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Conserved domains on  [gi|19718766|ref|NP_000453|]
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ubiquitin-protein ligase E3A isoform 2 [Homo sapiens]

Protein Classification

AZUL and HECTc domain-containing protein( domain architecture ID 11243968)

AZUL and HECTc domain-containing protein

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 ...
523-873 4.40e-163

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: 478.98  E-value: 4.40e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 523 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-STKLFWF 601
Cdd:cd00078   1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 602 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNvEDDMMI 678
Cdd:cd00078  78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 679 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 758
Cdd:cd00078 157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 759 ICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTER 836
Cdd:cd00078 236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 19718766 837 LPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 873
Cdd:cd00078 316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
29-83 1.19e-21

Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal zinc-binding domain of ubiquitin E3a ligase is found in eukaryotes, and is an unusual zinc-finger domain. The final cysteine is usually mutated in Angelman syndrome patients. It is likely that AZUL plays a role in Ube3A substrate-recognition.


:

Pssm-ID: 465173  Cd Length: 59  Bit Score: 88.89  E-value: 1.19e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 19718766    29 AKHLIERYYHQLTEGCGNEACTNEFCASCPTF--LRMDNNAAAIKALELYK--INAKLC 83
Cdd:pfam16558   1 FKLLVERYFYQLTYGCGSPNCTNPTCASCRDFpvRRLSPNSAAALALYLASqdPEAGLC 59
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
523-873 4.40e-163

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: 478.98  E-value: 4.40e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 523 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-STKLFWF 601
Cdd:cd00078   1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 602 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNvEDDMMI 678
Cdd:cd00078  78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 679 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 758
Cdd:cd00078 157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 759 ICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTER 836
Cdd:cd00078 236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 19718766 837 LPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 873
Cdd:cd00078 316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
550-872 3.83e-151

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: 447.07  E-value: 3.83e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766    550 DLKKQ-LYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEG----QFTLIGIVLGLAIY 624
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766    625 NNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDL-LEYEGNVEDDmmITFQISQTDLFGNPMMYDLKENGDKI 703
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSIVLTSEFGQVKVVELKPGGSNI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766    704 PITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRD 783
Cdd:smart00119 159 PVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSAN 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766    784 SVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKER 861
Cdd:smart00119 238 SQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
                          330
                   ....*....|.
gi 19718766    862 LLKAITYAKGF 872
Cdd:smart00119 318 LLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
576-874 9.62e-128

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 385.81  E-value: 9.62e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766   576 QLVVEEIFNPDIGMFTY-DESTKLFWFNPSSFETEG-----QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFR 649
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPDlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766   650 DLGDSHPVLYQSLKDLLEYEGNVEDDMMITFQISQtdlFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQ 729
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV---FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766   730 FKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFT 809
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFV 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19718766   810 TGTDRAPVGGLGKL-KMIIAK-NGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGM 874
Cdd:pfam00632 237 TGSSRLPVGGFKSLpKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
459-875 2.59e-107

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 350.99  E-value: 2.59e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 459 EMDKDYTFFKVETENKfSFMTCPFILNAvtKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALv 538
Cdd:COG5021 454 RLNNLYRFYFVEHRKK-TLTKNDSRLGS--FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSY- 529
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 539 rlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKL-FWFNPSSFETEGQ---FTL 614
Cdd:COG5021 530 --REIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLPINPLSSINPEHlsyFKF 607
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 615 IGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNVEDdMMITFQIsQTDLFGNPMMY 694
Cdd:COG5021 608 LGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETI-LDLTFTV-EDDSFGESRTV 685
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 695 DLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYlFRPEEIELLICGSR-NLDFQALEET 773
Cdd:COG5021 686 ELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI-FDESELELLIGGIPeDIDIDDWKSN 764
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 774 TEYDGgYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGG-------LGKLKMIIAKNGPDTERLPTSHTCFNV 846
Cdd:COG5021 765 TAYHG-YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGfkdlqgsDGVRKFTIEKGGTDDDRLPSAHTCFNR 843
                       410       420
                ....*....|....*....|....*....
gi 19718766 847 LLLPEYSSKEKLKERLLKAITYAKGFGML 875
Cdd:COG5021 844 LKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
29-83 1.19e-21

Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal zinc-binding domain of ubiquitin E3a ligase is found in eukaryotes, and is an unusual zinc-finger domain. The final cysteine is usually mutated in Angelman syndrome patients. It is likely that AZUL plays a role in Ube3A substrate-recognition.


Pssm-ID: 465173  Cd Length: 59  Bit Score: 88.89  E-value: 1.19e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 19718766    29 AKHLIERYYHQLTEGCGNEACTNEFCASCPTF--LRMDNNAAAIKALELYK--INAKLC 83
Cdd:pfam16558   1 FKLLVERYFYQLTYGCGSPNCTNPTCASCRDFpvRRLSPNSAAALALYLASqdPEAGLC 59
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
523-873 4.40e-163

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: 478.98  E-value: 4.40e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 523 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-STKLFWF 601
Cdd:cd00078   1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 602 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNvEDDMMI 678
Cdd:cd00078  78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 679 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 758
Cdd:cd00078 157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 759 ICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTER 836
Cdd:cd00078 236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 19718766 837 LPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 873
Cdd:cd00078 316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
550-872 3.83e-151

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: 447.07  E-value: 3.83e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766    550 DLKKQ-LYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEG----QFTLIGIVLGLAIY 624
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766    625 NNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDL-LEYEGNVEDDmmITFQISQTDLFGNPMMYDLKENGDKI 703
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSIVLTSEFGQVKVVELKPGGSNI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766    704 PITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRD 783
Cdd:smart00119 159 PVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSAN 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766    784 SVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKER 861
Cdd:smart00119 238 SQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
                          330
                   ....*....|.
gi 19718766    862 LLKAITYAKGF 872
Cdd:smart00119 318 LLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
576-874 9.62e-128

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 385.81  E-value: 9.62e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766   576 QLVVEEIFNPDIGMFTY-DESTKLFWFNPSSFETEG-----QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFR 649
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPDlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766   650 DLGDSHPVLYQSLKDLLEYEGNVEDDMMITFQISQtdlFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQ 729
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV---FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766   730 FKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFT 809
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFV 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19718766   810 TGTDRAPVGGLGKL-KMIIAK-NGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGM 874
Cdd:pfam00632 237 TGSSRLPVGGFKSLpKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
459-875 2.59e-107

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 350.99  E-value: 2.59e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 459 EMDKDYTFFKVETENKfSFMTCPFILNAvtKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALv 538
Cdd:COG5021 454 RLNNLYRFYFVEHRKK-TLTKNDSRLGS--FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSY- 529
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 539 rlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKL-FWFNPSSFETEGQ---FTL 614
Cdd:COG5021 530 --REIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLPINPLSSINPEHlsyFKF 607
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 615 IGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNVEDdMMITFQIsQTDLFGNPMMY 694
Cdd:COG5021 608 LGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETI-LDLTFTV-EDDSFGESRTV 685
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 695 DLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYlFRPEEIELLICGSR-NLDFQALEET 773
Cdd:COG5021 686 ELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI-FDESELELLIGGIPeDIDIDDWKSN 764
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718766 774 TEYDGgYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGG-------LGKLKMIIAKNGPDTERLPTSHTCFNV 846
Cdd:COG5021 765 TAYHG-YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGfkdlqgsDGVRKFTIEKGGTDDDRLPSAHTCFNR 843
                       410       420
                ....*....|....*....|....*....
gi 19718766 847 LLLPEYSSKEKLKERLLKAITYAKGFGML 875
Cdd:COG5021 844 LKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
29-83 1.19e-21

Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal zinc-binding domain of ubiquitin E3a ligase is found in eukaryotes, and is an unusual zinc-finger domain. The final cysteine is usually mutated in Angelman syndrome patients. It is likely that AZUL plays a role in Ube3A substrate-recognition.


Pssm-ID: 465173  Cd Length: 59  Bit Score: 88.89  E-value: 1.19e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 19718766    29 AKHLIERYYHQLTEGCGNEACTNEFCASCPTF--LRMDNNAAAIKALELYK--INAKLC 83
Cdd:pfam16558   1 FKLLVERYFYQLTYGCGSPNCTNPTCASCRDFpvRRLSPNSAAALALYLASqdPEAGLC 59
 
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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