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Conserved domains on  [gi|884884987|ref|XP_013002835|]
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tubulin--tyrosine ligase isoform X2 [Cavia porcellus]

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 ...
 81-389 2.12e-81

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: 251.49  E-value: 2.12e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987   81 IKTSPELAESCTWFPESYVIYPTNLKTPVAPVQNGI--QPPVHNSRTDEREFFLASYNRKKEDGEGNIWIAKSSAGAKam 158
Cdd:pfam03133   1 FLLDEPYHQALNHFPGSYEITRKDLLWKNIKRTPCDrgLKGDFLPRTFILPTDLAEFVDYFEDRERNTWIVKPSASAR-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987  159 rqegitwdllkvgewdschqpGEGILISSEAAELLDFidNQGQVHVIQKYLERPLLLepGHRKFDIRSWVLV--DHQYNI 236
Cdd:pfam03133  79 ---------------------GRGIRVTNKLSQIPKW--SQSRPLVVQKYIERPLLI--DGRKFDIRLYVLVtsVNPLRV 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987  237 YLYREGVLRTASEPYH--VDNFQDKTCHLTNHCIQKEYSKNYGKYEEGNEMFFEEFNRYLMSAlNITLETSILQQIKHII 314
Cdd:pfam03133 134 YVYREGLLRFASVKYSpsSSDLDDVEMHLTNYSIQKKSSSLNEDYNEPHGHKWSLQNFWKYLE-EKDKDEIWLEIESIII 212

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 884884987  315 RSCLLS-VEPAISTRHLPYQSFQLFGFDFMVDEELKVWLIEVNGAP--ACAQKLYAELCQGIVDLAISSVFPPPDVEQ 389
Cdd:pfam03133 213 KTILAAeVEASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPslHSTTKLDARLKEQLIDDVLNSVVPPDLEKD 290
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 81-389 2.12e-81

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: 251.49  E-value: 2.12e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987   81 IKTSPELAESCTWFPESYVIYPTNLKTPVAPVQNGI--QPPVHNSRTDEREFFLASYNRKKEDGEGNIWIAKSSAGAKam 158
Cdd:pfam03133   1 FLLDEPYHQALNHFPGSYEITRKDLLWKNIKRTPCDrgLKGDFLPRTFILPTDLAEFVDYFEDRERNTWIVKPSASAR-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987  159 rqegitwdllkvgewdschqpGEGILISSEAAELLDFidNQGQVHVIQKYLERPLLLepGHRKFDIRSWVLV--DHQYNI 236
Cdd:pfam03133  79 ---------------------GRGIRVTNKLSQIPKW--SQSRPLVVQKYIERPLLI--DGRKFDIRLYVLVtsVNPLRV 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987  237 YLYREGVLRTASEPYH--VDNFQDKTCHLTNHCIQKEYSKNYGKYEEGNEMFFEEFNRYLMSAlNITLETSILQQIKHII 314
Cdd:pfam03133 134 YVYREGLLRFASVKYSpsSSDLDDVEMHLTNYSIQKKSSSLNEDYNEPHGHKWSLQNFWKYLE-EKDKDEIWLEIESIII 212

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 884884987  315 RSCLLS-VEPAISTRHLPYQSFQLFGFDFMVDEELKVWLIEVNGAP--ACAQKLYAELCQGIVDLAISSVFPPPDVEQ 389
Cdd:pfam03133 213 KTILAAeVEASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPslHSTTKLDARLKEQLIDDVLNSVVPPDLEKD 290
YheC COG5891
Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, ...
 190-359 1.62e-05

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: 46.52  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987 190 AELLDFIDNQ--GQVHVIQKYLErplLLEPGHRKFDIRswVLVdhQYNiylyREG-------VLRTASepyhvdnfqdKT 260
Cdd:COG5891  230 DELLAFLRRLlrRKRYIIQQGIP---LATIDGRPFDFR--VLV--QKN----GRGewvvtgiVARIAG----------PG 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987 261 CHLTNHciqkeyskNYGkyeeGNEMFFEEFnryLMSALNITLETSILQQIKHIIRSCLLSVEPAistrhlpYQSFQLFGF 340
Cdd:COG5891  289 SITTNL--------SGG----GTALPLEEL---LRRAFGDSKAEEILQKLERIALEIARALEES-------YGGLGELGI 346

                        170
                 ....*....|....*....
gi 884884987 341 DFMVDEELKVWLIEVNGAP 359
Cdd:COG5891  347 DLGIDRDGKIWLLEVNSKP 365
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 81-389 2.12e-81

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: 251.49  E-value: 2.12e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987   81 IKTSPELAESCTWFPESYVIYPTNLKTPVAPVQNGI--QPPVHNSRTDEREFFLASYNRKKEDGEGNIWIAKSSAGAKam 158
Cdd:pfam03133   1 FLLDEPYHQALNHFPGSYEITRKDLLWKNIKRTPCDrgLKGDFLPRTFILPTDLAEFVDYFEDRERNTWIVKPSASAR-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987  159 rqegitwdllkvgewdschqpGEGILISSEAAELLDFidNQGQVHVIQKYLERPLLLepGHRKFDIRSWVLV--DHQYNI 236
Cdd:pfam03133  79 ---------------------GRGIRVTNKLSQIPKW--SQSRPLVVQKYIERPLLI--DGRKFDIRLYVLVtsVNPLRV 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987  237 YLYREGVLRTASEPYH--VDNFQDKTCHLTNHCIQKEYSKNYGKYEEGNEMFFEEFNRYLMSAlNITLETSILQQIKHII 314
Cdd:pfam03133 134 YVYREGLLRFASVKYSpsSSDLDDVEMHLTNYSIQKKSSSLNEDYNEPHGHKWSLQNFWKYLE-EKDKDEIWLEIESIII 212

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 884884987  315 RSCLLS-VEPAISTRHLPYQSFQLFGFDFMVDEELKVWLIEVNGAP--ACAQKLYAELCQGIVDLAISSVFPPPDVEQ 389
Cdd:pfam03133 213 KTILAAeVEASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPslHSTTKLDARLKEQLIDDVLNSVVPPDLEKD 290
YheC COG5891
Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, ...
 190-359 1.62e-05

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: 46.52  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987 190 AELLDFIDNQ--GQVHVIQKYLErplLLEPGHRKFDIRswVLVdhQYNiylyREG-------VLRTASepyhvdnfqdKT 260
Cdd:COG5891  230 DELLAFLRRLlrRKRYIIQQGIP---LATIDGRPFDFR--VLV--QKN----GRGewvvtgiVARIAG----------PG 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987 261 CHLTNHciqkeyskNYGkyeeGNEMFFEEFnryLMSALNITLETSILQQIKHIIRSCLLSVEPAistrhlpYQSFQLFGF 340
Cdd:COG5891  289 SITTNL--------SGG----GTALPLEEL---LRRAFGDSKAEEILQKLERIALEIARALEES-------YGGLGELGI 346

                        170
                 ....*....|....*....
gi 884884987 341 DFMVDEELKVWLIEVNGAP 359
Cdd:COG5891  347 DLGIDRDGKIWLLEVNSKP 365
ATPgrasp_YheCD pfam14398
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ...
 190-362 1.08e-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: 43.32  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987  190 AELLDFIDNQ--GQVHVIQKYLErplLLEPGHRKFDIRswVLVdhQYNiylyREG-------VLRTASEpyhvdnfQDKT 260
Cdd:pfam14398  93 SELESFLRRLlgKKRYIIQQGID---LATIDGRPFDFR--VLV--QKN----GKGkwvvtgiAARIAGP-------GSIT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 884884987  261 CHLTNHciqkeysknygkyeeGNEMFFEEFNRYLMSALNITLetsILQQIKHIIRSCLLSVEpaistrhlpyQSFQLF-- 338
Cdd:pfam14398 155 TNLSGG---------------GTAIPLEEALRRAFGEERAEK---ILEKLEELALELARALE----------ESFGGLge 206

                         170       180
                  ....*....|....*....|....*
gi 884884987  339 -GFDFMVDEELKVWLIEVNGAPACA 362
Cdd:pfam14398 207 lGLDLGIDKNGRVWLLEVNSKPGRS 231
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 332-378 6.73e-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: 38.16  E-value: 6.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 884884987 332 YQSFQLFGF---DFMVDEELKVWLIEVNGAP----------ACAQKL--YAELCQGIVDLAI 378
Cdd:COG1181  242 FRALGCRGYarvDFRLDEDGEPYLLEVNTLPgmtptsllpkAAAAAGisYEELIERIIELAL 303
 
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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