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Conserved domains on  [gi|67462065|sp|Q80U95|]
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RecName: Full=Ubiquitin-protein ligase E3C; AltName: Full=HECT-type ubiquitin transferase E3C; AltName: Full=RTA-associated ubiquitin ligase; Short=RAUL

Protein Classification

IQ calmodulin-binding motif-containing protein; HECT domain-containing protein( domain architecture ID 10635655)

IQ calmodulin-binding motif-containing protein may be involved in cooperative interactions with calmodulins or calmodulin-like proteins| HECT domain-containing protein may function as an E3 ubiquitin-protein ligase that 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 ...
723-1081 2.16e-147

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: 444.32  E-value: 2.16e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  723 INVTIRRNYIYEDAYDKLSPENEPDLKKRIRVHLLNahgldEAGIDGGGIFREFLNELLKSGFNPNQGFFKTTNE--GLL 800
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDdsGLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  801 YPNPAAQMLvgDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKLLGTSadVDIHHLASLDPEVYRNLLFLKSYEEDV 880
Cdd:cd00078   76 YPNPSSFAD--EDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--LSLEDLEELDPELYKSLKELLDNDGDE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  881 EELGLNFTVV-NNDLGEAQVVELKFGGKDIPVTGANRIAYIHLVADYRLNKQIRPHCLAFRQGLANVVSLEWLRMFDQQE 959
Cdd:cd00078  152 DDLELTFTIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  960 IQVLISGAQvPVSLEDLKSFTNYSGGYSADHPVIKIFWRVVEGFTDEEKRKLLKFVTSCSRPPLLGFKELYPAFCIHNGG 1039
Cdd:cd00078  232 LELLICGSE-DIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 67462065 1040 SDLERLPTASTCMNLLKLPEFYDEALLRSKLLYAIECAAGFE 1081
Cdd:cd00078  311 SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
47-64 5.68e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.38  E-value: 5.68e-03
                            10
                    ....*....|....*...
gi 67462065      47 KNAVIIQSFIRGYRDRKQ 64
Cdd:smart00015    4 RAAIIIQAAWRGYLARKR 21
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
723-1081 2.16e-147

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: 444.32  E-value: 2.16e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  723 INVTIRRNYIYEDAYDKLSPENEPDLKKRIRVHLLNahgldEAGIDGGGIFREFLNELLKSGFNPNQGFFKTTNE--GLL 800
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDdsGLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  801 YPNPAAQMLvgDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKLLGTSadVDIHHLASLDPEVYRNLLFLKSYEEDV 880
Cdd:cd00078   76 YPNPSSFAD--EDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--LSLEDLEELDPELYKSLKELLDNDGDE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  881 EELGLNFTVV-NNDLGEAQVVELKFGGKDIPVTGANRIAYIHLVADYRLNKQIRPHCLAFRQGLANVVSLEWLRMFDQQE 959
Cdd:cd00078  152 DDLELTFTIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  960 IQVLISGAQvPVSLEDLKSFTNYSGGYSADHPVIKIFWRVVEGFTDEEKRKLLKFVTSCSRPPLLGFKELYPAFCIHNGG 1039
Cdd:cd00078  232 LELLICGSE-DIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 67462065 1040 SDLERLPTASTCMNLLKLPEFYDEALLRSKLLYAIECAAGFE 1081
Cdd:cd00078  311 SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
747-1080 7.97e-142

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: 428.96  E-value: 7.97e-142
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065     747 DLKK-RIRVHLLNahgldEAGIDGGGIFREFLNELLKSGFNPNQGFFKTTNEG-LLYPNPAAQMLVGDSFArHYYFLGRM 824
Cdd:smart00119    1 DLKKrVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDyLLYPNPRSGFANEEHLS-YFRFIGRV 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065     825 LGKALYENMLVELPFAGFFLSKLLGTSadVDIHHLASLDPEVYRNLLFLKSYEEDVEELGLNFT-VVNNDLGEAQVVELK 903
Cdd:smart00119   75 LGKALYDNRLLDLFFARPFYKKLLGKP--VTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELK 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065     904 FGGKDIPVTGANRIAYIHLVADYRLNKQIRPHCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQvPVSLEDLKSFTNYS 983
Cdd:smart00119  153 PGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSP-EIDVDDLKSNTEYK 231
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065     984 GGYSADHPVIKIFWRVVEGFTDEEKRKLLKFVTSCSRPPLLGFKELYPAFCIHNGGSDLERLPTASTCMNLLKLPEFYDE 1063
Cdd:smart00119  232 GGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSK 311
                           330
                    ....*....|....*..
gi 67462065    1064 ALLRSKLLYAIECAAGF 1080
Cdd:smart00119  312 EILREKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
778-1083 5.66e-109

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 341.51  E-value: 5.66e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065    778 NELLKSGFNPNQGFFK--TTNEGLLYPNPAAQMLVGDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKLLGTsaDVD 855
Cdd:pfam00632    1 TLLSKELFDPNYGLFEyeTEDDRTYWFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGE--PLT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065    856 IHHLASLDPEVYRNLLFLKSYEED-VEELGLNFTVvnNDLGEAQVVELKFGGKDIPVTGANRIAYIHLVADYRLNKQIRP 934
Cdd:pfam00632   79 LEDLESIDPELYKSLKSLLNMDNDdDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065    935 HCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQVpVSLEDLKSFTNYSGGYSADHPVIKIFWRVVEGFTDEEKRKLLKF 1014
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICGSPE-IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKF 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065   1015 VTSCSRPPLLGFKELyPAFCIH-NGGSDLERLPTASTCMNLLKLPEFYDEALLRSKLLYAIECAAGFELS 1083
Cdd:pfam00632  236 VTGSSRLPVGGFKSL-PKFTIVrKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
694-1083 2.91e-99

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 334.04  E-value: 2.91e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  694 PFEERVKIFQRLIYADKQE------VQGDGPFLDGINVTIRRNYIYEDAYDKLSPENEPDLKKRIRVHLLNahgldEAGI 767
Cdd:COG5021  480 SFISLNKLDIRRIKEDKRRklfyslKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGI 554
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  768 DGGGIFREFLNELLKSGFNPNQGFFKTTNEGLLYPNPAAQMLVGDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKL 847
Cdd:COG5021  555 DAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKL 634
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  848 LGTSADVDihHLASLDPEVYRNLLFLKSYEEDVEELGLNFTVVNNDLGEAQVVELKFGGKDIPVTGANRIAYIHLVADYR 927
Cdd:COG5021  635 LGKPVSLV--DLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYK 712
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  928 LNKQIRPHCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQVPVSLEDLKSFTNYsGGYSADHPVIKIFWRVVEGFTDEE 1007
Cdd:COG5021  713 LNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEE 791
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065 1008 KRKLLKFVTSCSRPPLLGFKELYPA-----FCIHNGGSDLERLPTASTCMNLLKLPEFYDEALLRSKLLYAIECAAGFEL 1082
Cdd:COG5021  792 RAKLLQFVTGTSRIPINGFKDLQGSdgvrkFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGL 871

                 .
gi 67462065 1083 S 1083
Cdd:COG5021  872 L 872
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
47-64 5.68e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.38  E-value: 5.68e-03
                            10
                    ....*....|....*...
gi 67462065      47 KNAVIIQSFIRGYRDRKQ 64
Cdd:smart00015    4 RAAIIIQAAWRGYLARKR 21
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
723-1081 2.16e-147

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: 444.32  E-value: 2.16e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  723 INVTIRRNYIYEDAYDKLSPENEPDLKKRIRVHLLNahgldEAGIDGGGIFREFLNELLKSGFNPNQGFFKTTNE--GLL 800
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDdsGLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  801 YPNPAAQMLvgDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKLLGTSadVDIHHLASLDPEVYRNLLFLKSYEEDV 880
Cdd:cd00078   76 YPNPSSFAD--EDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--LSLEDLEELDPELYKSLKELLDNDGDE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  881 EELGLNFTVV-NNDLGEAQVVELKFGGKDIPVTGANRIAYIHLVADYRLNKQIRPHCLAFRQGLANVVSLEWLRMFDQQE 959
Cdd:cd00078  152 DDLELTFTIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  960 IQVLISGAQvPVSLEDLKSFTNYSGGYSADHPVIKIFWRVVEGFTDEEKRKLLKFVTSCSRPPLLGFKELYPAFCIHNGG 1039
Cdd:cd00078  232 LELLICGSE-DIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVG 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 67462065 1040 SDLERLPTASTCMNLLKLPEFYDEALLRSKLLYAIECAAGFE 1081
Cdd:cd00078  311 SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
747-1080 7.97e-142

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: 428.96  E-value: 7.97e-142
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065     747 DLKK-RIRVHLLNahgldEAGIDGGGIFREFLNELLKSGFNPNQGFFKTTNEG-LLYPNPAAQMLVGDSFArHYYFLGRM 824
Cdd:smart00119    1 DLKKrVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDyLLYPNPRSGFANEEHLS-YFRFIGRV 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065     825 LGKALYENMLVELPFAGFFLSKLLGTSadVDIHHLASLDPEVYRNLLFLKSYEEDVEELGLNFT-VVNNDLGEAQVVELK 903
Cdd:smart00119   75 LGKALYDNRLLDLFFARPFYKKLLGKP--VTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELK 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065     904 FGGKDIPVTGANRIAYIHLVADYRLNKQIRPHCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQvPVSLEDLKSFTNYS 983
Cdd:smart00119  153 PGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSP-EIDVDDLKSNTEYK 231
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065     984 GGYSADHPVIKIFWRVVEGFTDEEKRKLLKFVTSCSRPPLLGFKELYPAFCIHNGGSDLERLPTASTCMNLLKLPEFYDE 1063
Cdd:smart00119  232 GGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSK 311
                           330
                    ....*....|....*..
gi 67462065    1064 ALLRSKLLYAIECAAGF 1080
Cdd:smart00119  312 EILREKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
778-1083 5.66e-109

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 341.51  E-value: 5.66e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065    778 NELLKSGFNPNQGFFK--TTNEGLLYPNPAAQMLVGDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKLLGTsaDVD 855
Cdd:pfam00632    1 TLLSKELFDPNYGLFEyeTEDDRTYWFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGE--PLT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065    856 IHHLASLDPEVYRNLLFLKSYEED-VEELGLNFTVvnNDLGEAQVVELKFGGKDIPVTGANRIAYIHLVADYRLNKQIRP 934
Cdd:pfam00632   79 LEDLESIDPELYKSLKSLLNMDNDdDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065    935 HCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQVpVSLEDLKSFTNYSGGYSADHPVIKIFWRVVEGFTDEEKRKLLKF 1014
Cdd:pfam00632  157 QLEAFRKGFYSVIPKEALSLFTPEELELLICGSPE-IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKF 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065   1015 VTSCSRPPLLGFKELyPAFCIH-NGGSDLERLPTASTCMNLLKLPEFYDEALLRSKLLYAIECAAGFELS 1083
Cdd:pfam00632  236 VTGSSRLPVGGFKSL-PKFTIVrKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
694-1083 2.91e-99

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 334.04  E-value: 2.91e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  694 PFEERVKIFQRLIYADKQE------VQGDGPFLDGINVTIRRNYIYEDAYDKLSPENEPDLKKRIRVHLLNahgldEAGI 767
Cdd:COG5021  480 SFISLNKLDIRRIKEDKRRklfyslKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGI 554
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  768 DGGGIFREFLNELLKSGFNPNQGFFKTTNEGLLYPNPAAQMLVGDSFARHYYFLGRMLGKALYENMLVELPFAGFFLSKL 847
Cdd:COG5021  555 DAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKL 634
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  848 LGTSADVDihHLASLDPEVYRNLLFLKSYEEDVEELGLNFTVVNNDLGEAQVVELKFGGKDIPVTGANRIAYIHLVADYR 927
Cdd:COG5021  635 LGKPVSLV--DLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYK 712
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065  928 LNKQIRPHCLAFRQGLANVVSLEWLRMFDQQEIQVLISGAQVPVSLEDLKSFTNYsGGYSADHPVIKIFWRVVEGFTDEE 1007
Cdd:COG5021  713 LNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEE 791
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67462065 1008 KRKLLKFVTSCSRPPLLGFKELYPA-----FCIHNGGSDLERLPTASTCMNLLKLPEFYDEALLRSKLLYAIECAAGFEL 1082
Cdd:COG5021  792 RAKLLQFVTGTSRIPINGFKDLQGSdgvrkFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGL 871

                 .
gi 67462065 1083 S 1083
Cdd:COG5021  872 L 872
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
47-64 5.68e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.38  E-value: 5.68e-03
                            10
                    ....*....|....*...
gi 67462065      47 KNAVIIQSFIRGYRDRKQ 64
Cdd:smart00015    4 RAAIIIQAAWRGYLARKR 21
 
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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