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Conserved domains on  [gi|568953330|ref|XP_006508864|]
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gamma-tubulin complex component 3 isoform X2 [Mus musculus]

Protein Classification

tubulin gamma complex associated family protein( domain architecture ID 16049209)

tubulin gamma complex associated (TUBGCP) family protein such as various gamma-tubulin complex components, which are part of the gamma-tubulin complex that is necessary for microtubule nucleation at the centrosome

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GCP_C_terminal pfam04130
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components ...
145-476 1.27e-103

Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains.


:

Pssm-ID: 461187  Cd Length: 297  Bit Score: 311.86  E-value: 1.27e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  145 LLEHMQAMRRYLLLGQGDFIRHLMDLLKPELVRPATTLYQHNLTGILETAVRATNAQFDSPEILKRLDVRLLEVSPGdtG 224
Cdd:pfam04130   1 LLDHLRALKRYLLLGQGDFISRLMDALFDELWKPASSLLRHNLTGLLEEAIRSSNAQRDLPDVLRRLDARLDPDSLG--G 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  225 WDVFSLDYHVDGPIATVFTRECMSHYLRVFNFLWRAKRMEYILTDI-RKGHMCNAKllrnmpefSGVLHQCHILASEMVH 303
Cdd:pfam04130  79 WDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVLSSLwRRRQMSGSR--------SVLWHRARLLRQEMIH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  304 FIHQMQYYITFEVLECSWDELWNRVQQA-QDLDHIIAAHEAFLNTITSRCLLDSNSRVLLNQLRAVFDQIIELQNAQDVM 382
Cdd:pfam04130 151 FVSQLQYYVMFEVIEPSWREFEEKLQKAaSDLDDLIEAHEDFLDRILKKCFLTSPQQPLLKLLEEILSLILDFAEALDGL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  383 YRAAleelqrrlqfeekkkqreiegqwgvtaaeeeEENKRIREFQDSIPKMCSQLRILTHFYQGVVQQFLVLL----TTS 458
Cdd:pfam04130 231 YLSV-------------------------------SESARAEAEDELPELERERLRRLEKQFRKKVSLLLKVLrglkSHP 279
                         330
                  ....*....|....*...
gi 568953330  459 SDESLQFLSFRLDFNEHY 476
Cdd:pfam04130 280 DESHLRQLLLRLDFNGYY 297
GCP_N_terminal pfam17681
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
1-142 1.68e-39

Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1.


:

Pssm-ID: 465456  Cd Length: 298  Bit Score: 144.74  E-value: 1.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330    1 MKSLVQHILSLVSHPVLSFLYRWIYDGELEDTYHEFFVASDPTVK-----TDRLWHDKYTLRKSMIPSFITMDQSRKVLL 75
Cdd:pfam17681 156 VRELLSRLLQRVSRPYLEMLERWIYEGELDDPYNEFFVEENPSVAkesltSDDLWEDKYTLRPEMLPSFLSPDLAEKILL 235
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953330   76 IGKSINFLHQVCHDqtptTKMIAVTKSAESPRDAADLFTDLENAFQGKIDAAYFETSKYLLDVLNKK 142
Cdd:pfam17681 236 TGKSLNFLRECCGD----SWRIEDTASELEYGDDLSESSIFSLSLEELIDSAYKLASRRLLDLLFEE 298
 
Name Accession Description Interval E-value
GCP_C_terminal pfam04130
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components ...
145-476 1.27e-103

Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains.


Pssm-ID: 461187  Cd Length: 297  Bit Score: 311.86  E-value: 1.27e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  145 LLEHMQAMRRYLLLGQGDFIRHLMDLLKPELVRPATTLYQHNLTGILETAVRATNAQFDSPEILKRLDVRLLEVSPGdtG 224
Cdd:pfam04130   1 LLDHLRALKRYLLLGQGDFISRLMDALFDELWKPASSLLRHNLTGLLEEAIRSSNAQRDLPDVLRRLDARLDPDSLG--G 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  225 WDVFSLDYHVDGPIATVFTRECMSHYLRVFNFLWRAKRMEYILTDI-RKGHMCNAKllrnmpefSGVLHQCHILASEMVH 303
Cdd:pfam04130  79 WDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVLSSLwRRRQMSGSR--------SVLWHRARLLRQEMIH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  304 FIHQMQYYITFEVLECSWDELWNRVQQA-QDLDHIIAAHEAFLNTITSRCLLDSNSRVLLNQLRAVFDQIIELQNAQDVM 382
Cdd:pfam04130 151 FVSQLQYYVMFEVIEPSWREFEEKLQKAaSDLDDLIEAHEDFLDRILKKCFLTSPQQPLLKLLEEILSLILDFAEALDGL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  383 YRAAleelqrrlqfeekkkqreiegqwgvtaaeeeEENKRIREFQDSIPKMCSQLRILTHFYQGVVQQFLVLL----TTS 458
Cdd:pfam04130 231 YLSV-------------------------------SESARAEAEDELPELERERLRRLEKQFRKKVSLLLKVLrglkSHP 279
                         330
                  ....*....|....*...
gi 568953330  459 SDESLQFLSFRLDFNEHY 476
Cdd:pfam04130 280 DESHLRQLLLRLDFNGYY 297
GCP_N_terminal pfam17681
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
1-142 1.68e-39

Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1.


Pssm-ID: 465456  Cd Length: 298  Bit Score: 144.74  E-value: 1.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330    1 MKSLVQHILSLVSHPVLSFLYRWIYDGELEDTYHEFFVASDPTVK-----TDRLWHDKYTLRKSMIPSFITMDQSRKVLL 75
Cdd:pfam17681 156 VRELLSRLLQRVSRPYLEMLERWIYEGELDDPYNEFFVEENPSVAkesltSDDLWEDKYTLRPEMLPSFLSPDLAEKILL 235
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953330   76 IGKSINFLHQVCHDqtptTKMIAVTKSAESPRDAADLFTDLENAFQGKIDAAYFETSKYLLDVLNKK 142
Cdd:pfam17681 236 TGKSLNFLRECCGD----SWRIEDTASELEYGDDLSESSIFSLSLEELIDSAYKLASRRLLDLLFEE 298
 
Name Accession Description Interval E-value
GCP_C_terminal pfam04130
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components ...
145-476 1.27e-103

Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains.


Pssm-ID: 461187  Cd Length: 297  Bit Score: 311.86  E-value: 1.27e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  145 LLEHMQAMRRYLLLGQGDFIRHLMDLLKPELVRPATTLYQHNLTGILETAVRATNAQFDSPEILKRLDVRLLEVSPGdtG 224
Cdd:pfam04130   1 LLDHLRALKRYLLLGQGDFISRLMDALFDELWKPASSLLRHNLTGLLEEAIRSSNAQRDLPDVLRRLDARLDPDSLG--G 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  225 WDVFSLDYHVDGPIATVFTRECMSHYLRVFNFLWRAKRMEYILTDI-RKGHMCNAKllrnmpefSGVLHQCHILASEMVH 303
Cdd:pfam04130  79 WDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVLSSLwRRRQMSGSR--------SVLWHRARLLRQEMIH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  304 FIHQMQYYITFEVLECSWDELWNRVQQA-QDLDHIIAAHEAFLNTITSRCLLDSNSRVLLNQLRAVFDQIIELQNAQDVM 382
Cdd:pfam04130 151 FVSQLQYYVMFEVIEPSWREFEEKLQKAaSDLDDLIEAHEDFLDRILKKCFLTSPQQPLLKLLEEILSLILDFAEALDGL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330  383 YRAAleelqrrlqfeekkkqreiegqwgvtaaeeeEENKRIREFQDSIPKMCSQLRILTHFYQGVVQQFLVLL----TTS 458
Cdd:pfam04130 231 YLSV-------------------------------SESARAEAEDELPELERERLRRLEKQFRKKVSLLLKVLrglkSHP 279
                         330
                  ....*....|....*...
gi 568953330  459 SDESLQFLSFRLDFNEHY 476
Cdd:pfam04130 280 DESHLRQLLLRLDFNGYY 297
GCP_N_terminal pfam17681
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
1-142 1.68e-39

Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1.


Pssm-ID: 465456  Cd Length: 298  Bit Score: 144.74  E-value: 1.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953330    1 MKSLVQHILSLVSHPVLSFLYRWIYDGELEDTYHEFFVASDPTVK-----TDRLWHDKYTLRKSMIPSFITMDQSRKVLL 75
Cdd:pfam17681 156 VRELLSRLLQRVSRPYLEMLERWIYEGELDDPYNEFFVEENPSVAkesltSDDLWEDKYTLRPEMLPSFLSPDLAEKILL 235
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953330   76 IGKSINFLHQVCHDqtptTKMIAVTKSAESPRDAADLFTDLENAFQGKIDAAYFETSKYLLDVLNKK 142
Cdd:pfam17681 236 TGKSLNFLRECCGD----SWRIEDTASELEYGDDLSESSIFSLSLEELIDSAYKLASRRLLDLLFEE 298
 
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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