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Conserved domains on  [gi|1958669920|ref|XP_038945807|]
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probable E3 ubiquitin-protein ligase HECTD4 isoform X10 [Rattus norvegicus]

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 ...
3508-3901 7.92e-89

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: 294.86  E-value: 7.92e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3508 EIRASENSYFCQAARQLASVPSSqlcvklasggDPTYAFNIRFTGEEVHGTSGSFRHFLWQVCKELQSSSLSLLLLCpss 3587
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSS----------DLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYT--- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3588 avNKNKGKYILTPSPITY-GEEQLLHFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPdQDLQEADILTYNYVKKFE 3666
Cdd:cd00078     69 --PDDSGLLYPNPSSFADeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSL-EDLEELDPELYKSLKELL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3667 SINDEselealcAEIASQHLATDSPEGpkpccrftylTMTGEEVELCSRGRHIPVAWENKDIYAAAIRSLRLrELQNMEC 3746
Cdd:cd00078    146 DNDGD-------EDDLELTFTIELDSS----------FGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRL-NKGIEEQ 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3747 VTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYVNLEFLKAHTMYQVGLMETDQHIELFWGALETFTQEELCKFIKFAC 3826
Cdd:cd00078    208 VEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVT 287
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958669920 3827 NQERIPFtcpckDGGPDTahvpPYPMKIAPPDgtagPPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAIHYRE 3901
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 ...
1888-2043 1.34e-87

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: 282.88  E-value: 1.34e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 1888 RGTFIYATSPLPVQAPSFYWEIEIVSYGDTDDDTGPIVSFGFATEAEKRDGAWTNPVGTCLFHNNGRAVHYNGSSLLQWK 1967
Cdd:cd13735      1 RGVFVYANSPIPAQAPSFYWEVEVVSLGETDDSDGPIISVGFAPPAEDRDGAWTNPVGTCLFHNNGRAVHYRGSSLTQWK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958669920 1968 SVRLDVTLCPGDVAGIGWERTEgtppppGQPAKGRVYFTYCGQRLTPYLEDVSGGMWPVVHIQKKNTKTRANFGSR 2043
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 ...
3508-3901 7.92e-89

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: 294.86  E-value: 7.92e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3508 EIRASENSYFCQAARQLASVPSSqlcvklasggDPTYAFNIRFTGEEVHGTSGSFRHFLWQVCKELQSSSLSLLLLCpss 3587
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSS----------DLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYT--- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3588 avNKNKGKYILTPSPITY-GEEQLLHFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPdQDLQEADILTYNYVKKFE 3666
Cdd:cd00078     69 --PDDSGLLYPNPSSFADeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSL-EDLEELDPELYKSLKELL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3667 SINDEselealcAEIASQHLATDSPEGpkpccrftylTMTGEEVELCSRGRHIPVAWENKDIYAAAIRSLRLrELQNMEC 3746
Cdd:cd00078    146 DNDGD-------EDDLELTFTIELDSS----------FGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRL-NKGIEEQ 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3747 VTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYVNLEFLKAHTMYQVGLMETDQHIELFWGALETFTQEELCKFIKFAC 3826
Cdd:cd00078    208 VEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVT 287
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958669920 3827 NQERIPFtcpckDGGPDTahvpPYPMKIAPPDgtagPPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAIHYRE 3901
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 ...
1888-2043 1.34e-87

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: 282.88  E-value: 1.34e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 1888 RGTFIYATSPLPVQAPSFYWEIEIVSYGDTDDDTGPIVSFGFATEAEKRDGAWTNPVGTCLFHNNGRAVHYNGSSLLQWK 1967
Cdd:cd13735      1 RGVFVYANSPIPAQAPSFYWEVEVVSLGETDDSDGPIISVGFAPPAEDRDGAWTNPVGTCLFHNNGRAVHYRGSSLTQWK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958669920 1968 SVRLDVTLCPGDVAGIGWERTEgtppppGQPAKGRVYFTYCGQRLTPYLEDVSGGMWPVVHIQKKNTKTRANFGSR 2043
Cdd:cd13735     81 SIRTDVTLSIGDVAGCGWERTD------TPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFGSR 150
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
3592-3901 4.54e-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: 172.79  E-value: 4.54e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3592 NKGKYILTPSPITYGEEQLLH---FLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPDqDLQEADILTYNYVKKFESI 3668
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELLDyfkFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKSLLNM 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3669 nDESELEALCaeiasqhLatdspegpkpccRFTYLTM-TGEEVELCSRGRHIPVAWENKDIYAAAIRSLRL-RELQNMec 3746
Cdd:pfam00632  100 -DNDDDEDLG-------L------------TFTIPVFgESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLnKSIEPQ-- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3747 VTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYVNLEFLKAHTMYQVGLMETDQHIELFWGALETFTQEELCKFIKFAC 3826
Cdd:pfam00632  158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958669920 3827 NQERIPFtcpckdGGPdtAHVPpyPMKIAPPDGTagpPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAIHYRE 3901
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 ...
3548-3897 3.38e-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: 3.38e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920  3548 IRFTGEEVHGTSGSFRHFLWQVCKElqssslsllllcpssAVNK-------NKGKYILTPSPITYG--EEQL--LHFLGQ 3616
Cdd:smart00119    9 IEFEGEEGLDGGGVTREFFFLLSKE---------------LFNPdyglfrySPNDYLLYPNPRSGFanEEHLsyFRFIGR 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920  3617 LLGIAIRADVPLPLDLLPSFWKTLVGEPLDPdQDLQEADILTYNYVKKFESINDESELEALCAEIAsqhLATDSPEGpkp 3696
Cdd:smart00119   74 VLGKALYDNRLLDLFFARPFYKKLLGKPVTL-HDLESLDPELYKSLKWLLLNNDTSEELDLTFSIV---LTSEFGQV--- 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920  3697 ccrftyltmtgEEVELCSRGRHIPVAWENKDIY---AAAIRSLRLRELQnmecVTAVRAGLGSIIPLQLLTTLSPLEMEL 3773
Cdd:smart00119  147 -----------KVVELKPGGSNIPVTEENKKEYvhlVIEYRLNKGIEKQ----LEAFREGFSEVIPENLLKLFDPEELEL 211
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920  3774 RTCGLPYVNLEFLKAHTMYQVGLMETDQHIELFWGALETFTQEELCKFIKFACNQERIPFtcpckdGGpdTAHVPPyPMK 3853
Cdd:smart00119  212 LICGSPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV------GG--FAALSP-KFT 282
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|....
gi 1958669920  3854 IAPpdgtAGPPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAI 3897
Cdd:smart00119  283 IRK----AGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAI 322
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
3594-3897 1.01e-22

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 107.55  E-value: 1.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3594 GKYILTPSPITYGEEQLL---HFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLdPDQDLQEADILTY-NYVKKFE-SI 3668
Cdd:COG5021    585 DLYTLPINPLSSINPEHLsyfKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPV-SLVDLESLDPELYrSLVWLLNnDI 663
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3669 NDESeleaLCAEIASQHlatDSPEGPKPccrftyltmtgeeVELCSRGRHIPVAWENKDIYAAAIRSLRLR---ELQnme 3745
Cdd:COG5021    664 DETI----LDLTFTVED---DSFGESRT-------------VELIPNGRNISVTNENKKEYVKKVVDYKLNkrvEKQ--- 720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3746 cVTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLP-YVNLEFLKAHTMYqVGLMETDQHIELFWGALETFTQEELCKFIKF 3824
Cdd:COG5021    721 -FSAFKSGFSEIIPPDLLQIFDESELELLIGGIPeDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQF 798
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958669920 3825 ACNQERIPFtcpckdGGPDTAHVPPYPMK-IAPPDGTagpPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAI 3897
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 ...
3508-3901 7.92e-89

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: 294.86  E-value: 7.92e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3508 EIRASENSYFCQAARQLASVPSSqlcvklasggDPTYAFNIRFTGEEVHGTSGSFRHFLWQVCKELQSSSLSLLLLCpss 3587
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSS----------DLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYT--- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3588 avNKNKGKYILTPSPITY-GEEQLLHFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPdQDLQEADILTYNYVKKFE 3666
Cdd:cd00078     69 --PDDSGLLYPNPSSFADeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSL-EDLEELDPELYKSLKELL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3667 SINDEselealcAEIASQHLATDSPEGpkpccrftylTMTGEEVELCSRGRHIPVAWENKDIYAAAIRSLRLrELQNMEC 3746
Cdd:cd00078    146 DNDGD-------EDDLELTFTIELDSS----------FGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRL-NKGIEEQ 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3747 VTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYVNLEFLKAHTMYQVGLMETDQHIELFWGALETFTQEELCKFIKFAC 3826
Cdd:cd00078    208 VEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVT 287
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958669920 3827 NQERIPFtcpckDGGPDTahvpPYPMKIAPPDgtagPPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAIHYRE 3901
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 ...
1888-2043 1.34e-87

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: 282.88  E-value: 1.34e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 1888 RGTFIYATSPLPVQAPSFYWEIEIVSYGDTDDDTGPIVSFGFATEAEKRDGAWTNPVGTCLFHNNGRAVHYNGSSLLQWK 1967
Cdd:cd13735      1 RGVFVYANSPIPAQAPSFYWEVEVVSLGETDDSDGPIISVGFAPPAEDRDGAWTNPVGTCLFHNNGRAVHYRGSSLTQWK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958669920 1968 SVRLDVTLCPGDVAGIGWERTEgtppppGQPAKGRVYFTYCGQRLTPYLEDVSGGMWPVVHIQKKNTKTRANFGSR 2043
Cdd:cd13735     81 SIRTDVTLSIGDVAGCGWERTD------TPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFGSR 150
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
3592-3901 4.54e-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: 172.79  E-value: 4.54e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3592 NKGKYILTPSPITYGEEQLLH---FLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPDqDLQEADILTYNYVKKFESI 3668
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELLDyfkFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKSLLNM 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3669 nDESELEALCaeiasqhLatdspegpkpccRFTYLTM-TGEEVELCSRGRHIPVAWENKDIYAAAIRSLRL-RELQNMec 3746
Cdd:pfam00632  100 -DNDDDEDLG-------L------------TFTIPVFgESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLnKSIEPQ-- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3747 VTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYVNLEFLKAHTMYQVGLMETDQHIELFWGALETFTQEELCKFIKFAC 3826
Cdd:pfam00632  158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958669920 3827 NQERIPFtcpckdGGPdtAHVPpyPMKIAPPDGTagpPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAIHYRE 3901
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 ...
3548-3897 3.38e-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: 3.38e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920  3548 IRFTGEEVHGTSGSFRHFLWQVCKElqssslsllllcpssAVNK-------NKGKYILTPSPITYG--EEQL--LHFLGQ 3616
Cdd:smart00119    9 IEFEGEEGLDGGGVTREFFFLLSKE---------------LFNPdyglfrySPNDYLLYPNPRSGFanEEHLsyFRFIGR 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920  3617 LLGIAIRADVPLPLDLLPSFWKTLVGEPLDPdQDLQEADILTYNYVKKFESINDESELEALCAEIAsqhLATDSPEGpkp 3696
Cdd:smart00119   74 VLGKALYDNRLLDLFFARPFYKKLLGKPVTL-HDLESLDPELYKSLKWLLLNNDTSEELDLTFSIV---LTSEFGQV--- 146
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920  3697 ccrftyltmtgEEVELCSRGRHIPVAWENKDIY---AAAIRSLRLRELQnmecVTAVRAGLGSIIPLQLLTTLSPLEMEL 3773
Cdd:smart00119  147 -----------KVVELKPGGSNIPVTEENKKEYvhlVIEYRLNKGIEKQ----LEAFREGFSEVIPENLLKLFDPEELEL 211
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920  3774 RTCGLPYVNLEFLKAHTMYQVGLMETDQHIELFWGALETFTQEELCKFIKFACNQERIPFtcpckdGGpdTAHVPPyPMK 3853
Cdd:smart00119  212 LICGSPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV------GG--FAALSP-KFT 282
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|....
gi 1958669920  3854 IAPpdgtAGPPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAI 3897
Cdd:smart00119  283 IRK----AGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAI 322
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
3594-3897 1.01e-22

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 107.55  E-value: 1.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3594 GKYILTPSPITYGEEQLL---HFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLdPDQDLQEADILTY-NYVKKFE-SI 3668
Cdd:COG5021    585 DLYTLPINPLSSINPEHLsyfKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPV-SLVDLESLDPELYrSLVWLLNnDI 663
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3669 NDESeleaLCAEIASQHlatDSPEGPKPccrftyltmtgeeVELCSRGRHIPVAWENKDIYAAAIRSLRLR---ELQnme 3745
Cdd:COG5021    664 DETI----LDLTFTVED---DSFGESRT-------------VELIPNGRNISVTNENKKEYVKKVVDYKLNkrvEKQ--- 720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 3746 cVTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLP-YVNLEFLKAHTMYqVGLMETDQHIELFWGALETFTQEELCKFIKF 3824
Cdd:COG5021    721 -FSAFKSGFSEIIPPDLLQIFDESELELLIGGIPeDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQF 798
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958669920 3825 ACNQERIPFtcpckdGGPDTAHVPPYPMK-IAPPDGTagpPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAI 3897
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 ...
1891-2041 2.11e-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: 2.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669920 1891 FIYATSPLPVQAPSFYWEIEIVsygdtDDDTGPIVSFGFATEAEKRDGAWTNPVGTCLFH-NNGRAVHYNGssllqwKSV 1969
Cdd:cd12885      2 SVRADHPIPPKVPVFYFEVTIL-----DLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHgDDGRVYLGGG------EGE 70
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958669920 1970 RLDVTLCPGDVAGIGWERTEGTppppgqpakgrVYFTYCGQRLTPYLEDV-SGGMWPVVHIQKKNTKTRANFG 2041
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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