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Conserved domains on  [gi|1191017938|ref|NP_001338426|]
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ribitol-5-phosphate transferase FKTN isoform c [Homo sapiens]

Protein Classification

LicD family protein( domain architecture ID 1908561)

LicD family protein similar to phosphorylcholine transferase LicD, ribitol-5-phosphate transferase FKTN (also known as Fukutin), and ribitol 5-phosphate transferase FKRP (also known as Fukutin-related protein)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FKTN_N super family cl45139
Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane ...
 33-255 1.26e-158

Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane domain required for its localization to the Golgi and participates in the interaction with POMGnT1 for normal POMGnT1 location and activity. Fukutin is a ribitol-phosphate transferase that forms a complex with FKRP and TMEM5 which may contribute to specific biosynthesis of glycans required for dystroglycan function.


The actual alignment was detected with superfamily member pfam19737:

Pssm-ID: 466166  Cd Length: 278  Bit Score: 448.75  E-value: 1.26e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017938  33 RAVKKFIMLTSNQNVPVFLIDPLILELINKNFEQVKNTSHGSTSQCKFFCVPRDFTAFALQYHLWKNEEGWFRIAENMGF 112
Cdd:pfam19737  56 HVVKKFLGLVSKHNLPVFLIDPLVLGLISQDAEQLRDSSDGSSPECKYFCAPRDFTTFALLDKLWKNEAGLFRAAEEMGF 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017938 113 QCLKIESKDPRLDGIDSLSGTEIPLHYICKLATHAIHLVVFHERSGNYLWHGHLRLKEHIDRKFVPFRKLQFGRYPGAFD 192
Cdd:pfam19737 136 QWLEIQGKDPRLEGMDDLSGTEIPLHYIFRLAGHAVHLVVFYERSGNYLWHGQLRLKQNMDRKFVPFRKLDFGRYPGAYD 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191017938 193 RPELQQVTVDGLEVLIPKDPMHFVEEVPHSRFIECRYKEARAFFQQYLDDNTVEAVAFRKSAK 255
Cdd:pfam19737 216 RPELLLVSIDGLNVQIPKNPSRFLEEVSHSRFLECRYREARAFFQLYPDDTSLEAVEFRKKAK 278
LicD super family cl01378
LicD family; The LICD family of proteins show high sequence similarity and are involved in ...
 266-304 2.01e-03

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 pfam04991:

Pssm-ID: 470175  Cd Length: 228  Bit Score: 39.67  E-value: 2.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1191017938 266 NKLGVPFWLSSGTCLGWYRQCNIIPYSKDVDLGIFIQDY 304
Cdd:pfam04991   2 KKNGLIYWLSGGTLLGAVRHGGFIPWDDDIDIQMPRKDY 40
 
Name Accession Description Interval E-value
FKTN_N pfam19737
Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane ...
 33-255 1.26e-158

Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane domain required for its localization to the Golgi and participates in the interaction with POMGnT1 for normal POMGnT1 location and activity. Fukutin is a ribitol-phosphate transferase that forms a complex with FKRP and TMEM5 which may contribute to specific biosynthesis of glycans required for dystroglycan function.


Pssm-ID: 466166  Cd Length: 278  Bit Score: 448.75  E-value: 1.26e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017938  33 RAVKKFIMLTSNQNVPVFLIDPLILELINKNFEQVKNTSHGSTSQCKFFCVPRDFTAFALQYHLWKNEEGWFRIAENMGF 112
Cdd:pfam19737  56 HVVKKFLGLVSKHNLPVFLIDPLVLGLISQDAEQLRDSSDGSSPECKYFCAPRDFTTFALLDKLWKNEAGLFRAAEEMGF 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017938 113 QCLKIESKDPRLDGIDSLSGTEIPLHYICKLATHAIHLVVFHERSGNYLWHGHLRLKEHIDRKFVPFRKLQFGRYPGAFD 192
Cdd:pfam19737 136 QWLEIQGKDPRLEGMDDLSGTEIPLHYIFRLAGHAVHLVVFYERSGNYLWHGQLRLKQNMDRKFVPFRKLDFGRYPGAYD 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191017938 193 RPELQQVTVDGLEVLIPKDPMHFVEEVPHSRFIECRYKEARAFFQQYLDDNTVEAVAFRKSAK 255
Cdd:pfam19737 216 RPELLLVSIDGLNVQIPKNPSRFLEEVSHSRFLECRYREARAFFQLYPDDTSLEAVEFRKKAK 278
LicD pfam04991
LicD family; The LICD family of proteins show high sequence similarity and are involved in ...
 266-304 2.01e-03

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: 39.67  E-value: 2.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1191017938 266 NKLGVPFWLSSGTCLGWYRQCNIIPYSKDVDLGIFIQDY 304
Cdd:pfam04991   2 KKNGLIYWLSGGTLLGAVRHGGFIPWDDDIDIQMPRKDY 40
 
Name Accession Description Interval E-value
FKTN_N pfam19737
Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane ...
 33-255 1.26e-158

Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane domain required for its localization to the Golgi and participates in the interaction with POMGnT1 for normal POMGnT1 location and activity. Fukutin is a ribitol-phosphate transferase that forms a complex with FKRP and TMEM5 which may contribute to specific biosynthesis of glycans required for dystroglycan function.


Pssm-ID: 466166  Cd Length: 278  Bit Score: 448.75  E-value: 1.26e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017938  33 RAVKKFIMLTSNQNVPVFLIDPLILELINKNFEQVKNTSHGSTSQCKFFCVPRDFTAFALQYHLWKNEEGWFRIAENMGF 112
Cdd:pfam19737  56 HVVKKFLGLVSKHNLPVFLIDPLVLGLISQDAEQLRDSSDGSSPECKYFCAPRDFTTFALLDKLWKNEAGLFRAAEEMGF 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191017938 113 QCLKIESKDPRLDGIDSLSGTEIPLHYICKLATHAIHLVVFHERSGNYLWHGHLRLKEHIDRKFVPFRKLQFGRYPGAFD 192
Cdd:pfam19737 136 QWLEIQGKDPRLEGMDDLSGTEIPLHYIFRLAGHAVHLVVFYERSGNYLWHGQLRLKQNMDRKFVPFRKLDFGRYPGAYD 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191017938 193 RPELQQVTVDGLEVLIPKDPMHFVEEVPHSRFIECRYKEARAFFQQYLDDNTVEAVAFRKSAK 255
Cdd:pfam19737 216 RPELLLVSIDGLNVQIPKNPSRFLEEVSHSRFLECRYREARAFFQLYPDDTSLEAVEFRKKAK 278
LicD pfam04991
LicD family; The LICD family of proteins show high sequence similarity and are involved in ...
 266-304 2.01e-03

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: 39.67  E-value: 2.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1191017938 266 NKLGVPFWLSSGTCLGWYRQCNIIPYSKDVDLGIFIQDY 304
Cdd:pfam04991   2 KKNGLIYWLSGGTLLGAVRHGGFIPWDDDIDIQMPRKDY 40
 
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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