NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|320542404|ref|NP_001189174|]
View 

circadian trip, isoform F [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 ...
2817-3137 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 320542404 2817 HGLFPLPLGKSSKlpqmtKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEehSIGLADLMRVAPEVQNTLVRLQ 2896
Cdd:cd00078    73 GLLYPNPSSFADE-----DHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELYKSLKELL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 2897 DLvrqreyilsDPNIDAMEKTEKIEqldldgcpiadlgLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEG 2976
Cdd:cd00078   146 DN---------DGDEDDLELTFTIE-------------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 2977 VQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRD 3056
Cdd:cd00078   204 IEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED------IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNE 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 3057 EQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTldenqNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSmSF 3136
Cdd:cd00078   278 ERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG-----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA-GF 351

                  .
gi 320542404 3137 H 3137
Cdd:cd00078   352 G 352
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
1408-1480 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 320542404   1408 VHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVA 1480
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 320542404   688 PHYYHSsvavlhqPPPHHFTSTGAGPPPALFQQQAPPQLTRYTP 731
Cdd:pfam04554   18 PYYYKS-------PPPPVKSPVYKSPPPPVYKSPPPPKYVYKSP 54
SRP1 super family cl34886
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
1086-1311 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 320542404 1086 QLLQGLQSHDESQQLQAAIEMCQMLvmGNEDTLagfPIKQV-----VPALIQLLRmEHNFDIMN-NACRALAYMLEALPR 1159
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLL--SKETSP---PIQPVidagvVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 1160 SSGTVVE--AVPVFLEKLQVIQcMDVAEQSLSALEIL---SRRHNKAILQANGISACLTYLD----FFSIVaqRAALAIA 1230
Cdd:COG5064   149 QTKVVVDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLssaiHISML--RNATWTL 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 1231 ANCCLNMHPE-EFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASP----DLLKNcQQLLLVTP 1305
Cdd:COG5064   226 SNLCRGKNPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTP 304

                  ....*.
gi 320542404 1306 AILNTG 1311
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 ...
2817-3137 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 320542404 2817 HGLFPLPLGKSSKlpqmtKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEehSIGLADLMRVAPEVQNTLVRLQ 2896
Cdd:cd00078    73 GLLYPNPSSFADE-----DHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELYKSLKELL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 2897 DLvrqreyilsDPNIDAMEKTEKIEqldldgcpiadlgLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEG 2976
Cdd:cd00078   146 DN---------DGDEDDLELTFTIE-------------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 2977 VQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRD 3056
Cdd:cd00078   204 IEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED------IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNE 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 3057 EQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTldenqNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSmSF 3136
Cdd:cd00078   278 ERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG-----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA-GF 351

                  .
gi 320542404 3137 H 3137
Cdd:cd00078   352 G 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
2817-3139 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 320542404  2817 HGLFP--------LPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEhsIGLADLMRVAPEV 2888
Cdd:pfam00632   12 YGLFEyeteddrtYWFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP--LTLEDLESIDPEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404  2889 QNTLVRLQDLVRQREyilsdpnidamektekieqldldgcpiADLGLDFVLP---GHANIELCRGGRDTPVTVHNLHQYI 2965
Cdd:pfam00632   90 YKSLKSLLNMDNDDD---------------------------EDLGLTFTIPvfgESKTIELIPNGRNIPVTNENKEEYI 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404  2966 SLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSgseqqhSRWEIKMLQESCRTDHGFHQDSQAIQY 3045
Cdd:pfam00632  143 RLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS------PEIDVEDLKKNTEYDGGYTKNSPTIQW 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404  3046 LYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALtPPLTIVRKtldeNQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKL 3125
Cdd:pfam00632  217 FWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRK----GGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKL 291
                          330
                   ....*....|....
gi 320542404  3126 KVAANEGSmSFHLS 3139
Cdd:pfam00632  292 LIAIEEGE-GFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
2838-3132 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 320542404   2838 AKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLqdlvrqreyILSDPNIDAMEKT 2917
Cdd:smart00119   66 SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL---------LLNNDTSEELDLT 134
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404   2918 EKIeqldldgcpiadlGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRL 2997
Cdd:smart00119  135 FSI-------------VLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLL 201
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404   2998 RMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFK 3077
Cdd:smart00119  202 KLFDPEELELLICGSPE------IDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFA 275
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 320542404   3078 ALTPPLTIVRKTLDEnqnpnDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEG 3132
Cdd:smart00119  276 ALSPKFTIRKAGSDD-----ERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEG 325
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2840-3138 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 320542404 2840 FKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLQDlvrqreyilsdpnidaMEKTEK 2919
Cdd:COG5021   605 FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG--KPVSLVDLESLDPELYRSLVWLLN----------------NDIDET 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 2920 IEQLDLDgcpIADLGLDFVLPghanIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRM 2999
Cdd:COG5021   667 ILDLTFT---VEDDSFGESRT----VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 3000 FYPEELECVFCGSgSEQqhsrWEIKMLQESCrTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKAL 3079
Cdd:COG5021   740 FDESELELLIGGI-PED----IDIDDWKSNT-AYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDL 813
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 320542404 3080 TPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHL 3138
Cdd:COG5021   814 QGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
1408-1480 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 320542404   1408 VHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVA 1480
Cdd:smart00678    1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
1409-1472 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 320542404  1409 HWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLS--TFGRTYTVDFHAMQQINEDTGTTRPVQR 1472
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 320542404   688 PHYYHSsvavlhqPPPHHFTSTGAGPPPALFQQQAPPQLTRYTP 731
Cdd:pfam04554   18 PYYYKS-------PPPPVKSPVYKSPPPPVYKSPPPPKYVYKSP 54
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
1086-1311 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 320542404 1086 QLLQGLQSHDESQQLQAAIEMCQMLvmGNEDTLagfPIKQV-----VPALIQLLRmEHNFDIMN-NACRALAYMLEALPR 1159
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLL--SKETSP---PIQPVidagvVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 1160 SSGTVVE--AVPVFLEKLQVIQcMDVAEQSLSALEIL---SRRHNKAILQANGISACLTYLD----FFSIVaqRAALAIA 1230
Cdd:COG5064   149 QTKVVVDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLssaiHISML--RNATWTL 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 1231 ANCCLNMHPE-EFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASP----DLLKNcQQLLLVTP 1305
Cdd:COG5064   226 SNLCRGKNPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTP 304

                  ....*.
gi 320542404 1306 AILNTG 1311
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 ...
2817-3137 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 320542404 2817 HGLFPLPLGKSSKlpqmtKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEehSIGLADLMRVAPEVQNTLVRLQ 2896
Cdd:cd00078    73 GLLYPNPSSFADE-----DHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELYKSLKELL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 2897 DLvrqreyilsDPNIDAMEKTEKIEqldldgcpiadlgLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEG 2976
Cdd:cd00078   146 DN---------DGDEDDLELTFTIE-------------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 2977 VQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRD 3056
Cdd:cd00078   204 IEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED------IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNE 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 3057 EQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTldenqNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSmSF 3136
Cdd:cd00078   278 ERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG-----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA-GF 351

                  .
gi 320542404 3137 H 3137
Cdd:cd00078   352 G 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
2817-3139 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 320542404  2817 HGLFP--------LPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEhsIGLADLMRVAPEV 2888
Cdd:pfam00632   12 YGLFEyeteddrtYWFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP--LTLEDLESIDPEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404  2889 QNTLVRLQDLVRQREyilsdpnidamektekieqldldgcpiADLGLDFVLP---GHANIELCRGGRDTPVTVHNLHQYI 2965
Cdd:pfam00632   90 YKSLKSLLNMDNDDD---------------------------EDLGLTFTIPvfgESKTIELIPNGRNIPVTNENKEEYI 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404  2966 SLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSgseqqhSRWEIKMLQESCRTDHGFHQDSQAIQY 3045
Cdd:pfam00632  143 RLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS------PEIDVEDLKKNTEYDGGYTKNSPTIQW 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404  3046 LYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALtPPLTIVRKtldeNQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKL 3125
Cdd:pfam00632  217 FWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRK----GGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKL 291
                          330
                   ....*....|....
gi 320542404  3126 KVAANEGSmSFHLS 3139
Cdd:pfam00632  292 LIAIEEGE-GFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
2838-3132 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 320542404   2838 AKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLqdlvrqreyILSDPNIDAMEKT 2917
Cdd:smart00119   66 SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL---------LLNNDTSEELDLT 134
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404   2918 EKIeqldldgcpiadlGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRL 2997
Cdd:smart00119  135 FSI-------------VLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLL 201
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404   2998 RMFYPEELECVFCGSGSeqqhsrWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFK 3077
Cdd:smart00119  202 KLFDPEELELLICGSPE------IDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFA 275
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 320542404   3078 ALTPPLTIVRKTLDEnqnpnDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEG 3132
Cdd:smart00119  276 ALSPKFTIRKAGSDD-----ERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEG 325
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2840-3138 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 320542404 2840 FKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSeeHSIGLADLMRVAPEVQNTLVRLQDlvrqreyilsdpnidaMEKTEK 2919
Cdd:COG5021   605 FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG--KPVSLVDLESLDPELYRSLVWLLN----------------NDIDET 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 2920 IEQLDLDgcpIADLGLDFVLPghanIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRM 2999
Cdd:COG5021   667 ILDLTFT---VEDDSFGESRT----VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 3000 FYPEELECVFCGSgSEQqhsrWEIKMLQESCrTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKAL 3079
Cdd:COG5021   740 FDESELELLIGGI-PED----IDIDDWKSNT-AYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDL 813
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 320542404 3080 TPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHL 3138
Cdd:COG5021   814 QGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
1408-1480 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 320542404   1408 VHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVA 1480
Cdd:smart00678    1 YVWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
1409-1472 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 320542404  1409 HWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLS--TFGRTYTVDFHAMQQINEDTGTTRPVQR 1472
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 320542404   688 PHYYHSsvavlhqPPPHHFTSTGAGPPPALFQQQAPPQLTRYTP 731
Cdd:pfam04554   18 PYYYKS-------PPPPVKSPVYKSPPPPVYKSPPPPKYVYKSP 54
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
1086-1311 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 320542404 1086 QLLQGLQSHDESQQLQAAIEMCQMLvmGNEDTLagfPIKQV-----VPALIQLLRmEHNFDIMN-NACRALAYMLEALPR 1159
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLL--SKETSP---PIQPVidagvVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 1160 SSGTVVE--AVPVFLEKLQVIQcMDVAEQSLSALEIL---SRRHNKAILQANGISACLTYLD----FFSIVaqRAALAIA 1230
Cdd:COG5064   149 QTKVVVDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLssaiHISML--RNATWTL 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542404 1231 ANCCLNMHPE-EFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASP----DLLKNcQQLLLVTP 1305
Cdd:COG5064   226 SNLCRGKNPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTP 304

                  ....*.
gi 320542404 1306 AILNTG 1311
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