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Conserved domains on  [gi|110625871|ref|NP_082227|]
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tektin-4 isoform 1 [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 ...
56-438 2.76e-173

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: 490.52  E-value: 2.76e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871   56 WFQNSYARYHQAFADRDYSERQRHESGQLVAETGALAQRTQLDSTRKVGERLEDMHCWKSELQREIDELSSETDLMMAQK 135
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871  136 LRLQRALDATSVPYSIATDNLQCRERRQHPDLVRDYVEVELLKETELIRNIQELLKRTIGQAVDQIRLNREHKESCEMNW 215
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871  216 SDKVEVYNIDDTCSRYTNESTQVQFYPHSSKFEESASTPETWAKFNHDNLLRAERERLASVNLRKLIDCILRDTAEDLRL 295
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871  296 QCDAVNSAFSSRCQELDDSLQKLQYHLRKTLTEITDQEHQIAALKQAIKDKEAPLRVAQTRLYQRSHRPNVELCRDNAQF 375
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625871  376 RLLSEVEELNMSLRALKEKLQDAEQALRNLEDSRMSLEKDIAVKTNSLFIDRQKCMTHRNRYP 438
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 ...
56-438 2.76e-173

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: 490.52  E-value: 2.76e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871   56 WFQNSYARYHQAFADRDYSERQRHESGQLVAETGALAQRTQLDSTRKVGERLEDMHCWKSELQREIDELSSETDLMMAQK 135
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871  136 LRLQRALDATSVPYSIATDNLQCRERRQHPDLVRDYVEVELLKETELIRNIQELLKRTIGQAVDQIRLNREHKESCEMNW 215
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871  216 SDKVEVYNIDDTCSRYTNESTQVQFYPHSSKFEESASTPETWAKFNHDNLLRAERERLASVNLRKLIDCILRDTAEDLRL 295
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871  296 QCDAVNSAFSSRCQELDDSLQKLQYHLRKTLTEITDQEHQIAALKQAIKDKEAPLRVAQTRLYQRSHRPNVELCRDNAQF 375
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625871  376 RLLSEVEELNMSLRALKEKLQDAEQALRNLEDSRMSLEKDIAVKTNSLFIDRQKCMTHRNRYP 438
Cdd:pfam03148 321 GLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDREKCMGLRKRLP 383
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
291-416 1.51e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871   291 EDLRLQCDAVNSAFSSRCQELDDS-LQKLQYHLRKTLTEITDQEHQIAALKQAIKDKEaplrvaQTRLYQRSHRPNVELC 369
Cdd:TIGR02169  768 EELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT------LEKEYLEKEIQELQEQ 841
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 110625871   370 RDNAQFRLLS---EVEELNMSLRALKEKLQDAEQALRNLEDSRMSLEKDI 416
Cdd:TIGR02169  842 RIDLKEQIKSiekEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
56-438 2.76e-173

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: 490.52  E-value: 2.76e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871   56 WFQNSYARYHQAFADRDYSERQRHESGQLVAETGALAQRTQLDSTRKVGERLEDMHCWKSELQREIDELSSETDLMMAQK 135
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871  136 LRLQRALDATSVPYSIATDNLQCRERRQHPDLVRDYVEVELLKETELIRNIQELLKRTIGQAVDQIRLNREHKESCEMNW 215
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871  216 SDKVEVYNIDDTCSRYTNESTQVQFYPHSSKFEESASTPETWAKFNHDNLLRAERERLASVNLRKLIDCILRDTAEDLRL 295
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871  296 QCDAVNSAFSSRCQELDDSLQKLQYHLRKTLTEITDQEHQIAALKQAIKDKEAPLRVAQTRLYQRSHRPNVELCRDNAQF 375
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625871  376 RLLSEVEELNMSLRALKEKLQDAEQALRNLEDSRMSLEKDIAVKTNSLFIDRQKCMTHRNRYP 438
Cdd:pfam03148 321 GLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDREKCMGLRKRLP 383
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
291-416 1.51e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625871   291 EDLRLQCDAVNSAFSSRCQELDDS-LQKLQYHLRKTLTEITDQEHQIAALKQAIKDKEaplrvaQTRLYQRSHRPNVELC 369
Cdd:TIGR02169  768 EELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT------LEKEYLEKEIQELQEQ 841
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 110625871   370 RDNAQFRLLS---EVEELNMSLRALKEKLQDAEQALRNLEDSRMSLEKDI 416
Cdd:TIGR02169  842 RIDLKEQIKSiekEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
 
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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