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Conserved domains on  [gi|2521548349|ref|WP_285891443|]
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MULTISPECIES: ComF family protein [Bacillus]

Protein Classification

ComF family protein( domain architecture ID 16072570)

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

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 ...
 53-240 1.01e-48

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


:

Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 158.83  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349  53 PTCPKCGRAQSNDqLCQDCSRwdkrrdfaeilvmnRSVYAYNDFMKDILARFKFRGDTALADLFKKDVQSAFKRSFSIKE 132
Cdd:COG1040    15 PRCLLCGAAPGGG-LCPDCRA--------------KAAFRYEGPLRRLILALKYRGRLDLARLLARLLARALREALLPRP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349 133 PVLVPIPLSKERLKERGFNQSMMLASMI----GGPILEP-LIKVHQSK-QSKKRKNERLHQ-QNLFQLRQSNPIVLKDVI 205
Cdd:COG1040    80 DLIVPVPLHRRRLRRRGFNQAELLARALaralGIPVLPDlLRRVRATPsQAGLSRAERRRNlRGAFAVRPPARLAGKHVL 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2521548349 206 LIDDIYTTGATVYHAAKILKDAGAKSVSSFTLIRS 240
Cdd:COG1040   160 LVDDVLTTGATLAEAARALKAAGAARVDVLVLART 194
DZR_2 pfam18912
Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, ...
 15-71 2.70e-07

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: 46.13  E-value: 2.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2521548349  15 CPICESHfvaaftwksflLLNEDRLCVACKNHLMKIQGPTCPKCGRAQSNDQLCQDC 71
Cdd:pfam18912  10 CPLCGAI-----------VAEGGGLCAACWAELPFITEPRCPRCGKPLEEGELCGDC 55
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 53-240 1.01e-48

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 158.83  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349  53 PTCPKCGRAQSNDqLCQDCSRwdkrrdfaeilvmnRSVYAYNDFMKDILARFKFRGDTALADLFKKDVQSAFKRSFSIKE 132
Cdd:COG1040    15 PRCLLCGAAPGGG-LCPDCRA--------------KAAFRYEGPLRRLILALKYRGRLDLARLLARLLARALREALLPRP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349 133 PVLVPIPLSKERLKERGFNQSMMLASMI----GGPILEP-LIKVHQSK-QSKKRKNERLHQ-QNLFQLRQSNPIVLKDVI 205
Cdd:COG1040    80 DLIVPVPLHRRRLRRRGFNQAELLARALaralGIPVLPDlLRRVRATPsQAGLSRAERRRNlRGAFAVRPPARLAGKHVL 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2521548349 206 LIDDIYTTGATVYHAAKILKDAGAKSVSSFTLIRS 240
Cdd:COG1040   160 LVDDVLTTGATLAEAARALKAAGAARVDVLVLART 194
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 55-239 1.35e-38

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: 132.64  E-value: 1.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349  55 CPKCGRA-QSNDQLCQDCSRWDKRRDFAEILVMN-RSVYAYNDFMKDILARFKFRGDTALADLFKKDVQSAFKRSFSIKE 132
Cdd:TIGR00201   1 CSLCGRPyQSVHALCRQCGSWRTRIRDSLCLRQNlVSVYTYNEPLKELISRFKFRGQAEIIRALASLLSLTVSKAYRDLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349 133 PVLVPIPLSKERLKERGFNQSMMLA---SMIGGPILEPLIKVHQSKQSKKRKNER-LHQQNLFQLRqSNPIVLKDVILID 208
Cdd:TIGR00201  81 DVIVPVPLSKEREWRRGFNQADLLAqclSRWLFNYHNIVIRLNNETQSKLKATLRfLNLENAFDLK-NNSFQGRNIVLVD 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2521548349 209 DIYTTGATVYHAAKILKDAGAKSVSSFTLIR 239
Cdd:TIGR00201 160 DVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 32-240 4.97e-14

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 68.91  E-value: 4.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349  32 LLLNEDRLCVACKNHLMKIQgPTCPKCG-RAQSNDQLCQDC----SRWDKrrdfaeiLVmnrSVYAYNDFMKDILARFKF 106
Cdd:PRK11595   15 LALSHWGICSVCSRALRTLK-TCCPQCGlPATHPHLPCGRClqkpPPWQR-------LV---FVSDYAPPLSGLIHQLKF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349 107 RGDT----ALADLFKKDVQSAFKRSFSIKEPVLVPIPLSKERLKERGFNQSMMLAsmigGPILEPLIKVHQSKQSKKRK- 181
Cdd:PRK11595   84 SRRSelasVLARLLLLEWLQARRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLC----RPLARWLGCDYDSEALTRTRa 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2521548349 182 -------NERLHQQNL---FQLRQsnPIVLKDVILIDDIYTTGATVYHAAKILKDAGAKSVSSFTLIRS 240
Cdd:PRK11595  160 tatqhflSARLRKRNLknaFRLEL--PVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRT 226
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 111-238 3.09e-13

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: 64.72  E-value: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349 111 ALADLFKKDVqsafkrsfsIKEPVLVPIPlskerlkERGFNQSMMLASMIGgpilEPLIKVHqskqsKKRKNERLHQQNL 190
Cdd:cd06223     4 LLAEEIREDL---------LEPDVVVGIL-------RGGLPLAAALARALG----LPLAFIR-----KERKGPGRTPSEP 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2521548349 191 FQLRQSNPIVL--KDVILIDDIYTTGATVYHAAKILKDAGAKSVSSFTLI 238
Cdd:cd06223    59 YGLELPLGGDVkgKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLL 108
DZR_2 pfam18912
Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, ...
 15-71 2.70e-07

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: 46.13  E-value: 2.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2521548349  15 CPICESHfvaaftwksflLLNEDRLCVACKNHLMKIQGPTCPKCGRAQSNDQLCQDC 71
Cdd:pfam18912  10 CPLCGAI-----------VAEGGGLCAACWAELPFITEPRCPRCGKPLEEGELCGDC 55
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 180-239 1.03e-04

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: 41.20  E-value: 1.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2521548349 180 RKNERLHQQNLFQLRQSNPIVLKD--VILIDDIYTTGATVYHAAKILKDAGAKSVSSFTLIR 239
Cdd:pfam00156  59 RKVSYNPDTSEVMKTSSALPDLKGktVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 53-240 1.01e-48

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 158.83  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349  53 PTCPKCGRAQSNDqLCQDCSRwdkrrdfaeilvmnRSVYAYNDFMKDILARFKFRGDTALADLFKKDVQSAFKRSFSIKE 132
Cdd:COG1040    15 PRCLLCGAAPGGG-LCPDCRA--------------KAAFRYEGPLRRLILALKYRGRLDLARLLARLLARALREALLPRP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349 133 PVLVPIPLSKERLKERGFNQSMMLASMI----GGPILEP-LIKVHQSK-QSKKRKNERLHQ-QNLFQLRQSNPIVLKDVI 205
Cdd:COG1040    80 DLIVPVPLHRRRLRRRGFNQAELLARALaralGIPVLPDlLRRVRATPsQAGLSRAERRRNlRGAFAVRPPARLAGKHVL 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2521548349 206 LIDDIYTTGATVYHAAKILKDAGAKSVSSFTLIRS 240
Cdd:COG1040   160 LVDDVLTTGATLAEAARALKAAGAARVDVLVLART 194
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 55-239 1.35e-38

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: 132.64  E-value: 1.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349  55 CPKCGRA-QSNDQLCQDCSRWDKRRDFAEILVMN-RSVYAYNDFMKDILARFKFRGDTALADLFKKDVQSAFKRSFSIKE 132
Cdd:TIGR00201   1 CSLCGRPyQSVHALCRQCGSWRTRIRDSLCLRQNlVSVYTYNEPLKELISRFKFRGQAEIIRALASLLSLTVSKAYRDLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349 133 PVLVPIPLSKERLKERGFNQSMMLA---SMIGGPILEPLIKVHQSKQSKKRKNER-LHQQNLFQLRqSNPIVLKDVILID 208
Cdd:TIGR00201  81 DVIVPVPLSKEREWRRGFNQADLLAqclSRWLFNYHNIVIRLNNETQSKLKATLRfLNLENAFDLK-NNSFQGRNIVLVD 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2521548349 209 DIYTTGATVYHAAKILKDAGAKSVSSFTLIR 239
Cdd:TIGR00201 160 DVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 32-240 4.97e-14

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 68.91  E-value: 4.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349  32 LLLNEDRLCVACKNHLMKIQgPTCPKCG-RAQSNDQLCQDC----SRWDKrrdfaeiLVmnrSVYAYNDFMKDILARFKF 106
Cdd:PRK11595   15 LALSHWGICSVCSRALRTLK-TCCPQCGlPATHPHLPCGRClqkpPPWQR-------LV---FVSDYAPPLSGLIHQLKF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349 107 RGDT----ALADLFKKDVQSAFKRSFSIKEPVLVPIPLSKERLKERGFNQSMMLAsmigGPILEPLIKVHQSKQSKKRK- 181
Cdd:PRK11595   84 SRRSelasVLARLLLLEWLQARRSTGLQKPDRIISVPLHQRRHWRRGFNQSDLLC----RPLARWLGCDYDSEALTRTRa 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2521548349 182 -------NERLHQQNL---FQLRQsnPIVLKDVILIDDIYTTGATVYHAAKILKDAGAKSVSSFTLIRS 240
Cdd:PRK11595  160 tatqhflSARLRKRNLknaFRLEL--PVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRT 226
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 111-238 3.09e-13

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: 64.72  E-value: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521548349 111 ALADLFKKDVqsafkrsfsIKEPVLVPIPlskerlkERGFNQSMMLASMIGgpilEPLIKVHqskqsKKRKNERLHQQNL 190
Cdd:cd06223     4 LLAEEIREDL---------LEPDVVVGIL-------RGGLPLAAALARALG----LPLAFIR-----KERKGPGRTPSEP 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2521548349 191 FQLRQSNPIVL--KDVILIDDIYTTGATVYHAAKILKDAGAKSVSSFTLI 238
Cdd:cd06223    59 YGLELPLGGDVkgKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLL 108
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
202-232 2.67e-07

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 50.12  E-value: 2.67e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2521548349 202 KDVILIDDIYTTGATVYHAAKILKDAGAKSV 232
Cdd:PRK01259  209 RDCILVDDMIDTAGTLCKAAEALKERGAKSV 239
DZR_2 pfam18912
Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, ...
 15-71 2.70e-07

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: 46.13  E-value: 2.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2521548349  15 CPICESHfvaaftwksflLLNEDRLCVACKNHLMKIQGPTCPKCGRAQSNDQLCQDC 71
Cdd:pfam18912  10 CPLCGAI-----------VAEGGGLCAACWAELPFITEPRCPRCGKPLEEGELCGDC 55
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 202-232 9.15e-07

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: 48.81  E-value: 9.15e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2521548349 202 KDVILIDDIYTTGATVYHAAKILKDAGAKSV 232
Cdd:TIGR01251 211 KDVVIVDDIIDTGGTIAKAAEILKSAGAKRV 241
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 202-232 1.57e-06

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 47.99  E-value: 1.57e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2521548349 202 KDVILIDDIYTTGATVYHAAKILKDAGAKSV 232
Cdd:PRK00934  205 KDVLIVDDIISTGGTMATAIKILKEQGAKKV 235
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 202-232 2.42e-06

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: 47.36  E-value: 2.42e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2521548349 202 KDVILIDDIYTTGATVYHAAKILKDAGAKSV 232
Cdd:COG0462   212 KTCIIVDDMIDTGGTLVEAAEALKEAGAKSV 242
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 202-239 6.33e-06

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: 45.02  E-value: 6.33e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2521548349 202 KDVILIDDIYTTGATVYHAAKILKDAGAKSVSSFTLIR 239
Cdd:COG0634    92 RDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLD 129
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 180-239 1.03e-04

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: 41.20  E-value: 1.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2521548349 180 RKNERLHQQNLFQLRQSNPIVLKD--VILIDDIYTTGATVYHAAKILKDAGAKSVSSFTLIR 239
Cdd:pfam00156  59 RKVSYNPDTSEVMKTSSALPDLKGktVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
202-232 1.93e-04

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 41.86  E-value: 1.93e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2521548349 202 KDVILIDDIYTTGATVYHAAKILKDAGAKSV 232
Cdd:PRK03092  202 RTCVLVDDMIDTGGTIAGAVRALKEAGAKDV 232
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 188-235 1.49e-03

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 38.90  E-value: 1.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2521548349 188 QNLFQLRQSNPIVlKDVILIDDIYTTGATVYHAAKILKDAGAKSVSSF 235
Cdd:PLN02297  218 KRIVRIKEGNPAG-RHVVIVDDLVQSGGTLIECQKVLAAHGAAKVSAY 264
PLN02369 PLN02369
ribose-phosphate pyrophosphokinase
 202-232 1.69e-03

ribose-phosphate pyrophosphokinase


Pssm-ID: 215209 [Multi-domain]  Cd Length: 302  Bit Score: 38.91  E-value: 1.69e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2521548349 202 KDVILIDDIYTTGATVYHAAKILKDAGAKSV 232
Cdd:PLN02369  203 KVAIMVDDMIDTAGTITKGAALLHQEGAREV 233
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 202-232 1.92e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 38.57  E-value: 1.92e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2521548349 202 KDVILIDDIYTTGATVYHAAKILKDAGAKSV 232
Cdd:PRK02458  219 KKAILIDDILNTGKTFAEAAKIVEREGATEI 249
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 198-238 2.78e-03

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 37.54  E-value: 2.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2521548349 198 PIVLKDVILIDDIYTTGATVYHAAKILKDAGAKSVSSFTLI 238
Cdd:PRK02277  137 SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLI 177
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 197-237 2.94e-03

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 38.39  E-value: 2.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2521548349 197 NPIVL----------KDVILIDDIYTTGATVYHAAKILKDAGAKSV---SSFTL 237
Cdd:PRK06827  250 NPIVAheflgrdvegKDVLIVDDMIASGGSMIDAAKELKSRGAKKIivaATFGF 303
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 204-238 3.17e-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: 3.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2521548349 204 VILIDDIYTTGATVYHAAKILKDAGAKSVSSFTLI 238
Cdd:COG0461   115 VLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIV 149
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 204-230 4.84e-03

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 37.06  E-value: 4.84e-03
                          10        20
                  ....*....|....*....|....*..
gi 2521548349 204 VILIDDIYTTGATVYHAAKILKDAGAK 230
Cdd:PRK00455  116 VLVVEDVITTGGSVLEAVEAIRAAGAE 142
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 202-238 4.86e-03

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 36.94  E-value: 4.86e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2521548349 202 KDVILIDDIYTTGATVYHAAKILKDAGAKSVSSFTLI 238
Cdd:PLN02238   98 KHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALL 134
PRK02269 PRK02269
ribose-phosphate diphosphokinase;
202-232 7.16e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 167353 [Multi-domain]  Cd Length: 320  Bit Score: 37.08  E-value: 7.16e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2521548349 202 KDVILIDDIYTTGATVYHAAKILKDAGAKSV 232
Cdd:PRK02269  218 KKCILIDDMIDTAGTICHAADALAEAGATEV 248
 
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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