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Conserved domains on  [gi|926353073|ref|WP_053684712|]
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MULTISPECIES: hypothetical protein [unclassified Streptomyces]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyphos_transf super family cl42225
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
 328-436 7.02e-03

CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid.


The actual alignment was detected with superfamily member pfam04464:

Pssm-ID: 478041  Cd Length: 360  Bit Score: 39.25  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926353073  328 DKLASSNRVSKvfdEIWvaGRAgrdryerikHAVTHNQIVEVGRPQLMPLHRWTGRAVNPVPT----------VIYAPTW 397
Cdd:pfam04464 127 DYLISANPHST---NIF--ARA---------FNIDKERILETGYPRNDVLFNANNEDVQRIRErlgiplgkkvILYAPTW 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 926353073  398 EGWTDDACYTSVLPAG---EKLIQALLDhelDIRVIYKPHPL 436
Cdd:pfam04464 193 RDDERGSIGSYRFELLidlERLAFALGN---DYVILLKMHPL 231
 
Name Accession Description Interval E-value
Glyphos_transf pfam04464
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
 328-436 7.02e-03

CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid.


Pssm-ID: 398259  Cd Length: 360  Bit Score: 39.25  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926353073  328 DKLASSNRVSKvfdEIWvaGRAgrdryerikHAVTHNQIVEVGRPQLMPLHRWTGRAVNPVPT----------VIYAPTW 397
Cdd:pfam04464 127 DYLISANPHST---NIF--ARA---------FNIDKERILETGYPRNDVLFNANNEDVQRIRErlgiplgkkvILYAPTW 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 926353073  398 EGWTDDACYTSVLPAG---EKLIQALLDhelDIRVIYKPHPL 436
Cdd:pfam04464 193 RDDERGSIGSYRFELLidlERLAFALGN---DYVILLKMHPL 231
 
Name Accession Description Interval E-value
Glyphos_transf pfam04464
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
 328-436 7.02e-03

CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid.


Pssm-ID: 398259  Cd Length: 360  Bit Score: 39.25  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926353073  328 DKLASSNRVSKvfdEIWvaGRAgrdryerikHAVTHNQIVEVGRPQLMPLHRWTGRAVNPVPT----------VIYAPTW 397
Cdd:pfam04464 127 DYLISANPHST---NIF--ARA---------FNIDKERILETGYPRNDVLFNANNEDVQRIRErlgiplgkkvILYAPTW 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 926353073  398 EGWTDDACYTSVLPAG---EKLIQALLDhelDIRVIYKPHPL 436
Cdd:pfam04464 193 RDDERGSIGSYRFELLidlERLAFALGN---DYVILLKMHPL 231
 
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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