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Conserved domains on  [gi|1707052544|ref|NP_001358578|]
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inactive polyglycylase TTLL10 isoform 1 [Homo sapiens]

Protein Classification

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 ...
282-548 7.45e-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: 450176  Cd Length: 291  Bit Score: 164.82  E-value: 7.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 282 EEFFPETYRLDLkhEREAFFTLF--DETQIWICKPTASNQGKGIFLlrnqeevaalqakTRSMEDDPIHHKTpfrgpQAR 359
Cdd:pfam03133  41 GDFLPRTFILPT--DLAEFVDYFedRERNTWIVKPSASARGRGIRV-------------TNKLSQIPKWSQS-----RPL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 360 VVQRYIQNPLLVDGRKFDVRSYLLIACTTPYMIFFGH-GYARLTLSLYDPHSSDLGG---HLTNQFMQKKSPL----YML 431
Cdd:pfam03133 101 VVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYReGLLRFASVKYSPSSSDLDDvemHLTNYSIQKKSSSlnedYNE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 432 LKEHTvWSMEHLNRYIsdtfwkaRGLAKDWVFTTLKK-RMQQIMAHCFLAAKPKLDCKLGYFDLIGCDFLIDDNFKVWLL 510
Cdd:pfam03133 181 PHGHK-WSLQNFWKYL-------EEKDKDEIWLEIESiIIKTILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLL 252
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1707052544 511 EMNSNPALHTNCEVLKEVIPGVVIETL-DLVLETFRKSL 548
Cdd:pfam03133 253 EVNSSPSLHSTTKLDARLKEQLIDDVLnSVVPPDLEKDI 291
PHA03247 super family cl33720
large tegument protein UL36; Provisional
9-99 3.15e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544    9 IHRRGPPTRTRAGFKRGKRPRIQQRPRARVS---GTIPASRLHPAPASQPGPCPAPGHCPVGPAHERPMGSSQEEGLRCQ 85
Cdd:PHA03247  2862 VRRRPPSRSPAAKPAAPARPPVRRLARPAVSrstESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQP 2941
                           90
                   ....*....|....
gi 1707052544   86 PSQPDHDADGHCGP 99
Cdd:PHA03247  2942 PLAPTTDPAGAGEP 2955
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
568-673 9.54e-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: 39.20  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 568 GEADPRPHLGgscslRRWPPLPTRQAKSSGPPMPHAPDQPGARRPAPpplvPQRPRPPGPDLDSAHDGEPQAPGTEQSGT 647
Cdd:PRK07764  695 GAAPAQPAPA-----PAATPPAGQADDPAAQPPQAAQGASAPSPAAD----DPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765
                          90       100
                  ....*....|....*....|....*.
gi 1707052544 648 GNRHPAQEPSPGTAKEEREEPENARP 673
Cdd:PRK07764  766 PAAAPAAAPPPSPPSEEEEMAEDDAP 791
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
282-548 7.45e-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 tumor 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: 164.82  E-value: 7.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 282 EEFFPETYRLDLkhEREAFFTLF--DETQIWICKPTASNQGKGIFLlrnqeevaalqakTRSMEDDPIHHKTpfrgpQAR 359
Cdd:pfam03133  41 GDFLPRTFILPT--DLAEFVDYFedRERNTWIVKPSASARGRGIRV-------------TNKLSQIPKWSQS-----RPL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 360 VVQRYIQNPLLVDGRKFDVRSYLLIACTTPYMIFFGH-GYARLTLSLYDPHSSDLGG---HLTNQFMQKKSPL----YML 431
Cdd:pfam03133 101 VVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYReGLLRFASVKYSPSSSDLDDvemHLTNYSIQKKSSSlnedYNE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 432 LKEHTvWSMEHLNRYIsdtfwkaRGLAKDWVFTTLKK-RMQQIMAHCFLAAKPKLDCKLGYFDLIGCDFLIDDNFKVWLL 510
Cdd:pfam03133 181 PHGHK-WSLQNFWKYL-------EEKDKDEIWLEIESiIIKTILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLL 252
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1707052544 511 EMNSNPALHTNCEVLKEVIPGVVIETL-DLVLETFRKSL 548
Cdd:pfam03133 253 EVNSSPSLHSTTKLDARLKEQLIDDVLnSVVPPDLEKDI 291
PHA03247 PHA03247
large tegument protein UL36; Provisional
9-99 3.15e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544    9 IHRRGPPTRTRAGFKRGKRPRIQQRPRARVS---GTIPASRLHPAPASQPGPCPAPGHCPVGPAHERPMGSSQEEGLRCQ 85
Cdd:PHA03247  2862 VRRRPPSRSPAAKPAAPARPPVRRLARPAVSrstESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQP 2941
                           90
                   ....*....|....
gi 1707052544   86 PSQPDHDADGHCGP 99
Cdd:PHA03247  2942 PLAPTTDPAGAGEP 2955
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
568-673 9.54e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 568 GEADPRPHLGgscslRRWPPLPTRQAKSSGPPMPHAPDQPGARRPAPpplvPQRPRPPGPDLDSAHDGEPQAPGTEQSGT 647
Cdd:PRK07764  695 GAAPAQPAPA-----PAATPPAGQADDPAAQPPQAAQGASAPSPAAD----DPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765
                          90       100
                  ....*....|....*....|....*.
gi 1707052544 648 GNRHPAQEPSPGTAKEEREEPENARP 673
Cdd:PRK07764  766 PAAAPAAAPPPSPPSEEEEMAEDDAP 791
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
282-548 7.45e-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 tumor 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: 164.82  E-value: 7.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 282 EEFFPETYRLDLkhEREAFFTLF--DETQIWICKPTASNQGKGIFLlrnqeevaalqakTRSMEDDPIHHKTpfrgpQAR 359
Cdd:pfam03133  41 GDFLPRTFILPT--DLAEFVDYFedRERNTWIVKPSASARGRGIRV-------------TNKLSQIPKWSQS-----RPL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 360 VVQRYIQNPLLVDGRKFDVRSYLLIACTTPYMIFFGH-GYARLTLSLYDPHSSDLGG---HLTNQFMQKKSPL----YML 431
Cdd:pfam03133 101 VVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYReGLLRFASVKYSPSSSDLDDvemHLTNYSIQKKSSSlnedYNE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 432 LKEHTvWSMEHLNRYIsdtfwkaRGLAKDWVFTTLKK-RMQQIMAHCFLAAKPKLDCKLGYFDLIGCDFLIDDNFKVWLL 510
Cdd:pfam03133 181 PHGHK-WSLQNFWKYL-------EEKDKDEIWLEIESiIIKTILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLL 252
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1707052544 511 EMNSNPALHTNCEVLKEVIPGVVIETL-DLVLETFRKSL 548
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 ...
264-516 4.68e-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: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 264 DLPWTSPGYLRPQRV---LRMEEFF----PETYRLDlkhEREAFFTLFDETQIWICKPTASNQGKGIFLLRNQEEVAALQ 336
Cdd:pfam14398   1 GIPFFNPGFFNKWEVyelLSKDPELrpylPETELLQ---SPEDLERMLEKYGSVYLKPVNGSLGKGILRIEKDGGGYYLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 337 AKTRsMEDDPIHHKTP---------FRGPQARVVQRYIqNPLLVDGRKFDVRsyLLI--------ACTTpymiffghGYA 399
Cdd:pfam14398  78 GRYG-KNSKTNRFLDFselesflrrLLGKKRYIIQQGI-DLATIDGRPFDFR--VLVqkngkgkwVVTG--------IAA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 400 RltlslydphssdLGGH---LTNqfmqkksplymlLKEH-TVWSMEHlnrYISDTFWKARGLAkdwvfttLKKRMQQIma 475
Cdd:pfam14398 146 R------------IAGPgsiTTN------------LSGGgTAIPLEE---ALRRAFGEERAEK-------ILEKLEEL-- 189
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1707052544 476 hCFLAAKpKLDCKLGYFDLIGCDFLIDDNFKVWLLEMNSNP 516
Cdd:pfam14398 190 -ALELAR-ALEESFGGLGELGLDLGIDKNGRVWLLEVNSKP 228
PHA03247 PHA03247
large tegument protein UL36; Provisional
9-99 3.15e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544    9 IHRRGPPTRTRAGFKRGKRPRIQQRPRARVS---GTIPASRLHPAPASQPGPCPAPGHCPVGPAHERPMGSSQEEGLRCQ 85
Cdd:PHA03247  2862 VRRRPPSRSPAAKPAAPARPPVRRLARPAVSrstESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQP 2941
                           90
                   ....*....|....
gi 1707052544   86 PSQPDHDADGHCGP 99
Cdd:PHA03247  2942 PLAPTTDPAGAGEP 2955
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
10-157 7.72e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.77  E-value: 7.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544   10 HRRGPPTRTRAGFKRGKRPRIQQRPRARVSGTIPASRLHPAPASQPGPCPAPGHCPVG-PAHERPMGSSQEEGLRCQPSQ 88
Cdd:PHA03307   207 PRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITlPTRIWEASGWNGPSSRPGPAS 286
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1707052544   89 PDHDADGHCGPDLEGAERASATPGPP---GLLNSHRPADSDDTNAAGPSAALLEGLLLGGGKPSPHSTRPGP 157
Cdd:PHA03307   287 SSSSPRERSPSPSPSSPGSGPAPSSPrasSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP 358
PHA03247 PHA03247
large tegument protein UL36; Provisional
11-115 8.21e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 8.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544   11 RRGPPTRTR-------AGFKRGKRPRIQQRPRARVSGTIPASRLHPAPASQPGPCPAPGHCPVGPAHERPMGSSQEEGLR 83
Cdd:PHA03247   377 RASLPTRKRrsarhaaTPFARGPGGDDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPA 456
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1707052544   84 CQPSQPDHDADGHCGPDLEgAERASATPGPPG 115
Cdd:PHA03247   457 PATEPAPDDPDDATRKALD-ALRERRPPEPPG 487
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
568-673 9.54e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052544 568 GEADPRPHLGgscslRRWPPLPTRQAKSSGPPMPHAPDQPGARRPAPpplvPQRPRPPGPDLDSAHDGEPQAPGTEQSGT 647
Cdd:PRK07764  695 GAAPAQPAPA-----PAATPPAGQADDPAAQPPQAAQGASAPSPAAD----DPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765
                          90       100
                  ....*....|....*....|....*.
gi 1707052544 648 GNRHPAQEPSPGTAKEEREEPENARP 673
Cdd:PRK07764  766 PAAAPAAAPPPSPPSEEEEMAEDDAP 791
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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