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Conserved domains on  [gi|1958755504|ref|XP_038959802|]
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tubulin polyglutamylase TTLL7 isoform X3 [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 ...
 91-376 5.76e-78

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: 254.95  E-value: 5.76e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504  91 NYQRINHFPGMGEICRKDFLARNMTKMIKSRPMDYTFVPRTWIFPSEYTQFQNYvkelKKKRKQKTFIIKPANGAMGHGI 170
Cdd:pfam03133   7 YHQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKGDFLPRTFILPTDLAEFVDY----FEDRERNTWIVKPSASARGRGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504 171 SLIRNGDKIP--SQD-HLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPnESNLTQLYMH 247
Cdd:pfam03133  83 RVTNKLSQIPkwSQSrPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPS-SSDLDDVEMH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504 248 LTNYSVNKHNERFERNETEDKGSKRSIKWFTEFLQanQHDVTKFWSDISELVVKTLIVAEphvlhaYRMCRPGQPPGSEs 327
Cdd:pfam03133 162 LTNYSIQKKSSSLNEDYNEPHGHKWSLQNFWKYLE--EKDKDEIWLEIESIIIKTILAAE------VEASRLNVQPLPN- 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958755504 328 vCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALK 376
Cdd:pfam03133 233 -CFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLN 280
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
384-474 5.28e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504 384 DKRKNLAKQKAEAQRRLYGQNPIRRLSPGSSD---WEQQRHQLERRKEELKERLLQVRKQISQEEHENRHMGNYRRIypp 460
Cdd:COG4717   395 EEYQELKEELEELEEQLEELLGELEELLEALDeeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--- 471

                          90
                  ....*....|....
gi 1958755504 461 edKTLLEKYEGLLA 474
Cdd:COG4717   472 --AELLQELEELKA 483
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 91-376 5.76e-78

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: 254.95  E-value: 5.76e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504  91 NYQRINHFPGMGEICRKDFLARNMTKMIKSRPMDYTFVPRTWIFPSEYTQFQNYvkelKKKRKQKTFIIKPANGAMGHGI 170
Cdd:pfam03133   7 YHQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKGDFLPRTFILPTDLAEFVDY----FEDRERNTWIVKPSASARGRGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504 171 SLIRNGDKIP--SQD-HLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPnESNLTQLYMH 247
Cdd:pfam03133  83 RVTNKLSQIPkwSQSrPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPS-SSDLDDVEMH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504 248 LTNYSVNKHNERFERNETEDKGSKRSIKWFTEFLQanQHDVTKFWSDISELVVKTLIVAEphvlhaYRMCRPGQPPGSEs 327
Cdd:pfam03133 162 LTNYSIQKKSSSLNEDYNEPHGHKWSLQNFWKYLE--EKDKDEIWLEIESIIIKTILAAE------VEASRLNVQPLPN- 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958755504 328 vCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALK 376
Cdd:pfam03133 233 -CFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLN 280
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 128-209 4.46e-05

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: 46.47  E-value: 4.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504 128 VPRTWIFPS--EYTQFQNYVKElkkkrkqkTFIIKPANGAMGHGISLIRNGDKIPS---------QDHLIVQEYIEKPfl 196
Cdd:COG0189   111 VPPTLVTRDpdDLRAFLEELGG--------PVVLKPLDGSGGRGVFLVEDEDALESilealtelgSEPVLVQEFIPEE-- 180

                          90
                  ....*....|...
gi 1958755504 197 mEGykFDLRIYIL 209
Cdd:COG0189   181 -DG--RDIRVLVV 190
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
384-474 5.28e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504 384 DKRKNLAKQKAEAQRRLYGQNPIRRLSPGSSD---WEQQRHQLERRKEELKERLLQVRKQISQEEHENRHMGNYRRIypp 460
Cdd:COG4717   395 EEYQELKEELEELEEQLEELLGELEELLEALDeeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--- 471

                          90
                  ....*....|....
gi 1958755504 461 edKTLLEKYEGLLA 474
Cdd:COG4717   472 --AELLQELEELKA 483
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 385-448 7.74e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 38.92  E-value: 7.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958755504 385 KRKNLAKQKAEAQRRLYGQNPIRRLSPGSS-----DWE-------QQRHQLERRKEELKERLLQVRKQISQEEHEN 448
Cdd:pfam13904 111 KREESHKQKAAESASKSLAKPERKVSQEEAkevlqEWErkkleqqQRKREEEQREQLKKEEEEQERKQLAEKAWQK 186
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 91-376 5.76e-78

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: 254.95  E-value: 5.76e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504  91 NYQRINHFPGMGEICRKDFLARNMTKMIKSRPMDYTFVPRTWIFPSEYTQFQNYvkelKKKRKQKTFIIKPANGAMGHGI 170
Cdd:pfam03133   7 YHQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKGDFLPRTFILPTDLAEFVDY----FEDRERNTWIVKPSASARGRGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504 171 SLIRNGDKIP--SQD-HLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPnESNLTQLYMH 247
Cdd:pfam03133  83 RVTNKLSQIPkwSQSrPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPS-SSDLDDVEMH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504 248 LTNYSVNKHNERFERNETEDKGSKRSIKWFTEFLQanQHDVTKFWSDISELVVKTLIVAEphvlhaYRMCRPGQPPGSEs 327
Cdd:pfam03133 162 LTNYSIQKKSSSLNEDYNEPHGHKWSLQNFWKYLE--EKDKDEIWLEIESIIIKTILAAE------VEASRLNVQPLPN- 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958755504 328 vCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALK 376
Cdd:pfam03133 233 -CFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLN 280
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 128-209 4.46e-05

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: 46.47  E-value: 4.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504 128 VPRTWIFPS--EYTQFQNYVKElkkkrkqkTFIIKPANGAMGHGISLIRNGDKIPS---------QDHLIVQEYIEKPfl 196
Cdd:COG0189   111 VPPTLVTRDpdDLRAFLEELGG--------PVVLKPLDGSGGRGVFLVEDEDALESilealtelgSEPVLVQEFIPEE-- 180

                          90
                  ....*....|...
gi 1958755504 197 mEGykFDLRIYIL 209
Cdd:COG0189   181 -DG--RDIRVLVV 190
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 156-192 1.57e-03

ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).


Pssm-ID: 396979 [Multi-domain]  Cd Length: 160  Bit Score: 40.06  E-value: 1.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958755504 156 TFIIKPANGAMGHGISLIRNGDKI-PSQDHLIVQEYIE 192
Cdd:pfam02655  33 KYVVKPRDGCGGEGVRKVENGREDeAFIENVLVQEFIE 70
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
384-474 5.28e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755504 384 DKRKNLAKQKAEAQRRLYGQNPIRRLSPGSSD---WEQQRHQLERRKEELKERLLQVRKQISQEEHENRHMGNYRRIypp 460
Cdd:COG4717   395 EEYQELKEELEELEEQLEELLGELEELLEALDeeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--- 471

                          90
                  ....*....|....
gi 1958755504 461 edKTLLEKYEGLLA 474
Cdd:COG4717   472 --AELLQELEELKA 483
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 385-448 7.74e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 38.92  E-value: 7.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958755504 385 KRKNLAKQKAEAQRRLYGQNPIRRLSPGSS-----DWE-------QQRHQLERRKEELKERLLQVRKQISQEEHEN 448
Cdd:pfam13904 111 KREESHKQKAAESASKSLAKPERKVSQEEAkevlqEWErkkleqqQRKREEEQREQLKKEEEEQERKQLAEKAWQK 186
 
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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