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Conserved domains on  [gi|157738609|ref|NP_078878|]
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E3 ubiquitin-protein ligase HECTD3 [Homo sapiens]

Protein Classification

HECT-type E3 ubiquitin-protein ligase( domain architecture ID 10171405)

HECT-type E3 ubiquitin-protein ligase catalyzes the attachment of ubiquitin chains to target proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APC10-HECTD3 cd08666
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ...
 238-371 1.86e-93

APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in HECTD3, a HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein. HECT E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), and are a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. They also regulate the trafficking of many receptors, channels, transporters and viral proteins. HECTD3 (HECT domain-containing protein3) contains a C-terminal HECT domain with the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain, which is responsible for substrate recognition and binding. HECTD3 specifically recognizes the Trio-binding protein, Tara (Trio-associated repeat on actin), implicated in regulating actin cytoskeletal, cell motility and cell growth. Tara also binds to TRF1 and may participate in telomere maintenance and/or mitotic regulation through interacting with TRF1. HECTD3 interacts with and promotes the ubiquitination of Syntaxin 8, an endosomal syntaxin proposed to mediate distinct steps of endosomal protein trafficking. HECTD3-mediated Syntaxin 8 degradation has been suggested to contribute to the pathophysiology of neurodegenerative diseases.


:

Pssm-ID: 176487  Cd Length: 134  Bit Score: 289.31  E-value: 1.86e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 238 GSVKQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEG 317
Cdd:cd08666    1 GSVKQYVESIEVSSYTDDFNVSCLTDGDPDTYWESDGSQGQHWIRLHMKKGTIIKKLLLTVDATDDNYMPKRVAVYGGEG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157738609 318 DNLKKLSDVSIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIK 371
Cdd:cd08666   81 DNLKKLNDVSIDETLIGDVCILEDMTTHLPVIEIRIKECKDEGIDVRIRGIKIK 134
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 579-845 6.51e-67

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


:

Pssm-ID: 459880  Cd Length: 304  Bit Score: 225.18  E-value: 6.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  579 TGEARDMYV-PNPSCRDFA------KYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSkDFPAVDSVLVKLLEV 651
Cdd:pfam00632  17 YETEDDRTYwFNPSSSESPdlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  652 MEGMDKETFEFKfgkELTFT-TVLSDQQVVELIPGGAGIVVGYGDRSRFIQLVQKARLEES-KEQVAAMQAGLLKVVPQA 729
Cdd:pfam00632  96 LLNMDNDDDEDL---GLTFTiPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVIPKE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  730 VLDLLTWQELEKKVCGDPEVTVDALRKLTRFED-FEPSDSRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA-------R 801
Cdd:pfam00632 173 ALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVggfkslpK 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 157738609  802 IYIypDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYA 845
Cdd:pfam00632 253 FTI--VRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIA 294
 
Name Accession Description Interval E-value
APC10-HECTD3 cd08666
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ...
 238-371 1.86e-93

APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in HECTD3, a HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein. HECT E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), and are a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. They also regulate the trafficking of many receptors, channels, transporters and viral proteins. HECTD3 (HECT domain-containing protein3) contains a C-terminal HECT domain with the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain, which is responsible for substrate recognition and binding. HECTD3 specifically recognizes the Trio-binding protein, Tara (Trio-associated repeat on actin), implicated in regulating actin cytoskeletal, cell motility and cell growth. Tara also binds to TRF1 and may participate in telomere maintenance and/or mitotic regulation through interacting with TRF1. HECTD3 interacts with and promotes the ubiquitination of Syntaxin 8, an endosomal syntaxin proposed to mediate distinct steps of endosomal protein trafficking. HECTD3-mediated Syntaxin 8 degradation has been suggested to contribute to the pathophysiology of neurodegenerative diseases.


Pssm-ID: 176487  Cd Length: 134  Bit Score: 289.31  E-value: 1.86e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 238 GSVKQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEG 317
Cdd:cd08666    1 GSVKQYVESIEVSSYTDDFNVSCLTDGDPDTYWESDGSQGQHWIRLHMKKGTIIKKLLLTVDATDDNYMPKRVAVYGGEG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157738609 318 DNLKKLSDVSIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIK 371
Cdd:cd08666   81 DNLKKLNDVSIDETLIGDVCILEDMTTHLPVIEIRIKECKDEGIDVRIRGIKIK 134
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 579-845 6.51e-67

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 225.18  E-value: 6.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  579 TGEARDMYV-PNPSCRDFA------KYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSkDFPAVDSVLVKLLEV 651
Cdd:pfam00632  17 YETEDDRTYwFNPSSSESPdlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  652 MEGMDKETFEFKfgkELTFT-TVLSDQQVVELIPGGAGIVVGYGDRSRFIQLVQKARLEES-KEQVAAMQAGLLKVVPQA 729
Cdd:pfam00632  96 LLNMDNDDDEDL---GLTFTiPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVIPKE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  730 VLDLLTWQELEKKVCGDPEVTVDALRKLTRFED-FEPSDSRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA-------R 801
Cdd:pfam00632 173 ALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVggfkslpK 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 157738609  802 IYIypDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYA 845
Cdd:pfam00632 253 FTI--VRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIA 294
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 528-853 4.50e-63

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: 216.28  E-value: 4.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 528 WECKFIAEGIIDQGGGFRDSLADMSEELCPSSadtpvpLPFFVRTANqgngtgeARDMYVPNPSCRDFAK----YEWIGQ 603
Cdd:cd00078   30 LEVEFVGEEGIDAGGVTREFFTLVSKELFNPS------YGLFRYTPD-------DSGLLYPNPSSFADEDhlklFRFLGR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 604 LMGAALRGKEFLVLALPGFVWKQLSGEEVSWSkDFPAVDSVLVKLLEVMEGMDKETFEFkfgkELTFTTVLSDQ----QV 679
Cdd:cd00078   97 LLGKALYEGRLLDLPFSRAFYKKLLGKPLSLE-DLEELDPELYKSLKELLDNDGDEDDL----ELTFTIELDSSfggaVT 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 680 VELIPGGAGIVVGYGDRSRFIQLVQKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLT 758
Cdd:cd00078  172 VELKPGGRDIPVTNENKEEYVDLYVDYRLNKGiEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNT 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 759 RFEDFEPSDSR-VQYFWEALNNFTNEDRSRFLRFVTGRSRLPA--------RIYIYPDklgYETTDALPESSTCSSTLFL 829
Cdd:cd00078  252 EYKGGYSSDSPtIQWFWEVLESFTNEERKKFLQFVTGSSRLPVggfadlnpKFTIRRV---GSPDDRLPTAHTCFNLLKL 328

                        330       340
                 ....*....|....*....|....
gi 157738609 830 PHYASAKVCEEKLRYAAYNCVAID 853
Cdd:cd00078  329 PPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 528-849 8.16e-55

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: 192.83  E-value: 8.16e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609   528 WECKFIAEGIIDQGGGFRDSLADMSEELCPSSadtpvpLPFFVRTANqgngtgeARDMYVPNPSC----RDFAKYEWIGQ 603
Cdd:smart00119   7 LEIEFEGEEGLDGGGVTREFFFLLSKELFNPD------YGLFRYSPN-------DYLLYPNPRSGfaneEHLSYFRFIGR 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609   604 LMGAALRGKEFLVLALPGFVWKQLSGEEVSWsKDFPAVDSVLVKLLEVMEgMDKETFEfkfGKELTFTTVLSDQ----QV 679
Cdd:smart00119  74 VLGKALYDNRLLDLFFARPFYKKLLGKPVTL-HDLESLDPELYKSLKWLL-LNNDTSE---ELDLTFSIVLTSEfgqvKV 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609   680 VELIPGGAGIVVGYGDRSRFIQLVQKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLT 758
Cdd:smart00119 149 VELKPGGSNIPVTEENKKEYVHLVIEYRLNKGiEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNT 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609   759 RFED-FEPSDSRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA--------RIYIYPDKLGYETtdaLPESSTCSSTLFL 829
Cdd:smart00119 229 EYKGgYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVggfaalspKFTIRKAGSDDER---LPTAHTCFNRLKL 305

                          330       340
                   ....*....|....*....|
gi 157738609   830 PHYASAKVCEEKLRYAAYNC 849
Cdd:smart00119 306 PPYSSKEILREKLLLAINEG 325
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
589-845 9.80e-39

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 155.31  E-value: 9.80e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 589 NPSCRDFakYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSwSKDFPAVDSVLVKLLEVMEGMDKEtfefKFGKEL 668
Cdd:COG5021  598 NPEHLSY--FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVS-LVDLESLDPELYRSLVWLLNNDID----ETILDL 670

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 669 TFTT---VLSDQQVVELIPGGAGIVVGYGDRSRFIQLVQKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVC 744
Cdd:COG5021  671 TFTVeddSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRvEKQFSAFKSGFSEIIPPDLLQIFDESELELLIG 750

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 745 GDPEVT-VDALRKLTRFEDFEPSDSRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA-------------RIYIypdKLG 810
Cdd:COG5021  751 GIPEDIdIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPIngfkdlqgsdgvrKFTI---EKG 827

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157738609 811 YETTDALPESSTCSSTLFLPHYASAKVCEEKLRYA 845
Cdd:COG5021  828 GTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTA 862
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
232-391 2.24e-08

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 54.76  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  232 KEDENLGSVKQYVE-----SIDVSSYTEEFNVSCLTDSNADTYWESDGSQcQHWVRLTMKKGTIVKKLLLTVD-TTDDNF 305
Cdd:pfam03256  11 KQLSRAGRVRHQREigsqaVWSLSSCKPGFGVDLLRDDNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLDyKLDESY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  306 MPKRVVVYGGEG-DNLKKLSDVSIDEtligdvcvlEDMTVHLPI------------IEIRIVECRDDGIDVRLRGVKIKS 372
Cdd:pfam03256  90 TPSKISVRAGTGfNDLQEVRVVDLEE---------PTGWVHIPLrdangkplrtfmLQIAVLSNHQNGRDTHVRQIKIYG 160

                         170
                  ....*....|....*....
gi 157738609  373 SRQRELGLNADLFQPTSLV 391
Cdd:pfam03256 161 PVEERSAVAARLGHFTTSD 179
DOC1 COG5156
Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / ...
 247-390 6.62e-08

Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227485  Cd Length: 189  Bit Score: 53.44  E-value: 6.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 247 IDVSSYTEEFNVSCLTDSNADTYWESDGSQcQHWVRLTMKKGTIVKKLLLTVD-TTDDNFMPKRVVVYGGEG-DNLKKLS 324
Cdd:COG5156   32 WRLSSFKRGHPLRELLDDNMDTYWQSDGVQ-PHSIQISFDKRRYIQSVQLFLSfTQDESYTPSKIGVRAGLTrEDVREIS 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157738609 325 DVSIDE-----TL-IGDVCVLEDMTVHLpiIEIRIVECRDDGIDVRLRGVKIKSSRQRELGLNADLFQPTSL 390
Cdd:COG5156  111 SVEVVEpegwvTLsVADKREDDLLKCIY--ILVVINSNHQEGKDSHVRHIKIYEPSTEEIYYKIEWAQTLPE 180
 
Name Accession Description Interval E-value
APC10-HECTD3 cd08666
APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ...
 238-371 1.86e-93

APC10-like DOC1 domain of HECTD3, a HECT E3 ubiquitin ligase protein that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in HECTD3, a HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein. HECT E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), and are a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. They also regulate the trafficking of many receptors, channels, transporters and viral proteins. HECTD3 (HECT domain-containing protein3) contains a C-terminal HECT domain with the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain, which is responsible for substrate recognition and binding. HECTD3 specifically recognizes the Trio-binding protein, Tara (Trio-associated repeat on actin), implicated in regulating actin cytoskeletal, cell motility and cell growth. Tara also binds to TRF1 and may participate in telomere maintenance and/or mitotic regulation through interacting with TRF1. HECTD3 interacts with and promotes the ubiquitination of Syntaxin 8, an endosomal syntaxin proposed to mediate distinct steps of endosomal protein trafficking. HECTD3-mediated Syntaxin 8 degradation has been suggested to contribute to the pathophysiology of neurodegenerative diseases.


Pssm-ID: 176487  Cd Length: 134  Bit Score: 289.31  E-value: 1.86e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 238 GSVKQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEG 317
Cdd:cd08666    1 GSVKQYVESIEVSSYTDDFNVSCLTDGDPDTYWESDGSQGQHWIRLHMKKGTIIKKLLLTVDATDDNYMPKRVAVYGGEG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157738609 318 DNLKKLSDVSIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIK 371
Cdd:cd08666   81 DNLKKLNDVSIDETLIGDVCILEDMTTHLPVIEIRIKECKDEGIDVRIRGIKIK 134
APC10-like1 cd08365
APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 240-371 2.80e-71

APC10-like DOC1 domains of E3 ubiquitin ligases that mediate substrate ubiquitination; This model represens the APC10-like DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. APC10/DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included here. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10/DOC1 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176483  Cd Length: 131  Bit Score: 230.47  E-value: 2.80e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 240 VKQYVESIDVSSYTEefNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGE-GD 318
Cdd:cd08365    1 TKCYVESIEVSSNPA--DASRLTDGNTSTYWQSDGSQGSHWIRLKMKPDVLVRHLSLAVDATDSSYMPQRVVVAGGRsAS 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157738609 319 NLKKLSDVSIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIK 371
Cdd:cd08365   79 NLQELRDVNIPPSVTGYVTLLEDATISQPYIEIRIKRCRSDGIDTRIHGLRIL 131
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 579-845 6.51e-67

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 225.18  E-value: 6.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  579 TGEARDMYV-PNPSCRDFA------KYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSkDFPAVDSVLVKLLEV 651
Cdd:pfam00632  17 YETEDDRTYwFNPSSSESPdlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  652 MEGMDKETFEFKfgkELTFT-TVLSDQQVVELIPGGAGIVVGYGDRSRFIQLVQKARLEES-KEQVAAMQAGLLKVVPQA 729
Cdd:pfam00632  96 LLNMDNDDDEDL---GLTFTiPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVIPKE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  730 VLDLLTWQELEKKVCGDPEVTVDALRKLTRFED-FEPSDSRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA-------R 801
Cdd:pfam00632 173 ALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVggfkslpK 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 157738609  802 IYIypDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYA 845
Cdd:pfam00632 253 FTI--VRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIA 294
APC10-like cd08159
APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This ...
 241-371 1.83e-63

APC10-like DOC1 domains in E3 ubiquitin ligases that mediate substrate ubiquitination; This family contains the single domain protein, APC10, a subunit of the anaphase-promoting complex (APC), as well as the DOC1 domain of multi-domain proteins present in E3 ubiquitin ligases. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC, a multi-protein complex (or cyclosome), is a cell cycle-regulated, E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. APC10-like DOC1 domains such as those present in HECT (Homologous to the E6-AP Carboxyl Terminus) and Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase proteins, HECTD3, and CUL7, respectively, are also included in this hierarchy. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling a SCF-ROC1-like E3 ubiquitin ligase complex consisting of Skp1, CUL7, Fbx29 F-box protein, and ROC1 (RING-box protein 1) and promotes ubiquitination. CUL7 is a multi-domain protein with a C-terminal cullin domain that binds ROC1 and a centrally positioned APC10/DOC1 domain. HECTD3 contains a C-terminal HECT domain which contains the active site for ubiquitin transfer onto substrates, and an N-terminal APC10 domain which is responsible for substrate recognition and binding. An APC10/DOC1 domain homolog is also present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT domain. Recent studies have shown that the protein complex HERC2-RNF8 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Also included in this hierarchy is an uncharacterized APC10/DOC1-like domain found in a multi-domain protein, which also contains CUB, zinc finger ZZ-type, and EF-hand domains. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176482  Cd Length: 129  Bit Score: 209.25  E-value: 1.83e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 241 KQYVESIDVSSYTEefNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEG-DN 319
Cdd:cd08159    1 KCYTASIEVSSNPL--PVSRLTDGNYDTYWQSDGSQGSHWIRLFMKKDVLIRVLAIFVDMADSSYMPSLVVVYGGHSpSD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157738609 320 LKKLSDVSIDETlIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIK 371
Cdd:cd08159   79 LRELKDVNIRPS-NGWVALLEDDTLKCPYIEIRIKRCRSDGIDTRIRGLRLL 129
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 528-853 4.50e-63

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: 216.28  E-value: 4.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 528 WECKFIAEGIIDQGGGFRDSLADMSEELCPSSadtpvpLPFFVRTANqgngtgeARDMYVPNPSCRDFAK----YEWIGQ 603
Cdd:cd00078   30 LEVEFVGEEGIDAGGVTREFFTLVSKELFNPS------YGLFRYTPD-------DSGLLYPNPSSFADEDhlklFRFLGR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 604 LMGAALRGKEFLVLALPGFVWKQLSGEEVSWSkDFPAVDSVLVKLLEVMEGMDKETFEFkfgkELTFTTVLSDQ----QV 679
Cdd:cd00078   97 LLGKALYEGRLLDLPFSRAFYKKLLGKPLSLE-DLEELDPELYKSLKELLDNDGDEDDL----ELTFTIELDSSfggaVT 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 680 VELIPGGAGIVVGYGDRSRFIQLVQKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLT 758
Cdd:cd00078  172 VELKPGGRDIPVTNENKEEYVDLYVDYRLNKGiEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNT 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 759 RFEDFEPSDSR-VQYFWEALNNFTNEDRSRFLRFVTGRSRLPA--------RIYIYPDklgYETTDALPESSTCSSTLFL 829
Cdd:cd00078  252 EYKGGYSSDSPtIQWFWEVLESFTNEERKKFLQFVTGSSRLPVggfadlnpKFTIRRV---GSPDDRLPTAHTCFNLLKL 328

                        330       340
                 ....*....|....*....|....
gi 157738609 830 PHYASAKVCEEKLRYAAYNCVAID 853
Cdd:cd00078  329 PPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 528-849 8.16e-55

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: 192.83  E-value: 8.16e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609   528 WECKFIAEGIIDQGGGFRDSLADMSEELCPSSadtpvpLPFFVRTANqgngtgeARDMYVPNPSC----RDFAKYEWIGQ 603
Cdd:smart00119   7 LEIEFEGEEGLDGGGVTREFFFLLSKELFNPD------YGLFRYSPN-------DYLLYPNPRSGfaneEHLSYFRFIGR 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609   604 LMGAALRGKEFLVLALPGFVWKQLSGEEVSWsKDFPAVDSVLVKLLEVMEgMDKETFEfkfGKELTFTTVLSDQ----QV 679
Cdd:smart00119  74 VLGKALYDNRLLDLFFARPFYKKLLGKPVTL-HDLESLDPELYKSLKWLL-LNNDTSE---ELDLTFSIVLTSEfgqvKV 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609   680 VELIPGGAGIVVGYGDRSRFIQLVQKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLT 758
Cdd:smart00119 149 VELKPGGSNIPVTEENKKEYVHLVIEYRLNKGiEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNT 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609   759 RFED-FEPSDSRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA--------RIYIYPDKLGYETtdaLPESSTCSSTLFL 829
Cdd:smart00119 229 EYKGgYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVggfaalspKFTIRKAGSDDER---LPTAHTCFNRLKL 305

                          330       340
                   ....*....|....*....|
gi 157738609   830 PHYASAKVCEEKLRYAAYNC 849
Cdd:smart00119 306 PPYSSKEILREKLLLAINEG 325
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
589-845 9.80e-39

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 155.31  E-value: 9.80e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 589 NPSCRDFakYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSwSKDFPAVDSVLVKLLEVMEGMDKEtfefKFGKEL 668
Cdd:COG5021  598 NPEHLSY--FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVS-LVDLESLDPELYRSLVWLLNNDID----ETILDL 670

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 669 TFTT---VLSDQQVVELIPGGAGIVVGYGDRSRFIQLVQKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVC 744
Cdd:COG5021  671 TFTVeddSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRvEKQFSAFKSGFSEIIPPDLLQIFDESELELLIG 750

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 745 GDPEVT-VDALRKLTRFEDFEPSDSRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA-------------RIYIypdKLG 810
Cdd:COG5021  751 GIPEDIdIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPIngfkdlqgsdgvrKFTI---EKG 827

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157738609 811 YETTDALPESSTCSSTLFLPHYASAKVCEEKLRYA 845
Cdd:COG5021  828 GTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTA 862
APC10-HERC2 cd08664
APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the ...
 244-370 7.55e-27

APC10-like DOC1 domain present in HERC2 (HECT domain and RLD2); This model represents the APC10/DOC1 domain present in HERC2 (HECT domain and RLD2), a large multi-domain protein with three RCC1-like domains (RLDs), additional internal domains including a zinc finger ZZ-type and Cyt-b5 (Cytochrome b5-like Heme/Steroid binding) domains, and a C-terminal HECT (Homologous to the E6-AP Carboxyl Terminus) domain. The APC10/DOC1 domain of HERC2 is a homolog of the APC10 subunit and the DOC1 domain present in E3 ubiquitin ligases which mediate substrate ubiquitination (or ubiquitylation), a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. As suggested by structural relationships between HERC2 and other proteins such as HERC1, the proposed role for HERC2 in protein trafficking and degradation pathways is consistent with observations that mutations in HERC2 lead to neuromuscular secretory vesicle and sperm acrosome defects, other developmental abnormalities, and juvenile lethality of jdf2 mice. Recent studies have shown that the protein complex, HERC2-RNF8, coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes.


Pssm-ID: 176485  Cd Length: 152  Bit Score: 107.07  E-value: 7.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 244 VESIDVSSytEEFNVSCLTDsNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEG-DNLKK 322
Cdd:cd08664   28 VRSLTVSS--NENQAKRLID-GSGSYWQSSGSQGKHWIRLELHPDVLIHSLKIIVDPADSSYMPSLVVVSGGDSlNSLKE 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 157738609 323 LSDVSIDETligDVCV--LEDMTVHLPIIEIRIVECRDDGIDVRLRGVKI 370
Cdd:cd08664  105 LKTINVNAT---DTLVtlLQDVKEYYRYIEIAIKQCRNNGIDCKIHGLNI 151
APC10-CUL7 cd08665
APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that ...
 245-370 8.37e-27

APC10-like DOC1 domain of CUL7, subunit of the SCF-ROC1-like E3 ubiquitin ligase complex that mediates substrate ubiquitination; This model represents the APC10/DOC1 domain present in CUL7, a subunit of the SCF-ROC1-like E3 Ubiquitin (Ub) ligase complex, which mediates substrate ubiquitination (or ubiquitylation), and is a component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. CUL7 is a member of the Cullin-RING ligase family and functions as a molecular scaffold assembling the SCF-ROC1-like E3 Ub ligase complex consisting of the adapter protein Skp1, CUL7, the WD40 repeat-containing F-box Fbw8 (also known as Fbx29), and ROC1 (RING-box protein 1). CUL7 is a large protein with a C-terminal cullin domain that binds ROC1 and additional domains, including an APC10/DOC1 domain. While the Fbw8 protein is responsible for substrate protein recognition, the ROC1 RING domain recruits an Ub-charged E2 Ub-conjugating enzyme for substrate ubiquitination. It remains to be determined how CUL7 binds to the Skp1-Fbw8 heterodimer. The CUL7 E3 Ub ligase has been implicated in the proteasomal degradation of the cellular proteins, cyclin D1, an important regulator of the G1 to S-phase cell cycle progression, and insulin receptor substrate 1, a critical component of the signaling pathways downstream of the insulin and insulin-like growth factor 1 receptor. CUL7 appears to be an important regulator of placental development. Germ line mutations of CUL7 are linked to 3-M syndrome and Yakuts short stature syndrome.


Pssm-ID: 176486  Cd Length: 131  Bit Score: 106.16  E-value: 8.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 245 ESIDVSSytEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGE--GDNLKK 322
Cdd:cd08665    5 EKVEVSS--NPHRANKLTDGNPKTYWESNGSTGSHYINIHMHRGVVIRQLYMLVASEDSSYMPARVVVLGGDspSCITTE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 157738609 323 LSDVSIDETlIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKI 370
Cdd:cd08665   83 LNAVNVSPT-ASRVVLLENMTRFWPIIQIRIKRCQQGGIDTRVRGLEI 129
APC10-ZZEF1 cd08667
APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing ...
 247-369 6.70e-26

APC10/DOC1-like domain of uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) and homologs; This model represents the APC10/DOC1-like domain present in the uncharacterized Zinc finger ZZ-type and EF-hand domain-containing protein 1 (ZZEF1) of Mus musculus. Members of this family contain EF-hand, APC10, CUB, and zinc finger ZZ-type domains. ZZEF1-like APC10 domains are homologous to the APC10 subunit/DOC1 domains present in E3 ubiquitin ligases, which mediate substrate ubiquitination (or ubiquitylation), and are components of the ubiquitin-26S proteasome pathway for selective proteolytic degradation.


Pssm-ID: 176488  Cd Length: 131  Bit Score: 103.45  E-value: 6.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 247 IDVSSYTEEFNVscLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGG-EGDNLKKLSD 325
Cdd:cd08667    7 IEVSSNSADIDR--MTDGETSTYWQSDGSARSHWIRLKMKPDVVLRHLSIAVAATDQSYMPQQVTVSVGrSASSLQEVRD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 157738609 326 VSIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVK 369
Cdd:cd08667   85 VHIPSNVTGYVTLLENANISYLVVQINIKRCHSDGCDTRIHGLK 128
APC10 cd08366
APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; ...
 249-370 5.79e-15

APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination; This model represents the single domain protein APC10, a subunit of the anaphase-promoting complex (APC), which is a multi-subunit E3 ubiquitin ligase. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a vital component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC (also known as the cyclosome), is a cell cycle-regulated E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. In mitosis, the APC initiates sister chromatid separation by ubiquitinating the anaphase inhibitor securin and triggers exit from mitosis by ubiquitinating cyclin B. The C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats. APC10 domains are homologous to the DOC1 domains present in the HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein, and the Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase complex. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.


Pssm-ID: 176484  Cd Length: 139  Bit Score: 72.59  E-value: 5.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 249 VSSYTEEFNVSCLTDSNADTYWESDGSQcQHWVRLTMKKGTIVKKLLLTVD-TTDDNFMPKRVVVYGGEGDN-LKKLSDV 326
Cdd:cd08366   11 LSSAKPGNGVDQLRDDSLDTYWQSDGPQ-PHLINIQFSKKTDISAVALYLDyKLDESYTPSKISIRAGTSPHdLQEVRTV 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157738609 327 SIDEtLIGDVCV-LEDMTVHLPI----IEIRIVECRDDGIDVRLRGVKI 370
Cdd:cd08366   90 ELEE-PNGWVHIpLEDNRDGKPLrtffLQIAILSNHQNGRDTHIRQIKV 137
ANAPC10 pfam03256
Anaphase-promoting complex, subunit 10 (APC10);
232-391 2.24e-08

Anaphase-promoting complex, subunit 10 (APC10);


Pssm-ID: 367420  Cd Length: 185  Bit Score: 54.76  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  232 KEDENLGSVKQYVE-----SIDVSSYTEEFNVSCLTDSNADTYWESDGSQcQHWVRLTMKKGTIVKKLLLTVD-TTDDNF 305
Cdd:pfam03256  11 KQLSRAGRVRHQREigsqaVWSLSSCKPGFGVDLLRDDNLDTYWQSDGSQ-PHLVNIQFRKKTPVKYVAIYLDyKLDESY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  306 MPKRVVVYGGEG-DNLKKLSDVSIDEtligdvcvlEDMTVHLPI------------IEIRIVECRDDGIDVRLRGVKIKS 372
Cdd:pfam03256  90 TPSKISVRAGTGfNDLQEVRVVDLEE---------PTGWVHIPLrdangkplrtfmLQIAVLSNHQNGRDTHVRQIKIYG 160

                         170
                  ....*....|....*....
gi 157738609  373 SRQRELGLNADLFQPTSLV 391
Cdd:pfam03256 161 PVEERSAVAARLGHFTTSD 179
DOC1 COG5156
Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / ...
 247-390 6.62e-08

Anaphase-promoting complex (APC), subunit 10 [Cell division and chromosome partitioning / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227485  Cd Length: 189  Bit Score: 53.44  E-value: 6.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609 247 IDVSSYTEEFNVSCLTDSNADTYWESDGSQcQHWVRLTMKKGTIVKKLLLTVD-TTDDNFMPKRVVVYGGEG-DNLKKLS 324
Cdd:COG5156   32 WRLSSFKRGHPLRELLDDNMDTYWQSDGVQ-PHSIQISFDKRRYIQSVQLFLSfTQDESYTPSKIGVRAGLTrEDVREIS 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157738609 325 DVSIDE-----TL-IGDVCVLEDMTVHLpiIEIRIVECRDDGIDVRLRGVKIKSSRQRELGLNADLFQPTSL 390
Cdd:COG5156  111 SVEVVEpegwvTLsVADKREDDLLKCIY--ILVVINSNHQEGKDSHVRHIKIYEPSTEEIYYKIEWAQTLPE 180
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 250-354 3.74e-04

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 41.28  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738609  250 SSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGE-GDNLKKLSDVSI 328
Cdd:pfam00754   6 SSYSGEGPAAAALDGDPNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSNGYVTSYKIEYSLdGENWTTVKDEKI 85

                          90       100
                  ....*....|....*....|....*...
gi 157738609  329 DETLIGDVCVLEdmTVHLPIIE--IRIV 354
Cdd:pfam00754  86 PGNNDNNTPVTN--TFDPPIKAryVRIV 111
 
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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