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Conserved domains on  [gi|148223131|ref|NP_001079467|]
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tektin 2 L homeolog [Xenopus laevis]

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 ...
17-398 1.72e-159

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: 454.70  E-value: 1.72e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131   17 WHTNSALISTNAERQRISSHQIRQEARALRNETSNQTKWDEQNNSTRLDERIDDVEKWRQVLGKCLSEVDAEINALTQIK 96
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131   97 DEAEQALQAKNVPLDVAIECLTHRESRREIDLVKDPVEDELHKEVEVIEGVRRALQQKISEAFEQLCLLQEARHQLNFDQ 176
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131  177 RNKTETVEIDQTCLSLTRNSPNISLKVDPARVLNGTTTPQEWVQFSRYSKERAEAEVRASGRLRESIALTIAQTNNECEA 256
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131  257 QRVAVEFSFRKRIHEFERALAELNWQEKNTKEEIEEMEGDIRHLDEDLRAKKGSLKLAHTRLETRLHRPSVELCRDQVQY 336
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223131  337 GLTDEVCQIEGTIAALKEKLAQSQNALDALYKQLARIEVDTKWKQNSLSLDN-KCLDTRRKLT 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 ...
17-398 1.72e-159

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: 454.70  E-value: 1.72e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131   17 WHTNSALISTNAERQRISSHQIRQEARALRNETSNQTKWDEQNNSTRLDERIDDVEKWRQVLGKCLSEVDAEINALTQIK 96
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131   97 DEAEQALQAKNVPLDVAIECLTHRESRREIDLVKDPVEDELHKEVEVIEGVRRALQQKISEAFEQLCLLQEARHQLNFDQ 176
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131  177 RNKTETVEIDQTCLSLTRNSPNISLKVDPARVLNGTTTPQEWVQFSRYSKERAEAEVRASGRLRESIALTIAQTNNECEA 256
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131  257 QRVAVEFSFRKRIHEFERALAELNWQEKNTKEEIEEMEGDIRHLDEDLRAKKGSLKLAHTRLETRLHRPSVELCRDQVQY 336
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223131  337 GLTDEVCQIEGTIAALKEKLAQSQNALDALYKQLARIEVDTKWKQNSLSLDN-KCLDTRRKLT 398
Cdd:pfam03148 321 GLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDReKCMGLRKRLP 383
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
78-366 5.90e-04

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: 42.35  E-value: 5.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131    78 LGKCLSEVDAEINALTQIKDEAEQALQAKN---VPLDVAIECLTHRESRREIDLVKDPVE--------DELHKEVEVIEG 146
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEveqleeriAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131   147 VRRALQQKISEAFEQLCLLQEARHQLNFDQRNKTETVEIDQTCLSLTRNSpnisLKVDPARVLNGTTTPQEWVQFSRYSK 226
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE----LTLLNEEAANLRERLESLERRIAATE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131   227 ERAEAEVRASGRLRESIA---LTIAQTNNECEAQRVAVEfSFRKRIHEFERALAELNWQEKNTKEEIEEMEGDIRHLDED 303
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELE-ALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223131   304 LRAKKGSLKLAHTRLETRLHRPSVELCRDQVQYGLTDEVCQ-----IEGTIAALKEKLAQSQNALDAL 366
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEalenkIEDDEEEARRRLKRLENKIKEL 984
 
Name Accession Description Interval E-value
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
17-398 1.72e-159

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: 454.70  E-value: 1.72e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131   17 WHTNSALISTNAERQRISSHQIRQEARALRNETSNQTKWDEQNNSTRLDERIDDVEKWRQVLGKCLSEVDAEINALTQIK 96
Cdd:pfam03148   1 WRANNQELYREAEAQRNDAERLRQESRRLRNETDAKTKWDQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131   97 DEAEQALQAKNVPLDVAIECLTHRESRREIDLVKDPVEDELHKEVEVIEGVRRALQQKISEAFEQLCLLQEARHQLNFDQ 176
Cdd:pfam03148  81 RRLEKALEALEEPLHIAQECLTLREKRQGIDLVHDEVEKELLKEVELIEGIQELLQRTLEQAWEQLRLLRAARHKLEKDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131  177 RNKTETVEIDQTCLSLTRNSPNISLKVDPARVLNGTTTPQEWVQFSRYSKERAEAEVRASGRLRESIALTIAQTNNECEA 256
Cdd:pfam03148 161 SDKKEALEIDEKCLSLNNTSPNISYKPGPTRIPPNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131  257 QRVAVEFSFRKRIHEFERALAELNWQEKNTKEEIEEMEGDIRHLDEDLRAKKGSLKLAHTRLETRLHRPSVELCRDQVQY 336
Cdd:pfam03148 241 QADAVNFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELCRDEAQY 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148223131  337 GLTDEVCQIEGTIAALKEKLAQSQNALDALYKQLARIEVDTKWKQNSLSLDN-KCLDTRRKLT 398
Cdd:pfam03148 321 GLVDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDIAVKANSLFIDReKCMGLRKRLP 383
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
78-366 5.90e-04

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: 42.35  E-value: 5.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131    78 LGKCLSEVDAEINALTQIKDEAEQALQAKN---VPLDVAIECLTHRESRREIDLVKDPVE--------DELHKEVEVIEG 146
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEveqleeriAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131   147 VRRALQQKISEAFEQLCLLQEARHQLNFDQRNKTETVEIDQTCLSLTRNSpnisLKVDPARVLNGTTTPQEWVQFSRYSK 226
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE----LTLLNEEAANLRERLESLERRIAATE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223131   227 ERAEAEVRASGRLRESIA---LTIAQTNNECEAQRVAVEfSFRKRIHEFERALAELNWQEKNTKEEIEEMEGDIRHLDED 303
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELE-ALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223131   304 LRAKKGSLKLAHTRLETRLHRPSVELCRDQVQYGLTDEVCQ-----IEGTIAALKEKLAQSQNALDAL 366
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEalenkIEDDEEEARRRLKRLENKIKEL 984
 
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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