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Conserved domains on  [gi|530417230|ref|XP_005259304.1|]
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PREDICTED: fukutin-related protein isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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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 ...
334-371 6.68e-12

LicD family; The LICD family of proteins show high sequence similarity and are involved in phosphorylcholine metabolizm. 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 pfam04991:

Pssm-ID: 294823  Cd Length: 223  Bit Score: 63.91  E-value: 6.68e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 530417230  334 EAAGVRYWLEGGSLLGAARHGDIIPWDYDVDLGIYLED 371
Cdd:pfam04991   2 KKHGLIYWLSGGTLLGAVRHGGFIPWDDDIDIQMPRKD 39
 
Name Accession Description Interval E-value
LicD pfam04991
LicD family; The LICD family of proteins show high sequence similarity and are involved in ...
334-371 6.68e-12

LicD family; The LICD family of proteins show high sequence similarity and are involved in phosphorylcholine metabolizm. 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: 282800  Cd Length: 223  Bit Score: 63.91  E-value: 6.68e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 530417230  334 EAAGVRYWLEGGSLLGAARHGDIIPWDYDVDLGIYLED 371
Cdd:pfam04991   2 KKHGLIYWLSGGTLLGAVRHGGFIPWDDDIDIQMPRKD 39
LicD COG3475
Phosphorylcholine metabolism protein LicD [Lipid transport and metabolism];
324-371 7.89e-08

Phosphorylcholine metabolism protein LicD [Lipid transport and metabolism];


Pssm-ID: 226006  Cd Length: 256  Bit Score: 52.01  E-value: 7.89e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530417230 324 ETARYVVGVLEAAGVRYWLEGGSLLGAARHGDIIPWDYDVDLGIYLED 371
Cdd:COG3475   16 ELLIYIDILCKEYKIEYWLRYGTLIGAIRHKGFIPWDDDIDIYMLRKD 63
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
67-161 2.24e-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: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417230  67 VDSFLQQDPAQPVVVAA--DTLPYPPLALPRIPNVRLALlqpaldrpAAASRPET------YVATEFVaLVPDGARAEAP 138
Cdd:PRK09382  40 LENLSSAPAFKEIVVVIhpDDIAYMKKALPEIKFVTLVT--------GGATRQESvrnaleALDSEYV-LIHDAARPFVP 110
                         90       100
                 ....*....|....*....|....
gi 530417230 139 G-LLERMVEALRAGSARLVAAPVA 161
Cdd:PRK09382 111 KeLIDRLIEALDKADCVLPALPVA 134
 
Name Accession Description Interval E-value
LicD pfam04991
LicD family; The LICD family of proteins show high sequence similarity and are involved in ...
334-371 6.68e-12

LicD family; The LICD family of proteins show high sequence similarity and are involved in phosphorylcholine metabolizm. 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: 282800  Cd Length: 223  Bit Score: 63.91  E-value: 6.68e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 530417230  334 EAAGVRYWLEGGSLLGAARHGDIIPWDYDVDLGIYLED 371
Cdd:pfam04991   2 KKHGLIYWLSGGTLLGAVRHGGFIPWDDDIDIQMPRKD 39
LicD COG3475
Phosphorylcholine metabolism protein LicD [Lipid transport and metabolism];
324-371 7.89e-08

Phosphorylcholine metabolism protein LicD [Lipid transport and metabolism];


Pssm-ID: 226006  Cd Length: 256  Bit Score: 52.01  E-value: 7.89e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530417230 324 ETARYVVGVLEAAGVRYWLEGGSLLGAARHGDIIPWDYDVDLGIYLED 371
Cdd:COG3475   16 ELLIYIDILCKEYKIEYWLRYGTLIGAIRHKGFIPWDDDIDIYMLRKD 63
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
67-161 2.24e-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: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417230  67 VDSFLQQDPAQPVVVAA--DTLPYPPLALPRIPNVRLALlqpaldrpAAASRPET------YVATEFVaLVPDGARAEAP 138
Cdd:PRK09382  40 LENLSSAPAFKEIVVVIhpDDIAYMKKALPEIKFVTLVT--------GGATRQESvrnaleALDSEYV-LIHDAARPFVP 110
                         90       100
                 ....*....|....*....|....
gi 530417230 139 G-LLERMVEALRAGSARLVAAPVA 161
Cdd:PRK09382 111 KeLIDRLIEALDKADCVLPALPVA 134
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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