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Conserved domains on  [gi|530387309|ref|XP_005249621|]
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ubiquitin-protein ligase E3C isoform X2 [Homo sapiens]

Protein Classification

HECT-type E3 ubiquitin-protein ligase( domain architecture ID 10050984)

HECT-type E3 ubiquitin-protein ligase catalyzes the attachment of ubiquitin chains to target proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
700-1056 5.14e-150

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


:

Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 450.48  E-value: 5.14e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  700 VTIRRNYIYEDAYDKLSPENEPDLKKRIRVHLLNahgldEAGIDGGGIFREFLNELLKSGFNPNQGFFKTTNE--GLLYP 777
Cdd:cd00078     3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDdsGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  778 NPAAQMLvgDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKLLGTSadVDIHHLASLDPEVYKNLLFLKSYEDDVEE 857
Cdd:cd00078    78 NPSSFAD--EDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--LSLEDLEELDPELYKSLKELLDNDGDEDD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  858 LGLNFTVV-NNDLGEAQVVELKFGGKDIPVTSANRIAYIHLVADYRLNRQIRQHCLAFRQGLANVVSLEWLRMFDQQEIQ 936
Cdd:cd00078   154 LELTFTIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  937 VLISGAQvPISLEDLKSFTNYSGGYSADHPVIKVFWRVVEGFTDEEKRKLLKFVTSCSRPPLLGFKELYPAFCIHNGGSD 1016
Cdd:cd00078   234 LLICGSE-DIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSP 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 530387309 1017 LERLPTASTCMNLLKLPEFYDETLLRSKLLYAIECAAGFE 1056
Cdd:cd00078   313 DDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
700-1056 5.14e-150

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 450.48  E-value: 5.14e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  700 VTIRRNYIYEDAYDKLSPENEPDLKKRIRVHLLNahgldEAGIDGGGIFREFLNELLKSGFNPNQGFFKTTNE--GLLYP 777
Cdd:cd00078     3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDdsGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  778 NPAAQMLvgDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKLLGTSadVDIHHLASLDPEVYKNLLFLKSYEDDVEE 857
Cdd:cd00078    78 NPSSFAD--EDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--LSLEDLEELDPELYKSLKELLDNDGDEDD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  858 LGLNFTVV-NNDLGEAQVVELKFGGKDIPVTSANRIAYIHLVADYRLNRQIRQHCLAFRQGLANVVSLEWLRMFDQQEIQ 936
Cdd:cd00078   154 LELTFTIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  937 VLISGAQvPISLEDLKSFTNYSGGYSADHPVIKVFWRVVEGFTDEEKRKLLKFVTSCSRPPLLGFKELYPAFCIHNGGSD 1016
Cdd:cd00078   234 LLICGSE-DIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSP 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 530387309 1017 LERLPTASTCMNLLKLPEFYDETLLRSKLLYAIECAAGFE 1056
Cdd:cd00078   313 DDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
722-1055 8.59e-145

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 435.89  E-value: 8.59e-145
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309    722 DLKK-RIRVHLLNahgldEAGIDGGGIFREFLNELLKSGFNPNQGFFKTTNEG-LLYPNPAAQMLVGDSFArHYYFLGRM 799
Cdd:smart00119    1 DLKKrVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDyLLYPNPRSGFANEEHLS-YFRFIGRV 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309    800 LGKALYENMLVELPFAGFFLSKLLGTSadVDIHHLASLDPEVYKNLLFLKSYEDDVEELGLNFT-VVNNDLGEAQVVELK 878
Cdd:smart00119   75 LGKALYDNRLLDLFFARPFYKKLLGKP--VTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELK 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309    879 FGGKDIPVTSANRIAYIHLVADYRLNRQIRQHCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQvPISLEDLKSFTNYS 958
Cdd:smart00119  153 PGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSP-EIDVDDLKSNTEYK 231
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309    959 GGYSADHPVIKVFWRVVEGFTDEEKRKLLKFVTSCSRPPLLGFKELYPAFCIHNGGSDLERLPTASTCMNLLKLPEFYDE 1038
Cdd:smart00119  232 GGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSK 311
                           330
                    ....*....|....*..
gi 530387309   1039 TLLRSKLLYAIECAAGF 1055
Cdd:smart00119  312 EILREKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
753-1058 4.50e-109

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 341.51  E-value: 4.50e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309   753 NELLKSGFNPNQGFFK--TTNEGLLYPNPAAQMLVGDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKLLGTsaDVD 830
Cdd:pfam00632    1 TLLSKELFDPNYGLFEyeTEDDRTYWFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGE--PLT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309   831 IHHLASLDPEVYKNLLFLKSYE-DDVEELGLNFTVvnNDLGEAQVVELKFGGKDIPVTSANRIAYIHLVADYRLNRQIRQ 909
Cdd:pfam00632   79 LEDLESIDPELYKSLKSLLNMDnDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309   910 HCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQVpISLEDLKSFTNYSGGYSADHPVIKVFWRVVEGFTDEEKRKLLKF 989
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICGSPE-IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKF 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309   990 VTSCSRPPLLGFKELyPAFCIH-NGGSDLERLPTASTCMNLLKLPEFYDETLLRSKLLYAIECAAGFELS 1058
Cdd:pfam00632  236 VTGSSRLPVGGFKSL-PKFTIVrKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
669-1058 8.63e-100

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 334.81  E-value: 8.63e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  669 PFEERVKIFQRLIYADKQE------VQGDGPFLDGINVTIRRNYIYEDAYDKLSPENEPDLKKRIRVHLLNahgldEAGI 742
Cdd:COG5021   480 SFISLNKLDIRRIKEDKRRklfyslKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGI 554
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  743 DGGGIFREFLNELLKSGFNPNQGFFKTTNEGLLYPNPAAQMLVGDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKL 822
Cdd:COG5021   555 DAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKL 634
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  823 LGTSADVDihHLASLDPEVYKNLLFLKSYEDDVEELGLNFTVVNNDLGEAQVVELKFGGKDIPVTSANRIAYIHLVADYR 902
Cdd:COG5021   635 LGKPVSLV--DLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYK 712
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  903 LNRQIRQHCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQVPISLEDLKSFTNYsGGYSADHPVIKVFWRVVEGFTDEE 982
Cdd:COG5021   713 LNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEE 791
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  983 KRKLLKFVTSCSRPPLLGFKELYPA-----FCIHNGGSDLERLPTASTCMNLLKLPEFYDETLLRSKLLYAIECAAGFEL 1057
Cdd:COG5021   792 RAKLLQFVTGTSRIPINGFKDLQGSdgvrkFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGL 871

                  .
gi 530387309 1058 S 1058
Cdd:COG5021   872 L 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
700-1056 5.14e-150

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 450.48  E-value: 5.14e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  700 VTIRRNYIYEDAYDKLSPENEPDLKKRIRVHLLNahgldEAGIDGGGIFREFLNELLKSGFNPNQGFFKTTNE--GLLYP 777
Cdd:cd00078     3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDdsGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  778 NPAAQMLvgDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKLLGTSadVDIHHLASLDPEVYKNLLFLKSYEDDVEE 857
Cdd:cd00078    78 NPSSFAD--EDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--LSLEDLEELDPELYKSLKELLDNDGDEDD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  858 LGLNFTVV-NNDLGEAQVVELKFGGKDIPVTSANRIAYIHLVADYRLNRQIRQHCLAFRQGLANVVSLEWLRMFDQQEIQ 936
Cdd:cd00078   154 LELTFTIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  937 VLISGAQvPISLEDLKSFTNYSGGYSADHPVIKVFWRVVEGFTDEEKRKLLKFVTSCSRPPLLGFKELYPAFCIHNGGSD 1016
Cdd:cd00078   234 LLICGSE-DIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSP 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 530387309 1017 LERLPTASTCMNLLKLPEFYDETLLRSKLLYAIECAAGFE 1056
Cdd:cd00078   313 DDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
722-1055 8.59e-145

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 435.89  E-value: 8.59e-145
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309    722 DLKK-RIRVHLLNahgldEAGIDGGGIFREFLNELLKSGFNPNQGFFKTTNEG-LLYPNPAAQMLVGDSFArHYYFLGRM 799
Cdd:smart00119    1 DLKKrVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDyLLYPNPRSGFANEEHLS-YFRFIGRV 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309    800 LGKALYENMLVELPFAGFFLSKLLGTSadVDIHHLASLDPEVYKNLLFLKSYEDDVEELGLNFT-VVNNDLGEAQVVELK 878
Cdd:smart00119   75 LGKALYDNRLLDLFFARPFYKKLLGKP--VTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELK 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309    879 FGGKDIPVTSANRIAYIHLVADYRLNRQIRQHCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQvPISLEDLKSFTNYS 958
Cdd:smart00119  153 PGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSP-EIDVDDLKSNTEYK 231
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309    959 GGYSADHPVIKVFWRVVEGFTDEEKRKLLKFVTSCSRPPLLGFKELYPAFCIHNGGSDLERLPTASTCMNLLKLPEFYDE 1038
Cdd:smart00119  232 GGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSK 311
                           330
                    ....*....|....*..
gi 530387309   1039 TLLRSKLLYAIECAAGF 1055
Cdd:smart00119  312 EILREKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
753-1058 4.50e-109

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 341.51  E-value: 4.50e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309   753 NELLKSGFNPNQGFFK--TTNEGLLYPNPAAQMLVGDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKLLGTsaDVD 830
Cdd:pfam00632    1 TLLSKELFDPNYGLFEyeTEDDRTYWFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGE--PLT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309   831 IHHLASLDPEVYKNLLFLKSYE-DDVEELGLNFTVvnNDLGEAQVVELKFGGKDIPVTSANRIAYIHLVADYRLNRQIRQ 909
Cdd:pfam00632   79 LEDLESIDPELYKSLKSLLNMDnDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309   910 HCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQVpISLEDLKSFTNYSGGYSADHPVIKVFWRVVEGFTDEEKRKLLKF 989
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICGSPE-IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKF 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309   990 VTSCSRPPLLGFKELyPAFCIH-NGGSDLERLPTASTCMNLLKLPEFYDETLLRSKLLYAIECAAGFELS 1058
Cdd:pfam00632  236 VTGSSRLPVGGFKSL-PKFTIVrKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
669-1058 8.63e-100

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 334.81  E-value: 8.63e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  669 PFEERVKIFQRLIYADKQE------VQGDGPFLDGINVTIRRNYIYEDAYDKLSPENEPDLKKRIRVHLLNahgldEAGI 742
Cdd:COG5021   480 SFISLNKLDIRRIKEDKRRklfyslKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGI 554
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  743 DGGGIFREFLNELLKSGFNPNQGFFKTTNEGLLYPNPAAQMLVGDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKL 822
Cdd:COG5021   555 DAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKL 634
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  823 LGTSADVDihHLASLDPEVYKNLLFLKSYEDDVEELGLNFTVVNNDLGEAQVVELKFGGKDIPVTSANRIAYIHLVADYR 902
Cdd:COG5021   635 LGKPVSLV--DLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYK 712
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  903 LNRQIRQHCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQVPISLEDLKSFTNYsGGYSADHPVIKVFWRVVEGFTDEE 982
Cdd:COG5021   713 LNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEE 791
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387309  983 KRKLLKFVTSCSRPPLLGFKELYPA-----FCIHNGGSDLERLPTASTCMNLLKLPEFYDETLLRSKLLYAIECAAGFEL 1057
Cdd:COG5021   792 RAKLLQFVTGTSRIPINGFKDLQGSdgvrkFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGL 871

                  .
gi 530387309 1058 S 1058
Cdd:COG5021   872 L 872
 
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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