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Conserved domains on  [gi|1246417641|ref|NP_001342646|]
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probable tubulin polyglutamylase TTLL9 isoform 3 [Mus musculus]

Protein Classification

ATP-grasp domain-containing protein( domain architecture ID 106900)

ATP-grasp domain-containing protein may be related to carbamoyl phosphate synthetase and predicted to be involved in the biosynthesis of a ribonucleoside involved in stress response

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CPSase_L_D2 super family cl17255
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
90-328 1.01e-62

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


The actual alignment was detected with superfamily member pfam03133:

Pssm-ID: 473076  Cd Length: 291  Bit Score: 203.34  E-value: 1.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641  90 ARSQGKGIFLFRRLKDIMDWRKGtsgkkptgvetqparanmnpsgshdtrssddqkddlpvENYVAQRYVENPYLIGGRK 169
Cdd:pfam03133  75 ASARGRGIRVTNKLSQIPKWSQS--------------------------------------RPLVVQKYIERPLLIDGRK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641 170 FDLRVYVLVMSYIPLRAWLYRDGFARFSNTRF--TLNSIDDHYVHLTNVAVQKTSP----DYHLKKGCKWMLQRFRQYLA 243
Cdd:pfam03133 117 FDIRLYVLVTSVNPLRVYVYREGLLRFASVKYspSSSDLDDVEMHLTNYSIQKKSSslneDYNEPHGHKWSLQNFWKYLE 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641 244 SKHGPKAVETLFSD-MDNIFIKSLQSVQKVIISDKHCFELYGYDILIDQDLKPWLLEVNASPSLTASSQEDYELKTCLLE 322
Cdd:pfam03133 197 EKDKDEIWLEIESIiIKTILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLID 276

                  ....*.
gi 1246417641 323 DTLHVV 328
Cdd:pfam03133 277 DVLNSV 282
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
90-328 1.01e-62

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: 203.34  E-value: 1.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641  90 ARSQGKGIFLFRRLKDIMDWRKGtsgkkptgvetqparanmnpsgshdtrssddqkddlpvENYVAQRYVENPYLIGGRK 169
Cdd:pfam03133  75 ASARGRGIRVTNKLSQIPKWSQS--------------------------------------RPLVVQKYIERPLLIDGRK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641 170 FDLRVYVLVMSYIPLRAWLYRDGFARFSNTRF--TLNSIDDHYVHLTNVAVQKTSP----DYHLKKGCKWMLQRFRQYLA 243
Cdd:pfam03133 117 FDIRLYVLVTSVNPLRVYVYREGLLRFASVKYspSSSDLDDVEMHLTNYSIQKKSSslneDYNEPHGHKWSLQNFWKYLE 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641 244 SKHGPKAVETLFSD-MDNIFIKSLQSVQKVIISDKHCFELYGYDILIDQDLKPWLLEVNASPSLTASSQEDYELKTCLLE 322
Cdd:pfam03133 197 EKDKDEIWLEIESIiIKTILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLID 276

                  ....*.
gi 1246417641 323 DTLHVV 328
Cdd:pfam03133 277 DVLNSV 282
YheC COG5891
Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, ...
92-315 3.15e-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: 48.83  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641  92 SQGKGIFlfrRLKdimdwrkgtsgKKPTGVETQPARANMNPSGshdTRSSDDQ-----KDDLPVENYVAQRYVeNPYLIG 166
Cdd:COG5891   196 SLGRGII---RIE-----------KKGDGYLLRYRRKKRNVRR---RFSSLDEllaflRRLLRRKRYIIQQGI-PLATID 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641 167 GRKFDLRVyvlVMSYIPLRAWLYRDGFARFSNTrftlNSIddhyvhLTNVAvqktspdyhlkKGCKwmLQRFRQYLASKH 246
Cdd:COG5891   258 GRPFDFRV---LVQKNGRGEWVVTGIVARIAGP----GSI------TTNLS-----------GGGT--ALPLEELLRRAF 311
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246417641 247 GPKAVETLFSDMDNIFIKSLQSVQKviiSDKHCFELyGYDILIDQDLKPWLLEVNASPSLTASSQEDYE 315
Cdd:COG5891   312 GDSKAEEILQKLERIALEIARALEE---SYGGLGEL-GIDLGIDRDGKIWLLEVNSKPGRSIFDEPGDK 376
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
90-328 1.01e-62

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: 203.34  E-value: 1.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641  90 ARSQGKGIFLFRRLKDIMDWRKGtsgkkptgvetqparanmnpsgshdtrssddqkddlpvENYVAQRYVENPYLIGGRK 169
Cdd:pfam03133  75 ASARGRGIRVTNKLSQIPKWSQS--------------------------------------RPLVVQKYIERPLLIDGRK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641 170 FDLRVYVLVMSYIPLRAWLYRDGFARFSNTRF--TLNSIDDHYVHLTNVAVQKTSP----DYHLKKGCKWMLQRFRQYLA 243
Cdd:pfam03133 117 FDIRLYVLVTSVNPLRVYVYREGLLRFASVKYspSSSDLDDVEMHLTNYSIQKKSSslneDYNEPHGHKWSLQNFWKYLE 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641 244 SKHGPKAVETLFSD-MDNIFIKSLQSVQKVIISDKHCFELYGYDILIDQDLKPWLLEVNASPSLTASSQEDYELKTCLLE 322
Cdd:pfam03133 197 EKDKDEIWLEIESIiIKTILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLID 276

                  ....*.
gi 1246417641 323 DTLHVV 328
Cdd:pfam03133 277 DVLNSV 282
YheC COG5891
Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, ...
92-315 3.15e-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: 48.83  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641  92 SQGKGIFlfrRLKdimdwrkgtsgKKPTGVETQPARANMNPSGshdTRSSDDQ-----KDDLPVENYVAQRYVeNPYLIG 166
Cdd:COG5891   196 SLGRGII---RIE-----------KKGDGYLLRYRRKKRNVRR---RFSSLDEllaflRRLLRRKRYIIQQGI-PLATID 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641 167 GRKFDLRVyvlVMSYIPLRAWLYRDGFARFSNTrftlNSIddhyvhLTNVAvqktspdyhlkKGCKwmLQRFRQYLASKH 246
Cdd:COG5891   258 GRPFDFRV---LVQKNGRGEWVVTGIVARIAGP----GSI------TTNLS-----------GGGT--ALPLEELLRRAF 311
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246417641 247 GPKAVETLFSDMDNIFIKSLQSVQKviiSDKHCFELyGYDILIDQDLKPWLLEVNASPSLTASSQEDYE 315
Cdd:COG5891   312 GDSKAEEILQKLERIALEIARALEE---SYGGLGEL-GIDLGIDRDGKIWLLEVNSKPGRSIFDEPGDK 376
ATPgrasp_YheCD pfam14398
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ...
152-305 4.12e-05

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: 44.86  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641 152 NYVAQRYVeNPYLIGGRKFDLRVyvLVMsyiplrawlyRDG---------FARFSNTrftlNSIddhyvhltnvavqkTS 222
Cdd:pfam14398 107 RYIIQQGI-DLATIDGRPFDFRV--LVQ----------KNGkgkwvvtgiAARIAGP----GSI--------------TT 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246417641 223 pdyHLKKGCKwmLQRFRQYLASKHGPKAVETLFSDMDNIFIKSLQSVQKVIisdKHCFELyGYDILIDQDLKPWLLEVNA 302
Cdd:pfam14398 156 ---NLSGGGT--AIPLEEALRRAFGEERAEKILEKLEELALELARALEESF---GGLGEL-GLDLGIDKNGRVWLLEVNS 226

                  ...
gi 1246417641 303 SPS 305
Cdd:pfam14398 227 KPG 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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