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Conserved domains on  [gi|557440741|ref|NP_001273488|]
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tektin-4 isoform 2 [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 ...
 2-244 5.04e-100

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: 296.38  E-value: 5.04e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440741    2 QAVSQIRLNREHKETCEMDWSDKMEAYNIDETCGRHHSQSTEVQAHPYSTTFQESASTPETRAKFTQDNLCRAQRERLAS 81
Cdd:pfam03148 141 QAWEQLRLLRAARHKLEKDLSDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAAS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440741   82 ANLRVLVDCILRDTSEDLRLQCDAVNLAFGRRCEELEDARYKLHHHLHKTLREITDQEHNVAALKQAIKDKEAPLHVAQT 161
Cdd:pfam03148 221 AQLRELIDSILEQTANDLRAQADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQT 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440741  162 RLYLRSHRPNMELCRDAAQFRLLSEVEELNMSLTALREKLLEAEQSLRNLEDIHMSLEKDIAAMTNSLFIDRQKCMAHRT 241
Cdd:pfam03148 301 RLENRTYRPNVELCRDEAQYGLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDREKCMGLRK 380


                  ...
gi 557440741  242 RYP 244
Cdd:pfam03148 381 RLP 383
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 2-244 5.04e-100

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: 296.38  E-value: 5.04e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440741    2 QAVSQIRLNREHKETCEMDWSDKMEAYNIDETCGRHHSQSTEVQAHPYSTTFQESASTPETRAKFTQDNLCRAQRERLAS 81
Cdd:pfam03148 141 QAWEQLRLLRAARHKLEKDLSDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAAS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440741   82 ANLRVLVDCILRDTSEDLRLQCDAVNLAFGRRCEELEDARYKLHHHLHKTLREITDQEHNVAALKQAIKDKEAPLHVAQT 161
Cdd:pfam03148 221 AQLRELIDSILEQTANDLRAQADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQT 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440741  162 RLYLRSHRPNMELCRDAAQFRLLSEVEELNMSLTALREKLLEAEQSLRNLEDIHMSLEKDIAAMTNSLFIDRQKCMAHRT 241
Cdd:pfam03148 301 RLENRTYRPNVELCRDEAQYGLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDREKCMGLRK 380


                  ...
gi 557440741  242 RYP 244
Cdd:pfam03148 381 RLP 383
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 2-244 5.04e-100

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: 296.38  E-value: 5.04e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440741    2 QAVSQIRLNREHKETCEMDWSDKMEAYNIDETCGRHHSQSTEVQAHPYSTTFQESASTPETRAKFTQDNLCRAQRERLAS 81
Cdd:pfam03148 141 QAWEQLRLLRAARHKLEKDLSDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAAS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440741   82 ANLRVLVDCILRDTSEDLRLQCDAVNLAFGRRCEELEDARYKLHHHLHKTLREITDQEHNVAALKQAIKDKEAPLHVAQT 161
Cdd:pfam03148 221 AQLRELIDSILEQTANDLRAQADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQT 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440741  162 RLYLRSHRPNMELCRDAAQFRLLSEVEELNMSLTALREKLLEAEQSLRNLEDIHMSLEKDIAAMTNSLFIDRQKCMAHRT 241
Cdd:pfam03148 301 RLENRTYRPNVELCRDEAQYGLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDREKCMGLRK 380


                  ...
gi 557440741  242 RYP 244
Cdd:pfam03148 381 RLP 383
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 68-234 6.67e-14

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: 70.27  E-value: 6.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440741   68 QDNLCRAQRERLASANLRVLVDCILRDTSED-LRLQCDaVNLAFGRRCEELEDARYKLHHHLHKTLREITDQEHNVAALK 146
Cdd:pfam03148   6 QELYREAEAQRNDAERLRQESRRLRNETDAKtKWDQYD-SNRRLGERIQDITFWKSELEKELEELDEEIELLLEEKRRLE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440741  147 QAIKDKEAPLHVAQTRLYLRSHRPNMELCRDAAQFRLLSEVEELNMSLTALREKLLEAEQSLRNLEDIHMSLEKDIAAMT 226
Cdd:pfam03148  85 KALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDLSDKK 164


                  ....*...
gi 557440741  227 NSLFIDRQ 234
Cdd:pfam03148 165 EALEIDEK 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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