NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|89941475|ref|NP_001034974|]
View 

ribitol 5-phosphate transferase FKRP [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LicD super family cl01378
LicD family; The LICD family of proteins show high sequence similarity and are involved in ...
 319-371 1.83e-13

LicD family; The LICD family of proteins show high sequence similarity and are involved in phosphorylcholine metabolism. There is evidence to show that LicD2 mutants have a reduced ability to take up choline, have decreased ability to adhere to host cells and are less virulent. These proteins are part of the nucleotidyltransferase superfamily.


The actual alignment was detected with superfamily member COG3475:

Pssm-ID: 470175  Cd Length: 266  Bit Score: 70.39  E-value: 1.83e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 89941475 319 LRALRET----ARYVVGVLEAAGVRYWLEGGSLLGAARHGDIIPWDYDVDLGIYLED 371
Cdd:COG3475   9 LRELQLVeleiLKEFDRICEKHGIRYFLDGGTLLGAVRHKGFIPWDDDIDIGMPRED 65
ispDF super family cl35819
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 67-161 6.30e-03

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


The actual alignment was detected with superfamily member PRK09382:

Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 38.68  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89941475   67 VDSFLQQDPAQPVVVAA--DTLPYPPLALPRIPNVRLALlqpaldrpAAASRPET------YVATEFVaLVPDGARAEAP 138
Cdd:PRK09382  40 LENLSSAPAFKEIVVVIhpDDIAYMKKALPEIKFVTLVT--------GGATRQESvrnaleALDSEYV-LIHDAARPFVP 110

                         90       100
                 ....*....|....*....|....
gi 89941475  139 G-LLERMVEALRAGSARLVAAPVA 161
Cdd:PRK09382 111 KeLIDRLIEALDKADCVLPALPVA 134
 
Name Accession Description Interval E-value
LicD COG3475
Phosphorylcholine metabolism protein LicD [Lipid transport and metabolism];
319-371 1.83e-13

Phosphorylcholine metabolism protein LicD [Lipid transport and metabolism];


Pssm-ID: 442698  Cd Length: 266  Bit Score: 70.39  E-value: 1.83e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 89941475 319 LRALRET----ARYVVGVLEAAGVRYWLEGGSLLGAARHGDIIPWDYDVDLGIYLED 371
Cdd:COG3475   9 LRELQLVeleiLKEFDRICEKHGIRYFLDGGTLLGAVRHKGFIPWDDDIDIGMPRED 65
LicD pfam04991
LicD family; The LICD family of proteins show high sequence similarity and are involved in ...
 334-371 2.32e-10

LicD family; The LICD family of proteins show high sequence similarity and are involved in phosphorylcholine metabolism. There is evidence to show that LicD2 mutants have a reduced ability to take up choline, have decreased ability to adhere to host cells and are less virulent. These proteins are part of the nucleotidyltransferase superfamily.


Pssm-ID: 428243  Cd Length: 228  Bit Score: 60.47  E-value: 2.32e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 89941475   334 EAAGVRYWLEGGSLLGAARHGDIIPWDYDVDLGIYLED 371
Cdd:pfam04991   2 KKNGLIYWLSGGTLLGAVRHGGFIPWDDDIDIQMPRKD 39
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 67-161 6.30e-03

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 38.68  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89941475   67 VDSFLQQDPAQPVVVAA--DTLPYPPLALPRIPNVRLALlqpaldrpAAASRPET------YVATEFVaLVPDGARAEAP 138
Cdd:PRK09382  40 LENLSSAPAFKEIVVVIhpDDIAYMKKALPEIKFVTLVT--------GGATRQESvrnaleALDSEYV-LIHDAARPFVP 110

                         90       100
                 ....*....|....*....|....
gi 89941475  139 G-LLERMVEALRAGSARLVAAPVA 161
Cdd:PRK09382 111 KeLIDRLIEALDKADCVLPALPVA 134
 
Name Accession Description Interval E-value
LicD COG3475
Phosphorylcholine metabolism protein LicD [Lipid transport and metabolism];
319-371 1.83e-13

Phosphorylcholine metabolism protein LicD [Lipid transport and metabolism];


Pssm-ID: 442698  Cd Length: 266  Bit Score: 70.39  E-value: 1.83e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 89941475 319 LRALRET----ARYVVGVLEAAGVRYWLEGGSLLGAARHGDIIPWDYDVDLGIYLED 371
Cdd:COG3475   9 LRELQLVeleiLKEFDRICEKHGIRYFLDGGTLLGAVRHKGFIPWDDDIDIGMPRED 65
LicD pfam04991
LicD family; The LICD family of proteins show high sequence similarity and are involved in ...
 334-371 2.32e-10

LicD family; The LICD family of proteins show high sequence similarity and are involved in phosphorylcholine metabolism. There is evidence to show that LicD2 mutants have a reduced ability to take up choline, have decreased ability to adhere to host cells and are less virulent. These proteins are part of the nucleotidyltransferase superfamily.


Pssm-ID: 428243  Cd Length: 228  Bit Score: 60.47  E-value: 2.32e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 89941475   334 EAAGVRYWLEGGSLLGAARHGDIIPWDYDVDLGIYLED 371
Cdd:pfam04991   2 KKNGLIYWLSGGTLLGAVRHGGFIPWDDDIDIQMPRKD 39
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 67-161 6.30e-03

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 38.68  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89941475   67 VDSFLQQDPAQPVVVAA--DTLPYPPLALPRIPNVRLALlqpaldrpAAASRPET------YVATEFVaLVPDGARAEAP 138
Cdd:PRK09382  40 LENLSSAPAFKEIVVVIhpDDIAYMKKALPEIKFVTLVT--------GGATRQESvrnaleALDSEYV-LIHDAARPFVP 110

                         90       100
                 ....*....|....*....|....
gi 89941475  139 G-LLERMVEALRAGSARLVAAPVA 161
Cdd:PRK09382 111 KeLIDRLIEALDKADCVLPALPVA 134
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH