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Conserved domains on  [gi|1958757288|ref|XP_038954686|]
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probable E3 ubiquitin-protein ligase HERC4 isoform X7 [Rattus norvegicus]

Protein Classification

E3 ubiquitin-protein ligase HERC family protein( domain architecture ID 13420603)

E3 ubiquitin-protein ligase HERC (HECT and RCC1 domain) family protein similar to human E3 ISG15--protein ligase HERC5, the major E3 ligase for ISG15 conjugation, that functions as part of the ISGylation machinery that recognizes target proteins in a broad and relatively non-specific manner

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
454-800 1.44e-156

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: 459.72  E-value: 1.44e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 454 LILVVRRENIVGDAMEVLRKTKNIDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDS-RLIWFSDK 532
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDsGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 533 TFEDSD---LFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQLLDYPEDdiEETFCLNF 609
Cdd:cd00078    81 SFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD--EDDLELTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 610 TITVEN-FGATEVKELVLNGADTAVNKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIG 688
Cdd:cd00078   159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 689 NTNYDWKELEKNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL--KLVIQSTGGGESYLPV 766
Cdd:cd00078   239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDRLPT 318
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1958757288 767 SHTCFNLLDLPKYTEKETLRCKLIQAIDHNEGFS 800
Cdd:cd00078   319 AHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
ATS1 super family cl34932
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3-88 5.21e-16

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


The actual alignment was detected with superfamily member COG5184:

Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 80.02  E-value: 5.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288   3 RTEGGVFTFGAGGYGQLGHNSTSHEINPRKVFELMGsiVTQIACGRQHTSAfVPSSGRIYSFGLGGNGQLGTGSTSNRKS 82
Cdd:COG5184   165 KSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCA-LKSDGTVWCWGSNSSGQLGDGTTTDRAT 241

                  ....*.
gi 1958757288  83 PFTVKG 88
Cdd:COG5184   242 PVQVAG 247
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
454-800 1.44e-156

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: 459.72  E-value: 1.44e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 454 LILVVRRENIVGDAMEVLRKTKNIDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDS-RLIWFSDK 532
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDsGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 533 TFEDSD---LFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQLLDYPEDdiEETFCLNF 609
Cdd:cd00078    81 SFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD--EDDLELTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 610 TITVEN-FGATEVKELVLNGADTAVNKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIG 688
Cdd:cd00078   159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 689 NTNYDWKELEKNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL--KLVIQSTGGGESYLPV 766
Cdd:cd00078   239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDRLPT 318
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1958757288 767 SHTCFNLLDLPKYTEKETLRCKLIQAIDHNEGFS 800
Cdd:cd00078   319 AHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
480-799 6.07e-123

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: 372.34  E-value: 6.07e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288  480 KKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDSRLIWFSDKTFEDSD----LFHLIGVICGLAIYNFT 555
Cdd:smart00119   4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALYDNR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288  556 IVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQL-LDYPEDDIEEtfcLNFTITVEN-FGATEVKELVLNGADTAV 633
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD---LTFSIVLTSeFGQVKVVELKPGGSNIPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288  634 NKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIGNTNYDWKELEKNTEYKGEYWAEHPT 713
Cdd:smart00119 161 TEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288  714 IKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL--KLVIQSTGGGESYLPVSHTCFNLLDLPKYTEKETLRCKLIQ 791
Cdd:smart00119 241 IKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLL 320

                   ....*...
gi 1958757288  792 AIDHNEGF 799
Cdd:smart00119 321 AINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
504-802 1.68e-114

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 349.60  E-value: 1.68e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 504 LLIMRELLDPKYGMFRY-YEDSRLIWFSDKTFED-----SDLFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKRKPSLD 577
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESpdlelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 578 DLKELMPDVGRSMQQLLDYpEDDIEETFCLNFTITVenFGATEVKELVLNGADTAVNKQNRQEFVDAYVDYIFNKSVASL 657
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNM-DNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 658 FDAFHAGFHKVCGGKVLLLFQPNELQAMVIGNTNYDWKELEKNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLT 737
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958757288 738 GSDRIPILGMKSL-KLVIQSTGG-GESYLPVSHTCFNLLDLPKYTEKETLRCKLIQAIDHNEGFSLI 802
Cdd:pfam00632 238 GSSRLPVGGFKSLpKFTIVRKGGdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
405-802 5.16e-99

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 326.72  E-value: 5.16e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 405 TYPFVFDAQAKTTLLQTD-----AVLQMQMAIDQ---AHRQNVSSLFLPVIESVNPCLILVVRRENIVGDAMEVLRKTKN 476
Cdd:COG5021   458 LYRFYFVEHRKKTLTKNDsrlgsFISLNKLDIRRikeDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESG 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 477 IDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDSRLIW----FSDKTFEDSDLFHLIGVICGLAIY 552
Cdd:COG5021   538 DDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLpinpLSSINPEHLSYFKFLGRVIGKAIY 617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 553 NFTIVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQLLDYPEDdiEETFCLNFTITVENFGATEVKELVLNGADTA 632
Cdd:COG5021   618 DSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDID--ETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 633 VNKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIG-NTNYDWKELEKNTEYKGeYWAEH 711
Cdd:COG5021   696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGiPEDIDIDDWKSNTAYHG-YTEDS 774
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 712 PTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL-------KLVIQSTGGGESYLPVSHTCFNLLDLPKYTEKET 784
Cdd:COG5021   775 PIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLqgsdgvrKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEK 854
                         410
                  ....*....|....*...
gi 1958757288 785 LRCKLIQAIDHNEGFSLI 802
Cdd:COG5021   855 LRSKLLTAINEGAGFGLL 872
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3-88 5.21e-16

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 80.02  E-value: 5.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288   3 RTEGGVFTFGAGGYGQLGHNSTSHEINPRKVFELMGsiVTQIACGRQHTSAfVPSSGRIYSFGLGGNGQLGTGSTSNRKS 82
Cdd:COG5184   165 KSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCA-LKSDGTVWCWGSNSSGQLGDGTTTDRAT 241

                  ....*.
gi 1958757288  83 PFTVKG 88
Cdd:COG5184   242 PVQVAG 247
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
5-53 6.83e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 66.39  E-value: 6.83e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958757288   5 EGGVFTFGAGGYGQLGHNSTSHEINPRKVFELMGSIVTQIACGRQHTSA 53
Cdd:pfam00415   1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVA 49
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
454-800 1.44e-156

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: 459.72  E-value: 1.44e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 454 LILVVRRENIVGDAMEVLRKTKNIDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDS-RLIWFSDK 532
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDsGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 533 TFEDSD---LFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQLLDYPEDdiEETFCLNF 609
Cdd:cd00078    81 SFADEDhlkLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGD--EDDLELTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 610 TITVEN-FGATEVKELVLNGADTAVNKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIG 688
Cdd:cd00078   159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 689 NTNYDWKELEKNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL--KLVIQSTGGGESYLPV 766
Cdd:cd00078   239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLnpKFTIRRVGSPDDRLPT 318
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1958757288 767 SHTCFNLLDLPKYTEKETLRCKLIQAIDHNEGFS 800
Cdd:cd00078   319 AHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
480-799 6.07e-123

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: 372.34  E-value: 6.07e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288  480 KKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDSRLIWFSDKTFEDSD----LFHLIGVICGLAIYNFT 555
Cdd:smart00119   4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEehlsYFRFIGRVLGKALYDNR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288  556 IVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQL-LDYPEDDIEEtfcLNFTITVEN-FGATEVKELVLNGADTAV 633
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELD---LTFSIVLTSeFGQVKVVELKPGGSNIPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288  634 NKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIGNTNYDWKELEKNTEYKGEYWAEHPT 713
Cdd:smart00119 161 TEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288  714 IKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL--KLVIQSTGGGESYLPVSHTCFNLLDLPKYTEKETLRCKLIQ 791
Cdd:smart00119 241 IKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALspKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREKLLL 320

                   ....*...
gi 1958757288  792 AIDHNEGF 799
Cdd:smart00119 321 AINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
504-802 1.68e-114

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 349.60  E-value: 1.68e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 504 LLIMRELLDPKYGMFRY-YEDSRLIWFSDKTFED-----SDLFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKRKPSLD 577
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYeTEDDRTYWFNPSSSESpdlelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 578 DLKELMPDVGRSMQQLLDYpEDDIEETFCLNFTITVenFGATEVKELVLNGADTAVNKQNRQEFVDAYVDYIFNKSVASL 657
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNM-DNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 658 FDAFHAGFHKVCGGKVLLLFQPNELQAMVIGNTNYDWKELEKNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLT 737
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958757288 738 GSDRIPILGMKSL-KLVIQSTGG-GESYLPVSHTCFNLLDLPKYTEKETLRCKLIQAIDHNEGFSLI 802
Cdd:pfam00632 238 GSSRLPVGGFKSLpKFTIVRKGGdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
405-802 5.16e-99

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 326.72  E-value: 5.16e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 405 TYPFVFDAQAKTTLLQTD-----AVLQMQMAIDQ---AHRQNVSSLFLPVIESVNPCLILVVRRENIVGDAMEVLRKTKN 476
Cdd:COG5021   458 LYRFYFVEHRKKTLTKNDsrlgsFISLNKLDIRRikeDKRRKLFYSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESG 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 477 IDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDSRLIW----FSDKTFEDSDLFHLIGVICGLAIY 552
Cdd:COG5021   538 DDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLpinpLSSINPEHLSYFKFLGRVIGKAIY 617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 553 NFTIVDLHFPLALYKKLLKRKPSLDDLKELMPDVGRSMQQLLDYPEDdiEETFCLNFTITVENFGATEVKELVLNGADTA 632
Cdd:COG5021   618 DSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDID--ETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 633 VNKQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIG-NTNYDWKELEKNTEYKGeYWAEH 711
Cdd:COG5021   696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGiPEDIDIDDWKSNTAYHG-YTEDS 774
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288 712 PTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSL-------KLVIQSTGGGESYLPVSHTCFNLLDLPKYTEKET 784
Cdd:COG5021   775 PIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLqgsdgvrKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEK 854
                         410
                  ....*....|....*...
gi 1958757288 785 LRCKLIQAIDHNEGFSLI 802
Cdd:COG5021   855 LRSKLLTAINEGAGFGLL 872
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3-88 5.21e-16

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 80.02  E-value: 5.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288   3 RTEGGVFTFGAGGYGQLGHNSTSHEINPRKVFELMGsiVTQIACGRQHTSAfVPSSGRIYSFGLGGNGQLGTGSTSNRKS 82
Cdd:COG5184   165 KSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCA-LKSDGTVWCWGSNSSGQLGDGTTTDRAT 241

                  ....*.
gi 1958757288  83 PFTVKG 88
Cdd:COG5184   242 PVQVAG 247
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3-88 1.18e-14

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 76.17  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288   3 RTEGGVFTFGAGGYGQLGHNSTSHEINPRKVFELMGsiVTQIACGRQHTSAfVPSSGRIYSFGLGGNGQLGTGSTSNRKS 82
Cdd:COG5184   215 KSDGTVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCA-LKSDGTVWCWGDNSYGQLGDGTTTDRST 291

                  ....*.
gi 1958757288  83 PFTVKG 88
Cdd:COG5184   292 PVKVPG 297
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3-83 3.67e-14

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 74.63  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288   3 RTEGGVFTFGAGGYGQLGHNSTSHEINPRKVFELMGsiVTQIACGRQHTSAfVPSSGRIYSFGLGGNGQLGTGSTSNRKS 82
Cdd:COG5184   265 KSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSG--VVAVAAGSSHTCA-LLTDGTVWCWGDNAYGQLGDGTTTDRST 341

                  .
gi 1958757288  83 P 83
Cdd:COG5184   342 P 342
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
5-53 6.83e-14

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 66.39  E-value: 6.83e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958757288   5 EGGVFTFGAGGYGQLGHNSTSHEINPRKVFELMGSIVTQIACGRQHTSA 53
Cdd:pfam00415   1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVA 49
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
1-88 6.36e-13

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 70.78  E-value: 6.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288   1 MMRTEGGVFTFGAGGYGQLGHNSTSHEINPRKVFELMGsiVTQIACGRQHTSAfVPSSGRIYSFGLGGNGQLGTGSTSNR 80
Cdd:COG5184    12 ALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGGDHTCA-LKADGTVWCWGNNSYGQLGDGTTTDR 88

                  ....*...
gi 1958757288  81 KSPFTVKG 88
Cdd:COG5184    89 TTPVKVPG 96
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
3-120 1.77e-12

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 69.62  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757288   3 RTEGGVFTFGAGGYGQLGHNSTSHEINPRKVFELmgSIVTQIACGRQHTSAfVPSSGRIYSFGLGGNGQLGTGSTSNRKS 82
Cdd:COG5184    64 KADGTVWCWGNNSYGQLGDGTTTDRTTPVKVPGL--TGVVAVAAGYYHSCA-LKSDGTVWCWGDNSSGQLGDGTTTNRLT 140
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958757288  83 PFTVkgnwfsyngqcpqDIGSEDyfcVKRIFSGGDQSF 120
Cdd:COG5184   141 PVQV-------------DAGLSG---VVAIAAGGYHTC 162
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
58-88 5.27e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 44.05  E-value: 5.27e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958757288  58 SGRIYSFGLGGNGQLGTGSTSNRKSPFTVKG 88
Cdd:pfam00415   1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEG 31
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
42-88 2.49e-05

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 47.28  E-value: 2.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958757288  42 TQIACGRQHTSAfVPSSGRIYSFGLGGNGQLGTGSTSNRKSPFTVKG 88
Cdd:COG5184     1 TQVAAGGSHSCA-LKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRVPG 46
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
41-71 2.80e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 38.56  E-value: 2.80e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958757288  41 VTQIACGRQHTsAFVPSSGRIYSFGLGGNGQ 71
Cdd:pfam13540   1 VVSVAAGDNHT-LALTSDGRVYCWGDNSYGQ 30
 
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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