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Conserved domains on  [gi|2209674675|ref|NP_001389492|]
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similar to hypothetical protein FLJ32871 [Rattus norvegicus]

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 ...
 93-338 1.31e-80

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: 251.31  E-value: 1.31e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674675  93 WDRSNDLLISVAEASRLRASRMTDDSLRIIHDKDQLIRQMQEGTSRNLGQRLSDIRFWKSGLCHERDMLMAESNSLKILK 172
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674675 173 RRLECAADEADSPLQMALDCLYNPGERLGIDLVYDNLGKNLIREADLLRYCQDQMRKLAKRIDFQIQNNRDAQHALERDI 252
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674675 253 EDKSCAQSIDERCLNLKNTPDSINFFRGMEKFEETISDPDTWAKFSNNNIRHAQNMRAKSAQLREEAEHLFETLSDQMWR 332
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240


                  ....*.
gi 2209674675 333 QFNNIN 338
Cdd:pfam03148 241 QADAVN 246
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 93-338 1.31e-80

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: 251.31  E-value: 1.31e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674675  93 WDRSNDLLISVAEASRLRASRMTDDSLRIIHDKDQLIRQMQEGTSRNLGQRLSDIRFWKSGLCHERDMLMAESNSLKILK 172
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674675 173 RRLECAADEADSPLQMALDCLYNPGERLGIDLVYDNLGKNLIREADLLRYCQDQMRKLAKRIDFQIQNNRDAQHALERDI 252
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674675 253 EDKSCAQSIDERCLNLKNTPDSINFFRGMEKFEETISDPDTWAKFSNNNIRHAQNMRAKSAQLREEAEHLFETLSDQMWR 332
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240


                  ....*.
gi 2209674675 333 QFNNIN 338
Cdd:pfam03148 241 QADAVN 246
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 93-338 1.31e-80

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: 251.31  E-value: 1.31e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674675  93 WDRSNDLLISVAEASRLRASRMTDDSLRIIHDKDQLIRQMQEGTSRNLGQRLSDIRFWKSGLCHERDMLMAESNSLKILK 172
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674675 173 RRLECAADEADSPLQMALDCLYNPGERLGIDLVYDNLGKNLIREADLLRYCQDQMRKLAKRIDFQIQNNRDAQHALERDI 252
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674675 253 EDKSCAQSIDERCLNLKNTPDSINFFRGMEKFEETISDPDTWAKFSNNNIRHAQNMRAKSAQLREEAEHLFETLSDQMWR 332
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240


                  ....*.
gi 2209674675 333 QFNNIN 338
Cdd:pfam03148 241 QADAVN 246
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 92-268 1.46e-04

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: 43.31  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674675  92 EWDRSNDLLISVAEASRLRASRMTDDSLRIIHDKDQLIRQMQEGTSRNLGQRLSDIRFWKSGLCHERDMLMAESNSLKIL 171
Cdd:pfam03148 201 EWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRAQADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKN 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674675 172 KRRLECAADEADSPLQMALDCLYNPGERLGIDLVYDNLGKNLIREADLLRycqDQMRKLAKRID---FQIQNNRDAQHAL 248
Cdd:pfam03148 281 IEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQYGLVDEVKELE---ETIEALKQKLAeaeASLQALERTRLRL 357

                         170       180
                  ....*....|....*....|.
gi 2209674675 249 ERDIEDKSCAQSID-ERCLNL 268
Cdd:pfam03148 358 EEDIAVKANSLFIDrEKCMGL 378
 
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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