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Conserved domains on  [gi|7291760|gb|AAF47181|]
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uncharacterized protein Dmel_CG3356 [Drosophila melanogaster]

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 ...
766-1120 6.11e-151

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: 454.72  E-value: 6.11e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   766 ITVRRSHLYEDAYDKLRPDNEPDLRFKFRIQFVsslglDEAGIDGGGVFREFLSELIKTAFDPNRGFFMVTTDNK--LYP 843
Cdd:cd00078    3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFV-----GEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSglLYP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   844 NPNvADLFEDYEKHYYFIGRILGKSIYENLLVELPLAEFFLTKLAGKYsdVDIHQLASLDPELYRNLLYLKDYSGDVSEL 923
Cdd:cd00078   78 NPS-SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--LSLEDLEELDPELYKSLKELLDNDGDEDDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   924 NLDFTVA-SSSLGQTQIVELKPQGQSIPVTNSNRIEYLQLIADYKLNVQIRRHCNAFRKGLSNVLPIEWLYMFSNKELQI 1002
Cdd:cd00078  155 ELTFTIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760  1003 LISGAEiPIDLEDLKKHCEYGGEFSPEHPSIVTFWEVLEGFDDMQRRQLLKFVTSCSRPPLLGFKDLDPPFFIQNTG-DM 1081
Cdd:cd00078  235 LICGSE-DIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGsPD 313
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 7291760  1082 ERLPTASTCTNLLKLPPFKTVEQMREKLLYAIQSGAGFE 1120
Cdd:cd00078  314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
766-1120 6.11e-151

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: 454.72  E-value: 6.11e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   766 ITVRRSHLYEDAYDKLRPDNEPDLRFKFRIQFVsslglDEAGIDGGGVFREFLSELIKTAFDPNRGFFMVTTDNK--LYP 843
Cdd:cd00078    3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFV-----GEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSglLYP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   844 NPNvADLFEDYEKHYYFIGRILGKSIYENLLVELPLAEFFLTKLAGKYsdVDIHQLASLDPELYRNLLYLKDYSGDVSEL 923
Cdd:cd00078   78 NPS-SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--LSLEDLEELDPELYKSLKELLDNDGDEDDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   924 NLDFTVA-SSSLGQTQIVELKPQGQSIPVTNSNRIEYLQLIADYKLNVQIRRHCNAFRKGLSNVLPIEWLYMFSNKELQI 1002
Cdd:cd00078  155 ELTFTIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760  1003 LISGAEiPIDLEDLKKHCEYGGEFSPEHPSIVTFWEVLEGFDDMQRRQLLKFVTSCSRPPLLGFKDLDPPFFIQNTG-DM 1081
Cdd:cd00078  235 LICGSE-DIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGsPD 313
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 7291760  1082 ERLPTASTCTNLLKLPPFKTVEQMREKLLYAIQSGAGFE 1120
Cdd:cd00078  314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
788-1119 1.97e-120

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: 373.88  E-value: 1.97e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760      788 DLRFK-FRIQFVsslglDEAGIDGGGVFREFLSELIKTAFDPNRGFFMVT-TDNKLYPNPNVADLFEDYEKHYYFIGRIL 865
Cdd:smart00119    1 DLKKRvLEIEFE-----GEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSpNDYLLYPNPRSGFANEEHLSYFRFIGRVL 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760      866 GKSIYENLLVELPLAEFFLTKLAGKysDVDIHQLASLDPELYRNLLYLKDYSGDVSELNLDFT-VASSSLGQTQIVELKP 944
Cdd:smart00119   76 GKALYDNRLLDLFFARPFYKKLLGK--PVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760      945 QGQSIPVTNSNRIEYLQLIADYKLNVQIRRHCNAFRKGLSNVLPIEWLYMFSNKELQILISGAEiPIDLEDLKKHCEYGG 1024
Cdd:smart00119  154 GGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSP-EIDVDDLKSNTEYKG 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760     1025 EFSPEHPSIVTFWEVLEGFDDMQRRQLLKFVTSCSRPPLLGFKDLDPPFFIQNTG-DMERLPTASTCTNLLKLPPFKTVE 1103
Cdd:smart00119  233 GYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKE 312
                           330
                    ....*....|....*.
gi 7291760     1104 QMREKLLYAIQSGAGF 1119
Cdd:smart00119  313 ILREKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
819-1122 1.26e-116

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 362.70  E-value: 1.26e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760     819 SELIKTAFDPNRGFFMVTT--DNKLYPNPNVAD-LFEDYEKHYYFIGRILGKSIYENLLVELPLAEFFLTKLAGKysDVD 895
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETedDRTYWFNPSSSEsPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGE--PLT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760     896 IHQLASLDPELYRNLLYLKDYSGDVSE-LNLDFTVasSSLGQTQIVELKPQGQSIPVTNSNRIEYLQLIADYKLNVQIRR 974
Cdd:pfam00632   79 LEDLESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760     975 HCNAFRKGLSNVLPIEWLYMFSNKELQILISGAEiPIDLEDLKKHCEYGGEFSPEHPSIVTFWEVLEGFDDMQRRQLLKF 1054
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKF 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760    1055 VTSCSRPPLLGFKDLdPPFFIQNTG--DMERLPTASTCTNLLKLPPFKTVEQMREKLLYAIQSGAGFELS 1122
Cdd:pfam00632  236 VTGSSRLPVGGFKSL-PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
766-1122 2.48e-98

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 332.12  E-value: 2.48e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   766 ITVRRSHLYEDAYDKLRPDNEPDLRFKFRIQFVsslglDEAGIDGGGVFREFLSELIKTAFDPNRGFFMVTTDNKLYPNP 845
Cdd:COG5021  517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFV-----GEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPI 591
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   846 N-VADLFEDYEKHYYFIGRILGKSIYENLLVELPLAEFFLTKLAGKYSDVDihQLASLDPELYRNLLYLKDYSGDVSELN 924
Cdd:COG5021  592 NpLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLV--DLESLDPELYRSLVWLLNNDIDETILD 669
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   925 LDFTVASSSLGQTQIVELKPQGQSIPVTNSNRIEYLQLIADYKLNVQIRRHCNAFRKGLSNVLPIEWLYMFSNKELQILI 1004
Cdd:COG5021  670 LTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLI 749
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760  1005 SGAEIPIDLEDLKKHCEYGGeFSPEHPSIVTFWEVLEGFDDMQRRQLLKFVTSCSRPPLLGFKDLDPPFFIQ------NT 1078
Cdd:COG5021  750 GGIPEDIDIDDWKSNTAYHG-YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRkftiekGG 828
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 7291760  1079 GDMERLPTASTCTNLLKLPPFKTVEQMREKLLYAIQSGAGFELS 1122
Cdd:COG5021  829 TDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
766-1120 6.11e-151

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: 454.72  E-value: 6.11e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   766 ITVRRSHLYEDAYDKLRPDNEPDLRFKFRIQFVsslglDEAGIDGGGVFREFLSELIKTAFDPNRGFFMVTTDNK--LYP 843
Cdd:cd00078    3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFV-----GEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSglLYP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   844 NPNvADLFEDYEKHYYFIGRILGKSIYENLLVELPLAEFFLTKLAGKYsdVDIHQLASLDPELYRNLLYLKDYSGDVSEL 923
Cdd:cd00078   78 NPS-SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--LSLEDLEELDPELYKSLKELLDNDGDEDDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   924 NLDFTVA-SSSLGQTQIVELKPQGQSIPVTNSNRIEYLQLIADYKLNVQIRRHCNAFRKGLSNVLPIEWLYMFSNKELQI 1002
Cdd:cd00078  155 ELTFTIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760  1003 LISGAEiPIDLEDLKKHCEYGGEFSPEHPSIVTFWEVLEGFDDMQRRQLLKFVTSCSRPPLLGFKDLDPPFFIQNTG-DM 1081
Cdd:cd00078  235 LICGSE-DIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGsPD 313
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 7291760  1082 ERLPTASTCTNLLKLPPFKTVEQMREKLLYAIQSGAGFE 1120
Cdd:cd00078  314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
788-1119 1.97e-120

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: 373.88  E-value: 1.97e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760      788 DLRFK-FRIQFVsslglDEAGIDGGGVFREFLSELIKTAFDPNRGFFMVT-TDNKLYPNPNVADLFEDYEKHYYFIGRIL 865
Cdd:smart00119    1 DLKKRvLEIEFE-----GEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSpNDYLLYPNPRSGFANEEHLSYFRFIGRVL 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760      866 GKSIYENLLVELPLAEFFLTKLAGKysDVDIHQLASLDPELYRNLLYLKDYSGDVSELNLDFT-VASSSLGQTQIVELKP 944
Cdd:smart00119   76 GKALYDNRLLDLFFARPFYKKLLGK--PVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760      945 QGQSIPVTNSNRIEYLQLIADYKLNVQIRRHCNAFRKGLSNVLPIEWLYMFSNKELQILISGAEiPIDLEDLKKHCEYGG 1024
Cdd:smart00119  154 GGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSP-EIDVDDLKSNTEYKG 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760     1025 EFSPEHPSIVTFWEVLEGFDDMQRRQLLKFVTSCSRPPLLGFKDLDPPFFIQNTG-DMERLPTASTCTNLLKLPPFKTVE 1103
Cdd:smart00119  233 GYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKE 312
                           330
                    ....*....|....*.
gi 7291760     1104 QMREKLLYAIQSGAGF 1119
Cdd:smart00119  313 ILREKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
819-1122 1.26e-116

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 362.70  E-value: 1.26e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760     819 SELIKTAFDPNRGFFMVTT--DNKLYPNPNVAD-LFEDYEKHYYFIGRILGKSIYENLLVELPLAEFFLTKLAGKysDVD 895
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETedDRTYWFNPSSSEsPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGE--PLT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760     896 IHQLASLDPELYRNLLYLKDYSGDVSE-LNLDFTVasSSLGQTQIVELKPQGQSIPVTNSNRIEYLQLIADYKLNVQIRR 974
Cdd:pfam00632   79 LEDLESIDPELYKSLKSLLNMDNDDDEdLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760     975 HCNAFRKGLSNVLPIEWLYMFSNKELQILISGAEiPIDLEDLKKHCEYGGEFSPEHPSIVTFWEVLEGFDDMQRRQLLKF 1054
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKF 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760    1055 VTSCSRPPLLGFKDLdPPFFIQNTG--DMERLPTASTCTNLLKLPPFKTVEQMREKLLYAIQSGAGFELS 1122
Cdd:pfam00632  236 VTGSSRLPVGGFKSL-PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
766-1122 2.48e-98

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 332.12  E-value: 2.48e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   766 ITVRRSHLYEDAYDKLRPDNEPDLRFKFRIQFVsslglDEAGIDGGGVFREFLSELIKTAFDPNRGFFMVTTDNKLYPNP 845
Cdd:COG5021  517 IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFV-----GEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPI 591
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   846 N-VADLFEDYEKHYYFIGRILGKSIYENLLVELPLAEFFLTKLAGKYSDVDihQLASLDPELYRNLLYLKDYSGDVSELN 924
Cdd:COG5021  592 NpLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLV--DLESLDPELYRSLVWLLNNDIDETILD 669
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760   925 LDFTVASSSLGQTQIVELKPQGQSIPVTNSNRIEYLQLIADYKLNVQIRRHCNAFRKGLSNVLPIEWLYMFSNKELQILI 1004
Cdd:COG5021  670 LTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLI 749
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7291760  1005 SGAEIPIDLEDLKKHCEYGGeFSPEHPSIVTFWEVLEGFDDMQRRQLLKFVTSCSRPPLLGFKDLDPPFFIQ------NT 1078
Cdd:COG5021  750 GGIPEDIDIDDWKSNTAYHG-YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRkftiekGG 828
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 7291760  1079 GDMERLPTASTCTNLLKLPPFKTVEQMREKLLYAIQSGAGFELS 1122
Cdd:COG5021  829 TDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 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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