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Conserved domains on  [gi|408360309|sp|Q9D4K7|]
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RecName: Full=Tektin-like protein 1; AltName: Full=Coiled-coil domain-containing protein 105

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tektin super family cl27112
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 140-364 8.55e-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.


The actual alignment was detected with superfamily member pfam03148:

Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 41.77  E-value: 8.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360309  140 LGRAQHQINGQLRLLLRQREATDRRLSEVRKGLLINQQSVKLRGYRPKCEKIPDKADSLLVWEKKELKSMKRKMEKDMEI 219
Cdd:pfam03148  62 LEKELEELDEEIELLLEEKRRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQ 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360309  220 SEDLLKALASCRDTLDFYCQERLQAVElmnqpLDKVLEQAGRHSwVDITRPPTP-RTQGLKTPPpdpiGTYTPACAKALF 298
Cdd:pfam03148 142 AWEQLRLLRAARHKLEKDLSDKKEALE-----IDEKCLSLNNTS-PNISYKPGPtRIPPNSSTP----EEWEKFTQDNIE 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408360309  299 EAKRLLMESKDILTEM------AKNevDIQNQQqeisNRVCSSLAQKMRETLELKERMTMTLGLMRGTIHRC 364
Cdd:pfam03148 212 RAEKERAASAQLRELIdsileqTAN--DLRAQA----DAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAEL 277
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 140-364 8.55e-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: 41.77  E-value: 8.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360309  140 LGRAQHQINGQLRLLLRQREATDRRLSEVRKGLLINQQSVKLRGYRPKCEKIPDKADSLLVWEKKELKSMKRKMEKDMEI 219
Cdd:pfam03148  62 LEKELEELDEEIELLLEEKRRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQ 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360309  220 SEDLLKALASCRDTLDFYCQERLQAVElmnqpLDKVLEQAGRHSwVDITRPPTP-RTQGLKTPPpdpiGTYTPACAKALF 298
Cdd:pfam03148 142 AWEQLRLLRAARHKLEKDLSDKKEALE-----IDEKCLSLNNTS-PNISYKPGPtRIPPNSSTP----EEWEKFTQDNIE 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408360309  299 EAKRLLMESKDILTEM------AKNevDIQNQQqeisNRVCSSLAQKMRETLELKERMTMTLGLMRGTIHRC 364
Cdd:pfam03148 212 RAEKERAASAQLRELIdsileqTAN--DLRAQA----DAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAEL 277
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 140-364 8.55e-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: 41.77  E-value: 8.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360309  140 LGRAQHQINGQLRLLLRQREATDRRLSEVRKGLLINQQSVKLRGYRPKCEKIPDKADSLLVWEKKELKSMKRKMEKDMEI 219
Cdd:pfam03148  62 LEKELEELDEEIELLLEEKRRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQ 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360309  220 SEDLLKALASCRDTLDFYCQERLQAVElmnqpLDKVLEQAGRHSwVDITRPPTP-RTQGLKTPPpdpiGTYTPACAKALF 298
Cdd:pfam03148 142 AWEQLRLLRAARHKLEKDLSDKKEALE-----IDEKCLSLNNTS-PNISYKPGPtRIPPNSSTP----EEWEKFTQDNIE 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408360309  299 EAKRLLMESKDILTEM------AKNevDIQNQQqeisNRVCSSLAQKMRETLELKERMTMTLGLMRGTIHRC 364
Cdd:pfam03148 212 RAEKERAASAQLRELIdsileqTAN--DLRAQA----DAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAEL 277
 
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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