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Conserved domains on  [gi|62078759|ref|NP_081936|]
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tektin-3 [Mus musculus]

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 ...
99-481 0e+00

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: 524.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759    99 WYRSNLVSFQESNSSRHNSERLRVDTSRLIQDKYQQIRKTQAHSTQNLGERVNDLAFWKSEITHELDEMIGETNALTDIK 178
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759   179 RRLERGLIETEGPLQVSRECLFHREKRMGIDLVHDEAEKELLAEVDTILCCQERMRQHLDKANAQLASDRSAQHELEKDL 258
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759   259 SDKQAALRIDDKCQHLRNTSEGVSYFRGVERVDATVSVPETWAKFTDDNVLRSQSERAASAKLREETENLLIVTANEMWN 338
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759   339 QFNKVNLAFTNRIAETVDAKNKIHTHLTKTLQEIFQIEMTIESIKKAIKEKSAFLKVAQTRLDERTRRPNVELCRDMAQL 418
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62078759   419 RLVNEVYEVDETIQTLQQRLRDSEDTLQSLAHTKATLEHDLAVKANTLYIDQEKCMSMRNSYP 481
Cdd:pfam03148 321 GLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDREKCMGLRKRLP 383
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
99-481 0e+00

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: 524.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759    99 WYRSNLVSFQESNSSRHNSERLRVDTSRLIQDKYQQIRKTQAHSTQNLGERVNDLAFWKSEITHELDEMIGETNALTDIK 178
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759   179 RRLERGLIETEGPLQVSRECLFHREKRMGIDLVHDEAEKELLAEVDTILCCQERMRQHLDKANAQLASDRSAQHELEKDL 258
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759   259 SDKQAALRIDDKCQHLRNTSEGVSYFRGVERVDATVSVPETWAKFTDDNVLRSQSERAASAKLREETENLLIVTANEMWN 338
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759   339 QFNKVNLAFTNRIAETVDAKNKIHTHLTKTLQEIFQIEMTIESIKKAIKEKSAFLKVAQTRLDERTRRPNVELCRDMAQL 418
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62078759   419 RLVNEVYEVDETIQTLQQRLRDSEDTLQSLAHTKATLEHDLAVKANTLYIDQEKCMSMRNSYP 481
Cdd:pfam03148 321 GLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDREKCMGLRKRLP 383
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
99-481 0e+00

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: 524.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759    99 WYRSNLVSFQESNSSRHNSERLRVDTSRLIQDKYQQIRKTQAHSTQNLGERVNDLAFWKSEITHELDEMIGETNALTDIK 178
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759   179 RRLERGLIETEGPLQVSRECLFHREKRMGIDLVHDEAEKELLAEVDTILCCQERMRQHLDKANAQLASDRSAQHELEKDL 258
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759   259 SDKQAALRIDDKCQHLRNTSEGVSYFRGVERVDATVSVPETWAKFTDDNVLRSQSERAASAKLREETENLLIVTANEMWN 338
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759   339 QFNKVNLAFTNRIAETVDAKNKIHTHLTKTLQEIFQIEMTIESIKKAIKEKSAFLKVAQTRLDERTRRPNVELCRDMAQL 418
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62078759   419 RLVNEVYEVDETIQTLQQRLRDSEDTLQSLAHTKATLEHDLAVKANTLYIDQEKCMSMRNSYP 481
Cdd:pfam03148 321 GLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDREKCMGLRKRLP 383
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
300-479 6.35e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.32  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759   300 WAKFTDDNVLRSQSERAASAKLREETENLLIvtanEMWNQFNKVNLAFTNRIAETVDAKNKIHTHLTKTLQEIFQIEmti 379
Cdd:pfam05483 156 LCNLLKETCARSAEKTKKYEYEREETRQVYM----DLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLE--- 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078759   380 ESIKKAIKEKSAFLKVAQTRLDERTRRPN-----VELCRDMA-----QLRLVNE-VYEVDETIQTLQQRLRDSEDTLQSL 448
Cdd:pfam05483 229 EEYKKEINDKEKQVSLLLIQITEKENKMKdltflLEESRDKAnqleeKTKLQDEnLKELIEKKDHLTKELEDIKMSLQRS 308
                         170       180       190
                  ....*....|....*....|....*....|..
gi 62078759   449 AHTKATLEHDLAVKANTLY-IDQEKCMSMRNS 479
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICqLTEEKEAQMEEL 340
 
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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