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Conserved domains on  [gi|217330594|ref|NP_055455|]
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tubulin monoglutamylase TTLL4 [Homo sapiens]

Protein Classification

tubulin--tyrosine ligase family protein( domain architecture ID 10504173)

tubulin--tyrosine ligase (TTL) family protein such as TTL that catalyzes the post-translational retyrosination of detyrosinated a-tubulin, and TTL-like (TTLL) enzymes that catalyze the glycylation and/or glutamylation, the post-translational addition of glycines and glutamates to genetically encoded glutamates in the intrinsically disordered tubulin C-terminal tails

CATH:  3.30.470.20
EC:  6.3.2.-
Gene Ontology:  GO:0005524

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
654-946 3.81e-115

Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several post-translational modifications of which the reversible detyrosination/tyrosination of the carboxy-terminal end of most alpha-tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL). The true physiological function of TTL has so far not been established. Tubulin-tyrosine ligase (TTL) catalyzes the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. In normally cycling cells, the tyrosinated form of tubulin predominates. However, in breast cancer cells, the detyrosinated form frequently predominates, with a correlation to tumour aggressiveness. On the other hand, 3-nitrotyrosine has been shown to be incorporated, by TTL, into the carboxy terminal end of detyrosinated alpha-tubulin. This reaction is not reversible by the carboxypeptidase enzyme. Cells cultured in 3-nitrotyrosine rich medium showed evidence of altered microtubule structure and function, including altered cell morphology, epithelial barrier dysfunction, and apoptosis. Bacterial homologs of TTL are predicted to form peptide tags. Some of these are fused to a 2-oxoglutarate Fe(II)-dependent dioxygenase domain.


:

Pssm-ID: 397308  Cd Length: 291  Bit Score: 359.73  E-value: 3.81e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217330594   654 REHQKLNHFPGSFQIGRKDRLWRNLSRMQSRFGKKeFSFFPQSFILPQDAKLLRKAWESSSRQKWIVKPPASARGIGIQV 733
Cdd:pfam03133    6 PYHQALNHFPGSYEITRKDLLWKNIKRTPCDRGLK-GDFLPRTFILPTDLAEFVDYFEDRERNTWIVKPSASARGRGIRV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217330594   734 IHKWSQLPK---RRPLLVQRYLHKPYLISGSKFDLRIYVYVTSYDPLRIYLFSDGLVRFASCKYSPSMKSLGNKFMHLTN 810
Cdd:pfam03133   85 TNKLSQIPKwsqSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPSSSDLDDVEMHLTN 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217330594   811 YSVNKKNAeyQANADEMACQGHKWALKALWNYLSQKgvNSDAIWEKIKDVVVKTIISSEpyvTSLLKMYVRRPYSCHELF 890
Cdd:pfam03133  165 YSIQKKSS--SLNEDYNEPHGHKWSLQNFWKYLEEK--DKDEIWLEIESIIIKTILAAE---VEASRLNVQPLPNCFELY 237
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 217330594   891 GFDIMLDENLKPWVLEVNISPSLHSSSPLDISIKGQMIRDLLNLAgfVLPNAEDII 946
Cdd:pfam03133  238 GFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSV--VPPDLEKDI 291
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
654-946 3.81e-115

Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several post-translational modifications of which the reversible detyrosination/tyrosination of the carboxy-terminal end of most alpha-tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL). The true physiological function of TTL has so far not been established. Tubulin-tyrosine ligase (TTL) catalyzes the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. In normally cycling cells, the tyrosinated form of tubulin predominates. However, in breast cancer cells, the detyrosinated form frequently predominates, with a correlation to tumour aggressiveness. On the other hand, 3-nitrotyrosine has been shown to be incorporated, by TTL, into the carboxy terminal end of detyrosinated alpha-tubulin. This reaction is not reversible by the carboxypeptidase enzyme. Cells cultured in 3-nitrotyrosine rich medium showed evidence of altered microtubule structure and function, including altered cell morphology, epithelial barrier dysfunction, and apoptosis. Bacterial homologs of TTL are predicted to form peptide tags. Some of these are fused to a 2-oxoglutarate Fe(II)-dependent dioxygenase domain.


Pssm-ID: 397308  Cd Length: 291  Bit Score: 359.73  E-value: 3.81e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217330594   654 REHQKLNHFPGSFQIGRKDRLWRNLSRMQSRFGKKeFSFFPQSFILPQDAKLLRKAWESSSRQKWIVKPPASARGIGIQV 733
Cdd:pfam03133    6 PYHQALNHFPGSYEITRKDLLWKNIKRTPCDRGLK-GDFLPRTFILPTDLAEFVDYFEDRERNTWIVKPSASARGRGIRV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217330594   734 IHKWSQLPK---RRPLLVQRYLHKPYLISGSKFDLRIYVYVTSYDPLRIYLFSDGLVRFASCKYSPSMKSLGNKFMHLTN 810
Cdd:pfam03133   85 TNKLSQIPKwsqSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPSSSDLDDVEMHLTN 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217330594   811 YSVNKKNAeyQANADEMACQGHKWALKALWNYLSQKgvNSDAIWEKIKDVVVKTIISSEpyvTSLLKMYVRRPYSCHELF 890
Cdd:pfam03133  165 YSIQKKSS--SLNEDYNEPHGHKWSLQNFWKYLEEK--DKDEIWLEIESIIIKTILAAE---VEASRLNVQPLPNCFELY 237
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 217330594   891 GFDIMLDENLKPWVLEVNISPSLHSSSPLDISIKGQMIRDLLNLAgfVLPNAEDII 946
Cdd:pfam03133  238 GFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSV--VPPDLEKDI 291
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
654-946 3.81e-115

Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several post-translational modifications of which the reversible detyrosination/tyrosination of the carboxy-terminal end of most alpha-tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL). The true physiological function of TTL has so far not been established. Tubulin-tyrosine ligase (TTL) catalyzes the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. In normally cycling cells, the tyrosinated form of tubulin predominates. However, in breast cancer cells, the detyrosinated form frequently predominates, with a correlation to tumour aggressiveness. On the other hand, 3-nitrotyrosine has been shown to be incorporated, by TTL, into the carboxy terminal end of detyrosinated alpha-tubulin. This reaction is not reversible by the carboxypeptidase enzyme. Cells cultured in 3-nitrotyrosine rich medium showed evidence of altered microtubule structure and function, including altered cell morphology, epithelial barrier dysfunction, and apoptosis. Bacterial homologs of TTL are predicted to form peptide tags. Some of these are fused to a 2-oxoglutarate Fe(II)-dependent dioxygenase domain.


Pssm-ID: 397308  Cd Length: 291  Bit Score: 359.73  E-value: 3.81e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217330594   654 REHQKLNHFPGSFQIGRKDRLWRNLSRMQSRFGKKeFSFFPQSFILPQDAKLLRKAWESSSRQKWIVKPPASARGIGIQV 733
Cdd:pfam03133    6 PYHQALNHFPGSYEITRKDLLWKNIKRTPCDRGLK-GDFLPRTFILPTDLAEFVDYFEDRERNTWIVKPSASARGRGIRV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217330594   734 IHKWSQLPK---RRPLLVQRYLHKPYLISGSKFDLRIYVYVTSYDPLRIYLFSDGLVRFASCKYSPSMKSLGNKFMHLTN 810
Cdd:pfam03133   85 TNKLSQIPKwsqSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPSSSDLDDVEMHLTN 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217330594   811 YSVNKKNAeyQANADEMACQGHKWALKALWNYLSQKgvNSDAIWEKIKDVVVKTIISSEpyvTSLLKMYVRRPYSCHELF 890
Cdd:pfam03133  165 YSIQKKSS--SLNEDYNEPHGHKWSLQNFWKYLEEK--DKDEIWLEIESIIIKTILAAE---VEASRLNVQPLPNCFELY 237
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 217330594   891 GFDIMLDENLKPWVLEVNISPSLHSSSPLDISIKGQMIRDLLNLAgfVLPNAEDII 946
Cdd:pfam03133  238 GFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSV--VPPDLEKDI 291
 
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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