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Conserved domains on  [gi|16753231|ref|NP_444515|]
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tektin-1 [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 ...
16-398 4.93e-179

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: 504.00  E-value: 4.93e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231    16 WHIANKNQYHRADAQRSRSERLVAESQRLVDEIEKTTRKSQSDVNKKLEQRLEEVQFWKKELDDKLEQLVNVTDDLLIYK 95
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231    96 IRLEKALETLKEPLHITETCLAYREKRIGIDLVHDTVEHELIKEAEIIQGIMALLTRTLEEASEQIRMNRSAKYNLEKDL 175
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231   176 KDKFVALTIDDICFSLNNNSPNIRYSENAVRIEPNSVSLEDWLDFSSTNVEKADKQRNNSLMLKALVDRILSQTANDLRK 255
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231   256 QCDVVDTAFKNGLKDTKDARDKLADHLAKVMEEIASQEKNITALEKAILDQEGPAKVAHTRLETRTHRPNVELCRDVAQY 335
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16753231   336 RLMKEVQEITHNVARLKETLAQAQAELKGLHRRQLALQEEIQVKENTIYIDEVLCMQMRKSIP 398
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 ...
16-398 4.93e-179

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: 504.00  E-value: 4.93e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231    16 WHIANKNQYHRADAQRSRSERLVAESQRLVDEIEKTTRKSQSDVNKKLEQRLEEVQFWKKELDDKLEQLVNVTDDLLIYK 95
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231    96 IRLEKALETLKEPLHITETCLAYREKRIGIDLVHDTVEHELIKEAEIIQGIMALLTRTLEEASEQIRMNRSAKYNLEKDL 175
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231   176 KDKFVALTIDDICFSLNNNSPNIRYSENAVRIEPNSVSLEDWLDFSSTNVEKADKQRNNSLMLKALVDRILSQTANDLRK 255
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231   256 QCDVVDTAFKNGLKDTKDARDKLADHLAKVMEEIASQEKNITALEKAILDQEGPAKVAHTRLETRTHRPNVELCRDVAQY 335
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16753231   336 RLMKEVQEITHNVARLKETLAQAQAELKGLHRRQLALQEEIQVKENTIYIDEVLCMQMRKSIP 398
Cdd:pfam03148 321 GLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDREKCMGLRKRLP 383
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
22-384 7.29e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 7.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231     22 NQYHRADAQRSRSERLVAESQRLVDEIEKTTRKSQSdvNKKLEQRLEEVQFW-----KKELDDKLEQLVNVTDdlliyki 96
Cdd:TIGR02168  179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAER--YKELKAELRELELAllvlrLEELREELEELQEELK------- 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231     97 RLEKALETLKEPLHITETCLAYREKRIgidlvhdtveHELIKEAEIIQGIMALLTRTLEEASEQIRMNRSAKYNLEKDLK 176
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231    177 DKFVALtiddicfsLNNNSPNIRYSENAVRIEpnsvsledwldfsstnvEKADKQRNNSLMLKALVDRILSQTANdlrkq 256
Cdd:TIGR02168  320 ELEAQL--------EELESKLDELAEELAELE-----------------EKLEELKEELESLEAELEELEAELEE----- 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231    257 cdvvdtaFKNGLKDTKDARDKLADHLAKVMEEIASQEKNITALEKAILDQEgpAKVAHTRLETRTHRPNVELcrdvaqyr 336
Cdd:TIGR02168  370 -------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE--DRRERLQQEIEELLKKLEE-------- 432
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 16753231    337 lmKEVQEITHNVARLKETLAQAQAELKGLHRRQLALQEEIQVKENTIY 384
Cdd:TIGR02168  433 --AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
16-398 4.93e-179

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: 504.00  E-value: 4.93e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231    16 WHIANKNQYHRADAQRSRSERLVAESQRLVDEIEKTTRKSQSDVNKKLEQRLEEVQFWKKELDDKLEQLVNVTDDLLIYK 95
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231    96 IRLEKALETLKEPLHITETCLAYREKRIGIDLVHDTVEHELIKEAEIIQGIMALLTRTLEEASEQIRMNRSAKYNLEKDL 175
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231   176 KDKFVALTIDDICFSLNNNSPNIRYSENAVRIEPNSVSLEDWLDFSSTNVEKADKQRNNSLMLKALVDRILSQTANDLRK 255
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231   256 QCDVVDTAFKNGLKDTKDARDKLADHLAKVMEEIASQEKNITALEKAILDQEGPAKVAHTRLETRTHRPNVELCRDVAQY 335
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16753231   336 RLMKEVQEITHNVARLKETLAQAQAELKGLHRRQLALQEEIQVKENTIYIDEVLCMQMRKSIP 398
Cdd:pfam03148 321 GLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDREKCMGLRKRLP 383
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
22-384 7.29e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 7.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231     22 NQYHRADAQRSRSERLVAESQRLVDEIEKTTRKSQSdvNKKLEQRLEEVQFW-----KKELDDKLEQLVNVTDdlliyki 96
Cdd:TIGR02168  179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAER--YKELKAELRELELAllvlrLEELREELEELQEELK------- 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231     97 RLEKALETLKEPLHITETCLAYREKRIgidlvhdtveHELIKEAEIIQGIMALLTRTLEEASEQIRMNRSAKYNLEKDLK 176
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEV----------SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231    177 DKFVALtiddicfsLNNNSPNIRYSENAVRIEpnsvsledwldfsstnvEKADKQRNNSLMLKALVDRILSQTANdlrkq 256
Cdd:TIGR02168  320 ELEAQL--------EELESKLDELAEELAELE-----------------EKLEELKEELESLEAELEELEAELEE----- 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16753231    257 cdvvdtaFKNGLKDTKDARDKLADHLAKVMEEIASQEKNITALEKAILDQEgpAKVAHTRLETRTHRPNVELcrdvaqyr 336
Cdd:TIGR02168  370 -------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE--DRRERLQQEIEELLKKLEE-------- 432
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 16753231    337 lmKEVQEITHNVARLKETLAQAQAELKGLHRRQLALQEEIQVKENTIY 384
Cdd:TIGR02168  433 --AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
 
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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