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Conserved domains on  [gi|665393198|ref|NP_001287163|]
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circadian trip, isoform M [Drosophila melanogaster]

Protein Classification

HECT-type E3 ubiquitin-protein ligase( domain architecture ID 13416657)

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 super family cl27008
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
2386-2706 1.36e-90

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.


The actual alignment was detected with superfamily member cd00078:

Pssm-ID: 474882 [Multi-domain]  Cd Length: 352  Bit Score: 299.48  E-value: 1.36e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2386 HGLFPLPLGKSSKlpqmtKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEehSIGLADLMRVAPEVQNTLVRLQ 2465
Cdd:cd00078    73 GLLYPNPSSFADE-----DHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELYKSLKELL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2466 DLvrqreyilsDPNIDAMEKTEKIEqldldgcpiadlgLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEG 2545
Cdd:cd00078   146 DN---------DGDEDDLELTFTIE-------------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2546 VQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRD 2625
Cdd:cd00078   204 IEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED------IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNE 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2626 EQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTldenqNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSmSF 2705
Cdd:cd00078   278 ERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG-----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA-GF 351

                  .
gi 665393198 2706 H 2706
Cdd:cd00078   352 G 352
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
977-1049 4.32e-26

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 103.57  E-value: 4.32e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665393198    977 VHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVA 1049
Cdd:smart00678    1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
SRP1 super family cl34886
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
655-880 1.75e-03

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


The actual alignment was detected with superfamily member COG5064:

Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 43.73  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  655 QLLQGLQSHDESQQLQAAIEMCQMLvmGNEDTLagfPIKQV-----VPALIQLLRmEHNFDIMN-NACRALAYMLEALPR 728
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLL--SKETSP---PIQPVidagvVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  729 SSGTVVE--AVPVFLEKLQVIQcMDVAEQSLSALEIL---SRRHNKAILQANGISACLTYLD----FFSIVaqRAALAIA 799
Cdd:COG5064   149 QTKVVVDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLssaiHISML--RNATWTL 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  800 ANCCLNMHPE-EFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASP----DLLKNcQQLLLVTP 874
Cdd:COG5064   226 SNLCRGKNPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTP 304

                  ....*.
gi 665393198  875 AILNTG 880
Cdd:COG5064   305 ALRSVG 310
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
2386-2706 1.36e-90

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: 299.48  E-value: 1.36e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2386 HGLFPLPLGKSSKlpqmtKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEehSIGLADLMRVAPEVQNTLVRLQ 2465
Cdd:cd00078    73 GLLYPNPSSFADE-----DHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELYKSLKELL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2466 DLvrqreyilsDPNIDAMEKTEKIEqldldgcpiadlgLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEG 2545
Cdd:cd00078   146 DN---------DGDEDDLELTFTIE-------------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2546 VQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRD 2625
Cdd:cd00078   204 IEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED------IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNE 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2626 EQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTldenqNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSmSF 2705
Cdd:cd00078   278 ERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG-----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA-GF 351

                  .
gi 665393198 2706 H 2706
Cdd:cd00078   352 G 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
2386-2708 2.60e-90

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 296.83  E-value: 2.60e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  2386 HGLFP--------LPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEhsIGLADLMRVAPEV 2457
Cdd:pfam00632   12 YGLFEyeteddrtYWFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP--LTLEDLESIDPEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  2458 QNTLVRLQDLVRQREyilsdpnidamektekieqldldgcpiADLGLDFVLP---GHANIELCRGGRDTPVTVHNLHQYI 2534
Cdd:pfam00632   90 YKSLKSLLNMDNDDD---------------------------EDLGLTFTIPvfgESKTIELIPNGRNIPVTNENKEEYI 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  2535 SLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSgseqqhSRWEIKMLQESCRTDHGFHQDSQAIQY 2614
Cdd:pfam00632  143 RLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS------PEIDVEDLKKNTEYDGGYTKNSPTIQW 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  2615 LYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALtPPLTIVRKtldeNQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKL 2694
Cdd:pfam00632  217 FWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRK----GGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKL 291
                          330
                   ....*....|....
gi 665393198  2695 KVAANEGSmSFHLS 2708
Cdd:pfam00632  292 LIAIEEGE-GFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
2407-2701 9.81e-84

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: 278.73  E-value: 9.81e-84
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198   2407 AKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLqdlvrqreyILSDPNIDAMEKT 2486
Cdd:smart00119   66 SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL---------LLNNDTSEELDLT 134
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198   2487 EKIeqldldgcpiadlGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRL 2566
Cdd:smart00119  135 FSI-------------VLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLL 201
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198   2567 RMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFK 2646
Cdd:smart00119  202 KLFDPEELELLICGSPE------IDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFA 275
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 665393198   2647 ALTPPLTIVRKTLDEnqnpnDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEG 2701
Cdd:smart00119  276 ALSPKFTIRKAGSDD-----ERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEG 325
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2409-2707 3.05e-68

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 250.07  E-value: 3.05e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2409 FKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLQDlvrqreyilsdpnidaMEKTEK 2488
Cdd:COG5021   605 FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG--KPVSLVDLESLDPELYRSLVWLLN----------------NDIDET 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2489 IEQLDLDgcpIADLGLDFVLPghanIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRM 2568
Cdd:COG5021   667 ILDLTFT---VEDDSFGESRT----VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2569 FYPEELECVFCGSgSEQqhsrWEIKMLQESCrTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKAL 2648
Cdd:COG5021   740 FDESELELLIGGI-PED----IDIDDWKSNT-AYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDL 813
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 665393198 2649 TPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHL 2707
Cdd:COG5021   814 QGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
977-1049 4.32e-26

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 103.57  E-value: 4.32e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665393198    977 VHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVA 1049
Cdd:smart00678    1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
978-1041 1.22e-24

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 98.91  E-value: 1.22e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665393198   978 HWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLS--TFGRTYTVDFHAMQQINEDTGTTRPVQR 1041
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
655-880 1.75e-03

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 43.73  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  655 QLLQGLQSHDESQQLQAAIEMCQMLvmGNEDTLagfPIKQV-----VPALIQLLRmEHNFDIMN-NACRALAYMLEALPR 728
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLL--SKETSP---PIQPVidagvVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  729 SSGTVVE--AVPVFLEKLQVIQcMDVAEQSLSALEIL---SRRHNKAILQANGISACLTYLD----FFSIVaqRAALAIA 799
Cdd:COG5064   149 QTKVVVDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLssaiHISML--RNATWTL 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  800 ANCCLNMHPE-EFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASP----DLLKNcQQLLLVTP 874
Cdd:COG5064   226 SNLCRGKNPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTP 304

                  ....*.
gi 665393198  875 AILNTG 880
Cdd:COG5064   305 ALRSVG 310
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
2386-2706 1.36e-90

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: 299.48  E-value: 1.36e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2386 HGLFPLPLGKSSKlpqmtKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEehSIGLADLMRVAPEVQNTLVRLQ 2465
Cdd:cd00078    73 GLLYPNPSSFADE-----DHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELYKSLKELL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2466 DLvrqreyilsDPNIDAMEKTEKIEqldldgcpiadlgLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEG 2545
Cdd:cd00078   146 DN---------DGDEDDLELTFTIE-------------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2546 VQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRD 2625
Cdd:cd00078   204 IEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED------IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNE 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2626 EQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTldenqNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSmSF 2705
Cdd:cd00078   278 ERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG-----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA-GF 351

                  .
gi 665393198 2706 H 2706
Cdd:cd00078   352 G 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
2386-2708 2.60e-90

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 296.83  E-value: 2.60e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  2386 HGLFP--------LPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEhsIGLADLMRVAPEV 2457
Cdd:pfam00632   12 YGLFEyeteddrtYWFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP--LTLEDLESIDPEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  2458 QNTLVRLQDLVRQREyilsdpnidamektekieqldldgcpiADLGLDFVLP---GHANIELCRGGRDTPVTVHNLHQYI 2534
Cdd:pfam00632   90 YKSLKSLLNMDNDDD---------------------------EDLGLTFTIPvfgESKTIELIPNGRNIPVTNENKEEYI 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  2535 SLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSgseqqhSRWEIKMLQESCRTDHGFHQDSQAIQY 2614
Cdd:pfam00632  143 RLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS------PEIDVEDLKKNTEYDGGYTKNSPTIQW 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  2615 LYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALtPPLTIVRKtldeNQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKL 2694
Cdd:pfam00632  217 FWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRK----GGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKL 291
                          330
                   ....*....|....
gi 665393198  2695 KVAANEGSmSFHLS 2708
Cdd:pfam00632  292 LIAIEEGE-GFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
2407-2701 9.81e-84

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: 278.73  E-value: 9.81e-84
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198   2407 AKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLqdlvrqreyILSDPNIDAMEKT 2486
Cdd:smart00119   66 SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL---------LLNNDTSEELDLT 134
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198   2487 EKIeqldldgcpiadlGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRL 2566
Cdd:smart00119  135 FSI-------------VLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLL 201
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198   2567 RMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFK 2646
Cdd:smart00119  202 KLFDPEELELLICGSPE------IDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFA 275
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 665393198   2647 ALTPPLTIVRKTLDEnqnpnDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEG 2701
Cdd:smart00119  276 ALSPKFTIRKAGSDD-----ERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEG 325
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2409-2707 3.05e-68

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 250.07  E-value: 3.05e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2409 FKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLQDlvrqreyilsdpnidaMEKTEK 2488
Cdd:COG5021   605 FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG--KPVSLVDLESLDPELYRSLVWLLN----------------NDIDET 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2489 IEQLDLDgcpIADLGLDFVLPghanIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRM 2568
Cdd:COG5021   667 ILDLTFT---VEDDSFGESRT----VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198 2569 FYPEELECVFCGSgSEQqhsrWEIKMLQESCrTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKAL 2648
Cdd:COG5021   740 FDESELELLIGGI-PED----IDIDDWKSNT-AYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDL 813
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 665393198 2649 TPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHL 2707
Cdd:COG5021   814 QGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
977-1049 4.32e-26

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 103.57  E-value: 4.32e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665393198    977 VHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVA 1049
Cdd:smart00678    1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
978-1041 1.22e-24

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 98.91  E-value: 1.22e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665393198   978 HWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLS--TFGRTYTVDFHAMQQINEDTGTTRPVQR 1041
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
655-880 1.75e-03

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 43.73  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  655 QLLQGLQSHDESQQLQAAIEMCQMLvmGNEDTLagfPIKQV-----VPALIQLLRmEHNFDIMN-NACRALAYMLEALPR 728
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLL--SKETSP---PIQPVidagvVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  729 SSGTVVE--AVPVFLEKLQVIQcMDVAEQSLSALEIL---SRRHNKAILQANGISACLTYLD----FFSIVaqRAALAIA 799
Cdd:COG5064   149 QTKVVVDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLssaiHISML--RNATWTL 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393198  800 ANCCLNMHPE-EFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASP----DLLKNcQQLLLVTP 874
Cdd:COG5064   226 SNLCRGKNPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTP 304

                  ....*.
gi 665393198  875 AILNTG 880
Cdd:COG5064   305 ALRSVG 310
 
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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