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Conserved domains on  [gi|490589506|ref|WP_004454526|]
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phosphoribosyltransferase family protein [Clostridioides difficile]

Protein Classification

phosphoribosyltransferase family protein( domain architecture ID 10634762)

phosphoribosyltransferase family protein may catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRTase_2 pfam15609
Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to ...
 25-211 1.24e-83

Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to OPRTases, and are predicted to use Orotate as substrate. These genes are found in the biosynthetic operon associated with the Ter stress-response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


:

Pssm-ID: 434809  Cd Length: 189  Bit Score: 253.63  E-value: 1.24e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589506   25 FLDVGIRNNSKRRFLFISKKLGKHLACKPSEMDNLGKLMATIYNEKNKEESNGT-VIAFAETGTAVGHSFFDYLCGDYEF 103
Cdd:pfam15609   1 LFGLAARRNPKRAFLFVSKVLGKHIPVRPSVMRDAGRLLAARVPELRADLPGPVlVIGFAETATGLGHGVADALAGDALY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589506  104 IHTTREQF-DELENLEFLEEHSHATDQNLYFGMLNNFKFGDEIILVDDEITTANTCMNIIRKIQSIYPKKKYTICSILNW 182
Cdd:pfam15609  81 LHTTRRPVpGVPPLLEFEEEHSHATDHLLYPEDRALLAGARPLVLVDDEISTGNTALNLIRALHAKLPRKRYVVVSLVDW 160

                         170       180
                  ....*....|....*....|....*....
gi 490589506  183 VSDENLSKVTRLERELDCKIDFVYLFKGN 211
Cdd:pfam15609 161 RSPEDRAAFAALAAELGIPIDVVSLLEGT 189
TRSP pfam12500
TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly ...
 264-398 1.84e-52

TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly conserved GXXE and TRSP signatures. It is found in bacteria. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


:

Pssm-ID: 463612 [Multi-domain]  Cd Length: 128  Bit Score: 171.61  E-value: 1.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589506  264 YTGRFGINRREQFRLKEIVKRESKKITMASKeslkneKEKILFLGTEEFMYIPMLFAKEKENqYDIYYHSTTRSPIINID 343
Cdd:pfam12500   1 DTGRFGLTPADRARLDAALKALAAKLRAART------GERVLVLGTEEFMYIPLRIAAALGD-GDVRYQSTTRSPVLPVD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490589506  344 KNNYPIKSKFMLKSFYNIDIQNYIYNIDKHNFSKCYLFVELNKSENSYLEFIDII 398
Cdd:pfam12500  74 DPGYAIRTAFTFPSPDDPGIVNYVYNIPPGGYDEVVLVVERPVDTEALGGLLDAL 128
 
Name Accession Description Interval E-value
PRTase_2 pfam15609
Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to ...
 25-211 1.24e-83

Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to OPRTases, and are predicted to use Orotate as substrate. These genes are found in the biosynthetic operon associated with the Ter stress-response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 434809  Cd Length: 189  Bit Score: 253.63  E-value: 1.24e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589506   25 FLDVGIRNNSKRRFLFISKKLGKHLACKPSEMDNLGKLMATIYNEKNKEESNGT-VIAFAETGTAVGHSFFDYLCGDYEF 103
Cdd:pfam15609   1 LFGLAARRNPKRAFLFVSKVLGKHIPVRPSVMRDAGRLLAARVPELRADLPGPVlVIGFAETATGLGHGVADALAGDALY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589506  104 IHTTREQF-DELENLEFLEEHSHATDQNLYFGMLNNFKFGDEIILVDDEITTANTCMNIIRKIQSIYPKKKYTICSILNW 182
Cdd:pfam15609  81 LHTTRRPVpGVPPLLEFEEEHSHATDHLLYPEDRALLAGARPLVLVDDEISTGNTALNLIRALHAKLPRKRYVVVSLVDW 160

                         170       180
                  ....*....|....*....|....*....
gi 490589506  183 VSDENLSKVTRLERELDCKIDFVYLFKGN 211
Cdd:pfam15609 161 RSPEDRAAFAALAAELGIPIDVVSLLEGT 189
TRSP pfam12500
TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly ...
 264-398 1.84e-52

TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly conserved GXXE and TRSP signatures. It is found in bacteria. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 463612 [Multi-domain]  Cd Length: 128  Bit Score: 171.61  E-value: 1.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589506  264 YTGRFGINRREQFRLKEIVKRESKKITMASKeslkneKEKILFLGTEEFMYIPMLFAKEKENqYDIYYHSTTRSPIINID 343
Cdd:pfam12500   1 DTGRFGLTPADRARLDAALKALAAKLRAART------GERVLVLGTEEFMYIPLRIAAALGD-GDVRYQSTTRSPVLPVD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490589506  344 KNNYPIKSKFMLKSFYNIDIQNYIYNIDKHNFSKCYLFVELNKSENSYLEFIDII 398
Cdd:pfam12500  74 DPGYAIRTAFTFPSPDDPGIVNYVYNIPPGGYDEVVLVVERPVDTEALGGLLDAL 128
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 59-179 1.03e-04

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: 42.00  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589506  59 LGKLMATIYNEKNKEESngTVIAFAETGTAVGHSFFDYLCGDYEFIHTTReqfdelenleFLEEHSHATDQNLYFGMLNN 138
Cdd:cd06223    1 AGRLLAEEIREDLLEPD--VVVGILRGGLPLAAALARALGLPLAFIRKER----------KGPGRTPSEPYGLELPLGGD 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490589506 139 FKfGDEIILVDDEITTANTCMNIIRKIQSIYPKKKYTICSI 179
Cdd:cd06223   69 VK-GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLL 108
 
Name Accession Description Interval E-value
PRTase_2 pfam15609
Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to ...
 25-211 1.24e-83

Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to OPRTases, and are predicted to use Orotate as substrate. These genes are found in the biosynthetic operon associated with the Ter stress-response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 434809  Cd Length: 189  Bit Score: 253.63  E-value: 1.24e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589506   25 FLDVGIRNNSKRRFLFISKKLGKHLACKPSEMDNLGKLMATIYNEKNKEESNGT-VIAFAETGTAVGHSFFDYLCGDYEF 103
Cdd:pfam15609   1 LFGLAARRNPKRAFLFVSKVLGKHIPVRPSVMRDAGRLLAARVPELRADLPGPVlVIGFAETATGLGHGVADALAGDALY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589506  104 IHTTREQF-DELENLEFLEEHSHATDQNLYFGMLNNFKFGDEIILVDDEITTANTCMNIIRKIQSIYPKKKYTICSILNW 182
Cdd:pfam15609  81 LHTTRRPVpGVPPLLEFEEEHSHATDHLLYPEDRALLAGARPLVLVDDEISTGNTALNLIRALHAKLPRKRYVVVSLVDW 160

                         170       180
                  ....*....|....*....|....*....
gi 490589506  183 VSDENLSKVTRLERELDCKIDFVYLFKGN 211
Cdd:pfam15609 161 RSPEDRAAFAALAAELGIPIDVVSLLEGT 189
TRSP pfam12500
TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly ...
 264-398 1.84e-52

TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly conserved GXXE and TRSP signatures. It is found in bacteria. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 463612 [Multi-domain]  Cd Length: 128  Bit Score: 171.61  E-value: 1.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589506  264 YTGRFGINRREQFRLKEIVKRESKKITMASKeslkneKEKILFLGTEEFMYIPMLFAKEKENqYDIYYHSTTRSPIINID 343
Cdd:pfam12500   1 DTGRFGLTPADRARLDAALKALAAKLRAART------GERVLVLGTEEFMYIPLRIAAALGD-GDVRYQSTTRSPVLPVD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490589506  344 KNNYPIKSKFMLKSFYNIDIQNYIYNIDKHNFSKCYLFVELNKSENSYLEFIDII 398
Cdd:pfam12500  74 DPGYAIRTAFTFPSPDDPGIVNYVYNIPPGGYDEVVLVVERPVDTEALGGLLDAL 128
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 59-179 1.03e-04

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: 42.00  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589506  59 LGKLMATIYNEKNKEESngTVIAFAETGTAVGHSFFDYLCGDYEFIHTTReqfdelenleFLEEHSHATDQNLYFGMLNN 138
Cdd:cd06223    1 AGRLLAEEIREDLLEPD--VVVGILRGGLPLAAALARALGLPLAFIRKER----------KGPGRTPSEPYGLELPLGGD 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490589506 139 FKfGDEIILVDDEITTANTCMNIIRKIQSIYPKKKYTICSI 179
Cdd:cd06223   69 VK-GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLL 108
 
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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