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Conserved domains on  [gi|1720421796|ref|XP_030098232|]
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ubiquitin-protein ligase E3A isoform X3 [Mus musculus]

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 ...
497-847 7.85e-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: 477.44  E-value: 7.85e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 497 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-ATKLFWF 575
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 576 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSvEDDMMI 652
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 653 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 732
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 733 ICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTER 810
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1720421796 811 LPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 847
Cdd:cd00078   316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 1.15e-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: 1.15e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421796   6 AKHLIERYYHQLTEGCGNEACTNEFCASCPTF--LRMDNNAAAIKALELYK--INAKLC 60
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 ...
497-847 7.85e-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: 477.44  E-value: 7.85e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 497 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-ATKLFWF 575
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 576 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSvEDDMMI 652
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 653 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 732
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 733 ICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTER 810
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1720421796 811 LPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 847
Cdd:cd00078   316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
524-846 6.95e-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: 445.91  E-value: 6.95e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796  524 DLKKQ-LYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATKLFWFNPSSFETEG----QFTLIGIVLGLAIY 598
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796  599 NNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDL-LEYEGSVEDDmmITFQISQTDLFGNPMMYDLKENGDKI 677
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSIVLTSEFGQVKVVELKPGGSNI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796  678 PITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRE 757
Cdd:smart00119 159 PVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSAN 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796  758 SVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKER 835
Cdd:smart00119 238 SQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
                          330
                   ....*....|.
gi 1720421796  836 LLKAITYAKGF 846
Cdd:smart00119 318 LLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
550-848 1.54e-127

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 384.65  E-value: 1.54e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 550 QLVVEEIFNPDIGMFTY-DEATKLFWFNPSSFETEG-----QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFR 623
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPDlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 624 DLGDSHPVLYQSLKDLLEYEGSVEDDMMITFQISQtdlFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQ 703
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV---FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 704 FKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFT 783
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFV 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421796 784 TGTDRAPVGGLGKL-KMIIAK-NGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGM 848
Cdd:pfam00632 237 TGSSRLPVGGFKSLpKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
378-849 1.03e-107

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 351.38  E-value: 1.03e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 378 SSELTLQELLGDERRNKKGPRVDpletELGVKTLDCRKPLISFEEFINEPLNDvlEMDKDYTFFKVEtENKFSFMTCPFI 457
Cdd:COG5021   405 SDFLTSSSTYEDLRREQLGRESD----ESFYVASNVQQQRASREGPLLSGWKT--RLNNLYRFYFVE-HRKKTLTKNDSR 477
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 458 LNAvtKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQ 537
Cdd:COG5021   478 LGS--FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSY---REIMDESGDDLKKTLEIEFVGEE 552
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 538 GVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATKL-FWFNPSSFETEGQ---FTLIGIVLGLAIYNNCILDVHFPMVVYR 613
Cdd:COG5021   553 GIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLPINPLSSINPEHlsyFKFLGRVIGKAIYDSRILDVQFSKAFYK 632
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 614 KLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSVEDdMMITFQIsQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSD 693
Cdd:COG5021   633 KLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETI-LDLTFTV-EDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVD 710
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 694 YILNKSVEKQFKAFRRGFHMVTNESPLKYlFRPEEIELLICGSR-NLDFQALEETTEYDGgYTRESVVIREFWEIVHSFT 772
Cdd:COG5021   711 YKLNKRVEKQFSAFKSGFSEIIPPDLLQI-FDESELELLIGGIPeDIDIDDWKSNTAYHG-YTEDSPIIVWFWEIISEFD 788
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 773 DEQKRLFLQFTTGTDRAPVGG-------LGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKG 845
Cdd:COG5021   789 FEERAKLLQFVTGTSRIPINGfkdlqgsDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAG 868

                  ....
gi 1720421796 846 FGML 849
Cdd:COG5021   869 FGLL 872
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 1.15e-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: 1.15e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421796   6 AKHLIERYYHQLTEGCGNEACTNEFCASCPTF--LRMDNNAAAIKALELYK--INAKLC 60
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 ...
497-847 7.85e-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: 477.44  E-value: 7.85e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 497 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-ATKLFWF 575
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 576 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSvEDDMMI 652
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 653 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 732
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 733 ICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTER 810
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1720421796 811 LPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 847
Cdd:cd00078   316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
524-846 6.95e-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: 445.91  E-value: 6.95e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796  524 DLKKQ-LYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATKLFWFNPSSFETEG----QFTLIGIVLGLAIY 598
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796  599 NNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDL-LEYEGSVEDDmmITFQISQTDLFGNPMMYDLKENGDKI 677
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSIVLTSEFGQVKVVELKPGGSNI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796  678 PITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRE 757
Cdd:smart00119 159 PVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSAN 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796  758 SVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKER 835
Cdd:smart00119 238 SQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
                          330
                   ....*....|.
gi 1720421796  836 LLKAITYAKGF 846
Cdd:smart00119 318 LLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
550-848 1.54e-127

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 384.65  E-value: 1.54e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 550 QLVVEEIFNPDIGMFTY-DEATKLFWFNPSSFETEG-----QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFR 623
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPDlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 624 DLGDSHPVLYQSLKDLLEYEGSVEDDMMITFQISQtdlFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQ 703
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV---FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 704 FKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFT 783
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFV 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421796 784 TGTDRAPVGGLGKL-KMIIAK-NGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGM 848
Cdd:pfam00632 237 TGSSRLPVGGFKSLpKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
378-849 1.03e-107

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 351.38  E-value: 1.03e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 378 SSELTLQELLGDERRNKKGPRVDpletELGVKTLDCRKPLISFEEFINEPLNDvlEMDKDYTFFKVEtENKFSFMTCPFI 457
Cdd:COG5021   405 SDFLTSSSTYEDLRREQLGRESD----ESFYVASNVQQQRASREGPLLSGWKT--RLNNLYRFYFVE-HRKKTLTKNDSR 477
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 458 LNAvtKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQ 537
Cdd:COG5021   478 LGS--FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSY---REIMDESGDDLKKTLEIEFVGEE 552
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 538 GVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATKL-FWFNPSSFETEGQ---FTLIGIVLGLAIYNNCILDVHFPMVVYR 613
Cdd:COG5021   553 GIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLPINPLSSINPEHlsyFKFLGRVIGKAIYDSRILDVQFSKAFYK 632
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 614 KLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSVEDdMMITFQIsQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSD 693
Cdd:COG5021   633 KLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETI-LDLTFTV-EDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVD 710
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 694 YILNKSVEKQFKAFRRGFHMVTNESPLKYlFRPEEIELLICGSR-NLDFQALEETTEYDGgYTRESVVIREFWEIVHSFT 772
Cdd:COG5021   711 YKLNKRVEKQFSAFKSGFSEIIPPDLLQI-FDESELELLIGGIPeDIDIDDWKSNTAYHG-YTEDSPIIVWFWEIISEFD 788
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421796 773 DEQKRLFLQFTTGTDRAPVGG-------LGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKG 845
Cdd:COG5021   789 FEERAKLLQFVTGTSRIPINGfkdlqgsDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAG 868

                  ....
gi 1720421796 846 FGML 849
Cdd:COG5021   869 FGLL 872
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 1.15e-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: 1.15e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421796   6 AKHLIERYYHQLTEGCGNEACTNEFCASCPTF--LRMDNNAAAIKALELYK--INAKLC 60
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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