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Conserved domains on  [gi|530360289|ref|XP_005244795|]
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inactive polyglycylase TTLL10 isoform X10 [Homo sapiens]

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 ...
 209-475 5.47e-46

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: 164.05  E-value: 5.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  209 EEFFPETYRLDLkhEREAFFTLF--DETQIWICKPTASNQGKGIFLlrnqeevaalqakTRSMEDDPIHHKTpfrgpQAR 286
Cdd:pfam03133  41 GDFLPRTFILPT--DLAEFVDYFedRERNTWIVKPSASARGRGIRV-------------TNKLSQIPKWSQS-----RPL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  287 VVQRYIQNPLLVDGRKFDVRSYLLIACTTPYMIFFGH-GYARLTLSLYDPHSSDLGG---HLTNQFMQKKSPL----YML 358
Cdd:pfam03133 101 VVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYReGLLRFASVKYSPSSSDLDDvemHLTNYSIQKKSSSlnedYNE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  359 LKEHTvWSMEHLNRYIsdtfwkaRGLAKDWVFTTLKK-RMQQIMAHCFLAAKPKLDCKLGYFDLIGCDFLIDDNFKVWLL 437
Cdd:pfam03133 181 PHGHK-WSLQNFWKYL-------EEKDKDEIWLEIESiIIKTILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLL 252

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 530360289  438 EMNSNPALHTNCEVLKEVIPGVVIETL-DLVLETFRKSL 475
Cdd:pfam03133 253 EVNSSPSLHSTTKLDARLKEQLIDDVLnSVVPPDLEKDI 291
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 495-600 4.22e-03

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289 495 GEADPRPHLGgscslRRWPPLPTRQAKSSGPPMPHAPDQPGARRPAPpplvPQRPRPPGPDLDSAHDGEPQAPGTEQSGT 574
Cdd:PRK07764 695 GAAPAQPAPA-----PAATPPAGQADDPAAQPPQAAQGASAPSPAAD----DPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765

                         90       100
                 ....*....|....*....|....*.
gi 530360289 575 GNRHPAQEPSPGTAKEEREEPENARP 600
Cdd:PRK07764 766 PAAAPAAAPPPSPPSEEEEMAEDDAP 791
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 209-475 5.47e-46

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: 164.05  E-value: 5.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  209 EEFFPETYRLDLkhEREAFFTLF--DETQIWICKPTASNQGKGIFLlrnqeevaalqakTRSMEDDPIHHKTpfrgpQAR 286
Cdd:pfam03133  41 GDFLPRTFILPT--DLAEFVDYFedRERNTWIVKPSASARGRGIRV-------------TNKLSQIPKWSQS-----RPL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  287 VVQRYIQNPLLVDGRKFDVRSYLLIACTTPYMIFFGH-GYARLTLSLYDPHSSDLGG---HLTNQFMQKKSPL----YML 358
Cdd:pfam03133 101 VVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYReGLLRFASVKYSPSSSDLDDvemHLTNYSIQKKSSSlnedYNE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  359 LKEHTvWSMEHLNRYIsdtfwkaRGLAKDWVFTTLKK-RMQQIMAHCFLAAKPKLDCKLGYFDLIGCDFLIDDNFKVWLL 437
Cdd:pfam03133 181 PHGHK-WSLQNFWKYL-------EEKDKDEIWLEIESiIIKTILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLL 252

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 530360289  438 EMNSNPALHTNCEVLKEVIPGVVIETL-DLVLETFRKSL 475
Cdd:pfam03133 253 EVNSSPSLHSTTKLDARLKEQLIDDVLnSVVPPDLEKDI 291
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 495-600 4.22e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289 495 GEADPRPHLGgscslRRWPPLPTRQAKSSGPPMPHAPDQPGARRPAPpplvPQRPRPPGPDLDSAHDGEPQAPGTEQSGT 574
Cdd:PRK07764 695 GAAPAQPAPA-----PAATPPAGQADDPAAQPPQAAQGASAPSPAAD----DPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765

                         90       100
                 ....*....|....*....|....*.
gi 530360289 575 GNRHPAQEPSPGTAKEEREEPENARP 600
Cdd:PRK07764 766 PAAAPAAAPPPSPPSEEEEMAEDDAP 791
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 238-310 4.62e-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: 39.54  E-value: 4.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530360289 238 ICKPTASNQGKGIFLLRNQEEVAALQAKTRSMEDDPIhhktpfrgpqarVVQRYIQNpllVDGRkfDVRSYLL 310
Cdd:COG0189  135 VLKPLDGSGGRGVFLVEDEDALESILEALTELGSEPV------------LVQEFIPE---EDGR--DIRVLVV 190
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 209-475 5.47e-46

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: 164.05  E-value: 5.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  209 EEFFPETYRLDLkhEREAFFTLF--DETQIWICKPTASNQGKGIFLlrnqeevaalqakTRSMEDDPIHHKTpfrgpQAR 286
Cdd:pfam03133  41 GDFLPRTFILPT--DLAEFVDYFedRERNTWIVKPSASARGRGIRV-------------TNKLSQIPKWSQS-----RPL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  287 VVQRYIQNPLLVDGRKFDVRSYLLIACTTPYMIFFGH-GYARLTLSLYDPHSSDLGG---HLTNQFMQKKSPL----YML 358
Cdd:pfam03133 101 VVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYReGLLRFASVKYSPSSSDLDDvemHLTNYSIQKKSSSlnedYNE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  359 LKEHTvWSMEHLNRYIsdtfwkaRGLAKDWVFTTLKK-RMQQIMAHCFLAAKPKLDCKLGYFDLIGCDFLIDDNFKVWLL 437
Cdd:pfam03133 181 PHGHK-WSLQNFWKYL-------EEKDKDEIWLEIESiIIKTILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLL 252

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 530360289  438 EMNSNPALHTNCEVLKEVIPGVVIETL-DLVLETFRKSL 475
Cdd:pfam03133 253 EVNSSPSLHSTTKLDARLKEQLIDDVLnSVVPPDLEKDI 291
ATPgrasp_YheCD pfam14398
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ...
 191-443 4.21e-06

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: 48.33  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  191 DLPWTSPGYLRPQRV---LRMEEFF----PETYRLDlkhEREAFFTLFDETQIWICKPTASNQGKGIFLLRNQEEVAALQ 263
Cdd:pfam14398   1 GIPFFNPGFFNKWEVyelLSKDPELrpylPETELLQ---SPEDLERMLEKYGSVYLKPVNGSLGKGILRIEKDGGGYYLY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  264 AKTRsMEDDPIHHKTP---------FRGPQARVVQRYIqNPLLVDGRKFDVRsyLLI--------ACTTpymiffghGYA 326
Cdd:pfam14398  78 GRYG-KNSKTNRFLDFselesflrrLLGKKRYIIQQGI-DLATIDGRPFDFR--VLVqkngkgkwVVTG--------IAA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289  327 RltlslydphssdLGGH---LTNqfmqkksplymlLKEH-TVWSMEHlnrYISDTFWKARGLAkdwvfttLKKRMQQIma 402
Cdd:pfam14398 146 R------------IAGPgsiTTN------------LSGGgTAIPLEE---ALRRAFGEERAEK-------ILEKLEEL-- 189

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 530360289  403 hCFLAAKpKLDCKLGYFDLIGCDFLIDDNFKVWLLEMNSNP 443
Cdd:pfam14398 190 -ALELAR-ALEESFGGLGELGLDLGIDKNGRVWLLEVNSKP 228
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 495-600 4.22e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289 495 GEADPRPHLGgscslRRWPPLPTRQAKSSGPPMPHAPDQPGARRPAPpplvPQRPRPPGPDLDSAHDGEPQAPGTEQSGT 574
Cdd:PRK07764 695 GAAPAQPAPA-----PAATPPAGQADDPAAQPPQAAQGASAPSPAAD----DPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765

                         90       100
                 ....*....|....*....|....*.
gi 530360289 575 GNRHPAQEPSPGTAKEEREEPENARP 600
Cdd:PRK07764 766 PAAAPAAAPPPSPPSEEEEMAEDDAP 791
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 238-310 4.62e-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: 39.54  E-value: 4.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530360289 238 ICKPTASNQGKGIFLLRNQEEVAALQAKTRSMEDDPIhhktpfrgpqarVVQRYIQNpllVDGRkfDVRSYLL 310
Cdd:COG0189  135 VLKPLDGSGGRGVFLVEDEDALESILEALTELGSEPV------------LVQEFIPE---EDGR--DIRVLVV 190
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 515-600 6.96e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 39.67  E-value: 6.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360289 515 LPTRQAKSSGPPMPHAPDQPGARRPAPPPLVPQRP-RPPGPDLDSAHDgEPQAPGTEQSGTGNRHPA--QEPSPGTAKEE 591
Cdd:PTZ00449 572 IPTLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPtRPKSPKLPELLD-IPKSPKRPESPKSPKRPPppQRPSSPERPEG 650


                 ....*....
gi 530360289 592 REEPENARP 600
Cdd:PTZ00449 651 PKIIKSPKP 659
 
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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