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Conserved domains on  [gi|1766947815|ref|XP_031165294|]
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ubiquitin-protein ligase E3A isoform X1 [Sander lucioperca]

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 ...
475-825 2.04e-153

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: 452.40  E-value: 2.04e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 475 LKLKVRRDHIIDDALVRLEMISmenPSDLKKQLFVEFEGEQGVDEGGVSKEFFQLVLEEIFNPDIGMFSYD-DDTKLFWF 553
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVS---SSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTpDDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 554 NSSSLENE---AQYTLVGLVLGLAIYNNCILDVHFPMVVYRKLMGKKGTYLDLSDSHPALYQSLKELLQYSGiVEEDMML 630
Cdd:cd00078    78 NPSSFADEdhlKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDG-DEDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 631 TYQISHTDLFGNPILYDLKEQGDQIPVTKENRQEFVDMYADYILNKSVERQFKAFKKGFLIVTNESPLKyLFRPEEVEML 710
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 711 ICGSRKLDFEALEKTTEYDGGYSKDSQIIKDFWETIHSFGEEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGSDTDR 788
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1766947815 789 LPTSHTCFNALLLPEYSSKEKLKERLLKAITYAKGFG 825
Cdd:cd00078   316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 3.78e-23

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: 93.13  E-value: 3.78e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1766947815   6 AKHLIERYFRQLTDGCGNGDCTNEFCASCRDF--QPLDNNSAAAKALELFK--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 ...
475-825 2.04e-153

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: 452.40  E-value: 2.04e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 475 LKLKVRRDHIIDDALVRLEMISmenPSDLKKQLFVEFEGEQGVDEGGVSKEFFQLVLEEIFNPDIGMFSYD-DDTKLFWF 553
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVS---SSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTpDDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 554 NSSSLENE---AQYTLVGLVLGLAIYNNCILDVHFPMVVYRKLMGKKGTYLDLSDSHPALYQSLKELLQYSGiVEEDMML 630
Cdd:cd00078    78 NPSSFADEdhlKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDG-DEDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 631 TYQISHTDLFGNPILYDLKEQGDQIPVTKENRQEFVDMYADYILNKSVERQFKAFKKGFLIVTNESPLKyLFRPEEVEML 710
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 711 ICGSRKLDFEALEKTTEYDGGYSKDSQIIKDFWETIHSFGEEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGSDTDR 788
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1766947815 789 LPTSHTCFNALLLPEYSSKEKLKERLLKAITYAKGFG 825
Cdd:cd00078   316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
502-824 9.46e-138

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: 411.24  E-value: 9.46e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815  502 DLKKQ-LFVEFEGEQGVDEGGVSKEFFQLVLEEIFNPDIGMFSYDDDTKLFWFN-SSSLENE---AQYTLVGLVLGLAIY 576
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNpRSGFANEehlSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815  577 NNCILDVHFPMVVYRKLMGKKGTYLDLSDSHPALYQSLKELLQYSGIvEEDMMLTYQISHTDLFGNPILYDLKEQGDQIP 656
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDT-SEELDLTFSIVLTSEFGQVKVVELKPGGSNIP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815  657 VTKENRQEFVDMYADYILNKSVERQFKAFKKGFLIVTNESPLKyLFRPEEVEMLICGSRKLDFEALEKTTEYDGGYSKDS 736
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815  737 QIIKDFWETIHSFGEEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGSDTDRLPTSHTCFNALLLPEYSSKEKLKERL 814
Cdd:smart00119 239 QTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKL 318
                          330
                   ....*....|
gi 1766947815  815 LKAITYAKGF 824
Cdd:smart00119 319 LLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
528-826 3.50e-121

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 367.71  E-value: 3.50e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 528 QLVLEEIFNPDIGMFSY-DDDTKLFWFNSSSLENE-----AQYTLVGLVLGLAIYNNCILDVHFPMVVYRKLMGKKGTYL 601
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPdlellDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 602 DLSDSHPALYQSLKELLQYSGIVEEDMMLTYQISHtdlFGNPILYDLKEQGDQIPVTKENRQEFVDMYADYILNKSVERQ 681
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV---FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 682 FKAFKKGFLIVTNESPLKyLFRPEEVEMLICGSRKLDFEALEKTTEYDGGYSKDSQIIKDFWETIHSFGEEQKRLFLQFT 761
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFV 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1766947815 762 TGTDRAPVGGLGKL-KMIIAK-NGSDTDRLPTSHTCFNALLLPEYSSKEKLKERLLKAITYAKGFGM 826
Cdd:pfam00632 237 TGSSRLPVGGFKSLpKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
398-827 5.69e-109

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 354.07  E-value: 5.69e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 398 FEEFVNESLNEVVEMDKDFTF-FKVNAETKFSFQscpFILNVITKNQGLYYDNR------------IRMYSERRLTALYS 464
Cdd:COG5021   427 DESFYVASNVQQQRASREGPLlSGWKTRLNNLYR---FYFVEHRKKTLTKNDSRlgsfislnkldiRRIKEDKRRKLFYS 503
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 465 MVQGQQP-NPYLKLKVRRDHIIDDALvrlEMISMENPSDLKKQLFVEFEGEQGVDEGGVSKEFFQLVLEEIFNPDIGMFS 543
Cdd:COG5021   504 LKQKAKIfDPYLHIKVRRDRVFEDSY---REIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFE 580
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 544 Y-DDDTKLFWFNSSSLENEAQ---YTLVGLVLGLAIYNNCILDVHFPMVVYRKLMGKKGTYLDLSDSHPALYQSLKELLQ 619
Cdd:COG5021   581 YiTEDLYTLPINPLSSINPEHlsyFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLN 660
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 620 YSgIVEEDMMLTYQISHtDLFGNPILYDLKEQGDQIPVTKENRQEFVDMYADYILNKSVERQFKAFKKGFLIVTNESPLK 699
Cdd:COG5021   661 ND-IDETILDLTFTVED-DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQ 738
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 700 YlFRPEEVEMLICGSR-KLDFEALEKTTEYDGgYSKDSQIIKDFWETIHSFGEEQKRLFLQFTTGTDRAPVGG------- 771
Cdd:COG5021   739 I-FDESELELLIGGIPeDIDIDDWKSNTAYHG-YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGfkdlqgs 816
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1766947815 772 LGKLKMIIAKNGSDTDRLPTSHTCFNALLLPEYSSKEKLKERLLKAITYAKGFGML 827
Cdd:COG5021   817 DGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 3.78e-23

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: 93.13  E-value: 3.78e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1766947815   6 AKHLIERYFRQLTDGCGNGDCTNEFCASCRDF--QPLDNNSAAAKALELFK--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 ...
475-825 2.04e-153

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: 452.40  E-value: 2.04e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 475 LKLKVRRDHIIDDALVRLEMISmenPSDLKKQLFVEFEGEQGVDEGGVSKEFFQLVLEEIFNPDIGMFSYD-DDTKLFWF 553
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVS---SSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTpDDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 554 NSSSLENE---AQYTLVGLVLGLAIYNNCILDVHFPMVVYRKLMGKKGTYLDLSDSHPALYQSLKELLQYSGiVEEDMML 630
Cdd:cd00078    78 NPSSFADEdhlKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDG-DEDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 631 TYQISHTDLFGNPILYDLKEQGDQIPVTKENRQEFVDMYADYILNKSVERQFKAFKKGFLIVTNESPLKyLFRPEEVEML 710
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 711 ICGSRKLDFEALEKTTEYDGGYSKDSQIIKDFWETIHSFGEEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGSDTDR 788
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1766947815 789 LPTSHTCFNALLLPEYSSKEKLKERLLKAITYAKGFG 825
Cdd:cd00078   316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
502-824 9.46e-138

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: 411.24  E-value: 9.46e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815  502 DLKKQ-LFVEFEGEQGVDEGGVSKEFFQLVLEEIFNPDIGMFSYDDDTKLFWFN-SSSLENE---AQYTLVGLVLGLAIY 576
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNpRSGFANEehlSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815  577 NNCILDVHFPMVVYRKLMGKKGTYLDLSDSHPALYQSLKELLQYSGIvEEDMMLTYQISHTDLFGNPILYDLKEQGDQIP 656
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDT-SEELDLTFSIVLTSEFGQVKVVELKPGGSNIP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815  657 VTKENRQEFVDMYADYILNKSVERQFKAFKKGFLIVTNESPLKyLFRPEEVEMLICGSRKLDFEALEKTTEYDGGYSKDS 736
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815  737 QIIKDFWETIHSFGEEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGSDTDRLPTSHTCFNALLLPEYSSKEKLKERL 814
Cdd:smart00119 239 QTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKL 318
                          330
                   ....*....|
gi 1766947815  815 LKAITYAKGF 824
Cdd:smart00119 319 LLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
528-826 3.50e-121

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 367.71  E-value: 3.50e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 528 QLVLEEIFNPDIGMFSY-DDDTKLFWFNSSSLENE-----AQYTLVGLVLGLAIYNNCILDVHFPMVVYRKLMGKKGTYL 601
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPdlellDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 602 DLSDSHPALYQSLKELLQYSGIVEEDMMLTYQISHtdlFGNPILYDLKEQGDQIPVTKENRQEFVDMYADYILNKSVERQ 681
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV---FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 682 FKAFKKGFLIVTNESPLKyLFRPEEVEMLICGSRKLDFEALEKTTEYDGGYSKDSQIIKDFWETIHSFGEEQKRLFLQFT 761
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFV 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1766947815 762 TGTDRAPVGGLGKL-KMIIAK-NGSDTDRLPTSHTCFNALLLPEYSSKEKLKERLLKAITYAKGFGM 826
Cdd:pfam00632 237 TGSSRLPVGGFKSLpKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
398-827 5.69e-109

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 354.07  E-value: 5.69e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 398 FEEFVNESLNEVVEMDKDFTF-FKVNAETKFSFQscpFILNVITKNQGLYYDNR------------IRMYSERRLTALYS 464
Cdd:COG5021   427 DESFYVASNVQQQRASREGPLlSGWKTRLNNLYR---FYFVEHRKKTLTKNDSRlgsfislnkldiRRIKEDKRRKLFYS 503
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 465 MVQGQQP-NPYLKLKVRRDHIIDDALvrlEMISMENPSDLKKQLFVEFEGEQGVDEGGVSKEFFQLVLEEIFNPDIGMFS 543
Cdd:COG5021   504 LKQKAKIfDPYLHIKVRRDRVFEDSY---REIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFE 580
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 544 Y-DDDTKLFWFNSSSLENEAQ---YTLVGLVLGLAIYNNCILDVHFPMVVYRKLMGKKGTYLDLSDSHPALYQSLKELLQ 619
Cdd:COG5021   581 YiTEDLYTLPINPLSSINPEHlsyFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLN 660
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 620 YSgIVEEDMMLTYQISHtDLFGNPILYDLKEQGDQIPVTKENRQEFVDMYADYILNKSVERQFKAFKKGFLIVTNESPLK 699
Cdd:COG5021   661 ND-IDETILDLTFTVED-DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQ 738
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766947815 700 YlFRPEEVEMLICGSR-KLDFEALEKTTEYDGgYSKDSQIIKDFWETIHSFGEEQKRLFLQFTTGTDRAPVGG------- 771
Cdd:COG5021   739 I-FDESELELLIGGIPeDIDIDDWKSNTAYHG-YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGfkdlqgs 816
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1766947815 772 LGKLKMIIAKNGSDTDRLPTSHTCFNALLLPEYSSKEKLKERLLKAITYAKGFGML 827
Cdd:COG5021   817 DGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 3.78e-23

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: 93.13  E-value: 3.78e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1766947815   6 AKHLIERYFRQLTDGCGNGDCTNEFCASCRDF--QPLDNNSAAAKALELFK--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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