NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217275664|ref|XP_047280614|]
View 

probable E3 ubiquitin-protein ligase HECTD2 isoform X2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
315-672 1.77e-121

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: 365.73  E-value: 1.77e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 315 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 392
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 393 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLS 469
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 470 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALM 548
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 549 LLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-- 625
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2217275664 626 ISKNETSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 672
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 ...
315-672 1.77e-121

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: 365.73  E-value: 1.77e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 315 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 392
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 393 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLS 469
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 470 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALM 548
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 549 LLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-- 625
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2217275664 626 ISKNETSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 672
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
364-673 6.78e-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: 333.81  E-value: 6.78e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 364 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPIips 437
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 438 dqnipvgicnvTVDDLCQIMPELAHGLSELLSHEGNVEEDFYSTFQVfqEEFGIIKSYNLKPGGDKISVTNQNRKEYVQL 517
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 518 YTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGF 596
Cdd:pfam00632 145 YVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217275664 597 PLDLQKKLLHFTTGSDRVPVGGMADL-NFKISKNE-TSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGL 673
Cdd:pfam00632 225 SPEQRRLFLKFVTGSSRLPVGGFKSLpKFTIVRKGgDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
338-671 2.75e-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: 325.73  E-value: 2.75e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664  338 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWFS--SFKCDN--YSEFRLVGILMGLAVY 412
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNprSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664  413 NSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLsHEGNVEEDFYSTFQ-VFQEEFGI 491
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKP--------------VTLHDLESLDPELYKSLKWLL-LNNDTSEELDLTFSiVLTSEFGQ 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664  492 IKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQ 571
Cdd:smart00119 146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664  572 RSTQY-DGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK--ISKNETSTNCLPVAHTCFNQLCL 648
Cdd:smart00119 226 SNTEYkGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKftIRKAGSDDERLPTAHTCFNRLKL 305
                          330       340
                   ....*....|....*....|...
gi 2217275664  649 PPYKSKKDLKQKLIIGISNSEGF 671
Cdd:smart00119 306 PPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
252-674 7.99e-105

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 338.66  E-value: 7.99e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 252 YHTWQNFGNSHRFSFCQYPFVIsvaakKIIIQRDSEQQMINIARQSLVDKVSRRQRPDMNilFLNMKVRRTHLVSDSLDE 331
Cdd:COG5021   459 YRFYFVEHRKKTLTKNDSRLGS-----FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDP--YLHIKVRRDRVFEDSYRE 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 332 LTRKRA-DLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGIL 406
Cdd:COG5021   532 IMDESGdDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGRV 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 407 MGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLSHEGNvEEDFYSTFQVFQ 486
Cdd:COG5021   612 IGKAIYDSRILDVQFSKAFYKKLLGKP--------------VSLVDLESLDPELYRSLVWLLNNDID-ETILDLTFTVED 676
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 487 EEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPD-L 565
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 566 DMHALQRSTQYDGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-------ISKNETSTNCLPV 638
Cdd:COG5021   757 DIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkftIEKGGTDDDRLPS 836
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2217275664 639 AHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGLE 674
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 ...
315-672 1.77e-121

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: 365.73  E-value: 1.77e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 315 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 392
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 393 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLS 469
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 470 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALM 548
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 549 LLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-- 625
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2217275664 626 ISKNETSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 672
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
364-673 6.78e-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: 333.81  E-value: 6.78e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 364 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPIips 437
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 438 dqnipvgicnvTVDDLCQIMPELAHGLSELLSHEGNVEEDFYSTFQVfqEEFGIIKSYNLKPGGDKISVTNQNRKEYVQL 517
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 518 YTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGF 596
Cdd:pfam00632 145 YVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217275664 597 PLDLQKKLLHFTTGSDRVPVGGMADL-NFKISKNE-TSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGL 673
Cdd:pfam00632 225 SPEQRRLFLKFVTGSSRLPVGGFKSLpKFTIVRKGgDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
338-671 2.75e-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: 325.73  E-value: 2.75e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664  338 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWFS--SFKCDN--YSEFRLVGILMGLAVY 412
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNprSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664  413 NSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLsHEGNVEEDFYSTFQ-VFQEEFGI 491
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKP--------------VTLHDLESLDPELYKSLKWLL-LNNDTSEELDLTFSiVLTSEFGQ 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664  492 IKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQ 571
Cdd:smart00119 146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664  572 RSTQY-DGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK--ISKNETSTNCLPVAHTCFNQLCL 648
Cdd:smart00119 226 SNTEYkGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKftIRKAGSDDERLPTAHTCFNRLKL 305
                          330       340
                   ....*....|....*....|...
gi 2217275664  649 PPYKSKKDLKQKLIIGISNSEGF 671
Cdd:smart00119 306 PPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
252-674 7.99e-105

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 338.66  E-value: 7.99e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 252 YHTWQNFGNSHRFSFCQYPFVIsvaakKIIIQRDSEQQMINIARQSLVDKVSRRQRPDMNilFLNMKVRRTHLVSDSLDE 331
Cdd:COG5021   459 YRFYFVEHRKKTLTKNDSRLGS-----FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDP--YLHIKVRRDRVFEDSYRE 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 332 LTRKRA-DLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGIL 406
Cdd:COG5021   532 IMDESGdDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGRV 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 407 MGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLSHEGNvEEDFYSTFQVFQ 486
Cdd:COG5021   612 IGKAIYDSRILDVQFSKAFYKKLLGKP--------------VSLVDLESLDPELYRSLVWLLNNDID-ETILDLTFTVED 676
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 487 EEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPD-L 565
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275664 566 DMHALQRSTQYDGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-------ISKNETSTNCLPV 638
Cdd:COG5021   757 DIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkftIEKGGTDDDRLPS 836
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2217275664 639 AHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGLE 674
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH