NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|320542396|ref|NP_001189170|]
View 

circadian trip, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
2818-3138 1.61e-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: 1.61e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2818 HGLFPLPLGKSSKlpqmtKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEehSIGLADLMRVAPEVQNTLVRLQ 2897
Cdd:cd00078    73 GLLYPNPSSFADE-----DHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELYKSLKELL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2898 DLvrqreyilsDPNIDAMEKTEKIEqldldgcpiadlgLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEG 2977
Cdd:cd00078   146 DN---------DGDEDDLELTFTIE-------------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2978 VQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRD 3057
Cdd:cd00078   204 IEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED------IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNE 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 3058 EQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTldenqNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSmSF 3137
Cdd:cd00078   278 ERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG-----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA-GF 351

                  .
gi 320542396 3138 H 3138
Cdd:cd00078   352 G 352
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
1409-1481 5.02e-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: 5.02e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320542396   1409 VHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVA 1481
Cdd:smart00678    1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
Extensin_2 super family cl25884
Extensin-like region;
688-731 9.72e-04

Extensin-like region;


The actual alignment was detected with superfamily member pfam04554:

Pssm-ID: 252669 [Multi-domain]  Cd Length: 57  Bit Score: 39.75  E-value: 9.72e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 320542396   688 PHYYHSsvavlhqPPPHHFTSTGAGPPPALFQQQAPPQLTRYTP 731
Cdd:pfam04554   18 PYYYKS-------PPPPVKSPVYKSPPPPVYKSPPPPKYVYKSP 54
SRP1 super family cl34886
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
1087-1312 1.67e-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: 44.11  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 1087 QLLQGLQSHDESQQLQAAIEMCQMLvmGNEDTLagfPIKQV-----VPALIQLLRmEHNFDIMN-NACRALAYMLEALPR 1160
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLL--SKETSP---PIQPVidagvVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 1161 SSGTVVE--AVPVFLEKLQVIQcMDVAEQSLSALEIL---SRRHNKAILQANGISACLTYLD----FFSIVaqRAALAIA 1231
Cdd:COG5064   149 QTKVVVDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLssaiHISML--RNATWTL 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 1232 ANCCLNMHPE-EFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASP----DLLKNcQQLLLVTP 1306
Cdd:COG5064   226 SNLCRGKNPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTP 304

                  ....*.
gi 320542396 1307 AILNTG 1312
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 ...
2818-3138 1.61e-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: 1.61e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2818 HGLFPLPLGKSSKlpqmtKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEehSIGLADLMRVAPEVQNTLVRLQ 2897
Cdd:cd00078    73 GLLYPNPSSFADE-----DHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELYKSLKELL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2898 DLvrqreyilsDPNIDAMEKTEKIEqldldgcpiadlgLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEG 2977
Cdd:cd00078   146 DN---------DGDEDDLELTFTIE-------------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2978 VQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRD 3057
Cdd:cd00078   204 IEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED------IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNE 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 3058 EQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTldenqNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSmSF 3137
Cdd:cd00078   278 ERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG-----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA-GF 351

                  .
gi 320542396 3138 H 3138
Cdd:cd00078   352 G 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
2818-3140 3.05e-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: 3.05e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396  2818 HGLFP--------LPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEhsIGLADLMRVAPEV 2889
Cdd:pfam00632   12 YGLFEyeteddrtYWFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP--LTLEDLESIDPEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396  2890 QNTLVRLQDLVRQREyilsdpnidamektekieqldldgcpiADLGLDFVLP---GHANIELCRGGRDTPVTVHNLHQYI 2966
Cdd:pfam00632   90 YKSLKSLLNMDNDDD---------------------------EDLGLTFTIPvfgESKTIELIPNGRNIPVTNENKEEYI 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396  2967 SLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSgseqqhSRWEIKMLQESCRTDHGFHQDSQAIQY 3046
Cdd:pfam00632  143 RLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS------PEIDVEDLKKNTEYDGGYTKNSPTIQW 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396  3047 LYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALtPPLTIVRKtldeNQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKL 3126
Cdd:pfam00632  217 FWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRK----GGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKL 291
                          330
                   ....*....|....
gi 320542396  3127 KVAANEGSmSFHLS 3140
Cdd:pfam00632  292 LIAIEEGE-GFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
2839-3133 1.15e-83

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: 1.15e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396   2839 AKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLqdlvrqreyILSDPNIDAMEKT 2918
Cdd:smart00119   66 SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL---------LLNNDTSEELDLT 134
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396   2919 EKIeqldldgcpiadlGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRL 2998
Cdd:smart00119  135 FSI-------------VLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLL 201
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396   2999 RMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFK 3078
Cdd:smart00119  202 KLFDPEELELLICGSPE------IDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFA 275
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 320542396   3079 ALTPPLTIVRKTLDEnqnpnDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEG 3133
Cdd:smart00119  276 ALSPKFTIRKAGSDD-----ERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEG 325
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2841-3139 3.73e-68

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 250.07  E-value: 3.73e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2841 FKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLQDlvrqreyilsdpnidaMEKTEK 2920
Cdd:COG5021   605 FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG--KPVSLVDLESLDPELYRSLVWLLN----------------NDIDET 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2921 IEQLDLDgcpIADLGLDFVLPghanIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRM 3000
Cdd:COG5021   667 ILDLTFT---VEDDSFGESRT----VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 3001 FYPEELECVFCGSgSEQqhsrWEIKMLQESCrTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKAL 3080
Cdd:COG5021   740 FDESELELLIGGI-PED----IDIDDWKSNT-AYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDL 813
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 320542396 3081 TPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHL 3139
Cdd:COG5021   814 QGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
1409-1481 5.02e-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: 5.02e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320542396   1409 VHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVA 1481
Cdd:smart00678    1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
1410-1473 1.42e-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: 1.42e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320542396  1410 HWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLS--TFGRTYTVDFHAMQQINEDTGTTRPVQR 1473
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
Extensin_2 pfam04554
Extensin-like region;
688-731 9.72e-04

Extensin-like region;


Pssm-ID: 252669 [Multi-domain]  Cd Length: 57  Bit Score: 39.75  E-value: 9.72e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 320542396   688 PHYYHSsvavlhqPPPHHFTSTGAGPPPALFQQQAPPQLTRYTP 731
Cdd:pfam04554   18 PYYYKS-------PPPPVKSPVYKSPPPPVYKSPPPPKYVYKSP 54
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
1087-1312 1.67e-03

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


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 44.11  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 1087 QLLQGLQSHDESQQLQAAIEMCQMLvmGNEDTLagfPIKQV-----VPALIQLLRmEHNFDIMN-NACRALAYMLEALPR 1160
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLL--SKETSP---PIQPVidagvVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 1161 SSGTVVE--AVPVFLEKLQVIQcMDVAEQSLSALEIL---SRRHNKAILQANGISACLTYLD----FFSIVaqRAALAIA 1231
Cdd:COG5064   149 QTKVVVDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLssaiHISML--RNATWTL 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 1232 ANCCLNMHPE-EFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASP----DLLKNcQQLLLVTP 1306
Cdd:COG5064   226 SNLCRGKNPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTP 304

                  ....*.
gi 320542396 1307 AILNTG 1312
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 ...
2818-3138 1.61e-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: 1.61e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2818 HGLFPLPLGKSSKlpqmtKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEehSIGLADLMRVAPEVQNTLVRLQ 2897
Cdd:cd00078    73 GLLYPNPSSFADE-----DHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELYKSLKELL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2898 DLvrqreyilsDPNIDAMEKTEKIEqldldgcpiadlgLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEG 2977
Cdd:cd00078   146 DN---------DGDEDDLELTFTIE-------------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2978 VQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRD 3057
Cdd:cd00078   204 IEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED------IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNE 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 3058 EQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTldenqNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSmSF 3137
Cdd:cd00078   278 ERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG-----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA-GF 351

                  .
gi 320542396 3138 H 3138
Cdd:cd00078   352 G 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
2818-3140 3.05e-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: 3.05e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396  2818 HGLFP--------LPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEhsIGLADLMRVAPEV 2889
Cdd:pfam00632   12 YGLFEyeteddrtYWFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP--LTLEDLESIDPEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396  2890 QNTLVRLQDLVRQREyilsdpnidamektekieqldldgcpiADLGLDFVLP---GHANIELCRGGRDTPVTVHNLHQYI 2966
Cdd:pfam00632   90 YKSLKSLLNMDNDDD---------------------------EDLGLTFTIPvfgESKTIELIPNGRNIPVTNENKEEYI 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396  2967 SLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSgseqqhSRWEIKMLQESCRTDHGFHQDSQAIQY 3046
Cdd:pfam00632  143 RLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS------PEIDVEDLKKNTEYDGGYTKNSPTIQW 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396  3047 LYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALtPPLTIVRKtldeNQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKL 3126
Cdd:pfam00632  217 FWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRK----GGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKL 291
                          330
                   ....*....|....
gi 320542396  3127 KVAANEGSmSFHLS 3140
Cdd:pfam00632  292 LIAIEEGE-GFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
2839-3133 1.15e-83

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: 1.15e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396   2839 AKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLqdlvrqreyILSDPNIDAMEKT 2918
Cdd:smart00119   66 SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL---------LLNNDTSEELDLT 134
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396   2919 EKIeqldldgcpiadlGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRL 2998
Cdd:smart00119  135 FSI-------------VLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLL 201
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396   2999 RMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFK 3078
Cdd:smart00119  202 KLFDPEELELLICGSPE------IDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFA 275
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 320542396   3079 ALTPPLTIVRKTLDEnqnpnDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEG 3133
Cdd:smart00119  276 ALSPKFTIRKAGSDD-----ERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEG 325
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2841-3139 3.73e-68

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 250.07  E-value: 3.73e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2841 FKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLQDlvrqreyilsdpnidaMEKTEK 2920
Cdd:COG5021   605 FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG--KPVSLVDLESLDPELYRSLVWLLN----------------NDIDET 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 2921 IEQLDLDgcpIADLGLDFVLPghanIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRM 3000
Cdd:COG5021   667 ILDLTFT---VEDDSFGESRT----VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 3001 FYPEELECVFCGSgSEQqhsrWEIKMLQESCrTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKAL 3080
Cdd:COG5021   740 FDESELELLIGGI-PED----IDIDDWKSNT-AYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDL 813
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 320542396 3081 TPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHL 3139
Cdd:COG5021   814 QGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
1409-1481 5.02e-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: 5.02e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320542396   1409 VHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVA 1481
Cdd:smart00678    1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
1410-1473 1.42e-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: 1.42e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320542396  1410 HWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLS--TFGRTYTVDFHAMQQINEDTGTTRPVQR 1473
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
Extensin_2 pfam04554
Extensin-like region;
688-731 9.72e-04

Extensin-like region;


Pssm-ID: 252669 [Multi-domain]  Cd Length: 57  Bit Score: 39.75  E-value: 9.72e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 320542396   688 PHYYHSsvavlhqPPPHHFTSTGAGPPPALFQQQAPPQLTRYTP 731
Cdd:pfam04554   18 PYYYKS-------PPPPVKSPVYKSPPPPVYKSPPPPKYVYKSP 54
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
1087-1312 1.67e-03

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


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 44.11  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 1087 QLLQGLQSHDESQQLQAAIEMCQMLvmGNEDTLagfPIKQV-----VPALIQLLRmEHNFDIMN-NACRALAYMLEALPR 1160
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLL--SKETSP---PIQPVidagvVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 1161 SSGTVVE--AVPVFLEKLQVIQcMDVAEQSLSALEIL---SRRHNKAILQANGISACLTYLD----FFSIVaqRAALAIA 1231
Cdd:COG5064   149 QTKVVVDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLssaiHISML--RNATWTL 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542396 1232 ANCCLNMHPE-EFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASP----DLLKNcQQLLLVTP 1306
Cdd:COG5064   226 SNLCRGKNPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTP 304

                  ....*.
gi 320542396 1307 AILNTG 1312
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH