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Conserved domains on  [gi|1958786175|ref|XP_038969254|]
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tubulin polyglutamylase TTLL5 isoform X15 [Rattus norvegicus]

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

Gene Ontology:  GO:0005524
PubMed:  23358242|9538689

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 ...
 117-395 4.22e-104

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: 315.04  E-value: 4.22e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 117 QKVNHFPRSYELTRKDRLYKNIIRMQHTHGFKaFHILPQTFLLPAEYAEFCNSYSKD-RGPWIVKPVASSRGRGVYLINN 195
Cdd:pfam03133   9 QALNHFPGSYEITRKDLLWKNIKRTPCDRGLK-GDFLPRTFILPTDLAEFVDYFEDReRNTWIVKPSASARGRGIRVTNK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 196 PNQISLEENI---LVSRYINNPLLIDDFKFDVRLYVLVTSYDPLVIYLYEEGLARFATVRYDQGSKNIRNQFMHLTNYSV 272
Cdd:pfam03133  88 LSQIPKWSQSrplVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPSSSDLDDVEMHLTNYSI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 273 NKKsgdYVSCDDPEVEDYGNKWSMSAMLRYLkqEGKDTTALMAHVEDLIIKTIISAElaiATACKTFVPHRSSCFELYGF 352
Cdd:pfam03133 168 QKK---SSSLNEDYNEPHGHKWSLQNFWKYL--EEKDKDEIWLEIESIIIKTILAAE---VEASRLNVQPLPNCFELYGF 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958786175 353 DVLIDNTLKPWLLEVNLSPSLACDAPLDLKIKASMISDMFTVV 395
Cdd:pfam03133 240 DFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSV 282
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 117-395 4.22e-104

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: 315.04  E-value: 4.22e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 117 QKVNHFPRSYELTRKDRLYKNIIRMQHTHGFKaFHILPQTFLLPAEYAEFCNSYSKD-RGPWIVKPVASSRGRGVYLINN 195
Cdd:pfam03133   9 QALNHFPGSYEITRKDLLWKNIKRTPCDRGLK-GDFLPRTFILPTDLAEFVDYFEDReRNTWIVKPSASARGRGIRVTNK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 196 PNQISLEENI---LVSRYINNPLLIDDFKFDVRLYVLVTSYDPLVIYLYEEGLARFATVRYDQGSKNIRNQFMHLTNYSV 272
Cdd:pfam03133  88 LSQIPKWSQSrplVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPSSSDLDDVEMHLTNYSI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 273 NKKsgdYVSCDDPEVEDYGNKWSMSAMLRYLkqEGKDTTALMAHVEDLIIKTIISAElaiATACKTFVPHRSSCFELYGF 352
Cdd:pfam03133 168 QKK---SSSLNEDYNEPHGHKWSLQNFWKYL--EEKDKDEIWLEIESIIIKTILAAE---VEASRLNVQPLPNCFELYGF 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958786175 353 DVLIDNTLKPWLLEVNLSPSLACDAPLDLKIKASMISDMFTVV 395
Cdd:pfam03133 240 DFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSV 282
YheC COG5891
Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, ...
 153-372 2.72e-03

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: 40.36  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 153 LPQTFLL--PAEYAEFCNSYSKdrgpWIVKPVASSRGRGVYLIN-NPNQISLEEnilVSRYINNPLLIDDFKfdvRLYVL 229
Cdd:COG5891   166 LPETELLtsPEDLLEFLKRYKS----VYLKPVNGSLGRGIIRIEkKGDGYLLRY---RRKKRNVRRRFSSLD---ELLAF 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 230 VTSYDPLVIYLYEEG--LARFATVRYDqgsknIRnqfMHltnysVNKksgdyvscddpeveDYGNKWSMSAML------- 300
Cdd:COG5891   236 LRRLLRRKRYIIQQGipLATIDGRPFD-----FR---VL-----VQK--------------NGRGEWVVTGIVariagpg 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 301 ----------------RYLKQEGKDTTAlmAHVEDLIIktiisaELAIATAcKTFVPHRSSCFELyGFDVLIDNTLKPWL 364
Cdd:COG5891   289 sittnlsgggtalpleELLRRAFGDSKA--EEILQKLE------RIALEIA-RALEESYGGLGEL-GIDLGIDRDGKIWL 358


                  ....*...
gi 1958786175 365 LEVNLSPS 372
Cdd:COG5891   359 LEVNSKPG 366
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 117-395 4.22e-104

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: 315.04  E-value: 4.22e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 117 QKVNHFPRSYELTRKDRLYKNIIRMQHTHGFKaFHILPQTFLLPAEYAEFCNSYSKD-RGPWIVKPVASSRGRGVYLINN 195
Cdd:pfam03133   9 QALNHFPGSYEITRKDLLWKNIKRTPCDRGLK-GDFLPRTFILPTDLAEFVDYFEDReRNTWIVKPSASARGRGIRVTNK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 196 PNQISLEENI---LVSRYINNPLLIDDFKFDVRLYVLVTSYDPLVIYLYEEGLARFATVRYDQGSKNIRNQFMHLTNYSV 272
Cdd:pfam03133  88 LSQIPKWSQSrplVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPSSSDLDDVEMHLTNYSI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 273 NKKsgdYVSCDDPEVEDYGNKWSMSAMLRYLkqEGKDTTALMAHVEDLIIKTIISAElaiATACKTFVPHRSSCFELYGF 352
Cdd:pfam03133 168 QKK---SSSLNEDYNEPHGHKWSLQNFWKYL--EEKDKDEIWLEIESIIIKTILAAE---VEASRLNVQPLPNCFELYGF 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958786175 353 DVLIDNTLKPWLLEVNLSPSLACDAPLDLKIKASMISDMFTVV 395
Cdd:pfam03133 240 DFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSV 282
YheC COG5891
Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, ...
 153-372 2.72e-03

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: 40.36  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 153 LPQTFLL--PAEYAEFCNSYSKdrgpWIVKPVASSRGRGVYLIN-NPNQISLEEnilVSRYINNPLLIDDFKfdvRLYVL 229
Cdd:COG5891   166 LPETELLtsPEDLLEFLKRYKS----VYLKPVNGSLGRGIIRIEkKGDGYLLRY---RRKKRNVRRRFSSLD---ELLAF 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 230 VTSYDPLVIYLYEEG--LARFATVRYDqgsknIRnqfMHltnysVNKksgdyvscddpeveDYGNKWSMSAML------- 300
Cdd:COG5891   236 LRRLLRRKRYIIQQGipLATIDGRPFD-----FR---VL-----VQK--------------NGRGEWVVTGIVariagpg 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 301 ----------------RYLKQEGKDTTAlmAHVEDLIIktiisaELAIATAcKTFVPHRSSCFELyGFDVLIDNTLKPWL 364
Cdd:COG5891   289 sittnlsgggtalpleELLRRAFGDSKA--EEILQKLE------RIALEIA-RALEESYGGLGEL-GIDLGIDRDGKIWL 358


                  ....*...
gi 1958786175 365 LEVNLSPS 372
Cdd:COG5891   359 LEVNSKPG 366
ATPgrasp_YheCD pfam14398
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ...
 153-372 3.37e-03

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: 39.47  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 153 LPQTFLL--PAEYAEFCNSYSKdrgpWIVKPVASSRGRGVYLINNPNqislEENILVSRYINNPLLIDDFKFDvRLYVLV 230
Cdd:pfam14398  29 LPETELLqsPEDLERMLEKYGS----VYLKPVNGSLGKGILRIEKDG----GGYYLYGRYGKNSKTNRFLDFS-ELESFL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 231 TSYDPLVIYLYEEG--LARFATVRYDqgsknIRnqfMHltnysVNKksgdyvscddpeveDYGNKWSMSAM--------- 299
Cdd:pfam14398 100 RRLLGKKRYIIQQGidLATIDGRPFD-----FR---VL-----VQK--------------NGKGKWVVTGIaariagpgs 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786175 300 --------------LRYLKQEGKDTTAlmahveDLIIKTIISAELAIATA-CKTFvphrSSCFELyGFDVLIDNTLKPWL 364
Cdd:pfam14398 153 ittnlsgggtaiplEEALRRAFGEERA------EKILEKLEELALELARAlEESF----GGLGEL-GLDLGIDKNGRVWL 221


                  ....*...
gi 1958786175 365 LEVNLSPS 372
Cdd:pfam14398 222 LEVNSKPG 229
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 174-229 5.27e-03

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 39.15  E-value: 5.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958786175 174 RGPWIVKPVASSRGRGVYLINNPNQIS--LE-------ENILVSRYINnplliDDFKFDVRLYVL 229
Cdd:COG0189   131 GGPVVLKPLDGSGGRGVFLVEDEDALEsiLEaltelgsEPVLVQEFIP-----EEDGRDIRVLVV 190
 
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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