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Conserved domains on  [gi|750154823|ref|WP_040458898|]
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ComF family protein [Limosilactobacillus antri]

Protein Classification

ComF family protein( domain architecture ID 11437133)

ComF family protein is a predicted amidophosphoribosyltransferase; similar to Haemophilus influenzae competence protein F, which is involved in DNA transformation

Gene Ontology:  GO:0030420
PubMed:  8412657|8901420

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 36-226 1.03e-38

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


:

Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 132.64  E-value: 1.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823  36 QQFVALDYVNCCPaCCRPQETDQLCPDCcswrqkypwqlTHRALYRYNGAMKEFMHRYKFAGDYRLRTVFAAEFTAAVRQ 115
Cdd:COG1040    6 RALLDLLFPPRCL-LCGAAPGGGLCPDC-----------RAKAAFRYEGPLRRLILALKYRGRLDLARLLARLLARALRE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823 116 LTAA---VVVPIPVTQVTMATRGFNQVTGLLDGV-DWTPC-LQNRAVKKT----AQSQKHRRERLRTPQ-PFVLSDSsKA 185
Cdd:COG1040   74 ALLPrpdLIVPVPLHRRRLRRRGFNQAELLARALaRALGIpVLPDLLRRVratpSQAGLSRAERRRNLRgAFAVRPP-AR 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 750154823 186 VAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISISLAR 226
Cdd:COG1040  153 LAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLAR 193
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 36-226 1.03e-38

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 132.64  E-value: 1.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823  36 QQFVALDYVNCCPaCCRPQETDQLCPDCcswrqkypwqlTHRALYRYNGAMKEFMHRYKFAGDYRLRTVFAAEFTAAVRQ 115
Cdd:COG1040    6 RALLDLLFPPRCL-LCGAAPGGGLCPDC-----------RAKAAFRYEGPLRRLILALKYRGRLDLARLLARLLARALRE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823 116 LTAA---VVVPIPVTQVTMATRGFNQVTGLLDGV-DWTPC-LQNRAVKKT----AQSQKHRRERLRTPQ-PFVLSDSsKA 185
Cdd:COG1040   74 ALLPrpdLIVPVPLHRRRLRRRGFNQAELLARALaRALGIpVLPDLLRRVratpSQAGLSRAERRRNLRgAFAVRPP-AR 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 750154823 186 VAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISISLAR 226
Cdd:COG1040  153 LAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLAR 193
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 47-226 5.79e-28

comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus influenzae) or do not (E. coli, Borrelia burgdorferi) have described systems for natural transformation with exogenous DNA. It is involved in competence for transformation in Bacillus subtilis. [Cellular processes, DNA transformation]


Pssm-ID: 272958 [Multi-domain]  Cd Length: 190  Bit Score: 104.52  E-value: 5.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823   47 CPACCRPQETDQ-LCPDCCSWRQKYPWQL----THRALYRYNGAMKEFMHRYKFAGDYRLRTVFAAEFTAAVRQL---TA 118
Cdd:TIGR00201   1 CSLCGRPYQSVHaLCRQCGSWRTRIRDSLclrqNLVSVYTYNEPLKELISRFKFRGQAEIIRALASLLSLTVSKAyrdLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823  119 AVVVPIPVTQVTMATRGFNQVTGLLDGVD-WTPCLQNRAVKKTAQSQKHRRERLRTPQ-PFVLSDSSKAVAGKRVLLVDD 196
Cdd:TIGR00201  81 DVIVPVPLSKEREWRRGFNQADLLAQCLSrWLFNYHNIVIRLNNETQSKLKATLRFLNlENAFDLKNNSFQGRNIVLVDD 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 750154823  197 VYTTGRTLYHAADLIYQAGAAGVISISLAR 226
Cdd:TIGR00201 161 VVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 113-224 3.56e-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: 61.26  E-value: 3.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823 113 VRQLTAAVVVPIPVtqVTMATRGFNQVTGLLD--GVDWTPCLqnravkktaqsqKHRRERLRTPQ--PFVLSDSSKAVAG 188
Cdd:cd06223    6 AEEIREDLLEPDVV--VGILRGGLPLAAALARalGLPLAFIR------------KERKGPGRTPSepYGLELPLGGDVKG 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 750154823 189 KRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISISL 224
Cdd:cd06223   72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL 107
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 14-219 2.64e-11

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 60.82  E-value: 2.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823  14 LTLRDLLWPGRLPPAT----VCPNCRQQFVALdyVNCCPACCRPQETDQL-CPDCCswRQKYPWQ-LThrALYRYNGAMK 87
Cdd:PRK11595   2 LTVPGLCWLCRMPLALshwgICSVCSRALRTL--KTCCPQCGLPATHPHLpCGRCL--QKPPPWQrLV--FVSDYAPPLS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823  88 EFMHRYKFAGDYRLRTVFAAEFTAAVRQLTAAV-------VVPIPVTQVTMATRGFNQvTGLLD-------GVDWTPCLQ 153
Cdd:PRK11595  76 GLIHQLKFSRRSELASVLARLLLLEWLQARRSTglqkpdrIISVPLHQRRHWRRGFNQ-SDLLCrplarwlGCDYDSEAL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 750154823 154 NRaVKKTAqSQKHRRERLRTPQ---PFVLSDSskaVAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGV 219
Cdd:PRK11595 155 TR-TRATA-TQHFLSARLRKRNlknAFRLELP---VQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASV 218
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 173-226 8.11e-07

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: 46.97  E-value: 8.11e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 750154823  173 TPQPFVLSDSSKAVAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISISLAR 226
Cdd:pfam00156  67 TSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 36-226 1.03e-38

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 132.64  E-value: 1.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823  36 QQFVALDYVNCCPaCCRPQETDQLCPDCcswrqkypwqlTHRALYRYNGAMKEFMHRYKFAGDYRLRTVFAAEFTAAVRQ 115
Cdd:COG1040    6 RALLDLLFPPRCL-LCGAAPGGGLCPDC-----------RAKAAFRYEGPLRRLILALKYRGRLDLARLLARLLARALRE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823 116 LTAA---VVVPIPVTQVTMATRGFNQVTGLLDGV-DWTPC-LQNRAVKKT----AQSQKHRRERLRTPQ-PFVLSDSsKA 185
Cdd:COG1040   74 ALLPrpdLIVPVPLHRRRLRRRGFNQAELLARALaRALGIpVLPDLLRRVratpSQAGLSRAERRRNLRgAFAVRPP-AR 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 750154823 186 VAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISISLAR 226
Cdd:COG1040  153 LAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLAR 193
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 47-226 5.79e-28

comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus influenzae) or do not (E. coli, Borrelia burgdorferi) have described systems for natural transformation with exogenous DNA. It is involved in competence for transformation in Bacillus subtilis. [Cellular processes, DNA transformation]


Pssm-ID: 272958 [Multi-domain]  Cd Length: 190  Bit Score: 104.52  E-value: 5.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823   47 CPACCRPQETDQ-LCPDCCSWRQKYPWQL----THRALYRYNGAMKEFMHRYKFAGDYRLRTVFAAEFTAAVRQL---TA 118
Cdd:TIGR00201   1 CSLCGRPYQSVHaLCRQCGSWRTRIRDSLclrqNLVSVYTYNEPLKELISRFKFRGQAEIIRALASLLSLTVSKAyrdLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823  119 AVVVPIPVTQVTMATRGFNQVTGLLDGVD-WTPCLQNRAVKKTAQSQKHRRERLRTPQ-PFVLSDSSKAVAGKRVLLVDD 196
Cdd:TIGR00201  81 DVIVPVPLSKEREWRRGFNQADLLAQCLSrWLFNYHNIVIRLNNETQSKLKATLRFLNlENAFDLKNNSFQGRNIVLVDD 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 750154823  197 VYTTGRTLYHAADLIYQAGAAGVISISLAR 226
Cdd:TIGR00201 161 VVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 113-224 3.56e-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: 61.26  E-value: 3.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823 113 VRQLTAAVVVPIPVtqVTMATRGFNQVTGLLD--GVDWTPCLqnravkktaqsqKHRRERLRTPQ--PFVLSDSSKAVAG 188
Cdd:cd06223    6 AEEIREDLLEPDVV--VGILRGGLPLAAALARalGLPLAFIR------------KERKGPGRTPSepYGLELPLGGDVKG 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 750154823 189 KRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISISL 224
Cdd:cd06223   72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL 107
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 14-219 2.64e-11

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 60.82  E-value: 2.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823  14 LTLRDLLWPGRLPPAT----VCPNCRQQFVALdyVNCCPACCRPQETDQL-CPDCCswRQKYPWQ-LThrALYRYNGAMK 87
Cdd:PRK11595   2 LTVPGLCWLCRMPLALshwgICSVCSRALRTL--KTCCPQCGLPATHPHLpCGRCL--QKPPPWQrLV--FVSDYAPPLS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823  88 EFMHRYKFAGDYRLRTVFAAEFTAAVRQLTAAV-------VVPIPVTQVTMATRGFNQvTGLLD-------GVDWTPCLQ 153
Cdd:PRK11595  76 GLIHQLKFSRRSELASVLARLLLLEWLQARRSTglqkpdrIISVPLHQRRHWRRGFNQ-SDLLCrplarwlGCDYDSEAL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 750154823 154 NRaVKKTAqSQKHRRERLRTPQ---PFVLSDSskaVAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGV 219
Cdd:PRK11595 155 TR-TRATA-TQHFLSARLRKRNlknAFRLELP---VQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASV 218
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 172-219 3.44e-08

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: 51.00  E-value: 3.44e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 750154823 172 RTPQPFVLSDSSKAVAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGV 219
Cdd:COG2236   72 RLEEPVVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEV 119
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 173-226 8.11e-07

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: 46.97  E-value: 8.11e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 750154823  173 TPQPFVLSDSSKAVAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISISLAR 226
Cdd:pfam00156  67 TSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 186-222 7.73e-06

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 45.15  E-value: 7.73e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 750154823 186 VAGKRVLLVDDVYTTGRTLYHAADLIYQAGA--AGVISI 222
Cdd:PRK00455 111 LFGKRVLVVEDVITTGGSVLEAVEAIRAAGAevVGVAVI 149
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 173-226 1.07e-05

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: 44.25  E-value: 1.07e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 750154823 173 TPQPFVLSDSSKAVAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISISLAR 226
Cdd:COG0634   76 SGEVRILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLD 129
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 186-222 1.97e-05

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 43.99  E-value: 1.97e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 750154823 186 VAGKRVLLVDDVYTTGRTLYHAADLIYQAGA--AGVISI 222
Cdd:COG0461  110 LPGERVLVVEDVITTGGSVLEAVEALREAGAevVGVAVI 148
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 186-220 2.08e-05

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: 44.28  E-value: 2.08e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 750154823 186 VAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVI 220
Cdd:COG0462  209 VEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVY 243
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
186-222 6.29e-05

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 42.80  E-value: 6.29e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 750154823 186 VAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISI 222
Cdd:PRK01259 206 VEGRDCILVDDMIDTAGTLCKAAEALKERGAKSVYAY 242
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 187-216 8.37e-05

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: 41.60  E-value: 8.37e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 750154823 187 AGKRVLLVDDVYTTGRTLYHAADLIYQAGA 216
Cdd:COG0503  111 PGDRVLIVDDLLATGGTAKAAIKLVEEAGA 140
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 171-222 1.62e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 41.12  E-value: 1.62e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 750154823 171 LRTPQPFVLsDSSKA--VAGKRVLLVDDVYTTGRTLYHAADLIYQAGA--AGVISI 222
Cdd:PRK07322 102 TGKPQLLVL-DGADAekLKGKRVAIVDDVVSTGGTLTALERLVERAGGqvVAKAAI 156
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
185-222 1.93e-04

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 41.46  E-value: 1.93e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 750154823 185 AVAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISI 222
Cdd:PRK07199 208 PWAGRTPVLVDDIVSTGRTLIEAARQLRAAGAASPDCV 245
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 168-223 2.38e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 41.13  E-value: 2.38e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 750154823 168 RERLRTPQPFVLSDSSKAV-AGKRVLLVDDVYTTGRTLYHAADLIYQAGA--AGV---ISIS 223
Cdd:PRK08558 155 YQRLASGIEVTLYLPASALkKGDRVLIVDDIIRSGETQRALLDLARQAGAdvVGVfflIAVG 216
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
186-220 4.20e-04

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 40.32  E-value: 4.20e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 750154823 186 VAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVI 220
Cdd:PRK03092 199 VEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVI 233
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
 118-219 4.48e-04

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 40.79  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823 118 AAVVVPIPVTQVTmATRGFNQVTGLLDGVDWtpcLQNRAVKKT--AQSQKHRRERLRTPqpfvLSDSSKAVAGKRVLLVD 195
Cdd:PRK05793 289 ADIVIGVPDSGIP-AAIGYAEASGIPYGIGF---IKNKYVGRTfiAPSQELRERAVRVK----LNPLKVNVEGKRVVLID 360

                         90       100
                 ....*....|....*....|....
gi 750154823 196 DVYTTGRTLYHAADLIYQAGAAGV 219
Cdd:PRK05793 361 DSIVRGTTSKRLVELLRKAGAKEV 384
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 187-216 5.13e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 39.29  E-value: 5.13e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 750154823 187 AGKRVLLVDDVYTTGRTLYHAADLIYQAGA 216
Cdd:PRK02304 113 PGDRVLIVDDLLATGGTLEAAIKLLERLGA 142
purF TIGR01134
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ...
 118-216 6.13e-04

amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273461 [Multi-domain]  Cd Length: 442  Bit Score: 40.38  E-value: 6.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823  118 AAVVVPIPVTQVTMATrGFNQVTGL--LDGVdwtpcLQNRAVKKT----AQSQKHRRERLRtpqpfvLSDSSKAVAGKRV 191
Cdd:TIGR01134 275 ADVVVPVPDSGRSAAL-GFAQASGIpyREGL-----IKNRYVGRTfimpTQELRELSVRLK------LNPVRAVFEGKRV 342

                          90       100
                  ....*....|....*....|....*
gi 750154823  192 LLVDDVYTTGRTLYHAADLIYQAGA 216
Cdd:TIGR01134 343 VLVDDSIVRGTTSRQIVEMLRDAGA 367
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 161-223 6.62e-04

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 40.11  E-value: 6.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 750154823 161 AQSQKHRRErlrtpqPFVLSDsskaVAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISIS 223
Cdd:PRK02458 201 AQDDSEREE------GYIIGD----VAGKKAILIDDILNTGKTFAEAAKIVEREGATEIYAVA 253
PRK02269 PRK02269
ribose-phosphate diphosphokinase;
186-219 1.02e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 167353 [Multi-domain]  Cd Length: 320  Bit Score: 39.39  E-value: 1.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 750154823 186 VAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGV 219
Cdd:PRK02269 215 VKGKKCILIDDMIDTAGTICHAADALAEAGATEV 248
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 188-222 1.35e-03

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: 38.18  E-value: 1.35e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 750154823  188 GKRVLLVDDVYTTGRTLYHAADLIYQAGA--AGVISI 222
Cdd:TIGR00336 108 GDKVVVVEDVITTGTSILEAVEIIQAAGGqvAGVIIA 144
DZR_2 pfam18912
Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, ...
 16-63 2.32e-03

Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam00156. This entry corresponds to two zinc ribbon motifs. This domain is found at the N-terminus of the ComF operon protein 3.


Pssm-ID: 465906 [Multi-domain]  Cd Length: 56  Bit Score: 35.34  E-value: 2.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 750154823   16 LRDLLWPGRLP--------PATVCPNCRQQFVALDYvNCCPACCRPQETDQLCPDC 63
Cdd:pfam18912   1 LLDLLFPPRCPlcgaivaeGGGLCAACWAELPFITE-PRCPRCGKPLEEGELCGDC 55
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 185-225 2.95e-03

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 37.54  E-value: 2.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 750154823 185 AVAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISISLA 225
Cdd:PRK02277 137 SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLI 177
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 181-224 4.46e-03

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 36.94  E-value: 4.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 750154823 181 DSSKAVAGKRVLLVDDVYTTGRTLYHAADLIYQAGAAGVISISL 224
Cdd:PLN02238  90 DLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCAL 133
PLN02293 PLN02293
adenine phosphoribosyltransferase
 187-216 6.42e-03

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 36.19  E-value: 6.42e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 750154823 187 AGKRVLLVDDVYTTGRTLYHAADLIYQAGA 216
Cdd:PLN02293 124 PGERALVIDDLIATGGTLCAAINLLERAGA 153
PRK05205 PRK05205
bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;
186-203 7.25e-03

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;


Pssm-ID: 235365  Cd Length: 176  Bit Score: 36.26  E-value: 7.25e-03
                         10
                 ....*....|....*...
gi 750154823 186 VAGKRVLLVDDVYTTGRT 203
Cdd:PRK05205  93 IEGKRVILVDDVLYTGRT 110
PLN02440 PLN02440
amidophosphoribosyltransferase
 120-219 7.50e-03

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 36.96  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 750154823 120 VVVPIPVTQVTMATrGFNQVTGL--LDGVdwtpcLQNRAVKKT--AQSQKHRRERLR---TPQPFVLsdsskavAGKRVL 192
Cdd:PLN02440 278 VVIPVPDSGRVAAL-GYAAKLGVpfQQGL-----IRSHYVGRTfiEPSQKIRDFSVKlklNPVRSVL-------EGKRVV 344

                         90       100
                 ....*....|....*....|....*..
gi 750154823 193 LVDDVYTTGRTLYHAADLIYQAGAAGV 219
Cdd:PLN02440 345 VVDDSIVRGTTSSKIVRMLREAGAKEV 371
PyrR COG2065
Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide ...
 186-203 9.96e-03

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: 35.80  E-value: 9.96e-03
                         10
                 ....*....|....*...
gi 750154823 186 VAGKRVLLVDDVYTTGRT 203
Cdd:COG2065   93 IDGKTVVLVDDVLYTGRT 110
 
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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