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Conserved domains on  [gi|555943745|ref|NP_001273208|]
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gamma-tubulin complex component 3 isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GCP_N_terminal pfam17681
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
 251-391 1.59e-34

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: 130.48  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943745  251 VRDILYVFQGIDGKNIKMNNTENCY--KVEGKANLSRSLRDTAVRLSELGWLHNKIRRYTDQRSLDrSFGLVGQSFCAAL 328
Cdd:pfam17681   1 LRDLLFALQGISGSYIRFDESDSRIvdDIRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESSSSF-EYGLVLQALCAAL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555943745  329 HQELREYYRLLSVLHSQLQLEDDQGvnlglessLTLRRLLVWTYDPKIRLKTLAALVDHCQGP 391
Cdd:pfam17681  80 QEELTEYYRLIAQLESQLLEASDSI--------LTLLRLVVWLQPPLLLLRVLSNLVEAVEKQ 134
 
Name Accession Description Interval E-value
GCP_N_terminal pfam17681
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
 251-391 1.59e-34

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: 130.48  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943745  251 VRDILYVFQGIDGKNIKMNNTENCY--KVEGKANLSRSLRDTAVRLSELGWLHNKIRRYTDQRSLDrSFGLVGQSFCAAL 328
Cdd:pfam17681   1 LRDLLFALQGISGSYIRFDESDSRIvdDIRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESSSSF-EYGLVLQALCAAL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555943745  329 HQELREYYRLLSVLHSQLQLEDDQGvnlglessLTLRRLLVWTYDPKIRLKTLAALVDHCQGP 391
Cdd:pfam17681  80 QEELTEYYRLIAQLESQLLEASDSI--------LTLLRLVVWLQPPLLLLRVLSNLVEAVEKQ 134
 
Name Accession Description Interval E-value
GCP_N_terminal pfam17681
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
 251-391 1.59e-34

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: 130.48  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555943745  251 VRDILYVFQGIDGKNIKMNNTENCY--KVEGKANLSRSLRDTAVRLSELGWLHNKIRRYTDQRSLDrSFGLVGQSFCAAL 328
Cdd:pfam17681   1 LRDLLFALQGISGSYIRFDESDSRIvdDIRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESSSSF-EYGLVLQALCAAL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555943745  329 HQELREYYRLLSVLHSQLQLEDDQGvnlglessLTLRRLLVWTYDPKIRLKTLAALVDHCQGP 391
Cdd:pfam17681  80 QEELTEYYRLIAQLESQLLEASDSI--------LTLLRLVVWLQPPLLLLRVLSNLVEAVEKQ 134
 
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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