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Conserved domains on  [gi|194385628|dbj|BAG65189|]
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unnamed protein product [Homo sapiens]

Protein Classification

tektin family protein( domain architecture ID 12042437)

tektin family protein; possible functional roles include the stabilization of tubulin protofilaments, attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles, and the binding of axonemal components.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 1-252 8.97e-116

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


:

Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 337.21  E-value: 8.97e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194385628    1 MALLTRTLEEASEQIRMNRSAKYNLEKDLKDKFVALTIDDICFSLNNNSPNIRYSENAVRIEPNSVSLEDWLDFSSTNVE 80
Cdd:pfam03148 132 QELLQRTLEQAWEQLRLLRAARHKLEKDLSDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIE 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194385628   81 KADKQRNNSLMLKALVDRILSQTANDLCKQCDVVDTAFKNGLKDTKDARDKLADHLAKVMEEIASQEKNITALEKAILDQ 160
Cdd:pfam03148 212 RAEKERAASAQLRELIDSILEQTANDLRAQADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDK 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194385628  161 EGPAKVAHTRLETRTHRPNVELCRDVAQYRLMKEVQEITHNVARLKETLAQAQAELKGLHRRQLALQEEIQVKENTIYID 240
Cdd:pfam03148 292 EAPLKLAQTRLENRTYRPNVELCRDEAQYGLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFID 371

                         250
                  ....*....|..
gi 194385628  241 EVLCMQMRKSIP 252
Cdd:pfam03148 372 REKCMGLRKRLP 383
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 1-252 8.97e-116

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 337.21  E-value: 8.97e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194385628    1 MALLTRTLEEASEQIRMNRSAKYNLEKDLKDKFVALTIDDICFSLNNNSPNIRYSENAVRIEPNSVSLEDWLDFSSTNVE 80
Cdd:pfam03148 132 QELLQRTLEQAWEQLRLLRAARHKLEKDLSDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIE 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194385628   81 KADKQRNNSLMLKALVDRILSQTANDLCKQCDVVDTAFKNGLKDTKDARDKLADHLAKVMEEIASQEKNITALEKAILDQ 160
Cdd:pfam03148 212 RAEKERAASAQLRELIDSILEQTANDLRAQADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDK 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194385628  161 EGPAKVAHTRLETRTHRPNVELCRDVAQYRLMKEVQEITHNVARLKETLAQAQAELKGLHRRQLALQEEIQVKENTIYID 240
Cdd:pfam03148 292 EAPLKLAQTRLENRTYRPNVELCRDEAQYGLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFID 371

                         250
                  ....*....|..
gi 194385628  241 EVLCMQMRKSIP 252
Cdd:pfam03148 372 REKCMGLRKRLP 383
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 1-252 8.97e-116

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 337.21  E-value: 8.97e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194385628    1 MALLTRTLEEASEQIRMNRSAKYNLEKDLKDKFVALTIDDICFSLNNNSPNIRYSENAVRIEPNSVSLEDWLDFSSTNVE 80
Cdd:pfam03148 132 QELLQRTLEQAWEQLRLLRAARHKLEKDLSDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIE 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194385628   81 KADKQRNNSLMLKALVDRILSQTANDLCKQCDVVDTAFKNGLKDTKDARDKLADHLAKVMEEIASQEKNITALEKAILDQ 160
Cdd:pfam03148 212 RAEKERAASAQLRELIDSILEQTANDLRAQADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDK 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194385628  161 EGPAKVAHTRLETRTHRPNVELCRDVAQYRLMKEVQEITHNVARLKETLAQAQAELKGLHRRQLALQEEIQVKENTIYID 240
Cdd:pfam03148 292 EAPLKLAQTRLENRTYRPNVELCRDEAQYGLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFID 371

                         250
                  ....*....|..
gi 194385628  241 EVLCMQMRKSIP 252
Cdd:pfam03148 372 REKCMGLRKRLP 383
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 71-242 1.15e-13

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 69.88  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194385628   71 WLDFSSTNVEKADKQRNNSLMLKALVDRILSQTANDLCKQCDVVDTAFKNGLKDTKDARDKLADHLAKVMEEIASQEKNI 150
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194385628  151 TALEKAILDQEGPAKVAHTRLETRTHRPNVELCRDVAQYRLMKEVQEITHNVARLKETLAQAQAELKGLHRRQLALQEEI 230
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160

                         170
                  ....*....|..
gi 194385628  231 QVKENTIYIDEV 242
Cdd:pfam03148 161 SDKKEALEIDEK 172
 
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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