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Conserved domains on  [gi|1622846758|ref|XP_028685760|]
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probable E3 ubiquitin-protein ligase HECTD4 isoform X8 [Macaca mulatta]

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 ...
3335-3729 4.57e-91

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: 301.41  E-value: 4.57e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3335 EIRASENSYFCQAARQLASVPSSqlcvklasggDPTYAFNIRFTGEEVHGTSGSFRHFLWQVCKELQSSSLSLLLLCpss 3414
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSS----------DLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYT--- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3415 avNKNKGKYILTPSPITY-GEEQLLHFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPEqDLQEADILTYNYVKKFE 3493
Cdd:cd00078     69 --PDDSGLLYPNPSSFADeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLE-DLEELDPELYKSLKELL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3494 SINDETElealcaeIASQHLATESPDSpnkpccrftylTMTGEEVELCSRGRHILVAWENKDIYAAAIRSLRLrELQNVE 3573
Cdd:cd00078    146 DNDGDED-------DLELTFTIELDSS-----------FGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRL-NKGIEE 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3574 CVTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYINLEFLKAHTMYQVGLMETDQHIEFFWGALEMFTQEELCKFIKFA 3653
Cdd:cd00078    207 QVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFV 286
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622846758 3654 CNQERIPFtcpckDGGPDTahvpPYPMKIAPPDgtagSPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAIHYRE 3729
Cdd:cd00078    287 TGSSRLPV-----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 ...
1715-1870 1.58e-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: 285.57  E-value: 1.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 1715 RGTFIYATSPLPVQAPSFYWEIEIVSYGDTDDDTGPIVSFGFTTEAEKRDGAWTNPVGTCLFHNNGRAVHYNGSSLLQWK 1794
Cdd:cd13735      1 RGVFVYANSPIPAQAPSFYWEVEVVSLGETDDSDGPIISVGFAPPAEDRDGAWTNPVGTCLFHNNGRAVHYRGSSLTQWK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622846758 1795 SVRLDVTLSPGDVAGIGWERTEgtppppGQPAKGRVYFTYCGQRLSPYLEDVSGGMWPVVHIQKKNTKTRANFGSR 1870
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 ...
3335-3729 4.57e-91

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: 301.41  E-value: 4.57e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3335 EIRASENSYFCQAARQLASVPSSqlcvklasggDPTYAFNIRFTGEEVHGTSGSFRHFLWQVCKELQSSSLSLLLLCpss 3414
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSS----------DLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYT--- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3415 avNKNKGKYILTPSPITY-GEEQLLHFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPEqDLQEADILTYNYVKKFE 3493
Cdd:cd00078     69 --PDDSGLLYPNPSSFADeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLE-DLEELDPELYKSLKELL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3494 SINDETElealcaeIASQHLATESPDSpnkpccrftylTMTGEEVELCSRGRHILVAWENKDIYAAAIRSLRLrELQNVE 3573
Cdd:cd00078    146 DNDGDED-------DLELTFTIELDSS-----------FGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRL-NKGIEE 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3574 CVTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYINLEFLKAHTMYQVGLMETDQHIEFFWGALEMFTQEELCKFIKFA 3653
Cdd:cd00078    207 QVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFV 286
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622846758 3654 CNQERIPFtcpckDGGPDTahvpPYPMKIAPPDgtagSPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAIHYRE 3729
Cdd:cd00078    287 TGSSRLPV-----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 ...
1715-1870 1.58e-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: 285.57  E-value: 1.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 1715 RGTFIYATSPLPVQAPSFYWEIEIVSYGDTDDDTGPIVSFGFTTEAEKRDGAWTNPVGTCLFHNNGRAVHYNGSSLLQWK 1794
Cdd:cd13735      1 RGVFVYANSPIPAQAPSFYWEVEVVSLGETDDSDGPIISVGFAPPAEDRDGAWTNPVGTCLFHNNGRAVHYRGSSLTQWK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622846758 1795 SVRLDVTLSPGDVAGIGWERTEgtppppGQPAKGRVYFTYCGQRLSPYLEDVSGGMWPVVHIQKKNTKTRANFGSR 1870
Cdd:cd13735     81 SIRTDVTLSIGDVAGCGWERTD------TPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFGSR 150
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
3419-3729 3.60e-46

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 170.10  E-value: 3.60e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3419 NKGKYILTPSPITYGEEQLLH---FLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPEqDLQEADILTYNYVKKFESI 3495
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELLDyfkFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKSLLNM 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3496 NDETELEAlcaeiasqhlatespdspnkpCCRFTYLTM-TGEEVELCSRGRHILVAWENKDIYAAAIRSLRLR---ELQn 3571
Cdd:pfam00632  100 DNDDDEDL---------------------GLTFTIPVFgESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNksiEPQ- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3572 vecVTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYINLEFLKAHTMYQVGLMETDQHIEFFWGALEMFTQEELCKFIK 3651
Cdd:pfam00632  158 ---LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLK 234
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622846758 3652 FACNQERIPFtcpckdGGPdtAHVPpyPMKIAPPDGTagsPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAIHYRE 3729
Cdd:pfam00632  235 FVTGSSRLPV------GGF--KSLP--KFTIVRKGGD---DDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGE 299
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
3375-3725 2.04e-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: 151.23  E-value: 2.04e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758  3375 IRFTGEEVHGTSGSFRHFLWQVCKElqssslsllllcpssAVNK-------NKGKYILTPSPITYG--EEQL--LHFLGQ 3443
Cdd:smart00119    9 IEFEGEEGLDGGGVTREFFFLLSKE---------------LFNPdyglfrySPNDYLLYPNPRSGFanEEHLsyFRFIGR 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758  3444 LLGIAIRADVPLPLDLLPSFWKTLVGEPLDPEqDLQEADILTYNYVKKFESINDETELEALCAEIasqhlaTESPDSPNk 3523
Cdd:smart00119   74 VLGKALYDNRLLDLFFARPFYKKLLGKPVTLH-DLESLDPELYKSLKWLLLNNDTSEELDLTFSI------VLTSEFGQ- 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758  3524 pccrftyltmtGEEVELCSRGRHILVAWENKDIY---AAAIRSLRLRELQnvecVTAVRAGLGSIIPLQLLTTLSPLEME 3600
Cdd:smart00119  146 -----------VKVVELKPGGSNIPVTEENKKEYvhlVIEYRLNKGIEKQ----LEAFREGFSEVIPENLLKLFDPEELE 210
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758  3601 LRTCGLPYINLEFLKAHTMYQVGLMETDQHIEFFWGALEMFTQEELCKFIKFACNQERIPFtcpckdGGpdTAHVPPyPM 3680
Cdd:smart00119  211 LLICGSPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV------GG--FAALSP-KF 281
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|....*
gi 1622846758  3681 KIAPpdgtAGSPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAI 3725
Cdd:smart00119  282 TIRK----AGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAI 322
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
3421-3725 7.04e-22

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 104.46  E-value: 7.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3421 GKYILTPSPITYGEEQLL---HFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLdPEQDLQEADILTY-NYVKKFEsiN 3496
Cdd:COG5021    585 DLYTLPINPLSSINPEHLsyfKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPV-SLVDLESLDPELYrSLVWLLN--N 661
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3497 DETElEALCAEIASQHLATESPDSpnkpccrftyltmtgeeVELCSRGRHILVAWENKDIYAAAIRSLRLR---ELQnve 3573
Cdd:COG5021    662 DIDE-TILDLTFTVEDDSFGESRT-----------------VELIPNGRNISVTNENKKEYVKKVVDYKLNkrvEKQ--- 720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3574 cVTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLP-YINLEFLKAHTMYqVGLMETDQHIEFFWGALEMFTQEELCKFIKF 3652
Cdd:COG5021    721 -FSAFKSGFSEIIPPDLLQIFDESELELLIGGIPeDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQF 798
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622846758 3653 ACNQERIPFtcpckdGGPDTAHVPPYPMK-IAPPDGTagsPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAI 3725
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 ...
3335-3729 4.57e-91

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: 301.41  E-value: 4.57e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3335 EIRASENSYFCQAARQLASVPSSqlcvklasggDPTYAFNIRFTGEEVHGTSGSFRHFLWQVCKELQSSSLSLLLLCpss 3414
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSS----------DLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYT--- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3415 avNKNKGKYILTPSPITY-GEEQLLHFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPEqDLQEADILTYNYVKKFE 3493
Cdd:cd00078     69 --PDDSGLLYPNPSSFADeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLE-DLEELDPELYKSLKELL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3494 SINDETElealcaeIASQHLATESPDSpnkpccrftylTMTGEEVELCSRGRHILVAWENKDIYAAAIRSLRLrELQNVE 3573
Cdd:cd00078    146 DNDGDED-------DLELTFTIELDSS-----------FGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRL-NKGIEE 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3574 CVTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYINLEFLKAHTMYQVGLMETDQHIEFFWGALEMFTQEELCKFIKFA 3653
Cdd:cd00078    207 QVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFV 286
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622846758 3654 CNQERIPFtcpckDGGPDTahvpPYPMKIAPPDgtagSPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAIHYRE 3729
Cdd:cd00078    287 TGSSRLPV-----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 ...
1715-1870 1.58e-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: 285.57  E-value: 1.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 1715 RGTFIYATSPLPVQAPSFYWEIEIVSYGDTDDDTGPIVSFGFTTEAEKRDGAWTNPVGTCLFHNNGRAVHYNGSSLLQWK 1794
Cdd:cd13735      1 RGVFVYANSPIPAQAPSFYWEVEVVSLGETDDSDGPIISVGFAPPAEDRDGAWTNPVGTCLFHNNGRAVHYRGSSLTQWK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622846758 1795 SVRLDVTLSPGDVAGIGWERTEgtppppGQPAKGRVYFTYCGQRLSPYLEDVSGGMWPVVHIQKKNTKTRANFGSR 1870
Cdd:cd13735     81 SIRTDVTLSIGDVAGCGWERTD------TPPAKGRVYFTHNGQRLPRSLQDVSGGLWPVVHVQKKNTRVRANFGSR 150
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
3419-3729 3.60e-46

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 170.10  E-value: 3.60e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3419 NKGKYILTPSPITYGEEQLLH---FLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLDPEqDLQEADILTYNYVKKFESI 3495
Cdd:pfam00632   21 DDRTYWFNPSSSESPDLELLDyfkFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKSLLNM 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3496 NDETELEAlcaeiasqhlatespdspnkpCCRFTYLTM-TGEEVELCSRGRHILVAWENKDIYAAAIRSLRLR---ELQn 3571
Cdd:pfam00632  100 DNDDDEDL---------------------GLTFTIPVFgESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNksiEPQ- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3572 vecVTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLPYINLEFLKAHTMYQVGLMETDQHIEFFWGALEMFTQEELCKFIK 3651
Cdd:pfam00632  158 ---LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLK 234
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622846758 3652 FACNQERIPFtcpckdGGPdtAHVPpyPMKIAPPDGTagsPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAIHYRE 3729
Cdd:pfam00632  235 FVTGSSRLPV------GGF--KSLP--KFTIVRKGGD---DDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGE 299
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
3375-3725 2.04e-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: 151.23  E-value: 2.04e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758  3375 IRFTGEEVHGTSGSFRHFLWQVCKElqssslsllllcpssAVNK-------NKGKYILTPSPITYG--EEQL--LHFLGQ 3443
Cdd:smart00119    9 IEFEGEEGLDGGGVTREFFFLLSKE---------------LFNPdyglfrySPNDYLLYPNPRSGFanEEHLsyFRFIGR 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758  3444 LLGIAIRADVPLPLDLLPSFWKTLVGEPLDPEqDLQEADILTYNYVKKFESINDETELEALCAEIasqhlaTESPDSPNk 3523
Cdd:smart00119   74 VLGKALYDNRLLDLFFARPFYKKLLGKPVTLH-DLESLDPELYKSLKWLLLNNDTSEELDLTFSI------VLTSEFGQ- 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758  3524 pccrftyltmtGEEVELCSRGRHILVAWENKDIY---AAAIRSLRLRELQnvecVTAVRAGLGSIIPLQLLTTLSPLEME 3600
Cdd:smart00119  146 -----------VKVVELKPGGSNIPVTEENKKEYvhlVIEYRLNKGIEKQ----LEAFREGFSEVIPENLLKLFDPEELE 210
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758  3601 LRTCGLPYINLEFLKAHTMYQVGLMETDQHIEFFWGALEMFTQEELCKFIKFACNQERIPFtcpckdGGpdTAHVPPyPM 3680
Cdd:smart00119  211 LLICGSPEIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV------GG--FAALSP-KF 281
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|....*
gi 1622846758  3681 KIAPpdgtAGSPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAI 3725
Cdd:smart00119  282 TIRK----AGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAI 322
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
1718-1868 9.47e-23

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: 96.58  E-value: 9.47e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 1718 FIYATSPLPVQAPSFYWEIEIVsygdtDDDTGPIVSFGFTTEAEKRDGAWTNPVGTCLFH-NNGRAVHYNGssllqwKSV 1796
Cdd:cd12885      2 SVRADHPIPPKVPVFYFEVTIL-----DLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHgDDGRVYLGGG------EGE 70
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622846758 1797 RLDVTLSPGDVAGIGWERTEGTppppgqpakgrVYFTYCGQRLSPYLEDV-SGGMWPVVHIQKKNTKTRANFG 1868
Cdd:cd12885     71 NYGPPFGTGDVVGCGINFKTGE-----------VFFTKNGELLGTAFENVvKGRLYPTVGLGSPGVKVRVNFG 132
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
3421-3725 7.04e-22

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 104.46  E-value: 7.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3421 GKYILTPSPITYGEEQLL---HFLGQLLGIAIRADVPLPLDLLPSFWKTLVGEPLdPEQDLQEADILTY-NYVKKFEsiN 3496
Cdd:COG5021    585 DLYTLPINPLSSINPEHLsyfKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPV-SLVDLESLDPELYrSLVWLLN--N 661
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3497 DETElEALCAEIASQHLATESPDSpnkpccrftyltmtgeeVELCSRGRHILVAWENKDIYAAAIRSLRLR---ELQnve 3573
Cdd:COG5021    662 DIDE-TILDLTFTVEDDSFGESRT-----------------VELIPNGRNISVTNENKKEYVKKVVDYKLNkrvEKQ--- 720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846758 3574 cVTAVRAGLGSIIPLQLLTTLSPLEMELRTCGLP-YINLEFLKAHTMYqVGLMETDQHIEFFWGALEMFTQEELCKFIKF 3652
Cdd:COG5021    721 -FSAFKSGFSEIIPPDLLQIFDESELELLIGGIPeDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIISEFDFEERAKLLQF 798
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622846758 3653 ACNQERIPFtcpckdGGPDTAHVPPYPMK-IAPPDGTagsPDSRYIRVETCMFMIKLPQYSSLEIMLEKLRCAI 3725
Cdd:COG5021    799 VTGTSRIPI------NGFKDLQGSDGVRKfTIEKGGT---DDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAI 863
 
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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