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Conserved domains on  [gi|257096967|sp|Q9VM92|]
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RecName: Full=Tubulin glycylase 3B; Short=dmTTLL3B

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
PubMed:  9538689|23358242|10685598|15890843

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 ...
 325-626 4.63e-95

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: 297.33  E-value: 4.63e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096967  325 VRHAEHYslDDARIKPPTPAEIVENQtFMVQSTDVLKSNAKFKVsekVMAEYARLAGLYLDQIESLRPDYRWdgsrNLWI 404
Cdd:pfam03133   1 FLLDEPY--HQALNHFPGSYEITRKD-LLWKNIKRTPCDRGLKG---DFLPRTFILPTDLAEFVDYFEDRER----NTWI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096967  405 LKPGYQSRGIGIVIRSSLDDILQWtsnNQNKKYIVQKYIERPLLIYRTKFDIRQYMLLTITDtKVSIWTYRDCYLRFSSQ 484
Cdd:pfam03133  71 VKPSASARGRGIRVTNKLSQIPKW---SQSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVN-PLRVYVYREGLLRFASV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096967  485 EF---TMDDLRESIHLTNNSVQKRYKnKTNRDSRLPKNNMWSLDQFKNYLRIMGaPDGSWSKTYNGFKQNLVAV-VMASL 560
Cdd:pfam03133 147 KYspsSSDLDDVEMHLTNYSIQKKSS-SLNEDYNEPHGHKWSLQNFWKYLEEKD-KDEIWLEIESIIIKTILAAeVEASR 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096967  561 DETELLQNAFELYGCDFMLDEHYNPILIEINSTPDLSPSTEITARICPMVLKDCIRVVVDLPKNPT 626
Cdd:pfam03133 225 LNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSVVPPDLEKD 290
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 325-626 4.63e-95

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: 297.33  E-value: 4.63e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096967  325 VRHAEHYslDDARIKPPTPAEIVENQtFMVQSTDVLKSNAKFKVsekVMAEYARLAGLYLDQIESLRPDYRWdgsrNLWI 404
Cdd:pfam03133   1 FLLDEPY--HQALNHFPGSYEITRKD-LLWKNIKRTPCDRGLKG---DFLPRTFILPTDLAEFVDYFEDRER----NTWI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096967  405 LKPGYQSRGIGIVIRSSLDDILQWtsnNQNKKYIVQKYIERPLLIYRTKFDIRQYMLLTITDtKVSIWTYRDCYLRFSSQ 484
Cdd:pfam03133  71 VKPSASARGRGIRVTNKLSQIPKW---SQSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVN-PLRVYVYREGLLRFASV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096967  485 EF---TMDDLRESIHLTNNSVQKRYKnKTNRDSRLPKNNMWSLDQFKNYLRIMGaPDGSWSKTYNGFKQNLVAV-VMASL 560
Cdd:pfam03133 147 KYspsSSDLDDVEMHLTNYSIQKKSS-SLNEDYNEPHGHKWSLQNFWKYLEEKD-KDEIWLEIESIIIKTILAAeVEASR 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096967  561 DETELLQNAFELYGCDFMLDEHYNPILIEINSTPDLSPSTEITARICPMVLKDCIRVVVDLPKNPT 626
Cdd:pfam03133 225 LNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSVVPPDLEKD 290
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 555-598 4.11e-03

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 40.09  E-value: 4.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 257096967 555 VVMASLDE--TELLQN----AFELYGC------DFMLDEHYNPILIEINSTPDLSP 598
Cdd:COG1181  221 ICPARLPEelEERIQElalkAFRALGCrgyarvDFRLDEDGEPYLLEVNTLPGMTP 276
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 325-626 4.63e-95

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: 297.33  E-value: 4.63e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096967  325 VRHAEHYslDDARIKPPTPAEIVENQtFMVQSTDVLKSNAKFKVsekVMAEYARLAGLYLDQIESLRPDYRWdgsrNLWI 404
Cdd:pfam03133   1 FLLDEPY--HQALNHFPGSYEITRKD-LLWKNIKRTPCDRGLKG---DFLPRTFILPTDLAEFVDYFEDRER----NTWI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096967  405 LKPGYQSRGIGIVIRSSLDDILQWtsnNQNKKYIVQKYIERPLLIYRTKFDIRQYMLLTITDtKVSIWTYRDCYLRFSSQ 484
Cdd:pfam03133  71 VKPSASARGRGIRVTNKLSQIPKW---SQSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVN-PLRVYVYREGLLRFASV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096967  485 EF---TMDDLRESIHLTNNSVQKRYKnKTNRDSRLPKNNMWSLDQFKNYLRIMGaPDGSWSKTYNGFKQNLVAV-VMASL 560
Cdd:pfam03133 147 KYspsSSDLDDVEMHLTNYSIQKKSS-SLNEDYNEPHGHKWSLQNFWKYLEEKD-KDEIWLEIESIIIKTILAAeVEASR 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096967  561 DETELLQNAFELYGCDFMLDEHYNPILIEINSTPDLSPSTEITARICPMVLKDCIRVVVDLPKNPT 626
Cdd:pfam03133 225 LNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSVVPPDLEKD 290
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 555-598 4.11e-03

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 40.09  E-value: 4.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 257096967 555 VVMASLDE--TELLQN----AFELYGC------DFMLDEHYNPILIEINSTPDLSP 598
Cdd:COG1181  221 ICPARLPEelEERIQElalkAFRALGCrgyarvDFRLDEDGEPYLLEVNTLPGMTP 276
 
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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