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Conserved domains on  [gi|1370456450|ref|XP_024303596|]
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probable E3 ubiquitin-protein ligase HECTD2 isoform X3 [Homo sapiens]

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 ...
310-667 7.15e-122

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: 366.50  E-value: 7.15e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 310 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 387
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 388 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLS 464
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 465 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALM 543
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 544 LLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-- 620
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1370456450 621 ISKNETSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 667
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
310-667 7.15e-122

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: 366.50  E-value: 7.15e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 310 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 387
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 388 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLS 464
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 465 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALM 543
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 544 LLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-- 620
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1370456450 621 ISKNETSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 667
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
359-668 3.01e-110

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 334.58  E-value: 3.01e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 359 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPIips 432
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 433 dqnipvgicnvTVDDLCQIMPELAHGLSELLSHEGNVEEDFYSTFQVfqEEFGIIKSYNLKPGGDKISVTNQNRKEYVQL 512
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 513 YTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGF 591
Cdd:pfam00632 145 YVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370456450 592 PLDLQKKLLHFTTGSDRVPVGGMADL-NFKISKNE-TSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGL 668
Cdd:pfam00632 225 SPEQRRLFLKFVTGSSRLPVGGFKSLpKFTIVRKGgDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
333-666 1.38e-106

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: 326.11  E-value: 1.38e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450  333 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWFS--SFKCDN--YSEFRLVGILMGLAVY 407
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNprSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450  408 NSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLsHEGNVEEDFYSTFQ-VFQEEFGI 486
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKP--------------VTLHDLESLDPELYKSLKWLL-LNNDTSEELDLTFSiVLTSEFGQ 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450  487 IKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQ 566
Cdd:smart00119 146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450  567 RSTQY-DGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK--ISKNETSTNCLPVAHTCFNQLCL 643
Cdd:smart00119 226 SNTEYkGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKftIRKAGSDDERLPTAHTCFNRLKL 305
                          330       340
                   ....*....|....*....|...
gi 1370456450  644 PPYKSKKDLKQKLIIGISNSEGF 666
Cdd:smart00119 306 PPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
247-669 4.26e-105

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 339.05  E-value: 4.26e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 247 YHTWQNFGNSHRFSFCQYPFVIsvaakKIIIQRDSEQQMINIARQSLVDKVSRRQRPDMNilFLNMKVRRTHLVSDSLDE 326
Cdd:COG5021   459 YRFYFVEHRKKTLTKNDSRLGS-----FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDP--YLHIKVRRDRVFEDSYRE 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 327 LTRKRAD-LKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGIL 401
Cdd:COG5021   532 IMDESGDdLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGRV 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 402 MGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLSHEGNvEEDFYSTFQVFQ 481
Cdd:COG5021   612 IGKAIYDSRILDVQFSKAFYKKLLGKP--------------VSLVDLESLDPELYRSLVWLLNNDID-ETILDLTFTVED 676
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 482 EEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPD-L 560
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 561 DMHALQRSTQYDGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-------ISKNETSTNCLPV 633
Cdd:COG5021   757 DIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkftIEKGGTDDDRLPS 836
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1370456450 634 AHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGLE 669
Cdd:COG5021   837 AHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
310-667 7.15e-122

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: 366.50  E-value: 7.15e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 310 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 387
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 388 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLS 464
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 465 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALM 543
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 544 LLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-- 620
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1370456450 621 ISKNETSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 667
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
359-668 3.01e-110

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 334.58  E-value: 3.01e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 359 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPIips 432
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 433 dqnipvgicnvTVDDLCQIMPELAHGLSELLSHEGNVEEDFYSTFQVfqEEFGIIKSYNLKPGGDKISVTNQNRKEYVQL 512
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 513 YTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGF 591
Cdd:pfam00632 145 YVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370456450 592 PLDLQKKLLHFTTGSDRVPVGGMADL-NFKISKNE-TSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGL 668
Cdd:pfam00632 225 SPEQRRLFLKFVTGSSRLPVGGFKSLpKFTIVRKGgDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
333-666 1.38e-106

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: 326.11  E-value: 1.38e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450  333 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWFS--SFKCDN--YSEFRLVGILMGLAVY 407
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNprSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450  408 NSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLsHEGNVEEDFYSTFQ-VFQEEFGI 486
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKP--------------VTLHDLESLDPELYKSLKWLL-LNNDTSEELDLTFSiVLTSEFGQ 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450  487 IKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQ 566
Cdd:smart00119 146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450  567 RSTQY-DGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK--ISKNETSTNCLPVAHTCFNQLCL 643
Cdd:smart00119 226 SNTEYkGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKftIRKAGSDDERLPTAHTCFNRLKL 305
                          330       340
                   ....*....|....*....|...
gi 1370456450  644 PPYKSKKDLKQKLIIGISNSEGF 666
Cdd:smart00119 306 PPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
247-669 4.26e-105

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 339.05  E-value: 4.26e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 247 YHTWQNFGNSHRFSFCQYPFVIsvaakKIIIQRDSEQQMINIARQSLVDKVSRRQRPDMNilFLNMKVRRTHLVSDSLDE 326
Cdd:COG5021   459 YRFYFVEHRKKTLTKNDSRLGS-----FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDP--YLHIKVRRDRVFEDSYRE 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 327 LTRKRAD-LKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGIL 401
Cdd:COG5021   532 IMDESGDdLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGRV 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 402 MGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLSHEGNvEEDFYSTFQVFQ 481
Cdd:COG5021   612 IGKAIYDSRILDVQFSKAFYKKLLGKP--------------VSLVDLESLDPELYRSLVWLLNNDID-ETILDLTFTVED 676
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 482 EEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPD-L 560
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456450 561 DMHALQRSTQYDGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-------ISKNETSTNCLPV 633
Cdd:COG5021   757 DIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkftIEKGGTDDDRLPS 836
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1370456450 634 AHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGLE 669
Cdd:COG5021   837 AHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 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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