NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|312176389|ref|NP_001185892|]
View 

ribitol-5-phosphate transferase FKTN isoform b [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
FKTN_N pfam19737
Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane ...
1-278 0e+00

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: 551.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176389    1 MSRINKNVVLALLTLTSSAFLLFQLYYYKHYLSTKNGAGLSKSKGSRIGFDSTQWRAVKKFIMLTSNQNVPVFLIDPLIL 80
Cdd:pfam19737   1 MPRINKNVVLALLTLTSSVFLLFQLYYYKHYLSPKNGAHFSKVKGSLSGQDSTQWHVVKKFLGLVSKHNLPVFLIDPLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176389   81 ELINKNFEQVKNTSHGSTSQCKFFCVPRDFTAFALQYHLWKNEEGWFRIAENMGFQCLKIESKDPRLDGIDSLSGTEIPL 160
Cdd:pfam19737  81 GLISQDAEQLRDSSDGSSPECKYFCAPRDFTTFALLDKLWKNEAGLFRAAEEMGFQWLEIQGKDPRLEGMDDLSGTEIPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176389  161 HYICKLATHAIHLVVFHERSGNYLWHGHLRLKEHIDRKFVPFRKLQFGRYPGAFDRPELQQVTVDGLEVLIPKDPMHFVE 240
Cdd:pfam19737 161 HYIFRLAGHAVHLVVFYERSGNYLWHGQLRLKQNMDRKFVPFRKLDFGRYPGAYDRPELLLVSIDGLNVQIPKNPSRFLE 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 312176389  241 EVPHSRFIECRYKEARAFFQQYLDDNTVEAVAFRKSAK 278
Cdd:pfam19737 241 EVSHSRFLECRYREARAFFQLYPDDTSLEAVEFRKKAK 278
LicD super family cl01378
LicD family; The LICD family of proteins show high sequence similarity and are involved in ...
289-327 1.87e-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: 1.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 312176389  289 NKLGVPFWLSSGTCLGWYRQCNIIPYSKDVDLGIFIQDY 327
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 ...
1-278 0e+00

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: 551.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176389    1 MSRINKNVVLALLTLTSSAFLLFQLYYYKHYLSTKNGAGLSKSKGSRIGFDSTQWRAVKKFIMLTSNQNVPVFLIDPLIL 80
Cdd:pfam19737   1 MPRINKNVVLALLTLTSSVFLLFQLYYYKHYLSPKNGAHFSKVKGSLSGQDSTQWHVVKKFLGLVSKHNLPVFLIDPLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176389   81 ELINKNFEQVKNTSHGSTSQCKFFCVPRDFTAFALQYHLWKNEEGWFRIAENMGFQCLKIESKDPRLDGIDSLSGTEIPL 160
Cdd:pfam19737  81 GLISQDAEQLRDSSDGSSPECKYFCAPRDFTTFALLDKLWKNEAGLFRAAEEMGFQWLEIQGKDPRLEGMDDLSGTEIPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176389  161 HYICKLATHAIHLVVFHERSGNYLWHGHLRLKEHIDRKFVPFRKLQFGRYPGAFDRPELQQVTVDGLEVLIPKDPMHFVE 240
Cdd:pfam19737 161 HYIFRLAGHAVHLVVFYERSGNYLWHGQLRLKQNMDRKFVPFRKLDFGRYPGAYDRPELLLVSIDGLNVQIPKNPSRFLE 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 312176389  241 EVPHSRFIECRYKEARAFFQQYLDDNTVEAVAFRKSAK 278
Cdd:pfam19737 241 EVSHSRFLECRYREARAFFQLYPDDTSLEAVEFRKKAK 278
LicD pfam04991
LicD family; The LICD family of proteins show high sequence similarity and are involved in ...
289-327 1.87e-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: 1.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 312176389  289 NKLGVPFWLSSGTCLGWYRQCNIIPYSKDVDLGIFIQDY 327
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 ...
1-278 0e+00

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: 551.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176389    1 MSRINKNVVLALLTLTSSAFLLFQLYYYKHYLSTKNGAGLSKSKGSRIGFDSTQWRAVKKFIMLTSNQNVPVFLIDPLIL 80
Cdd:pfam19737   1 MPRINKNVVLALLTLTSSVFLLFQLYYYKHYLSPKNGAHFSKVKGSLSGQDSTQWHVVKKFLGLVSKHNLPVFLIDPLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176389   81 ELINKNFEQVKNTSHGSTSQCKFFCVPRDFTAFALQYHLWKNEEGWFRIAENMGFQCLKIESKDPRLDGIDSLSGTEIPL 160
Cdd:pfam19737  81 GLISQDAEQLRDSSDGSSPECKYFCAPRDFTTFALLDKLWKNEAGLFRAAEEMGFQWLEIQGKDPRLEGMDDLSGTEIPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176389  161 HYICKLATHAIHLVVFHERSGNYLWHGHLRLKEHIDRKFVPFRKLQFGRYPGAFDRPELQQVTVDGLEVLIPKDPMHFVE 240
Cdd:pfam19737 161 HYIFRLAGHAVHLVVFYERSGNYLWHGQLRLKQNMDRKFVPFRKLDFGRYPGAYDRPELLLVSIDGLNVQIPKNPSRFLE 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 312176389  241 EVPHSRFIECRYKEARAFFQQYLDDNTVEAVAFRKSAK 278
Cdd:pfam19737 241 EVSHSRFLECRYREARAFFQLYPDDTSLEAVEFRKKAK 278
LicD pfam04991
LicD family; The LICD family of proteins show high sequence similarity and are involved in ...
289-327 1.87e-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: 1.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 312176389  289 NKLGVPFWLSSGTCLGWYRQCNIIPYSKDVDLGIFIQDY 327
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH