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Conserved domains on  [gi|6980181|gb|AAF23275|]
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KIAA0998, partial [Homo sapiens]

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 ...
 56-334 1.51e-100

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: 318.13  E-value: 1.51e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181      56 QKVNHFPRSYELTRKDRLYKNIIRMQHTHGFKaFHILPQTFLLPAEYAEFCNSYSKD-RGPWIVKPVASSRGRGVYLINN 134
Cdd:pfam03133    9 QALNHFPGSYEITRKDLLWKNIKRTPCDRGLK-GDFLPRTFILPTDLAEFVDYFEDReRNTWIVKPSASARGRGIRVTNK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181     135 PNQISLEENI---LVSRYINNPLLIDDFKFDVRLYVLVTSYDPLVIYLYEEGLARFATVRYDQGAKNIRNQFMHLTNYSV 211
Cdd:pfam03133   88 LSQIPKWSQSrplVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPSSSDLDDVEMHLTNYSI 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181     212 NKKsgdYVSCDDPEVEDYGNKWSMSAMLRYLKQEgrDTTALMAHVEDLIIKTIISAElaiATACKTFVPHRSSCFELYGF 291
Cdd:pfam03133  168 QKK---SSSLNEDYNEPHGHKWSLQNFWKYLEEK--DKDEIWLEIESIIIKTILAAE---VEASRLNVQPLPNCFELYGF 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 6980181     292 DVLIDSTLKPWLLEVNLSPSLACDAPLDLKIKASMISDMFTVV 334
Cdd:pfam03133  240 DFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSV 282
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 56-334 1.51e-100

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: 318.13  E-value: 1.51e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181      56 QKVNHFPRSYELTRKDRLYKNIIRMQHTHGFKaFHILPQTFLLPAEYAEFCNSYSKD-RGPWIVKPVASSRGRGVYLINN 134
Cdd:pfam03133    9 QALNHFPGSYEITRKDLLWKNIKRTPCDRGLK-GDFLPRTFILPTDLAEFVDYFEDReRNTWIVKPSASARGRGIRVTNK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181     135 PNQISLEENI---LVSRYINNPLLIDDFKFDVRLYVLVTSYDPLVIYLYEEGLARFATVRYDQGAKNIRNQFMHLTNYSV 211
Cdd:pfam03133   88 LSQIPKWSQSrplVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPSSSDLDDVEMHLTNYSI 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181     212 NKKsgdYVSCDDPEVEDYGNKWSMSAMLRYLKQEgrDTTALMAHVEDLIIKTIISAElaiATACKTFVPHRSSCFELYGF 291
Cdd:pfam03133  168 QKK---SSSLNEDYNEPHGHKWSLQNFWKYLEEK--DKDEIWLEIESIIIKTILAAE---VEASRLNVQPLPNCFELYGF 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 6980181     292 DVLIDSTLKPWLLEVNLSPSLACDAPLDLKIKASMISDMFTVV 334
Cdd:pfam03133  240 DFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSV 282
YheC COG5891
Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, ...
 48-311 1.11e-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: 42.67  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181    48 LLRTLSEAQKVNHFprSYELTRKDRLYKNIIRMQHTHgfkafHILPQTFLL--PAEYAEFCNSYSKdrgpWIVKPVASSR 125
Cdd:COG5891  129 LREKLKKRPGIPFF--NPRFFNKWEVYQLLSKDPRLR-----PYLPETELLtsPEDLLEFLKRYKS----VYLKPVNGSL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181   126 GRGVYLIN-NPNQISLEEnilVSRYINNPLLIDDFKfdvRLYVLVTSYDPLVIYLYEEG--LARFATVRYDqgaknIRnq 202
Cdd:COG5891  198 GRGIIRIEkKGDGYLLRY---RRKKRNVRRRFSSLD---ELLAFLRRLLRRKRYIIQQGipLATIDGRPFD-----FR-- 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181   203 fMHltnysVNKksgdyvscddpeveDYGNKWSMSAML-----------------------RYLKQEGRDTTAlmAHVEDL 259
Cdd:COG5891  265 -VL-----VQK--------------NGRGEWVVTGIVariagpgsittnlsgggtalpleELLRRAFGDSKA--EEILQK 322

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6980181   260 IIktiisaELAIATAcKTFVPHRSSCFELyGFDVLIDSTLKPWLLEVNLSPS 311
Cdd:COG5891  323 LE------RIALEIA-RALEESYGGLGEL-GIDLGIDRDGKIWLLEVNSKPG 366
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 56-334 1.51e-100

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: 318.13  E-value: 1.51e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181      56 QKVNHFPRSYELTRKDRLYKNIIRMQHTHGFKaFHILPQTFLLPAEYAEFCNSYSKD-RGPWIVKPVASSRGRGVYLINN 134
Cdd:pfam03133    9 QALNHFPGSYEITRKDLLWKNIKRTPCDRGLK-GDFLPRTFILPTDLAEFVDYFEDReRNTWIVKPSASARGRGIRVTNK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181     135 PNQISLEENI---LVSRYINNPLLIDDFKFDVRLYVLVTSYDPLVIYLYEEGLARFATVRYDQGAKNIRNQFMHLTNYSV 211
Cdd:pfam03133   88 LSQIPKWSQSrplVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPSSSDLDDVEMHLTNYSI 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181     212 NKKsgdYVSCDDPEVEDYGNKWSMSAMLRYLKQEgrDTTALMAHVEDLIIKTIISAElaiATACKTFVPHRSSCFELYGF 291
Cdd:pfam03133  168 QKK---SSSLNEDYNEPHGHKWSLQNFWKYLEEK--DKDEIWLEIESIIIKTILAAE---VEASRLNVQPLPNCFELYGF 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 6980181     292 DVLIDSTLKPWLLEVNLSPSLACDAPLDLKIKASMISDMFTVV 334
Cdd:pfam03133  240 DFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNSV 282
YheC COG5891
Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, ...
 48-311 1.11e-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: 42.67  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181    48 LLRTLSEAQKVNHFprSYELTRKDRLYKNIIRMQHTHgfkafHILPQTFLL--PAEYAEFCNSYSKdrgpWIVKPVASSR 125
Cdd:COG5891  129 LREKLKKRPGIPFF--NPRFFNKWEVYQLLSKDPRLR-----PYLPETELLtsPEDLLEFLKRYKS----VYLKPVNGSL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181   126 GRGVYLIN-NPNQISLEEnilVSRYINNPLLIDDFKfdvRLYVLVTSYDPLVIYLYEEG--LARFATVRYDqgaknIRnq 202
Cdd:COG5891  198 GRGIIRIEkKGDGYLLRY---RRKKRNVRRRFSSLD---ELLAFLRRLLRRKRYIIQQGipLATIDGRPFD-----FR-- 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6980181   203 fMHltnysVNKksgdyvscddpeveDYGNKWSMSAML-----------------------RYLKQEGRDTTAlmAHVEDL 259
Cdd:COG5891  265 -VL-----VQK--------------NGRGEWVVTGIVariagpgsittnlsgggtalpleELLRRAFGDSKA--EEILQK 322

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6980181   260 IIktiisaELAIATAcKTFVPHRSSCFELyGFDVLIDSTLKPWLLEVNLSPS 311
Cdd:COG5891  323 LE------RIALEIA-RALEESYGGLGEL-GIDLGIDRDGKIWLLEVNSKPG 366
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 113-168 9.24e-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: 9.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6980181   113 RGPWIVKPVASSRGRGVYLINNPNQIS--LE-------ENILVSRYINnplliDDFKFDVRLYVL 168
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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