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Conserved domains on  [gi|188219535|ref|NP_849200|]
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polyglutamylase complex subunit TTLL1 [Mus musculus]

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 ...
59-364 3.75e-126

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: 366.28  E-value: 3.75e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535   59 DQIVNHFPNHYELTRKDLMVKNIKRYRKELEKEGsplaekdengkylylDFVPVTYMLPADYNLFVEEFRKSPSSTWIMK 138
Cdd:pfam03133   8 HQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKG---------------DFLPRTFILPTDLAEFVDYFEDRERNTWIVK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535  139 PCGKAQGKGIFLINKLSQIKKWSrdsktssfvsqsTKEAYVISVYINNPLLIGGRKFDLRLYVLVSTYRPLRCYMYKLGF 218
Cdd:pfam03133  73 PSASARGRGIRVTNKLSQIPKWS------------QSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535  219 CRFCTVKYTPSTSELDNMFVHLTNVAIQKH----GEDYNHIHGGKWTVNNLRLYLESTRGREVTSKLFDEIHWIIVQS-L 293
Cdd:pfam03133 141 LRFASVKYSPSSSDLDDVEMHLTNYSIQKKssslNEDYNEPHGHKWSLQNFWKYLEEKDKDEIWLEIESIIIKTILAAeV 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219535  294 KAVAPVMNNDKHCFECYGYDIIIDDKLKPWLIEVNASPSLTSSTANDRILKYNLINDTLNIAVPNGEIPDC 364
Cdd:pfam03133 221 EASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSVVPPDLEKDI 291
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
59-364 3.75e-126

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: 366.28  E-value: 3.75e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535   59 DQIVNHFPNHYELTRKDLMVKNIKRYRKELEKEGsplaekdengkylylDFVPVTYMLPADYNLFVEEFRKSPSSTWIMK 138
Cdd:pfam03133   8 HQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKG---------------DFLPRTFILPTDLAEFVDYFEDRERNTWIVK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535  139 PCGKAQGKGIFLINKLSQIKKWSrdsktssfvsqsTKEAYVISVYINNPLLIGGRKFDLRLYVLVSTYRPLRCYMYKLGF 218
Cdd:pfam03133  73 PSASARGRGIRVTNKLSQIPKWS------------QSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535  219 CRFCTVKYTPSTSELDNMFVHLTNVAIQKH----GEDYNHIHGGKWTVNNLRLYLESTRGREVTSKLFDEIHWIIVQS-L 293
Cdd:pfam03133 141 LRFASVKYSPSSSDLDDVEMHLTNYSIQKKssslNEDYNEPHGHKWSLQNFWKYLEEKDKDEIWLEIESIIIKTILAAeV 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219535  294 KAVAPVMNNDKHCFECYGYDIIIDDKLKPWLIEVNASPSLTSSTANDRILKYNLINDTLNIAVPNGEIPDC 364
Cdd:pfam03133 221 EASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSVVPPDLEKDI 291
YheC COG5891
Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, ...
109-332 1.24e-06

Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444593 [Multi-domain]  Cd Length: 400  Bit Score: 50.37  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535 109 FVPVTYMLPADYNL--FVEEFRKSpsstwIMKPCGKAQGKGIFLI-------------NKLSQIKKWSRDSKTSSFV-SQ 172
Cdd:COG5891  165 YLPETELLTSPEDLleFLKRYKSV-----YLKPVNGSLGRGIIRIekkgdgyllryrrKKRNVRRRFSSLDELLAFLrRL 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535 173 STKEAYVISVYINnPLLIGGRKFDLRL---------YVLVSTYrplrcymyklgfcrfctVKYTPSTSeldnmfvHLTNV 243
Cdd:COG5891  240 LRRKRYIIQQGIP-LATIDGRPFDFRVlvqkngrgeWVVTGIV-----------------ARIAGPGS-------ITTNL 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535 244 AiqkhgedynhiHGGkwTVNNLRLYLESTRGREVTSKLFDEIHWIIVQSLKAVAPVMNndkHCFECyGYDIIIDDKLKPW 323
Cdd:COG5891  295 S-----------GGG--TALPLEELLRRAFGDSKAEEILQKLERIALEIARALEESYG---GLGEL-GIDLGIDRDGKIW 357

                 ....*....
gi 188219535 324 LIEVNASPS 332
Cdd:COG5891  358 LLEVNSKPG 366
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
59-364 3.75e-126

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: 366.28  E-value: 3.75e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535   59 DQIVNHFPNHYELTRKDLMVKNIKRYRKELEKEGsplaekdengkylylDFVPVTYMLPADYNLFVEEFRKSPSSTWIMK 138
Cdd:pfam03133   8 HQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKG---------------DFLPRTFILPTDLAEFVDYFEDRERNTWIVK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535  139 PCGKAQGKGIFLINKLSQIKKWSrdsktssfvsqsTKEAYVISVYINNPLLIGGRKFDLRLYVLVSTYRPLRCYMYKLGF 218
Cdd:pfam03133  73 PSASARGRGIRVTNKLSQIPKWS------------QSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535  219 CRFCTVKYTPSTSELDNMFVHLTNVAIQKH----GEDYNHIHGGKWTVNNLRLYLESTRGREVTSKLFDEIHWIIVQS-L 293
Cdd:pfam03133 141 LRFASVKYSPSSSDLDDVEMHLTNYSIQKKssslNEDYNEPHGHKWSLQNFWKYLEEKDKDEIWLEIESIIIKTILAAeV 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219535  294 KAVAPVMNNDKHCFECYGYDIIIDDKLKPWLIEVNASPSLTSSTANDRILKYNLINDTLNIAVPNGEIPDC 364
Cdd:pfam03133 221 EASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSVVPPDLEKDI 291
YheC COG5891
Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, ...
109-332 1.24e-06

Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444593 [Multi-domain]  Cd Length: 400  Bit Score: 50.37  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535 109 FVPVTYMLPADYNL--FVEEFRKSpsstwIMKPCGKAQGKGIFLI-------------NKLSQIKKWSRDSKTSSFV-SQ 172
Cdd:COG5891  165 YLPETELLTSPEDLleFLKRYKSV-----YLKPVNGSLGRGIIRIekkgdgyllryrrKKRNVRRRFSSLDELLAFLrRL 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535 173 STKEAYVISVYINnPLLIGGRKFDLRL---------YVLVSTYrplrcymyklgfcrfctVKYTPSTSeldnmfvHLTNV 243
Cdd:COG5891  240 LRRKRYIIQQGIP-LATIDGRPFDFRVlvqkngrgeWVVTGIV-----------------ARIAGPGS-------ITTNL 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535 244 AiqkhgedynhiHGGkwTVNNLRLYLESTRGREVTSKLFDEIHWIIVQSLKAVAPVMNndkHCFECyGYDIIIDDKLKPW 323
Cdd:COG5891  295 S-----------GGG--TALPLEELLRRAFGDSKAEEILQKLERIALEIARALEESYG---GLGEL-GIDLGIDRDGKIW 357

                 ....*....
gi 188219535 324 LIEVNASPS 332
Cdd:COG5891  358 LLEVNSKPG 366
ATPgrasp_YheCD pfam14398
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ...
136-332 2.79e-04

YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the modification/biosynthesis of spore-wall and capsular proteins.


Pssm-ID: 405146 [Multi-domain]  Cd Length: 256  Bit Score: 42.17  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535  136 IMKPCGKAQGKGIFLINKLSQ-IKKWSRD---SKTSSFVSQST----------KEAYVISVYInNPLLIGGRKFDLRlyV 201
Cdd:pfam14398  52 YLKPVNGSLGKGILRIEKDGGgYYLYGRYgknSKTNRFLDFSElesflrrllgKKRYIIQQGI-DLATIDGRPFDFR--V 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219535  202 LVstyrplrcymyklgfcrfctvkytpstseldnmfvhltnvaiQKHGEdynhihgGKWTVN--------------NLrl 267
Cdd:pfam14398 129 LV------------------------------------------QKNGK-------GKWVVTgiaariagpgsittNL-- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219535  268 yleSTRGREVT-----SKLFDEIHWI-IVQSLK----AVAPVMNND-KHCFEcYGYDIIIDDKLKPWLIEVNASPS 332
Cdd:pfam14398 158 ---SGGGTAIPleealRRAFGEERAEkILEKLEelalELARALEESfGGLGE-LGLDLGIDKNGRVWLLEVNSKPG 229
 
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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