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Conserved domains on  [gi|568937250|ref|XP_006530415|]
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probable E3 ubiquitin-protein ligase HECTD4 isoform X2 [Mus musculus]

Protein Classification

E3 ubiquitin-protein ligase HECT family protein( domain architecture ID 11599378)

E3 ubiquitin-protein ligase HECT family protein containing C-terminal catalytic domain that 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; also contains N-terminal SPRY domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc super family cl27008
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
4126-4519 8.83e-90

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.


The actual alignment was detected with superfamily member cd00078:

Pssm-ID: 474882 [Multi-domain]  Cd Length: 352  Bit Score: 297.94  E-value: 8.83e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4126 EIRASENSYFCQAARQLASVPSSqlcvklasggDPTYAFNIRFTGEEVHGTSGSFRHFLWQVCKELQSSSLSLLLLCpss 4205
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSS----------DLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYT--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4206 avNKNKGKYILTPSPITY-GEEQLLHFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPdQDLQEADILTYNYVKKFE 4284
Cdd:cd00078    69 --PDDSGLLYPNPSSFADeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSL-EDLEELDPELYKSLKELL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4285 SINDEselealcAEIASQHLATESPEGpkpccrftylTMTGEEVELCSRGRHIPVAWENKDIYAAAIRSLRLrELQNMEC 4364
Cdd:cd00078   146 DNDGD-------EDDLELTFTIELDSS----------FGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRL-NKGIEEQ 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4365 VTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYINLEFLKAHTMYQVGLMETDQHIELFWGALEMFTQEELCKFIKFAC 4444
Cdd:cd00078   208 VEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVT 287
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937250 4445 NQERIPFtcpckDGGPDTahvpPYPMKIAPPDgtagPPDSRYIRVETCMFMIKLPQYSSLETMLEKLRCAIHYRE 4519
Cdd:cd00078   288 GSSRLPV-----GGFADL----NPKFTIRRVG----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
SPRY_HECT_like cd13735
SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at ...
2506-2661 2.03e-88

SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at the N-terminus of the HECT (homologous to the E6AP carboxyl terminus) protein, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). HECT E3 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. It has a prominent role in protein trafficking and immune response, and is involved in crucial signaling pathways implicated in tumorigenesis.


:

Pssm-ID: 293970 [Multi-domain]  Cd Length: 150  Bit Score: 285.19  E-value: 2.03e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 2506 RGTFIYATSPLPVQAPSFYWEIEIVSYGDTDDDTGPIVSFGFATEAEKRDGAWTNPVGTCLFHNNGRAVHYNGSSLLQWK 2585
Cdd:cd13735     1 RGVFVYANSPIPAQAPSFYWEVEVVSLGETDDSDGPIISVGFAPPAEDRDGAWTNPVGTCLFHNNGRAVHYRGSSLTQWK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937250 2586 SVRLDVTLSPGDVAGIGWERTEgtppppGQPAKGRVYFTYCGQRLTPYLEDVSGGMWPVVHIQKKNTKTRANFGSR 2661
Cdd:cd13735    81 SIRTDVTLSIGDVAGCGWERTD------TPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFGSR 150
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
4126-4519 8.83e-90

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: 297.94  E-value: 8.83e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4126 EIRASENSYFCQAARQLASVPSSqlcvklasggDPTYAFNIRFTGEEVHGTSGSFRHFLWQVCKELQSSSLSLLLLCpss 4205
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSS----------DLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYT--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4206 avNKNKGKYILTPSPITY-GEEQLLHFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPdQDLQEADILTYNYVKKFE 4284
Cdd:cd00078    69 --PDDSGLLYPNPSSFADeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSL-EDLEELDPELYKSLKELL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4285 SINDEselealcAEIASQHLATESPEGpkpccrftylTMTGEEVELCSRGRHIPVAWENKDIYAAAIRSLRLrELQNMEC 4364
Cdd:cd00078   146 DNDGD-------EDDLELTFTIELDSS----------FGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRL-NKGIEEQ 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4365 VTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYINLEFLKAHTMYQVGLMETDQHIELFWGALEMFTQEELCKFIKFAC 4444
Cdd:cd00078   208 VEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVT 287
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937250 4445 NQERIPFtcpckDGGPDTahvpPYPMKIAPPDgtagPPDSRYIRVETCMFMIKLPQYSSLETMLEKLRCAIHYRE 4519
Cdd:cd00078   288 GSSRLPV-----GGFADL----NPKFTIRRVG----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
SPRY_HECT_like cd13735
SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at ...
2506-2661 2.03e-88

SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at the N-terminus of the HECT (homologous to the E6AP carboxyl terminus) protein, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). HECT E3 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. It has a prominent role in protein trafficking and immune response, and is involved in crucial signaling pathways implicated in tumorigenesis.


Pssm-ID: 293970 [Multi-domain]  Cd Length: 150  Bit Score: 285.19  E-value: 2.03e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 2506 RGTFIYATSPLPVQAPSFYWEIEIVSYGDTDDDTGPIVSFGFATEAEKRDGAWTNPVGTCLFHNNGRAVHYNGSSLLQWK 2585
Cdd:cd13735     1 RGVFVYANSPIPAQAPSFYWEVEVVSLGETDDSDGPIISVGFAPPAEDRDGAWTNPVGTCLFHNNGRAVHYRGSSLTQWK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937250 2586 SVRLDVTLSPGDVAGIGWERTEgtppppGQPAKGRVYFTYCGQRLTPYLEDVSGGMWPVVHIQKKNTKTRANFGSR 2661
Cdd:cd13735    81 SIRTDVTLSIGDVAGCGWERTD------TPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFGSR 150
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
4210-4519 2.63e-47

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 173.57  E-value: 2.63e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250  4210 NKGKYILTPSPITYGEEQLLH---FLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPDqDLQEADILTYNYVKKFESI 4286
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELLDyfkFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKSLLNM 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250  4287 nDESELEALCaeiasqhLatespegpkpccRFTYLTM-TGEEVELCSRGRHIPVAWENKDIYAAAIRSLRL-RELQNMec 4364
Cdd:pfam00632  100 -DNDDDEDLG-------L------------TFTIPVFgESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLnKSIEPQ-- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250  4365 VTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYINLEFLKAHTMYQVGLMETDQHIELFWGALEMFTQEELCKFIKFAC 4444
Cdd:pfam00632  158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937250  4445 NQERIPFtcpckdGGPdtAHVPpyPMKIAPPDGTagpPDSRYIRVETCMFMIKLPQYSSLETMLEKLRCAIHYRE 4519
Cdd:pfam00632  238 GSSRLPV------GGF--KSLP--KFTIVRKGGD---DDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGE 299
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
4166-4515 3.53e-39

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: 150.85  E-value: 3.53e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250   4166 IRFTGEEVHGTSGSFRHFLWQVCKElqssslsllllcpssAVNK-------NKGKYILTPSPITYG--EEQL--LHFLGQ 4234
Cdd:smart00119    9 IEFEGEEGLDGGGVTREFFFLLSKE---------------LFNPdyglfrySPNDYLLYPNPRSGFanEEHLsyFRFIGR 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250   4235 LLGIAIRADVPLPLDLLPSFWKTLVGEPLDPdQDLQEADILTYNYVKKFESINDESELEALCAEIAsqhLATESPEGpkp 4314
Cdd:smart00119   74 VLGKALYDNRLLDLFFARPFYKKLLGKPVTL-HDLESLDPELYKSLKWLLLNNDTSEELDLTFSIV---LTSEFGQV--- 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250   4315 ccrftyltmtgEEVELCSRGRHIPVAWENKDIY---AAAIRSLRLRELQnmecVTAVRAGLGSIIPLQLLTTLSPLEMEL 4391
Cdd:smart00119  147 -----------KVVELKPGGSNIPVTEENKKEYvhlVIEYRLNKGIEKQ----LEAFREGFSEVIPENLLKLFDPEELEL 211
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250   4392 RTCGLPYINLEFLKAHTMYQVGLMETDQHIELFWGALEMFTQEELCKFIKFACNQERIPFtcpckdGGpdTAHVPPyPMK 4471
Cdd:smart00119  212 LICGSPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV------GG--FAALSP-KFT 282
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|....
gi 568937250   4472 IAPpdgtAGPPDSRYIRVETCMFMIKLPQYSSLETMLEKLRCAI 4515
Cdd:smart00119  283 IRK----AGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAI 322
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4212-4515 7.92e-23

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 107.93  E-value: 7.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4212 GKYILTPSPITYGEEQLL---HFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLdPDQDLQEADILTY-NYVKKFE-SI 4286
Cdd:COG5021   585 DLYTLPINPLSSINPEHLsyfKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPV-SLVDLESLDPELYrSLVWLLNnDI 663
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4287 NDESeleaLCAEIASQHlatESPEGPKPccrftyltmtgeeVELCSRGRHIPVAWENKDIYAAAIRSLRLR---ELQnme 4363
Cdd:COG5021   664 DETI----LDLTFTVED---DSFGESRT-------------VELIPNGRNISVTNENKKEYVKKVVDYKLNkrvEKQ--- 720
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4364 cVTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLP-YINLEFLKAHTMYqVGLMETDQHIELFWGALEMFTQEELCKFIKF 4442
Cdd:COG5021   721 -FSAFKSGFSEIIPPDLLQIFDESELELLIGGIPeDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQF 798
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937250 4443 ACNQERIPFtcpckdGGPDTAHVPPYPMK-IAPPDGTagpPDSRYIRVETCMFMIKLPQYSSLETMLEKLRCAI 4515
Cdd:COG5021   799 VTGTSRIPI------NGFKDLQGSDGVRKfTIEKGGT---DDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
4126-4519 8.83e-90

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: 297.94  E-value: 8.83e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4126 EIRASENSYFCQAARQLASVPSSqlcvklasggDPTYAFNIRFTGEEVHGTSGSFRHFLWQVCKELQSSSLSLLLLCpss 4205
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSS----------DLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYT--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4206 avNKNKGKYILTPSPITY-GEEQLLHFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPdQDLQEADILTYNYVKKFE 4284
Cdd:cd00078    69 --PDDSGLLYPNPSSFADeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSL-EDLEELDPELYKSLKELL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4285 SINDEselealcAEIASQHLATESPEGpkpccrftylTMTGEEVELCSRGRHIPVAWENKDIYAAAIRSLRLrELQNMEC 4364
Cdd:cd00078   146 DNDGD-------EDDLELTFTIELDSS----------FGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRL-NKGIEEQ 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4365 VTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYINLEFLKAHTMYQVGLMETDQHIELFWGALEMFTQEELCKFIKFAC 4444
Cdd:cd00078   208 VEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVT 287
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937250 4445 NQERIPFtcpckDGGPDTahvpPYPMKIAPPDgtagPPDSRYIRVETCMFMIKLPQYSSLETMLEKLRCAIHYRE 4519
Cdd:cd00078   288 GSSRLPV-----GGFADL----NPKFTIRRVG----SPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGA 349
SPRY_HECT_like cd13735
SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at ...
2506-2661 2.03e-88

SPRY domain in HECT E3; This domain consists of the SPRY subdomain similar to those found at the N-terminus of the HECT (homologous to the E6AP carboxyl terminus) protein, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). HECT E3 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. It has a prominent role in protein trafficking and immune response, and is involved in crucial signaling pathways implicated in tumorigenesis.


Pssm-ID: 293970 [Multi-domain]  Cd Length: 150  Bit Score: 285.19  E-value: 2.03e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 2506 RGTFIYATSPLPVQAPSFYWEIEIVSYGDTDDDTGPIVSFGFATEAEKRDGAWTNPVGTCLFHNNGRAVHYNGSSLLQWK 2585
Cdd:cd13735     1 RGVFVYANSPIPAQAPSFYWEVEVVSLGETDDSDGPIISVGFAPPAEDRDGAWTNPVGTCLFHNNGRAVHYRGSSLTQWK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937250 2586 SVRLDVTLSPGDVAGIGWERTEgtppppGQPAKGRVYFTYCGQRLTPYLEDVSGGMWPVVHIQKKNTKTRANFGSR 2661
Cdd:cd13735    81 SIRTDVTLSIGDVAGCGWERTD------TPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFGSR 150
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
4210-4519 2.63e-47

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 173.57  E-value: 2.63e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250  4210 NKGKYILTPSPITYGEEQLLH---FLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPDqDLQEADILTYNYVKKFESI 4286
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELLDyfkFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKSLLNM 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250  4287 nDESELEALCaeiasqhLatespegpkpccRFTYLTM-TGEEVELCSRGRHIPVAWENKDIYAAAIRSLRL-RELQNMec 4364
Cdd:pfam00632  100 -DNDDDEDLG-------L------------TFTIPVFgESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLnKSIEPQ-- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250  4365 VTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYINLEFLKAHTMYQVGLMETDQHIELFWGALEMFTQEELCKFIKFAC 4444
Cdd:pfam00632  158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937250  4445 NQERIPFtcpckdGGPdtAHVPpyPMKIAPPDGTagpPDSRYIRVETCMFMIKLPQYSSLETMLEKLRCAIHYRE 4519
Cdd:pfam00632  238 GSSRLPV------GGF--KSLP--KFTIVRKGGD---DDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGE 299
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
4166-4515 3.53e-39

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: 150.85  E-value: 3.53e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250   4166 IRFTGEEVHGTSGSFRHFLWQVCKElqssslsllllcpssAVNK-------NKGKYILTPSPITYG--EEQL--LHFLGQ 4234
Cdd:smart00119    9 IEFEGEEGLDGGGVTREFFFLLSKE---------------LFNPdyglfrySPNDYLLYPNPRSGFanEEHLsyFRFIGR 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250   4235 LLGIAIRADVPLPLDLLPSFWKTLVGEPLDPdQDLQEADILTYNYVKKFESINDESELEALCAEIAsqhLATESPEGpkp 4314
Cdd:smart00119   74 VLGKALYDNRLLDLFFARPFYKKLLGKPVTL-HDLESLDPELYKSLKWLLLNNDTSEELDLTFSIV---LTSEFGQV--- 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250   4315 ccrftyltmtgEEVELCSRGRHIPVAWENKDIY---AAAIRSLRLRELQnmecVTAVRAGLGSIIPLQLLTTLSPLEMEL 4391
Cdd:smart00119  147 -----------KVVELKPGGSNIPVTEENKKEYvhlVIEYRLNKGIEKQ----LEAFREGFSEVIPENLLKLFDPEELEL 211
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250   4392 RTCGLPYINLEFLKAHTMYQVGLMETDQHIELFWGALEMFTQEELCKFIKFACNQERIPFtcpckdGGpdTAHVPPyPMK 4471
Cdd:smart00119  212 LICGSPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV------GG--FAALSP-KFT 282
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|....
gi 568937250   4472 IAPpdgtAGPPDSRYIRVETCMFMIKLPQYSSLETMLEKLRCAI 4515
Cdd:smart00119  283 IRK----AGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAI 322
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4212-4515 7.92e-23

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 107.93  E-value: 7.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4212 GKYILTPSPITYGEEQLL---HFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLdPDQDLQEADILTY-NYVKKFE-SI 4286
Cdd:COG5021   585 DLYTLPINPLSSINPEHLsyfKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPV-SLVDLESLDPELYrSLVWLLNnDI 663
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4287 NDESeleaLCAEIASQHlatESPEGPKPccrftyltmtgeeVELCSRGRHIPVAWENKDIYAAAIRSLRLR---ELQnme 4363
Cdd:COG5021   664 DETI----LDLTFTVED---DSFGESRT-------------VELIPNGRNISVTNENKKEYVKKVVDYKLNkrvEKQ--- 720
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 4364 cVTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLP-YINLEFLKAHTMYqVGLMETDQHIELFWGALEMFTQEELCKFIKF 4442
Cdd:COG5021   721 -FSAFKSGFSEIIPPDLLQIFDESELELLIGGIPeDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQF 798
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568937250 4443 ACNQERIPFtcpckdGGPDTAHVPPYPMK-IAPPDGTagpPDSRYIRVETCMFMIKLPQYSSLETMLEKLRCAI 4515
Cdd:COG5021   799 VTGTSRIPI------NGFKDLQGSDGVRKfTIEKGGT---DDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
2509-2659 2.65e-22

SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY domains found in Ran binding proteins (RBP or RanBPM) 9 and 10, SSH4 (suppressor of SHR3 null mutation protein 4), SPRY domain-containing protein 3 (SPRYD3) as well as HECT, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). RanBP9 and RanBP10 act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. SPRYD3 is highly expressed in most tissues in humans, possibly involved in important cellular processes. HECT E3 mediates the direct transfer of ubiquitin from E2 to substrate.


Pssm-ID: 293943  Cd Length: 132  Bit Score: 95.42  E-value: 2.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937250 2509 FIYATSPLPVQAPSFYWEIEIVsygdtDDDTGPIVSFGFATEAEKRDGAWTNPVGTCLFH-NNGRAVHYNGssllqwKSV 2587
Cdd:cd12885     2 SVRADHPIPPKVPVFYFEVTIL-----DLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHgDDGRVYLGGG------EGE 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937250 2588 RLDVTLSPGDVAGIGWERTEGTppppgqpakgrVYFTYCGQRLTPYLEDV-SGGMWPVVHIQKKNTKTRANFG 2659
Cdd:cd12885    71 NYGPPFGTGDVVGCGINFKTGE-----------VFFTKNGELLGTAFENVvKGRLYPTVGLGSPGVKVRVNFG 132
 
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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