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Conserved domains on  [gi|1229156697|ref|XP_022091110|]
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gamma-tubulin complex component 5-like isoform X1 [Acanthaster planci]

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 ...
726-1037 1.48e-41

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: 154.70  E-value: 1.48e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  726 HLTetfaSMRRYYLCEAGDtMFDFLSD-LFDKLrlcqhksqWQDT-----LYLNYQLQTAVAAgypSDADR-LTVSFEPV 798
Cdd:pfam04130    4 HLR----ALKRYLLLGQGD-FISRLMDaLFDEL--------WKPAssllrHNLTGLLEEAIRS---SNAQRdLPDVLRRL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  799 NVPstVSIQPIHALDGLTLHYKVPWPLDIIINAKTITAYNQVFRFLLQVKRAKYCLeqlrfssiirssfpaatttdpkdk 878
Cdd:pfam04130   68 DAR--LDPDSLGGWDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVL------------------------ 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  879 pevrgDSTPSARPQPLHKAQLLHRVFLLRFKLIHFVNAVHSYLMSRILHSTGLEFQADIE-RAPDLEAIVELHTTYLAKV 957
Cdd:pfam04130  122 -----SSLWRRRQMSGSRSVLWHRARLLRQEMIHFVSQLQYYVMFEVIEPSWREFEEKLQkAASDLDDLIEAHEDFLDRI 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  958 SERCLLHKKVGLVREAVLKALNLALVFQRRWD---------------AGLSAFNAERIDQMLSEFNKCSVFLLTMLDNIN 1022
Cdd:pfam04130  197 LKKCFLTSPQQPLLKLLEEILSLILDFAEALDglylsvsesaraeaeDELPELERERLRRLEKQFRKKVSLLLKVLRGLK 276
                          330
                   ....*....|....*
gi 1229156697 1023 KRGAFPHLEALALSL 1037
Cdd:pfam04130  277 SHPDESHLRQLLLRL 291
GCP5_NTD cd22572
N-terminal domain of gamma-tubulin complex component 5 (GCP-5) and similar proteins; GCP-5, ...
21-126 5.21e-36

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: 131.52  E-value: 5.21e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697   21 VEQEAKKLIQKLTSFKDsNDENFRRSLQFALSNFKFHRYLDVDSHKITRKLQGLFQKFEIHSQLEKAVSLRKLTDKFLQL 100
Cdd:cd22572      1 LEELLEELITALTGFQE-DDENFRLCLDFALSNLRYHRFLSTNSFEVERRLDGLVEKFRVHGQDDLADALRELLDELLKL 79
                           90       100
                   ....*....|....*....|....*.
gi 1229156697  101 PLSPKSrdaKTDLHYSVLSVLLNLSD 126
Cdd:cd22572     80 PLFDHS---QSDWHPSILSLLLELSD 102
GCP_N_terminal super family cl40875
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
278-572 1.64e-18

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: 87.34  E-value: 1.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  278 IRETIWVLMGAETSFVyQLHDSKFTSRQDIQVSHLTPKALHEFTSKLAETCTNAWTLQSFVDSIRAAPmsyikakddptR 357
Cdd:pfam17681    1 LRDLLFALQGISGSYI-RFDESDSRIVDDIRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESSSSFE-----------Y 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  358 GQTFESFAEALSVMLWEFRKELTAWERDIAKQ-ETSLTLSKFAADLEPWAKRL-ALLELVYQAGTARNEpaSCAqstwlL 435
Cdd:pfam17681   69 GLVLQALCAALQEELTEYYRLIAQLESQLLEAsDSILTLLRLVVWLQPPLLLLrVLSNLVEAVEKQNLK--GGA-----L 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  436 LTALQGTIEAeyeqGTHREENVL--ILLRVwlgtIRPYIHFLDNWLsGYP-LCDPAQEFVIQRNPEI---TVKSPDFWEK 509
Cdd:pfam17681  142 LSLLHEATSH----GDPFVRELLsrLLQRV----SRPYLEMLERWI-YEGeLDDPYNEFFVEENPSVakeSLTSDDLWED 212
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229156697  510 AFTLHhftppskhgttqlpqsgaqpsgPDQrqkegrvsaghlervaVPSFLQPVL-RQILLAGK 572
Cdd:pfam17681  213 KYTLR----------------------PEM----------------LPSFLSPDLaEKILLTGK 238
 
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 ...
726-1037 1.48e-41

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: 154.70  E-value: 1.48e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  726 HLTetfaSMRRYYLCEAGDtMFDFLSD-LFDKLrlcqhksqWQDT-----LYLNYQLQTAVAAgypSDADR-LTVSFEPV 798
Cdd:pfam04130    4 HLR----ALKRYLLLGQGD-FISRLMDaLFDEL--------WKPAssllrHNLTGLLEEAIRS---SNAQRdLPDVLRRL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  799 NVPstVSIQPIHALDGLTLHYKVPWPLDIIINAKTITAYNQVFRFLLQVKRAKYCLeqlrfssiirssfpaatttdpkdk 878
Cdd:pfam04130   68 DAR--LDPDSLGGWDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVL------------------------ 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  879 pevrgDSTPSARPQPLHKAQLLHRVFLLRFKLIHFVNAVHSYLMSRILHSTGLEFQADIE-RAPDLEAIVELHTTYLAKV 957
Cdd:pfam04130  122 -----SSLWRRRQMSGSRSVLWHRARLLRQEMIHFVSQLQYYVMFEVIEPSWREFEEKLQkAASDLDDLIEAHEDFLDRI 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  958 SERCLLHKKVGLVREAVLKALNLALVFQRRWD---------------AGLSAFNAERIDQMLSEFNKCSVFLLTMLDNIN 1022
Cdd:pfam04130  197 LKKCFLTSPQQPLLKLLEEILSLILDFAEALDglylsvsesaraeaeDELPELERERLRRLEKQFRKKVSLLLKVLRGLK 276
                          330
                   ....*....|....*
gi 1229156697 1023 KRGAFPHLEALALSL 1037
Cdd:pfam04130  277 SHPDESHLRQLLLRL 291
GCP5_NTD cd22572
N-terminal domain of gamma-tubulin complex component 5 (GCP-5) and similar proteins; GCP-5, ...
21-126 5.21e-36

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: 131.52  E-value: 5.21e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697   21 VEQEAKKLIQKLTSFKDsNDENFRRSLQFALSNFKFHRYLDVDSHKITRKLQGLFQKFEIHSQLEKAVSLRKLTDKFLQL 100
Cdd:cd22572      1 LEELLEELITALTGFQE-DDENFRLCLDFALSNLRYHRFLSTNSFEVERRLDGLVEKFRVHGQDDLADALRELLDELLKL 79
                           90       100
                   ....*....|....*....|....*.
gi 1229156697  101 PLSPKSrdaKTDLHYSVLSVLLNLSD 126
Cdd:cd22572     80 PLFDHS---QSDWHPSILSLLLELSD 102
GCP_N_terminal pfam17681
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
278-572 1.64e-18

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: 87.34  E-value: 1.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  278 IRETIWVLMGAETSFVyQLHDSKFTSRQDIQVSHLTPKALHEFTSKLAETCTNAWTLQSFVDSIRAAPmsyikakddptR 357
Cdd:pfam17681    1 LRDLLFALQGISGSYI-RFDESDSRIVDDIRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESSSSFE-----------Y 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  358 GQTFESFAEALSVMLWEFRKELTAWERDIAKQ-ETSLTLSKFAADLEPWAKRL-ALLELVYQAGTARNEpaSCAqstwlL 435
Cdd:pfam17681   69 GLVLQALCAALQEELTEYYRLIAQLESQLLEAsDSILTLLRLVVWLQPPLLLLrVLSNLVEAVEKQNLK--GGA-----L 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  436 LTALQGTIEAeyeqGTHREENVL--ILLRVwlgtIRPYIHFLDNWLsGYP-LCDPAQEFVIQRNPEI---TVKSPDFWEK 509
Cdd:pfam17681  142 LSLLHEATSH----GDPFVRELLsrLLQRV----SRPYLEMLERWI-YEGeLDDPYNEFFVEENPSVakeSLTSDDLWED 212
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229156697  510 AFTLHhftppskhgttqlpqsgaqpsgPDQrqkegrvsaghlervaVPSFLQPVL-RQILLAGK 572
Cdd:pfam17681  213 KYTLR----------------------PEM----------------LPSFLSPDLaEKILLTGK 238
 
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 ...
726-1037 1.48e-41

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: 154.70  E-value: 1.48e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  726 HLTetfaSMRRYYLCEAGDtMFDFLSD-LFDKLrlcqhksqWQDT-----LYLNYQLQTAVAAgypSDADR-LTVSFEPV 798
Cdd:pfam04130    4 HLR----ALKRYLLLGQGD-FISRLMDaLFDEL--------WKPAssllrHNLTGLLEEAIRS---SNAQRdLPDVLRRL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  799 NVPstVSIQPIHALDGLTLHYKVPWPLDIIINAKTITAYNQVFRFLLQVKRAKYCLeqlrfssiirssfpaatttdpkdk 878
Cdd:pfam04130   68 DAR--LDPDSLGGWDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVL------------------------ 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  879 pevrgDSTPSARPQPLHKAQLLHRVFLLRFKLIHFVNAVHSYLMSRILHSTGLEFQADIE-RAPDLEAIVELHTTYLAKV 957
Cdd:pfam04130  122 -----SSLWRRRQMSGSRSVLWHRARLLRQEMIHFVSQLQYYVMFEVIEPSWREFEEKLQkAASDLDDLIEAHEDFLDRI 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  958 SERCLLHKKVGLVREAVLKALNLALVFQRRWD---------------AGLSAFNAERIDQMLSEFNKCSVFLLTMLDNIN 1022
Cdd:pfam04130  197 LKKCFLTSPQQPLLKLLEEILSLILDFAEALDglylsvsesaraeaeDELPELERERLRRLEKQFRKKVSLLLKVLRGLK 276
                          330
                   ....*....|....*
gi 1229156697 1023 KRGAFPHLEALALSL 1037
Cdd:pfam04130  277 SHPDESHLRQLLLRL 291
GCP5_NTD cd22572
N-terminal domain of gamma-tubulin complex component 5 (GCP-5) and similar proteins; GCP-5, ...
21-126 5.21e-36

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: 131.52  E-value: 5.21e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697   21 VEQEAKKLIQKLTSFKDsNDENFRRSLQFALSNFKFHRYLDVDSHKITRKLQGLFQKFEIHSQLEKAVSLRKLTDKFLQL 100
Cdd:cd22572      1 LEELLEELITALTGFQE-DDENFRLCLDFALSNLRYHRFLSTNSFEVERRLDGLVEKFRVHGQDDLADALRELLDELLKL 79
                           90       100
                   ....*....|....*....|....*.
gi 1229156697  101 PLSPKSrdaKTDLHYSVLSVLLNLSD 126
Cdd:cd22572     80 PLFDHS---QSDWHPSILSLLLELSD 102
GCP_N_terminal pfam17681
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ...
278-572 1.64e-18

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: 87.34  E-value: 1.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  278 IRETIWVLMGAETSFVyQLHDSKFTSRQDIQVSHLTPKALHEFTSKLAETCTNAWTLQSFVDSIRAAPmsyikakddptR 357
Cdd:pfam17681    1 LRDLLFALQGISGSYI-RFDESDSRIVDDIRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESSSSFE-----------Y 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  358 GQTFESFAEALSVMLWEFRKELTAWERDIAKQ-ETSLTLSKFAADLEPWAKRL-ALLELVYQAGTARNEpaSCAqstwlL 435
Cdd:pfam17681   69 GLVLQALCAALQEELTEYYRLIAQLESQLLEAsDSILTLLRLVVWLQPPLLLLrVLSNLVEAVEKQNLK--GGA-----L 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229156697  436 LTALQGTIEAeyeqGTHREENVL--ILLRVwlgtIRPYIHFLDNWLsGYP-LCDPAQEFVIQRNPEI---TVKSPDFWEK 509
Cdd:pfam17681  142 LSLLHEATSH----GDPFVRELLsrLLQRV----SRPYLEMLERWI-YEGeLDDPYNEFFVEENPSVakeSLTSDDLWED 212
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229156697  510 AFTLHhftppskhgttqlpqsgaqpsgPDQrqkegrvsaghlervaVPSFLQPVL-RQILLAGK 572
Cdd:pfam17681  213 KYTLR----------------------PEM----------------LPSFLSPDLaEKILLTGK 238
 
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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