVPLAERLAERIEEIEGVKVPVGSLDITLYRDDLRRRP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  91 HRP-LERTMVPAGgVDGAIVILVDDVLYSGRTVRAALDALRDLGRPAAVQLAVLVDRGHRELPLRADYVGKNIPTAREEN 169
Cdd:COG2065    80 PRPvVNETEIPFD-IDGKTVVLVDDVLYTGRTVRAALDALMDFGRPAKIQLAVLVDRGHRELPIRADYVGKNVPTSRSER 158
                         170
                  ....*....|....*.
gi 1799599438 170 VAVHLTEHDGVDEVVL 185
Cdd:COG2065   159 VEVRLKEIDGEDAVVI 174
PRK05205 PRK05205
bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;
11-185 8.57e-88

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;


Pssm-ID: 235365  Cd Length: 176  Bit Score: 255.44  E-value: 8.57e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  11 RVLLDAADVSRTIARVAHQVIEKtaldAPDAPHVVLIGIPTRGTALAKRLGAKISEFAGTDIPVGYLDITLYRDDLRDK- 89
Cdd:PRK05205    4 KEILDAEALRRALTRIAHEIIER----NKGLDNLVLVGIKTRGVWLAERLAERLEQLEGVDVPVGELDITLYRDDLTKKg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  90 PHRPLERTMVPAGgVDGAIVILVDDVLYSGRTVRAALDALRDLGRPAAVQLAVLVDRGHRELPLRADYVGKNIPTAREEN 169
Cdd:PRK05205   80 LHPQVKPTDIPFD-IEGKRVILVDDVLYTGRTIRAALDALFDYGRPARVQLAVLVDRGHRELPIRADYVGKNIPTSRDER 158
                         170
                  ....*....|....*.
gi 1799599438 170 VAVHLTEHDGVDEVVL 185
Cdd:PRK05205  159 VVVRLAEVDGRDRVVL 174
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
44-158 1.15e-13

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: 65.08  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  44 VVLIGIPTRGTALAKRLGAKIsefagtDIPVGYLDITLYRDDLRdkphrPLERTMVPAGGVDGAIVILVDDVLYSGRTVR 123
Cdd:pfam00156  31 DVVVGILRGGLPFAGILARRL------DVPLAFVRKVSYNPDTS-----EVMKTSSALPDLKGKTVLIVDDILDTGGTLL 99
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1799599438 124 AALDALRDLGrPAAVQLAVLVDRGHRELPLRADYV 158
Cdd:pfam00156 100 KVLELLKNVG-PKEVKIAVLIDKPAGTEPKDKYDK 133
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
44-149 1.50e-11

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: 58.95  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  44 VVLIGIPTRGTALAKRLGAKIsefagtDIPVGYLDITLYRDDLrdKPHRPLERTMVPAGGVDGAIVILVDDVLYSGRTVR 123
Cdd:cd06223    17 DVVVGILRGGLPLAAALARAL------GLPLAFIRKERKGPGR--TPSEPYGLELPLGGDVKGKRVLLVDDVIATGGTLL 88
                          90       100
                  ....*....|....*....|....*.
gi 1799599438 124 AALDALRDLGrPAAVQLAVLVDRGHR 149
Cdd:cd06223    89 AAIELLKEAG-AKVVGVAVLLDKPEG 113
 
Name Accession Description Interval E-value
PyrR COG2065
Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide ...
11-185 6.21e-93

Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 441668  Cd Length: 178  Bit Score: 268.46  E-value: 6.21e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  11 RVLLDAADVSRTIARVAHQVIEKTaldaPDAPHVVLIGIPTRGTALAKRLGAKISEFAGTDIPVGYLDITLYRDDLRDKP 90
Cdd:COG2065     4 KEILDAADIDRALTRIAHEIIERN----KGLEDLVLVGIQTRGVPLAERLAERIEEIEGVKVPVGSLDITLYRDDLRRRP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  91 HRP-LERTMVPAGgVDGAIVILVDDVLYSGRTVRAALDALRDLGRPAAVQLAVLVDRGHRELPLRADYVGKNIPTAREEN 169
Cdd:COG2065    80 PRPvVNETEIPFD-IDGKTVVLVDDVLYTGRTVRAALDALMDFGRPAKIQLAVLVDRGHRELPIRADYVGKNVPTSRSER 158
                         170
                  ....*....|....*.
gi 1799599438 170 VAVHLTEHDGVDEVVL 185
Cdd:COG2065   159 VEVRLKEIDGEDAVVI 174
PRK05205 PRK05205
bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;
11-185 8.57e-88

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;


Pssm-ID: 235365  Cd Length: 176  Bit Score: 255.44  E-value: 8.57e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  11 RVLLDAADVSRTIARVAHQVIEKtaldAPDAPHVVLIGIPTRGTALAKRLGAKISEFAGTDIPVGYLDITLYRDDLRDK- 89
Cdd:PRK05205    4 KEILDAEALRRALTRIAHEIIER----NKGLDNLVLVGIKTRGVWLAERLAERLEQLEGVDVPVGELDITLYRDDLTKKg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  90 PHRPLERTMVPAGgVDGAIVILVDDVLYSGRTVRAALDALRDLGRPAAVQLAVLVDRGHRELPLRADYVGKNIPTAREEN 169
Cdd:PRK05205   80 LHPQVKPTDIPFD-IEGKRVILVDDVLYTGRTIRAALDALFDYGRPARVQLAVLVDRGHRELPIRADYVGKNIPTSRDER 158
                         170
                  ....*....|....*.
gi 1799599438 170 VAVHLTEHDGVDEVVL 185
Cdd:PRK05205  159 VVVRLAEVDGRDRVVL 174
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
44-158 1.15e-13

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: 65.08  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  44 VVLIGIPTRGTALAKRLGAKIsefagtDIPVGYLDITLYRDDLRdkphrPLERTMVPAGGVDGAIVILVDDVLYSGRTVR 123
Cdd:pfam00156  31 DVVVGILRGGLPFAGILARRL------DVPLAFVRKVSYNPDTS-----EVMKTSSALPDLKGKTVLIVDDILDTGGTLL 99
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1799599438 124 AALDALRDLGrPAAVQLAVLVDRGHRELPLRADYV 158
Cdd:pfam00156 100 KVLELLKNVG-PKEVKIAVLIDKPAGTEPKDKYDK 133
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
44-149 1.50e-11

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: 58.95  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  44 VVLIGIPTRGTALAKRLGAKIsefagtDIPVGYLDITLYRDDLrdKPHRPLERTMVPAGGVDGAIVILVDDVLYSGRTVR 123
Cdd:cd06223    17 DVVVGILRGGLPLAAALARAL------GLPLAFIRKERKGPGR--TPSEPYGLELPLGGDVKGKRVLLVDDVIATGGTLL 88
                          90       100
                  ....*....|....*....|....*.
gi 1799599438 124 AALDALRDLGrPAAVQLAVLVDRGHR 149
Cdd:cd06223    89 AAIELLKEAG-AKVVGVAVLLDKPEG 113
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
11-163 1.19e-09

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


Pssm-ID: 440399  Cd Length: 176  Bit Score: 55.03  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  11 RVLLDAADVSRTIARVAHQVIEktalDAPDAPhVVLIGIpTRG----TA-LAKRLGakisefagTDIPVGYLDITLYRDD 85
Cdd:COG0634     7 EVLISEEEIQARVKELAAQITA----DYAGKE-PLVVGV-LKGafvfMAdLLRALD--------FPLEIDFMHVSSYGGG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  86 --------LRDKPHRPLE-RTmvpaggvdgaiVILVDDVLYSGRTVRAALDALRDLGrPAAVQLAVLVDRGH-RELPLRA 155
Cdd:COG0634    73 tessgevrILKDLDEDIEgRD-----------VLIVEDIIDTGLTLSYLLELLKSRG-PASVKIATLLDKPErRKVDVPA 140

                  ....*...
gi 1799599438 156 DYVGKNIP 163
Cdd:COG0634   141 DYVGFEIP 148
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
13-163 3.03e-09

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 53.71  E-value: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  13 LLDAADVSRTIARVAHQVIEKTALDAPdaphVVLI----GIPTRGTaLAKRLGAkisefagtDIPVGYLDITLYRDDLRD 88
Cdd:PRK09162   16 LVSAAEVEAAIDRMADEITADLADENP----LVLCvmggGLVFTGQ-LLPRLDF--------PLEFDYLHATRYRNETTG 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799599438  89 KPhrpLERTMVPAGGVDGAIVILVDDVLYSGRTVRAALDALRDLGrPAAVQLAVLVDRGH-RELP-LRADYVGKNIP 163
Cdd:PRK09162   83 GE---LVWKVKPRESLKGRTVLVVDDILDEGHTLAAIRDRCLEMG-AAEVYSAVLVDKTHdRKAKpLKADFVGLEVP 155
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
8-164 1.33e-06

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: 45.99  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438   8 STHRVLLDAADVSRTIARVAHQVIEKTalDAPDaphvVLIGIpTRGTAlakRLGAKISEFAGTDiPVGYLDITLYRDDlr 87
Cdd:COG2236     3 KFKKEYLSWDEIHELSRRLAEQILESG--FRPD----VIVAI-ARGGL---VPARILADALGVP-DLASIRVSSYTGT-- 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799599438  88 DKPHRPLERTMVPAGGVDGAIVILVDDVLYSGRTVRAALDALRDLGrPAAVQLAVLVDRGHRElpLRADYVGKNIPT 164
Cdd:COG2236    70 AKRLEEPVVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAG-PAEVRTAVLYYKPSSK--FKPDYYAEETDA 143
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
100-142 2.83e-04

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 441529  Cd Length: 209  Bit Score: 40.06  E-value: 2.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1799599438 100 PAGGVDGAIVILVDDVLYSGRTVRAALDALRDLGrPAAVQLAV 142
Cdd:COG1926   115 PPPDLKGRTVILVDDGIATGATMRAALRALRRQG-PARIVVAV 156
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
102-155 1.05e-03

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 38.31  E-value: 1.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1799599438 102 GGVDGAIVILVDDVLYSGRTVRAALDALRDLG-RPAAVqlAVLVD-RGHREL---PLRA 155
Cdd:PRK02277  136 ASVEGKRCVIVDDVITSGTTMKETIEYLKEHGgKPVAV--VVLIDkSGIDEIdgvPVYS 192
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
104-147 1.27e-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: 38.21  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1799599438 104 VDGAIVILVDDVLYSGRTVRAALDALRDLG-RPAAVqlAVLVDRG 147
Cdd:COG0461   110 LPGERVLVVEDVITTGGSVLEAVEALREAGaEVVGV--AVIVDRE 152
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
11-156 1.47e-03

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 38.20  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  11 RVLLDA--ADVSRTIARVAHQVIEKTALD-----APDAPHVVlIGIPTRGTALAKRLGAKISEfaGTDIPVGYLDITLYR 83
Cdd:PRK06031   47 RGLPDGdrALASLIVNQASFEVLDALAEHlaekaRAFDPDVV-AGLPTLGLTLAAAVARKLGH--TRYVPLGTSRKFWYR 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  84 DDLRDkphrPLERTMVPAGG----VD--------GAIVILVDDVLYSGRTVRAALDALRDLG-RPAAVQLAVLVDRGHRE 150
Cdd:PRK06031  124 DELSV----PLSSITTPDQGkrlyIDprmlplleGRRVALIDDVISSGASIVAGLRLLAACGiEPAGIGAAMLQSERWRE 199

                  ....*.
gi 1799599438 151 LPLRAD 156
Cdd:PRK06031  200 SLAAAG 205
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
104-147 3.80e-03

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 36.67  E-value: 3.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1799599438 104 VDGAIVILVDDVLYSGRTVRAALDALRDLG-RPAAVqlAVLVDRG 147
Cdd:PRK00455  111 LFGKRVLVVEDVITTGGSVLEAVEAIRAAGaEVVGV--AVIVDRQ 153
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
18-143 5.14e-03

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 36.34  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799599438  18 DVSRTIARVAHQVIEKTALDAPDaphvVLIGIPTRGTALAKR-------LGAKISEFAGtdIPvgylditlYRDDL--RD 88
Cdd:COG1040    58 DLARLLARLLARALREALLPRPD----LIVPVPLHRRRLRRRgfnqaelLARALARALG--IP--------VLPDLlrRV 123
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799599438  89 KPHRPL------ER--------TMVPAGGVDGAIVILVDDVLYSGRTVRAALDALRDLGrPAAVQLAVL 143
Cdd:COG1040   124 RATPSQaglsraERrrnlrgafAVRPPARLAGKHVLLVDDVLTTGATLAEAARALKAAG-AARVDVLVL 191
 
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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