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Conserved domains on  [gi|1720421798|ref|XP_030098233|]
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ubiquitin-protein ligase E3A isoform X4 [Mus musculus]

Protein Classification

HECT-type E3 ubiquitin-protein ligase( domain architecture ID 10050984)

HECT-type E3 ubiquitin-protein ligase catalyzes the attachment of ubiquitin chains to target proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
458-808 9.14e-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: 475.90  E-value: 9.14e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 458 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-ATKLFWF 536
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 537 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSvEDDMMI 613
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 614 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 693
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 694 ICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTER 771
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1720421798 772 LPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 808
Cdd:cd00078   316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
458-808 9.14e-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: 475.90  E-value: 9.14e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 458 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-ATKLFWF 536
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 537 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSvEDDMMI 613
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 614 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 693
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 694 ICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTER 771
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1720421798 772 LPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 808
Cdd:cd00078   316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
485-807 1.15e-150

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: 443.98  E-value: 1.15e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798  485 DLKKQ-LYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATKLFWFNPSSFETEG----QFTLIGIVLGLAIY 559
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798  560 NNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDL-LEYEGSVEDDmmITFQISQTDLFGNPMMYDLKENGDKI 638
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSIVLTSEFGQVKVVELKPGGSNI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798  639 PITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRE 718
Cdd:smart00119 159 PVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSAN 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798  719 SVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKER 796
Cdd:smart00119 238 SQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
                          330
                   ....*....|.
gi 1720421798  797 LLKAITYAKGF 807
Cdd:smart00119 318 LLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
511-809 2.26e-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: 383.11  E-value: 2.26e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 511 QLVVEEIFNPDIGMFTY-DEATKLFWFNPSSFETEG-----QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFR 584
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPDlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 585 DLGDSHPVLYQSLKDLLEYEGSVEDDMMITFQISQtdlFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQ 664
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV---FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 665 FKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFT 744
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFV 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421798 745 TGTDRAPVGGLGKL-KMIIAK-NGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGM 809
Cdd:pfam00632 237 TGSSRLPVGGFKSLpKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
339-810 3.40e-107

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 349.07  E-value: 3.40e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 339 SSELTLQELLGDERRNKKGPRVDpletELGVKTLDCRKPLISFEEFINEPLNDvlEMDKDYTFFKVETENKfSFMTCPFI 418
Cdd:COG5021   405 SDFLTSSSTYEDLRREQLGRESD----ESFYVASNVQQQRASREGPLLSGWKT--RLNNLYRFYFVEHRKK-TLTKNDSR 477
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 419 LNAvtKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQ 498
Cdd:COG5021   478 LGS--FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSY---REIMDESGDDLKKTLEIEFVGEE 552
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 499 GVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATKL-FWFNPSSFETEGQ---FTLIGIVLGLAIYNNCILDVHFPMVVYR 574
Cdd:COG5021   553 GIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLPINPLSSINPEHlsyFKFLGRVIGKAIYDSRILDVQFSKAFYK 632
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 575 KLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSVEDdMMITFQIsQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSD 654
Cdd:COG5021   633 KLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETI-LDLTFTV-EDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVD 710
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 655 YILNKSVEKQFKAFRRGFHMVTNESPLKYlFRPEEIELLICGSR-NLDFQALEETTEYDGgYTRESVVIREFWEIVHSFT 733
Cdd:COG5021   711 YKLNKRVEKQFSAFKSGFSEIIPPDLLQI-FDESELELLIGGIPeDIDIDDWKSNTAYHG-YTEDSPIIVWFWEIISEFD 788
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 734 DEQKRLFLQFTTGTDRAPVGG-------LGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKG 806
Cdd:COG5021   789 FEERAKLLQFVTGTSRIPINGfkdlqgsDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAG 868

                  ....
gi 1720421798 807 FGML 810
Cdd:COG5021   869 FGLL 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
458-808 9.14e-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: 475.90  E-value: 9.14e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 458 LRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDE-ATKLFWF 536
Cdd:cd00078     1 LKITVRRDRILEDAL---RQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPdDSGLLYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 537 NPSSFETEG---QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSvEDDMMI 613
Cdd:cd00078    78 NPSSFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD-EDDLEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 614 TFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELL 693
Cdd:cd00078   157 TFTIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS-LFTPEELELL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 694 ICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTER 771
Cdd:cd00078   236 ICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDR 315
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1720421798 772 LPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFG 808
Cdd:cd00078   316 LPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
485-807 1.15e-150

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: 443.98  E-value: 1.15e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798  485 DLKKQ-LYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATKLFWFNPSSFETEG----QFTLIGIVLGLAIY 559
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798  560 NNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDL-LEYEGSVEDDmmITFQISQTDLFGNPMMYDLKENGDKI 638
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSIVLTSEFGQVKVVELKPGGSNI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798  639 PITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRE 718
Cdd:smart00119 159 PVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLK-LFDPEELELLICGSPEIDVDDLKSNTEYKGGYSAN 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798  719 SVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKL--KMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKER 796
Cdd:smart00119 238 SQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
                          330
                   ....*....|.
gi 1720421798  797 LLKAITYAKGF 807
Cdd:smart00119 318 LLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
511-809 2.26e-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: 383.11  E-value: 2.26e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 511 QLVVEEIFNPDIGMFTY-DEATKLFWFNPSSFETEG-----QFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFR 584
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESPDlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 585 DLGDSHPVLYQSLKDLLEYEGSVEDDMMITFQISQtdlFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQ 664
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV---FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 665 FKAFRRGFHMVTNESPLKyLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFT 744
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALS-LFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFV 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421798 745 TGTDRAPVGGLGKL-KMIIAK-NGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGM 809
Cdd:pfam00632 237 TGSSRLPVGGFKSLpKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
339-810 3.40e-107

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 349.07  E-value: 3.40e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 339 SSELTLQELLGDERRNKKGPRVDpletELGVKTLDCRKPLISFEEFINEPLNDvlEMDKDYTFFKVETENKfSFMTCPFI 418
Cdd:COG5021   405 SDFLTSSSTYEDLRREQLGRESD----ESFYVASNVQQQRASREGPLLSGWKT--RLNNLYRFYFVEHRKK-TLTKNDSR 477
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 419 LNAvtKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALvrlEMIAMENPADLKKQLYVEFEGEQ 498
Cdd:COG5021   478 LGS--FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSY---REIMDESGDDLKKTLEIEFVGEE 552
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 499 GVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATKL-FWFNPSSFETEGQ---FTLIGIVLGLAIYNNCILDVHFPMVVYR 574
Cdd:COG5021   553 GIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLPINPLSSINPEHlsyFKFLGRVIGKAIYDSRILDVQFSKAFYK 632
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 575 KLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSVEDdMMITFQIsQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSD 654
Cdd:COG5021   633 KLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETI-LDLTFTV-EDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVD 710
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 655 YILNKSVEKQFKAFRRGFHMVTNESPLKYlFRPEEIELLICGSR-NLDFQALEETTEYDGgYTRESVVIREFWEIVHSFT 733
Cdd:COG5021   711 YKLNKRVEKQFSAFKSGFSEIIPPDLLQI-FDESELELLIGGIPeDIDIDDWKSNTAYHG-YTEDSPIIVWFWEIISEFD 788
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421798 734 DEQKRLFLQFTTGTDRAPVGG-------LGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKG 806
Cdd:COG5021   789 FEERAKLLQFVTGTSRIPINGfkdlqgsDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAG 868

                  ....
gi 1720421798 807 FGML 810
Cdd:COG5021   869 FGLL 872
 
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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