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Conserved domains on  [gi|311771694|ref|NP_001185722|]
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ARPC4-TTLL3 fusion protein [Homo sapiens]

Protein Classification

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 ...
 274-566 5.11e-110

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: 332.38  E-value: 5.11e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694  274 MDIDKDL-EAPLYLTPEGWSLFLQRYYQVVHEGAELRHLDTQVQRCEDILQQLQAVVPQIDMEGDRNIWIVKPGAKSRGR 352
Cdd:pfam03133   1 FLLDEPYhQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKGDFLPRTFILPTDLAEFVDYFEDRERNTWIVKPSASARGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694  353 GIMCMDHLEEMLKLVngnpvvmKDGKWVVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFYRDSYIRFSTQPFS--LK 430
Cdd:pfam03133  81 GIRVTNKLSQIPKWS-------QSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSpsSS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694  431 NLDN-SVHLCNNSIQKHLEnSCHRHPLLPPDNMWSSQRFQAHLQEMGAPNAWSTIIVPGMKDAVIHALQTSQDTVQCRKA 509
Cdd:pfam03133 154 DLDDvEMHLTNYSIQKKSS-SLNEDYNEPHGHKWSLQNFWKYLEEKDKDEIWLEIESIIIKTILAAEVEASRLNVQPLPN 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 311771694  510 SFELYGADFVFGEDFQPWLIEINASPTMAPSTAVTARLCAGVQADTLR--VVIDRMLDR 566
Cdd:pfam03133 233 CFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNsvVPPDLEKDI 291
ARPC4 pfam05856
ARP2/3 complex 20 kDa subunit (ARPC4); This family consists of several eukaryotic ARP2/3 ...
 1-110 3.62e-68

ARP2/3 complex 20 kDa subunit (ARPC4); This family consists of several eukaryotic ARP2/3 complex 20 kDa subunit (P20-ARC) proteins. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells. The human complex consists of seven subunits which include the actin related proteins Arp2 and Arp3 it has been suggested that the complex promotes actin assembly in lamellipodia and may participate in lamellipodial protrusion.


:

Pssm-ID: 461760  Cd Length: 166  Bit Score: 219.01  E-value: 3.62e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694    1 MTATLRPYLSAVRATLQAALCLENFSSQVVERHNKPEVEVRSSKELLLQPVTISRNEKEKVLIEGSINSVRVSIAVKQAD 80
Cdd:pfam05856   1 MSSTLRPYLDAVRSTLNAALCLQNFPSQVVERHNKPEVEVKSSPELLLNPLIISRNEKEKCLIESSINSVRVSIKIKQAD 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 311771694   81 EIEKILCHKFMRFMMMRAENFFILRRKPVE 110
Cdd:pfam05856  81 EIERILAQKFTRFLMQRAEAFIILRRKPVE 110
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 274-566 5.11e-110

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: 332.38  E-value: 5.11e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694  274 MDIDKDL-EAPLYLTPEGWSLFLQRYYQVVHEGAELRHLDTQVQRCEDILQQLQAVVPQIDMEGDRNIWIVKPGAKSRGR 352
Cdd:pfam03133   1 FLLDEPYhQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKGDFLPRTFILPTDLAEFVDYFEDRERNTWIVKPSASARGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694  353 GIMCMDHLEEMLKLVngnpvvmKDGKWVVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFYRDSYIRFSTQPFS--LK 430
Cdd:pfam03133  81 GIRVTNKLSQIPKWS-------QSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSpsSS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694  431 NLDN-SVHLCNNSIQKHLEnSCHRHPLLPPDNMWSSQRFQAHLQEMGAPNAWSTIIVPGMKDAVIHALQTSQDTVQCRKA 509
Cdd:pfam03133 154 DLDDvEMHLTNYSIQKKSS-SLNEDYNEPHGHKWSLQNFWKYLEEKDKDEIWLEIESIIIKTILAAEVEASRLNVQPLPN 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 311771694  510 SFELYGADFVFGEDFQPWLIEINASPTMAPSTAVTARLCAGVQADTLR--VVIDRMLDR 566
Cdd:pfam03133 233 CFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNsvVPPDLEKDI 291
ARPC4 pfam05856
ARP2/3 complex 20 kDa subunit (ARPC4); This family consists of several eukaryotic ARP2/3 ...
 1-110 3.62e-68

ARP2/3 complex 20 kDa subunit (ARPC4); This family consists of several eukaryotic ARP2/3 complex 20 kDa subunit (P20-ARC) proteins. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells. The human complex consists of seven subunits which include the actin related proteins Arp2 and Arp3 it has been suggested that the complex promotes actin assembly in lamellipodia and may participate in lamellipodial protrusion.


Pssm-ID: 461760  Cd Length: 166  Bit Score: 219.01  E-value: 3.62e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694    1 MTATLRPYLSAVRATLQAALCLENFSSQVVERHNKPEVEVRSSKELLLQPVTISRNEKEKVLIEGSINSVRVSIAVKQAD 80
Cdd:pfam05856   1 MSSTLRPYLDAVRSTLNAALCLQNFPSQVVERHNKPEVEVKSSPELLLNPLIISRNEKEKCLIESSINSVRVSIKIKQAD 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 311771694   81 EIEKILCHKFMRFMMMRAENFFILRRKPVE 110
Cdd:pfam05856  81 EIERILAQKFTRFLMQRAEAFIILRRKPVE 110
PTZ00278 PTZ00278
ARP2/3 complex subunit; Provisional
 1-110 9.75e-52

ARP2/3 complex subunit; Provisional


Pssm-ID: 240342  Cd Length: 174  Bit Score: 176.08  E-value: 9.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694   1 MTATLRPYLSAVRATLQAALCLENFSSQVVERHNKPEVEV----RSSKELLLQPVTISRNEKEKVLIEGSINSVRVSIAV 76
Cdd:PTZ00278   1 MATTYQPYYDCIRKTLEAALCLGNFPSQIIERHNKPEVELngyeGKSKELVLNPIYIVRSEKEKCLIEPSINSVRISFSF 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 311771694  77 KQADEIEKILCHKFMRFMMMRAENFFILRRKPVE 110
Cdd:PTZ00278  81 KKSDELDVIIARKFVSFLAQRAEQFVILRRKPIP 114
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 274-566 5.11e-110

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: 332.38  E-value: 5.11e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694  274 MDIDKDL-EAPLYLTPEGWSLFLQRYYQVVHEGAELRHLDTQVQRCEDILQQLQAVVPQIDMEGDRNIWIVKPGAKSRGR 352
Cdd:pfam03133   1 FLLDEPYhQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKGDFLPRTFILPTDLAEFVDYFEDRERNTWIVKPSASARGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694  353 GIMCMDHLEEMLKLVngnpvvmKDGKWVVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFYRDSYIRFSTQPFS--LK 430
Cdd:pfam03133  81 GIRVTNKLSQIPKWS-------QSRPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSpsSS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694  431 NLDN-SVHLCNNSIQKHLEnSCHRHPLLPPDNMWSSQRFQAHLQEMGAPNAWSTIIVPGMKDAVIHALQTSQDTVQCRKA 509
Cdd:pfam03133 154 DLDDvEMHLTNYSIQKKSS-SLNEDYNEPHGHKWSLQNFWKYLEEKDKDEIWLEIESIIIKTILAAEVEASRLNVQPLPN 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 311771694  510 SFELYGADFVFGEDFQPWLIEINASPTMAPSTAVTARLCAGVQADTLR--VVIDRMLDR 566
Cdd:pfam03133 233 CFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLNsvVPPDLEKDI 291
ARPC4 pfam05856
ARP2/3 complex 20 kDa subunit (ARPC4); This family consists of several eukaryotic ARP2/3 ...
 1-110 3.62e-68

ARP2/3 complex 20 kDa subunit (ARPC4); This family consists of several eukaryotic ARP2/3 complex 20 kDa subunit (P20-ARC) proteins. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells. The human complex consists of seven subunits which include the actin related proteins Arp2 and Arp3 it has been suggested that the complex promotes actin assembly in lamellipodia and may participate in lamellipodial protrusion.


Pssm-ID: 461760  Cd Length: 166  Bit Score: 219.01  E-value: 3.62e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694    1 MTATLRPYLSAVRATLQAALCLENFSSQVVERHNKPEVEVRSSKELLLQPVTISRNEKEKVLIEGSINSVRVSIAVKQAD 80
Cdd:pfam05856   1 MSSTLRPYLDAVRSTLNAALCLQNFPSQVVERHNKPEVEVKSSPELLLNPLIISRNEKEKCLIESSINSVRVSIKIKQAD 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 311771694   81 EIEKILCHKFMRFMMMRAENFFILRRKPVE 110
Cdd:pfam05856  81 EIERILAQKFTRFLMQRAEAFIILRRKPVE 110
PTZ00278 PTZ00278
ARP2/3 complex subunit; Provisional
 1-110 9.75e-52

ARP2/3 complex subunit; Provisional


Pssm-ID: 240342  Cd Length: 174  Bit Score: 176.08  E-value: 9.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311771694   1 MTATLRPYLSAVRATLQAALCLENFSSQVVERHNKPEVEV----RSSKELLLQPVTISRNEKEKVLIEGSINSVRVSIAV 76
Cdd:PTZ00278   1 MATTYQPYYDCIRKTLEAALCLGNFPSQIIERHNKPEVELngyeGKSKELVLNPIYIVRSEKEKCLIEPSINSVRISFSF 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 311771694  77 KQADEIEKILCHKFMRFMMMRAENFFILRRKPVE 110
Cdd:PTZ00278  81 KKSDELDVIIARKFVSFLAQRAEQFVILRRKPIP 114
 
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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