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Conserved domains on  [gi|241944482|gb|EES17627|]
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hypothetical protein SORBI_3009G025200 [Sorghum bicolor]

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 ...
982-1363 1.02e-101

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: 328.37  E-value: 1.02e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  982 RVARSAILEGAVSVMTSHGSSSR--IIDVEFEGEVGTGR-GPTFEFYTTVTHELQRGGLGMWRGDSGEHGfihapfGLFP 1058
Cdd:cd00078     4 TVRRDRILEDALRQLSKVSSSDLkkVLEVEFVGEEGIDAgGVTREFFTLVSKELFNPSYGLFRYTPDDSG------LLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1059 KPWSPsgtssqgvDFTNMLQKFKLLGNLVARAVLDGRILDIPLSKAFYKVMLEQELDIYDIPLFDPELGKIVIEFQALVS 1138
Cdd:cd00078    78 NPSSF--------ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1139 RKNFLetssrasnpmvDLTyknvklEDLCLDFTLPGNPEYELVPGGSEKPVTLESLGEYVSLVADATLKSGIAKQIEAFK 1218
Cdd:cd00078   150 DEDDL-----------ELT------FTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFR 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1219 SGINEVFALKALKMFTEEEMECILCGEQDaWALKNLEDHMEFEHGYDMSSQPIIIFLEILREFGREEQRAFIQFSTGAPQ 1298
Cdd:cd00078   213 DGFSEVIPEELLSLFTPEELELLICGSED-IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSR 291
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241944482 1299 LPLGGLASLEPKLTVVRKqcdGNVDDELPSVNTCRHFIKLPPYSSKEIMRTKLKYAITEGLGsFH 1363
Cdd:cd00078   292 LPVGGFADLNPKFTIRRV---GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAG-FG 352
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
982-1363 1.02e-101

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: 328.37  E-value: 1.02e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  982 RVARSAILEGAVSVMTSHGSSSR--IIDVEFEGEVGTGR-GPTFEFYTTVTHELQRGGLGMWRGDSGEHGfihapfGLFP 1058
Cdd:cd00078     4 TVRRDRILEDALRQLSKVSSSDLkkVLEVEFVGEEGIDAgGVTREFFTLVSKELFNPSYGLFRYTPDDSG------LLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1059 KPWSPsgtssqgvDFTNMLQKFKLLGNLVARAVLDGRILDIPLSKAFYKVMLEQELDIYDIPLFDPELGKIVIEFQALVS 1138
Cdd:cd00078    78 NPSSF--------ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1139 RKNFLetssrasnpmvDLTyknvklEDLCLDFTLPGNPEYELVPGGSEKPVTLESLGEYVSLVADATLKSGIAKQIEAFK 1218
Cdd:cd00078   150 DEDDL-----------ELT------FTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFR 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1219 SGINEVFALKALKMFTEEEMECILCGEQDaWALKNLEDHMEFEHGYDMSSQPIIIFLEILREFGREEQRAFIQFSTGAPQ 1298
Cdd:cd00078   213 DGFSEVIPEELLSLFTPEELELLICGSED-IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSR 291
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241944482 1299 LPLGGLASLEPKLTVVRKqcdGNVDDELPSVNTCRHFIKLPPYSSKEIMRTKLKYAITEGLGsFH 1363
Cdd:cd00078   292 LPVGGFADLNPKFTIRRV---GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAG-FG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1026-1365 1.47e-89

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 292.59  E-value: 1.47e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  1026 TTVTHELQRGGLGMWRGDSGEHGFIHapfglfpkpwsPSGTSSQGVDFTnMLQKFKLLGNLVARAVLDGRILDIPLSKAF 1105
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYW-----------FNPSSSESPDLE-LLDYFKFLGKLLGKAIYNGILLDLPFPPFF 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  1106 YKVMLEQELDIYDIPLFDPELGKiviEFQALvsrknfletssrasnpmvdLTYKNVKLEDLCLDFTLP--GNP-EYELVP 1182
Cdd:pfam00632   69 YKKLLGEPLTLEDLESIDPELYK---SLKSL-------------------LNMDNDDDEDLGLTFTIPvfGESkTIELIP 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  1183 GGSEKPVTLESLGEYVSLVADATLKSGIAKQIEAFKSGINEVFALKALKMFTEEEMECILCGEQDaWALKNLEDHMEFEH 1262
Cdd:pfam00632  127 NGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPE-IDVEDLKKNTEYDG 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  1263 GYDMSSQPIIIFLEILREFGREEQRAFIQFSTGAPQLPLGGLASLePKLTVVRKQCDGnvDDELPSVNTCRHFIKLPPYS 1342
Cdd:pfam00632  206 GYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGGDD--DDRLPTAHTCFNRLKLPDYS 282
                          330       340
                   ....*....|....*....|...
gi 241944482  1343 SKEIMRTKLKYAITEGlGSFHLS 1365
Cdd:pfam00632  283 SKEILKEKLLIAIEEG-EGFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1003-1360 1.52e-87

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: 287.98  E-value: 1.52e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482   1003 SRIIDVEFEGEVG-TGRGPTFEFYTTVTHELQRGGLGMWRGDSGEHGFIHAPFGLFPKPwspsgtssqgvdftNMLQKFK 1081
Cdd:smart00119    4 KRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANE--------------EHLSYFR 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482   1082 LLGNLVARAVLDGRILDIPLSKAFYKVMLEQELDIYDIPLFDPELGKiviefqalvsRKNFLETSSRASNPMvDLTyknv 1161
Cdd:smart00119   70 FIGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYK----------SLKWLLLNNDTSEEL-DLT---- 134
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482   1162 klEDLCLDFTLPGNPEYELVPGGSEKPVTLESLGEYVSLVADATLKSGIAKQIEAFKSGINEVFALKALKMFTEEEMECI 1241
Cdd:smart00119  135 --FSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELL 212
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482   1242 LCGEQDaWALKNLEDHMEFEHGYDMSSQPIIIFLEILREFGREEQRAFIQFSTGAPQLPLGGLASLEPKLTVVRKQCDgn 1321
Cdd:smart00119  213 ICGSPE-IDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSD-- 289
                           330       340       350
                    ....*....|....*....|....*....|....*....
gi 241944482   1322 vDDELPSVNTCRHFIKLPPYSSKEIMRTKLKYAITEGLG 1360
Cdd:smart00119  290 -DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKG 327
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
987-1364 1.21e-68

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 249.30  E-value: 1.21e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  987 AILEGAVSVMTSHGSSSRIIDVEFEGEVGTGRGPTFEFYTTVTHELQRGGLGMWR--------GDSGEHGFIHAPFGLFP 1058
Cdd:COG5021   509 KIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWlfllskemFNPDYGLFEYITEDLYT 588
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1059 kpWSPSGTSSQGVDFtnmLQKFKLLGNLVARAVLDGRILDIPLSKAFYKVMLEQELDIYDIPLFDPELGKiviefqALVS 1138
Cdd:COG5021   589 --LPINPLSSINPEH---LSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYR------SLVW 657
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1139 RKNFLETssrasNPMVDLTYKnvkLEDLCLDFTLPgnpeYELVPGGSEKPVTLESLGEYVSLVADATLKSGIAKQIEAFK 1218
Cdd:COG5021   658 LLNNDID-----ETILDLTFT---VEDDSFGESRT----VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFK 725
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1219 SGINEVFALKALKMFTEEEMECILCGEQDAWALKNLEDHMEfEHGYDMSSQPIIIFLEILREFGREEQRAFIQFSTGAPQ 1298
Cdd:COG5021   726 SGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTA-YHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSR 804
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241944482 1299 LPLGGLASLEPKLTVVRK--QCDGNVDDELPSVNTCRHFIKLPPYSSKEIMRTKLKYAITEGLGSFHL 1364
Cdd:COG5021   805 IPINGFKDLQGSDGVRKFtiEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
982-1363 1.02e-101

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: 328.37  E-value: 1.02e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  982 RVARSAILEGAVSVMTSHGSSSR--IIDVEFEGEVGTGR-GPTFEFYTTVTHELQRGGLGMWRGDSGEHGfihapfGLFP 1058
Cdd:cd00078     4 TVRRDRILEDALRQLSKVSSSDLkkVLEVEFVGEEGIDAgGVTREFFTLVSKELFNPSYGLFRYTPDDSG------LLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1059 KPWSPsgtssqgvDFTNMLQKFKLLGNLVARAVLDGRILDIPLSKAFYKVMLEQELDIYDIPLFDPELGKIVIEFQALVS 1138
Cdd:cd00078    78 NPSSF--------ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1139 RKNFLetssrasnpmvDLTyknvklEDLCLDFTLPGNPEYELVPGGSEKPVTLESLGEYVSLVADATLKSGIAKQIEAFK 1218
Cdd:cd00078   150 DEDDL-----------ELT------FTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFR 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1219 SGINEVFALKALKMFTEEEMECILCGEQDaWALKNLEDHMEFEHGYDMSSQPIIIFLEILREFGREEQRAFIQFSTGAPQ 1298
Cdd:cd00078   213 DGFSEVIPEELLSLFTPEELELLICGSED-IDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSR 291
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241944482 1299 LPLGGLASLEPKLTVVRKqcdGNVDDELPSVNTCRHFIKLPPYSSKEIMRTKLKYAITEGLGsFH 1363
Cdd:cd00078   292 LPVGGFADLNPKFTIRRV---GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAG-FG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1026-1365 1.47e-89

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 292.59  E-value: 1.47e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  1026 TTVTHELQRGGLGMWRGDSGEHGFIHapfglfpkpwsPSGTSSQGVDFTnMLQKFKLLGNLVARAVLDGRILDIPLSKAF 1105
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYW-----------FNPSSSESPDLE-LLDYFKFLGKLLGKAIYNGILLDLPFPPFF 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  1106 YKVMLEQELDIYDIPLFDPELGKiviEFQALvsrknfletssrasnpmvdLTYKNVKLEDLCLDFTLP--GNP-EYELVP 1182
Cdd:pfam00632   69 YKKLLGEPLTLEDLESIDPELYK---SLKSL-------------------LNMDNDDDEDLGLTFTIPvfGESkTIELIP 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  1183 GGSEKPVTLESLGEYVSLVADATLKSGIAKQIEAFKSGINEVFALKALKMFTEEEMECILCGEQDaWALKNLEDHMEFEH 1262
Cdd:pfam00632  127 NGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPE-IDVEDLKKNTEYDG 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  1263 GYDMSSQPIIIFLEILREFGREEQRAFIQFSTGAPQLPLGGLASLePKLTVVRKQCDGnvDDELPSVNTCRHFIKLPPYS 1342
Cdd:pfam00632  206 GYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGGDD--DDRLPTAHTCFNRLKLPDYS 282
                          330       340
                   ....*....|....*....|...
gi 241944482  1343 SKEIMRTKLKYAITEGlGSFHLS 1365
Cdd:pfam00632  283 SKEILKEKLLIAIEEG-EGFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1003-1360 1.52e-87

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: 287.98  E-value: 1.52e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482   1003 SRIIDVEFEGEVG-TGRGPTFEFYTTVTHELQRGGLGMWRGDSGEHGFIHAPFGLFPKPwspsgtssqgvdftNMLQKFK 1081
Cdd:smart00119    4 KRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANE--------------EHLSYFR 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482   1082 LLGNLVARAVLDGRILDIPLSKAFYKVMLEQELDIYDIPLFDPELGKiviefqalvsRKNFLETSSRASNPMvDLTyknv 1161
Cdd:smart00119   70 FIGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYK----------SLKWLLLNNDTSEEL-DLT---- 134
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482   1162 klEDLCLDFTLPGNPEYELVPGGSEKPVTLESLGEYVSLVADATLKSGIAKQIEAFKSGINEVFALKALKMFTEEEMECI 1241
Cdd:smart00119  135 --FSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELL 212
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482   1242 LCGEQDaWALKNLEDHMEFEHGYDMSSQPIIIFLEILREFGREEQRAFIQFSTGAPQLPLGGLASLEPKLTVVRKQCDgn 1321
Cdd:smart00119  213 ICGSPE-IDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSD-- 289
                           330       340       350
                    ....*....|....*....|....*....|....*....
gi 241944482   1322 vDDELPSVNTCRHFIKLPPYSSKEIMRTKLKYAITEGLG 1360
Cdd:smart00119  290 -DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKG 327
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
987-1364 1.21e-68

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 249.30  E-value: 1.21e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482  987 AILEGAVSVMTSHGSSSRIIDVEFEGEVGTGRGPTFEFYTTVTHELQRGGLGMWR--------GDSGEHGFIHAPFGLFP 1058
Cdd:COG5021   509 KIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWlfllskemFNPDYGLFEYITEDLYT 588
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1059 kpWSPSGTSSQGVDFtnmLQKFKLLGNLVARAVLDGRILDIPLSKAFYKVMLEQELDIYDIPLFDPELGKiviefqALVS 1138
Cdd:COG5021   589 --LPINPLSSINPEH---LSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYR------SLVW 657
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1139 RKNFLETssrasNPMVDLTYKnvkLEDLCLDFTLPgnpeYELVPGGSEKPVTLESLGEYVSLVADATLKSGIAKQIEAFK 1218
Cdd:COG5021   658 LLNNDID-----ETILDLTFT---VEDDSFGESRT----VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFK 725
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241944482 1219 SGINEVFALKALKMFTEEEMECILCGEQDAWALKNLEDHMEfEHGYDMSSQPIIIFLEILREFGREEQRAFIQFSTGAPQ 1298
Cdd:COG5021   726 SGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTA-YHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSR 804
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241944482 1299 LPLGGLASLEPKLTVVRK--QCDGNVDDELPSVNTCRHFIKLPPYSSKEIMRTKLKYAITEGLGSFHL 1364
Cdd:COG5021   805 IPINGFKDLQGSDGVRKFtiEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 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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