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Conserved domains on  [gi|1958757290|ref|XP_038954687|]
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probable E3 ubiquitin-protein ligase HERC4 isoform X8 [Rattus norvegicus]

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 ...
291-637 1.77e-156

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: 453.95  E-value: 1.77e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 291 LILVVRRENIVGDAMEVLRKTKNIDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDS-RLIWFSDK 369
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDsGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 370 TFEDSD---LFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQLLDYPEDdiEETFCLNF 446
Cdd:cd00078    81 SFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD--EDDLELTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 447 TITVEN-FGATEVKELVLNGADTAVNKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIG 525
Cdd:cd00078   159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 526 NTNYDWKELEKNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL--KLVIQSTGGGESYLPV 603
Cdd:cd00078   239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDRLPT 318
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1958757290 604 SHTCFNLLDLPKYTEKETLRCKLIQAIDHNEGFS 637
Cdd:cd00078   319 AHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
291-637 1.77e-156

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: 453.95  E-value: 1.77e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 291 LILVVRRENIVGDAMEVLRKTKNIDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDS-RLIWFSDK 369
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDsGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 370 TFEDSD---LFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQLLDYPEDdiEETFCLNF 446
Cdd:cd00078    81 SFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD--EDDLELTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 447 TITVEN-FGATEVKELVLNGADTAVNKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIG 525
Cdd:cd00078   159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 526 NTNYDWKELEKNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL--KLVIQSTGGGESYLPV 603
Cdd:cd00078   239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDRLPT 318
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1958757290 604 SHTCFNLLDLPKYTEKETLRCKLIQAIDHNEGFS 637
Cdd:cd00078   319 AHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
317-636 3.83e-123

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: 367.71  E-value: 3.83e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290  317 KKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDSRLIWFSDKTFEDSD----LFHLIGVICGLAIYNFT 392
Cdd:smart00119   4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALYDNR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290  393 IVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQL-LDYPEDDIEEtfcLNFTITVEN-FGATEVKELVLNGADTAV 470
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD---LTFSIVLTSeFGQVKVVELKPGGSNIPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290  471 NKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIGNTNYDWKELEKNTEYKGEYWAEHPT 550
Cdd:smart00119 161 TEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290  551 IKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL--KLVIQSTGGGESYLPVSHTCFNLLDLPKYTEKETLRCKLIQ 628
Cdd:smart00119 241 IKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLL 320

                   ....*...
gi 1958757290  629 AIDHNEGF 636
Cdd:smart00119 321 AINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
341-639 1.94e-114

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 344.59  E-value: 1.94e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 341 LLIMRELLDPKYGMFRY-YEDSRLIWFSDKTFED-----SDLFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKRKPSLD 414
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESpdlelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 415 DLKELMPDVGRSMQQLLDYpEDDIEETFCLNFTITVenFGATEVKELVLNGADTAVNKQNRQEFVDAYVDYIFNKSVASL 494
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNM-DNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 495 FDAFHAGFHKVCGGKVLLLFQPNELQAMVIGNTNYDWKELEKNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLT 574
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958757290 575 GSDRIPILGMKSL-KLVIQSTGG-GESYLPVSHTCFNLLDLPKYTEKETLRCKLIQAIDHNEGFSLI 639
Cdd:pfam00632 238 GSSRLPVGGFKSLpKFTIVRKGGdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
242-639 1.27e-99

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 323.64  E-value: 1.27e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 242 TYPFVFDAQAKTTLLQTD-----AVLQMQMAIDQ---AHRQNVSSLFLPVIESVNPCLILVVRRENIVGDAMEVLRKTKN 313
Cdd:COG5021   458 LYRFYFVEHRKKTLTKNDsrlgsFISLNKLDIRRikeDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESG 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 314 IDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDSRLIW----FSDKTFEDSDLFHLIGVICGLAIY 389
Cdd:COG5021   538 DDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLpinpLSSINPEHLSYFKFLGRVIGKAIY 617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 390 NFTIVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQLLDYPEDdiEETFCLNFTITVENFGATEVKELVLNGADTA 469
Cdd:COG5021   618 DSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDID--ETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 470 VNKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIG-NTNYDWKELEKNTEYKGeYWAEH 548
Cdd:COG5021   696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGiPEDIDIDDWKSNTAYHG-YTEDS 774
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 549 PTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL-------KLVIQSTGGGESYLPVSHTCFNLLDLPKYTEKET 621
Cdd:COG5021   775 PIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLqgsdgvrKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEK 854
                         410
                  ....*....|....*...
gi 1958757290 622 LRCKLIQAIDHNEGFSLI 639
Cdd:COG5021   855 LRSKLLTAINEGAGFGLL 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
291-637 1.77e-156

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: 453.95  E-value: 1.77e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 291 LILVVRRENIVGDAMEVLRKTKNIDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDS-RLIWFSDK 369
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDsGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 370 TFEDSD---LFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQLLDYPEDdiEETFCLNF 446
Cdd:cd00078    81 SFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD--EDDLELTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 447 TITVEN-FGATEVKELVLNGADTAVNKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIG 525
Cdd:cd00078   159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 526 NTNYDWKELEKNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL--KLVIQSTGGGESYLPV 603
Cdd:cd00078   239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDRLPT 318
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1958757290 604 SHTCFNLLDLPKYTEKETLRCKLIQAIDHNEGFS 637
Cdd:cd00078   319 AHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
317-636 3.83e-123

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: 367.71  E-value: 3.83e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290  317 KKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDSRLIWFSDKTFEDSD----LFHLIGVICGLAIYNFT 392
Cdd:smart00119   4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALYDNR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290  393 IVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQL-LDYPEDDIEEtfcLNFTITVEN-FGATEVKELVLNGADTAV 470
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD---LTFSIVLTSeFGQVKVVELKPGGSNIPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290  471 NKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIGNTNYDWKELEKNTEYKGEYWAEHPT 550
Cdd:smart00119 161 TEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290  551 IKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL--KLVIQSTGGGESYLPVSHTCFNLLDLPKYTEKETLRCKLIQ 628
Cdd:smart00119 241 IKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLL 320

                   ....*...
gi 1958757290  629 AIDHNEGF 636
Cdd:smart00119 321 AINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
341-639 1.94e-114

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 344.59  E-value: 1.94e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 341 LLIMRELLDPKYGMFRY-YEDSRLIWFSDKTFED-----SDLFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKRKPSLD 414
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESpdlelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 415 DLKELMPDVGRSMQQLLDYpEDDIEETFCLNFTITVenFGATEVKELVLNGADTAVNKQNRQEFVDAYVDYIFNKSVASL 494
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNM-DNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 495 FDAFHAGFHKVCGGKVLLLFQPNELQAMVIGNTNYDWKELEKNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLT 574
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958757290 575 GSDRIPILGMKSL-KLVIQSTGG-GESYLPVSHTCFNLLDLPKYTEKETLRCKLIQAIDHNEGFSLI 639
Cdd:pfam00632 238 GSSRLPVGGFKSLpKFTIVRKGGdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
242-639 1.27e-99

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 323.64  E-value: 1.27e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 242 TYPFVFDAQAKTTLLQTD-----AVLQMQMAIDQ---AHRQNVSSLFLPVIESVNPCLILVVRRENIVGDAMEVLRKTKN 313
Cdd:COG5021   458 LYRFYFVEHRKKTLTKNDsrlgsFISLNKLDIRRikeDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESG 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 314 IDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDSRLIW----FSDKTFEDSDLFHLIGVICGLAIY 389
Cdd:COG5021   538 DDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLpinpLSSINPEHLSYFKFLGRVIGKAIY 617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 390 NFTIVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQLLDYPEDdiEETFCLNFTITVENFGATEVKELVLNGADTA 469
Cdd:COG5021   618 DSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDID--ETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 470 VNKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIG-NTNYDWKELEKNTEYKGeYWAEH 548
Cdd:COG5021   696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGiPEDIDIDDWKSNTAYHG-YTEDS 774
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757290 549 PTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL-------KLVIQSTGGGESYLPVSHTCFNLLDLPKYTEKET 621
Cdd:COG5021   775 PIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLqgsdgvrKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEK 854
                         410
                  ....*....|....*...
gi 1958757290 622 LRCKLIQAIDHNEGFSLI 639
Cdd:COG5021   855 LRSKLLTAINEGAGFGLL 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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