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Conserved domains on  [gi|156616299|ref|NP_001096080|]
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gamma-tubulin complex component 5 isoform b [Homo sapiens]

Protein Classification

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 ...
716-1019 9.01e-36

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: 137.75  E-value: 9.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   716 LVEYLQAMRNFFLMEGGDTMYDFYTSIFDkirekETWQNVSF-----LNVQLQEAVgqRYPEDSSRLSISFENVDTAKKK 790
Cdd:pfam04130    1 LLDHLRALKRYLLLGQGDFISRLMDALFD-----ELWKPASSllrhnLTGLLEEAI--RSSNAQRDLPDVLRRLDARLDP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   791 LPVHILDGLTLSYKVPWPVDIVISLECQKIYNQVFLLLLQIKWAKYSLDVLLFGELVSTAEKPrlkegliheqdtvaqfg 870
Cdd:pfam04130   74 DSLGGWDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVLSSLWRRRQMSGSRSV----------------- 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   871 pqkepvrqQIHRMFLLRVKLMHFVNSLHNYIMTRILHSTGLEFQHQVE-EAKDLDQLIKIHYRYLSTIHDRCLLREKVSF 949
Cdd:pfam04130  137 --------LWHRARLLRQEMIHFVSQLQYYVMFEVIEPSWREFEEKLQkAASDLDDLIEAHEDFLDRILKKCFLTSPQQP 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   950 VKEAIMKVLNLALMFAD---------------GWQAGLGTWRMESIEKMESDFKNCHMFLVTILNKAVCRGSFPHCEYIM 1014
Cdd:pfam04130  209 LLKLLEEILSLILDFAEaldglylsvsesaraEAEDELPELERERLRRLEKQFRKKVSLLLKVLRGLKSHPDESHLRQLL 288

                   ....*....
gi 156616299  1015 LK----YFY 1019
Cdd:pfam04130  289 LRldfnGYY 297
GCP5_NTD cd22572
N-terminal domain of gamma-tubulin complex component 5 (GCP-5) and similar proteins; GCP-5, ...
15-108 7.22e-28

N-terminal domain of gamma-tubulin complex component 5 (GCP-5) and similar proteins; GCP-5, also called TUBGCP5, is a component of the gamma-tubulin ring complex (gamma-TuRC), which is necessary for microtubule nucleation at the centrosome. The model corresponds to the N-terminal domain (NTD) of GCP-5, which is involved in protein-protein interactions. GCP-5 binds Mozart1, a microprotein that regulates subcellular targeting and microtubule formation activity of gamma-TuRC at different cell cycle stages, through its NTD.


:

Pssm-ID: 439339  Cd Length: 102  Bit Score: 108.41  E-value: 7.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   15 QERDVRELVRGVAGLQDEaDPNFQLALNFAWSNFRFHRFLDVNSHKIEKTIEGIYEKFVIHSDLSKAASWKRLTEEFLNA 94
Cdd:cd22572     1 LEELLEELITALTGFQED-DENFRLCLDFALSNLRYHRFLSTNSFEVERRLDGLVEKFRVHGQDDLADALRELLDELLKL 79
                          90
                  ....*....|....
gi 156616299   95 PLPsiKEIKTDAHY 108
Cdd:cd22572    80 PLF--DHSQSDWHP 91
GCP_N_terminal super family cl40875
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
271-577 9.93e-10

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.


The actual alignment was detected with superfamily member pfam17681:

Pssm-ID: 465456  Cd Length: 298  Bit Score: 60.76  E-value: 9.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   271 IRETLWLLSGVK-KLFIFQliDGKVTVRNNIIVTHLTHSCLRSVLEQIAAYGQVVFRLQEFIDEVMGHSSESMLpgsgsv 349
Cdd:pfam17681    1 LRDLLFALQGISgSYIRFD--ESDSRIVDDIRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESSSSFEYGLVL------ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   350 pkksteapfrtyQAFMWALYKYFISFKEELAEIEK-CIINNDTTITLAIVVDKLAPRLSQLKVLHKVfstgVAEVppdTR 428
Cdd:pfam17681   73 ------------QALCAALQEELTEYYRLIAQLESqLLEASDSILTLLRLVVWLQPPLLLLRVLSNL----VEAV---EK 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   429 NVVRASHLLNTLYKAILEYDnvgEASEQTVSLLFSlwvETVRPYLQTVDEWIVHGHLWDGAREFIIQRNKNVP---VNHR 505
Cdd:pfam17681  134 QNLKGGALLSLLHEATSHGD---PFVRELLSRLLQ---RVSRPYLEMLERWIYEGELDDPYNEFFVEENPSVAkesLTSD 207
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156616299   506 DFWYATYTLysvsekteneekmsdnasassgsdqgpssrQHTMV-SFLKPVL-KQIIMAGKSMQLLKNLqCAES 577
Cdd:pfam17681  208 DLWEDKYTL------------------------------RPEMLpSFLSPDLaEKILLTGKSLNFLREC-CGDS 250
 
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 ...
716-1019 9.01e-36

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: 137.75  E-value: 9.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   716 LVEYLQAMRNFFLMEGGDTMYDFYTSIFDkirekETWQNVSF-----LNVQLQEAVgqRYPEDSSRLSISFENVDTAKKK 790
Cdd:pfam04130    1 LLDHLRALKRYLLLGQGDFISRLMDALFD-----ELWKPASSllrhnLTGLLEEAI--RSSNAQRDLPDVLRRLDARLDP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   791 LPVHILDGLTLSYKVPWPVDIVISLECQKIYNQVFLLLLQIKWAKYSLDVLLFGELVSTAEKPrlkegliheqdtvaqfg 870
Cdd:pfam04130   74 DSLGGWDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVLSSLWRRRQMSGSRSV----------------- 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   871 pqkepvrqQIHRMFLLRVKLMHFVNSLHNYIMTRILHSTGLEFQHQVE-EAKDLDQLIKIHYRYLSTIHDRCLLREKVSF 949
Cdd:pfam04130  137 --------LWHRARLLRQEMIHFVSQLQYYVMFEVIEPSWREFEEKLQkAASDLDDLIEAHEDFLDRILKKCFLTSPQQP 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   950 VKEAIMKVLNLALMFAD---------------GWQAGLGTWRMESIEKMESDFKNCHMFLVTILNKAVCRGSFPHCEYIM 1014
Cdd:pfam04130  209 LLKLLEEILSLILDFAEaldglylsvsesaraEAEDELPELERERLRRLEKQFRKKVSLLLKVLRGLKSHPDESHLRQLL 288

                   ....*....
gi 156616299  1015 LK----YFY 1019
Cdd:pfam04130  289 LRldfnGYY 297
GCP5_NTD cd22572
N-terminal domain of gamma-tubulin complex component 5 (GCP-5) and similar proteins; GCP-5, ...
15-108 7.22e-28

N-terminal domain of gamma-tubulin complex component 5 (GCP-5) and similar proteins; GCP-5, also called TUBGCP5, is a component of the gamma-tubulin ring complex (gamma-TuRC), which is necessary for microtubule nucleation at the centrosome. The model corresponds to the N-terminal domain (NTD) of GCP-5, which is involved in protein-protein interactions. GCP-5 binds Mozart1, a microprotein that regulates subcellular targeting and microtubule formation activity of gamma-TuRC at different cell cycle stages, through its NTD.


Pssm-ID: 439339  Cd Length: 102  Bit Score: 108.41  E-value: 7.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   15 QERDVRELVRGVAGLQDEaDPNFQLALNFAWSNFRFHRFLDVNSHKIEKTIEGIYEKFVIHSDLSKAASWKRLTEEFLNA 94
Cdd:cd22572     1 LEELLEELITALTGFQED-DENFRLCLDFALSNLRYHRFLSTNSFEVERRLDGLVEKFRVHGQDDLADALRELLDELLKL 79
                          90
                  ....*....|....
gi 156616299   95 PLPsiKEIKTDAHY 108
Cdd:cd22572    80 PLF--DHSQSDWHP 91
GCP_N_terminal pfam17681
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
271-577 9.93e-10

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: 60.76  E-value: 9.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   271 IRETLWLLSGVK-KLFIFQliDGKVTVRNNIIVTHLTHSCLRSVLEQIAAYGQVVFRLQEFIDEVMGHSSESMLpgsgsv 349
Cdd:pfam17681    1 LRDLLFALQGISgSYIRFD--ESDSRIVDDIRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESSSSFEYGLVL------ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   350 pkksteapfrtyQAFMWALYKYFISFKEELAEIEK-CIINNDTTITLAIVVDKLAPRLSQLKVLHKVfstgVAEVppdTR 428
Cdd:pfam17681   73 ------------QALCAALQEELTEYYRLIAQLESqLLEASDSILTLLRLVVWLQPPLLLLRVLSNL----VEAV---EK 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   429 NVVRASHLLNTLYKAILEYDnvgEASEQTVSLLFSlwvETVRPYLQTVDEWIVHGHLWDGAREFIIQRNKNVP---VNHR 505
Cdd:pfam17681  134 QNLKGGALLSLLHEATSHGD---PFVRELLSRLLQ---RVSRPYLEMLERWIYEGELDDPYNEFFVEENPSVAkesLTSD 207
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156616299   506 DFWYATYTLysvsekteneekmsdnasassgsdqgpssrQHTMV-SFLKPVL-KQIIMAGKSMQLLKNLqCAES 577
Cdd:pfam17681  208 DLWEDKYTL------------------------------RPEMLpSFLSPDLaEKILLTGKSLNFLREC-CGDS 250
 
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 ...
716-1019 9.01e-36

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: 137.75  E-value: 9.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   716 LVEYLQAMRNFFLMEGGDTMYDFYTSIFDkirekETWQNVSF-----LNVQLQEAVgqRYPEDSSRLSISFENVDTAKKK 790
Cdd:pfam04130    1 LLDHLRALKRYLLLGQGDFISRLMDALFD-----ELWKPASSllrhnLTGLLEEAI--RSSNAQRDLPDVLRRLDARLDP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   791 LPVHILDGLTLSYKVPWPVDIVISLECQKIYNQVFLLLLQIKWAKYSLDVLLFGELVSTAEKPrlkegliheqdtvaqfg 870
Cdd:pfam04130   74 DSLGGWDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVLSSLWRRRQMSGSRSV----------------- 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   871 pqkepvrqQIHRMFLLRVKLMHFVNSLHNYIMTRILHSTGLEFQHQVE-EAKDLDQLIKIHYRYLSTIHDRCLLREKVSF 949
Cdd:pfam04130  137 --------LWHRARLLRQEMIHFVSQLQYYVMFEVIEPSWREFEEKLQkAASDLDDLIEAHEDFLDRILKKCFLTSPQQP 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   950 VKEAIMKVLNLALMFAD---------------GWQAGLGTWRMESIEKMESDFKNCHMFLVTILNKAVCRGSFPHCEYIM 1014
Cdd:pfam04130  209 LLKLLEEILSLILDFAEaldglylsvsesaraEAEDELPELERERLRRLEKQFRKKVSLLLKVLRGLKSHPDESHLRQLL 288

                   ....*....
gi 156616299  1015 LK----YFY 1019
Cdd:pfam04130  289 LRldfnGYY 297
GCP5_NTD cd22572
N-terminal domain of gamma-tubulin complex component 5 (GCP-5) and similar proteins; GCP-5, ...
15-108 7.22e-28

N-terminal domain of gamma-tubulin complex component 5 (GCP-5) and similar proteins; GCP-5, also called TUBGCP5, is a component of the gamma-tubulin ring complex (gamma-TuRC), which is necessary for microtubule nucleation at the centrosome. The model corresponds to the N-terminal domain (NTD) of GCP-5, which is involved in protein-protein interactions. GCP-5 binds Mozart1, a microprotein that regulates subcellular targeting and microtubule formation activity of gamma-TuRC at different cell cycle stages, through its NTD.


Pssm-ID: 439339  Cd Length: 102  Bit Score: 108.41  E-value: 7.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   15 QERDVRELVRGVAGLQDEaDPNFQLALNFAWSNFRFHRFLDVNSHKIEKTIEGIYEKFVIHSDLSKAASWKRLTEEFLNA 94
Cdd:cd22572     1 LEELLEELITALTGFQED-DENFRLCLDFALSNLRYHRFLSTNSFEVERRLDGLVEKFRVHGQDDLADALRELLDELLKL 79
                          90
                  ....*....|....
gi 156616299   95 PLPsiKEIKTDAHY 108
Cdd:cd22572    80 PLF--DHSQSDWHP 91
GCP_N_terminal pfam17681
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
271-577 9.93e-10

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: 60.76  E-value: 9.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   271 IRETLWLLSGVK-KLFIFQliDGKVTVRNNIIVTHLTHSCLRSVLEQIAAYGQVVFRLQEFIDEVMGHSSESMLpgsgsv 349
Cdd:pfam17681    1 LRDLLFALQGISgSYIRFD--ESDSRIVDDIRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESSSSFEYGLVL------ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   350 pkksteapfrtyQAFMWALYKYFISFKEELAEIEK-CIINNDTTITLAIVVDKLAPRLSQLKVLHKVfstgVAEVppdTR 428
Cdd:pfam17681   73 ------------QALCAALQEELTEYYRLIAQLESqLLEASDSILTLLRLVVWLQPPLLLLRVLSNL----VEAV---EK 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616299   429 NVVRASHLLNTLYKAILEYDnvgEASEQTVSLLFSlwvETVRPYLQTVDEWIVHGHLWDGAREFIIQRNKNVP---VNHR 505
Cdd:pfam17681  134 QNLKGGALLSLLHEATSHGD---PFVRELLSRLLQ---RVSRPYLEMLERWIYEGELDDPYNEFFVEENPSVAkesLTSD 207
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156616299   506 DFWYATYTLysvsekteneekmsdnasassgsdqgpssrQHTMV-SFLKPVL-KQIIMAGKSMQLLKNLqCAES 577
Cdd:pfam17681  208 DLWEDKYTL------------------------------RPEMLpSFLSPDLaEKILLTGKSLNFLREC-CGDS 250
 
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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