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Conserved domains on  [gi|1233951531|ref|NP_001341478|]
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ubiquitin-protein ligase E3A isoform 7 [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 ...
500-795 6.27e-131

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: 393.85  E-value: 6.27e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 500 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-STKLFWF 578
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 579 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHP---------------------- 633
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPelykslkelldndgdeddlelt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 634 --------------------------------EFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLI 681
Cdd:cd00078   158 ftieldssfggavtvelkpggrdipvtnenkeEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELLI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 682 CGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTERL 759
Cdd:cd00078   237 CGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDRL 316
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1233951531 760 PTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 795
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 1.08e-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: 1.08e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1233951531   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 ...
500-795 6.27e-131

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: 393.85  E-value: 6.27e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 500 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-STKLFWF 578
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 579 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHP---------------------- 633
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPelykslkelldndgdeddlelt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 634 --------------------------------EFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLI 681
Cdd:cd00078   158 ftieldssfggavtvelkpggrdipvtnenkeEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELLI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 682 CGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTERL 759
Cdd:cd00078   237 CGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDRL 316
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1233951531 760 PTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 795
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
527-794 1.05e-119

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: 363.86  E-value: 1.05e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531  527 DLKKQ-LYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEG----QFTLIGIVLGLAIY 601
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531  602 NNCILDVHFPMVVYRKLMGKKGTFRDLGDSHP------------------------------------------------ 633
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPelykslkwlllnndtseeldltfsivltsefgqvkvvelkpggsnipv 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531  634 ------EFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSV 707
Cdd:smart00119 161 teenkkEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531  708 LIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLL 785
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLL 319

                   ....*....
gi 1233951531  786 KAITYAKGF 794
Cdd:smart00119 320 LAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
553-796 1.26e-98

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 308.00  E-value: 1.26e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 553 QLVVEEIFNPDIGMFTY-DESTKLFWFNPSSFETEG-----QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFR 626
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPDlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 627 DLGDSHP----------------------------------------------------EFVNLYSDYILNKSVEKQFKA 654
Cdd:pfam00632  81 DLESIDPelykslksllnmdndddedlgltftipvfgesktielipngrnipvtnenkeEYIRLYVDYRLNKSIEPQLEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 655 FRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGT 734
Cdd:pfam00632 161 FRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1233951531 735 DRAPVGGLGKL-KMIIAK-NGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGM 796
Cdd:pfam00632 240 SRLPVGGFKSLpKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
436-797 2.43e-84

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 287.05  E-value: 2.43e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 436 EMDKDYTFFKVETENKfSFMTCPFILNAvtKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALv 515
Cdd:COG5021   454 RLNNLYRFYFVEHRKK-TLTKNDSRLGS--FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSY- 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 516 rlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKL-FWFNPSSFETEGQ---FTL 591
Cdd:COG5021   530 --REIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLPINPLSSINPEHlsyFKF 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 592 IGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHP-------------------------------------- 633
Cdd:COG5021   608 LGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPelyrslvwllnndidetildltftveddsfgesrtvel 687
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 634 ---------------EFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYlFRPEEIELLICGSR-NLDFQALEETTE 697
Cdd:COG5021   688 ipngrnisvtnenkkEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI-FDESELELLIGGIPeDIDIDDWKSNTA 766
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 698 YDGgYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGG-------LGKLKMIIAKNGPDTERLPTSHTCFNVLL 770
Cdd:COG5021   767 YHG-YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGfkdlqgsDGVRKFTIEKGGTDDDRLPSAHTCFNRLK 845
                         410       420
                  ....*....|....*....|....*..
gi 1233951531 771 LPEYSSKEKLKERLLKAITYAKGFGML 797
Cdd:COG5021   846 LPEYSSKEKLRSKLLTAINEGAGFGLL 872
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 1.08e-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: 1.08e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1233951531   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 ...
500-795 6.27e-131

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: 393.85  E-value: 6.27e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 500 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-STKLFWF 578
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 579 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHP---------------------- 633
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPelykslkelldndgdeddlelt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 634 --------------------------------EFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLI 681
Cdd:cd00078   158 ftieldssfggavtvelkpggrdipvtnenkeEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELLI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 682 CGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTERL 759
Cdd:cd00078   237 CGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDRL 316
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1233951531 760 PTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 795
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
527-794 1.05e-119

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: 363.86  E-value: 1.05e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531  527 DLKKQ-LYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFWFNPSSFETEG----QFTLIGIVLGLAIY 601
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531  602 NNCILDVHFPMVVYRKLMGKKGTFRDLGDSHP------------------------------------------------ 633
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPelykslkwlllnndtseeldltfsivltsefgqvkvvelkpggsnipv 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531  634 ------EFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSV 707
Cdd:smart00119 161 teenkkEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531  708 LIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLL 785
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLL 319

                   ....*....
gi 1233951531  786 KAITYAKGF 794
Cdd:smart00119 320 LAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
553-796 1.26e-98

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 308.00  E-value: 1.26e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 553 QLVVEEIFNPDIGMFTY-DESTKLFWFNPSSFETEG-----QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFR 626
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPDlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 627 DLGDSHP----------------------------------------------------EFVNLYSDYILNKSVEKQFKA 654
Cdd:pfam00632  81 DLESIDPelykslksllnmdndddedlgltftipvfgesktielipngrnipvtnenkeEYIRLYVDYRLNKSIEPQLEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 655 FRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGT 734
Cdd:pfam00632 161 FRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1233951531 735 DRAPVGGLGKL-KMIIAK-NGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGM 796
Cdd:pfam00632 240 SRLPVGGFKSLpKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
436-797 2.43e-84

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 287.05  E-value: 2.43e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 436 EMDKDYTFFKVETENKfSFMTCPFILNAvtKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALv 515
Cdd:COG5021   454 RLNNLYRFYFVEHRKK-TLTKNDSRLGS--FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSY- 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 516 rlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKL-FWFNPSSFETEGQ---FTL 591
Cdd:COG5021   530 --REIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLPINPLSSINPEHlsyFKF 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 592 IGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHP-------------------------------------- 633
Cdd:COG5021   608 LGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPelyrslvwllnndidetildltftveddsfgesrtvel 687
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 634 ---------------EFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYlFRPEEIELLICGSR-NLDFQALEETTE 697
Cdd:COG5021   688 ipngrnisvtnenkkEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI-FDESELELLIGGIPeDIDIDDWKSNTA 766
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951531 698 YDGgYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGG-------LGKLKMIIAKNGPDTERLPTSHTCFNVLL 770
Cdd:COG5021   767 YHG-YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGfkdlqgsDGVRKFTIEKGGTDDDRLPSAHTCFNRLK 845
                         410       420
                  ....*....|....*....|....*..
gi 1233951531 771 LPEYSSKEKLKERLLKAITYAKGFGML 797
Cdd:COG5021   846 LPEYSSKEKLRSKLLTAINEGAGFGLL 872
AZUL pfam16558
Amino-terminal Zinc-binding domain of ubiquitin ligase E3A; The AZUL or amino-terminal ...
6-60 1.08e-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: 1.08e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1233951531   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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