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Conserved domains on  [gi|557948106|ref|NP_001273685|]
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anaphase-promoting complex subunit 4 isoform 1 [Homo sapiens]

Protein Classification

ANAPC4_WD40 and ANAPC4 domain-containing protein( domain architecture ID 10583927)

ANAPC4_WD40 and ANAPC4 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANAPC4 pfam12896
Anaphase-promoting complex, cyclosome, subunit 4; Apc4 is one of the larger of the subunits of ...
 232-431 1.90e-66

Anaphase-promoting complex, cyclosome, subunit 4; Apc4 is one of the larger of the subunits of the anaphase-promoting complex or cyclosome. This family represents the long domain downstream of the WD40 repeat/s that are present on the Apc4 subunits. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Results in C.elegans show that the primary essential role of the spindle assembly checkpoint is not in the chromosome segregation process itself but rather in delaying anaphase onset until all chromosomes are properly attached to the spindle. the APC/C is likely to be required for all metaphase-to-anaphase transitions in a multicellular organizm.


:

Pssm-ID: 463744  Cd Length: 203  Bit Score: 219.39  E-value: 1.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  232 SYFQLETNLLYSFLPEVTRMARKFTHISALLQYINLSLTCMCEAWEEILMQMDSRLTKF---VQEKNTTTSVQDEFMHLL 308
Cdd:pfam12896   1 HLLPLDLPFLSSSGRELHLLASKSSQLQSLLRYINQTLKEMQEEWKNARELPDRKLRNLedlLKEQGGESSIVQELYHLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  309 LWGKASAELQTLLMNQLTVKGLKKLGQSIESSYSSIQKLVISHLQSGSESLLYHLSELKGMASWKQKYEPLGLDAAGIEE 388
Cdd:pfam12896  81 LTGHPSPPLKEFLVNQLGERGLKRWEKAVESSYENIRKLVHEHLLPALERLIILLSELRGLAKWHERYEILGLDPELIDE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 557948106  389 AITAVGSFILKANELLQVIDSSMKNFKAFFRWLYVAMLRMTED 431
Cdd:pfam12896 161 LLDTAGSLLLKAHELLQVINEELKLFKAFFRWLRYVIDRLADE 203
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 26-118 1.76e-32

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


:

Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 120.85  E-value: 1.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106   26 LVWSPKRDLIALANTAGEVLLHRLaSFHRVWSFPPnENTGKEVTCLAWRPDGKLLAFALADTkKIVLCDVEKPESLHSFS 105
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLHRL-NWQRVWTLSP-DKEDLEVTSLAWRPDGKLLAVGYSDG-TVRLLDAENGKIVHHFS 77

                          90
                  ....*....|....
gi 557948106  106 VEAP-VSCMHWMEV 118
Cdd:pfam12894  78 AGSDlITCLGWGEN 91
 
Name Accession Description Interval E-value
ANAPC4 pfam12896
Anaphase-promoting complex, cyclosome, subunit 4; Apc4 is one of the larger of the subunits of ...
 232-431 1.90e-66

Anaphase-promoting complex, cyclosome, subunit 4; Apc4 is one of the larger of the subunits of the anaphase-promoting complex or cyclosome. This family represents the long domain downstream of the WD40 repeat/s that are present on the Apc4 subunits. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Results in C.elegans show that the primary essential role of the spindle assembly checkpoint is not in the chromosome segregation process itself but rather in delaying anaphase onset until all chromosomes are properly attached to the spindle. the APC/C is likely to be required for all metaphase-to-anaphase transitions in a multicellular organizm.


Pssm-ID: 463744  Cd Length: 203  Bit Score: 219.39  E-value: 1.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  232 SYFQLETNLLYSFLPEVTRMARKFTHISALLQYINLSLTCMCEAWEEILMQMDSRLTKF---VQEKNTTTSVQDEFMHLL 308
Cdd:pfam12896   1 HLLPLDLPFLSSSGRELHLLASKSSQLQSLLRYINQTLKEMQEEWKNARELPDRKLRNLedlLKEQGGESSIVQELYHLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  309 LWGKASAELQTLLMNQLTVKGLKKLGQSIESSYSSIQKLVISHLQSGSESLLYHLSELKGMASWKQKYEPLGLDAAGIEE 388
Cdd:pfam12896  81 LTGHPSPPLKEFLVNQLGERGLKRWEKAVESSYENIRKLVHEHLLPALERLIILLSELRGLAKWHERYEILGLDPELIDE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 557948106  389 AITAVGSFILKANELLQVIDSSMKNFKAFFRWLYVAMLRMTED 431
Cdd:pfam12896 161 LLDTAGSLLLKAHELLQVINEELKLFKAFFRWLRYVIDRLADE 203
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 26-118 1.76e-32

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 120.85  E-value: 1.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106   26 LVWSPKRDLIALANTAGEVLLHRLaSFHRVWSFPPnENTGKEVTCLAWRPDGKLLAFALADTkKIVLCDVEKPESLHSFS 105
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLHRL-NWQRVWTLSP-DKEDLEVTSLAWRPDGKLLAVGYSDG-TVRLLDAENGKIVHHFS 77

                          90
                  ....*....|....
gi 557948106  106 VEAP-VSCMHWMEV 118
Cdd:pfam12894  78 AGSDlITCLGWGEN 91
WD40 COG2319
WD40 repeat [General function prediction only];
26-105 2.02e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 47.60  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  26 LVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENtgkEVTCLAWRPDGKLLAFALADtKKIVLCDVEKPESLHSFS 105
Cdd:COG2319  168 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTG---AVRSVAFSPDGKLLASGSAD-GTVRLWDLATGKLLRTLT 243
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 26-115 2.01e-03

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 41.17  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  26 LVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENTgkeVTCLAWRPDGKLLAFALADtKKIVLCDVEKPESLHSFS 105
Cdd:cd00200  183 VAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENG---VNSVAFSPDGYLLASGSED-GTIRVWDLRTGECVQTLS 258

                         90
                 ....*....|.
gi 557948106 106 -VEAPVSCMHW 115
Cdd:cd00200  259 gHTNSVTSLAW 269
 
Name Accession Description Interval E-value
ANAPC4 pfam12896
Anaphase-promoting complex, cyclosome, subunit 4; Apc4 is one of the larger of the subunits of ...
 232-431 1.90e-66

Anaphase-promoting complex, cyclosome, subunit 4; Apc4 is one of the larger of the subunits of the anaphase-promoting complex or cyclosome. This family represents the long domain downstream of the WD40 repeat/s that are present on the Apc4 subunits. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Results in C.elegans show that the primary essential role of the spindle assembly checkpoint is not in the chromosome segregation process itself but rather in delaying anaphase onset until all chromosomes are properly attached to the spindle. the APC/C is likely to be required for all metaphase-to-anaphase transitions in a multicellular organizm.


Pssm-ID: 463744  Cd Length: 203  Bit Score: 219.39  E-value: 1.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  232 SYFQLETNLLYSFLPEVTRMARKFTHISALLQYINLSLTCMCEAWEEILMQMDSRLTKF---VQEKNTTTSVQDEFMHLL 308
Cdd:pfam12896   1 HLLPLDLPFLSSSGRELHLLASKSSQLQSLLRYINQTLKEMQEEWKNARELPDRKLRNLedlLKEQGGESSIVQELYHLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  309 LWGKASAELQTLLMNQLTVKGLKKLGQSIESSYSSIQKLVISHLQSGSESLLYHLSELKGMASWKQKYEPLGLDAAGIEE 388
Cdd:pfam12896  81 LTGHPSPPLKEFLVNQLGERGLKRWEKAVESSYENIRKLVHEHLLPALERLIILLSELRGLAKWHERYEILGLDPELIDE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 557948106  389 AITAVGSFILKANELLQVIDSSMKNFKAFFRWLYVAMLRMTED 431
Cdd:pfam12896 161 LLDTAGSLLLKAHELLQVINEELKLFKAFFRWLRYVIDRLADE 203
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 26-118 1.76e-32

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 120.85  E-value: 1.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106   26 LVWSPKRDLIALANTAGEVLLHRLaSFHRVWSFPPnENTGKEVTCLAWRPDGKLLAFALADTkKIVLCDVEKPESLHSFS 105
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLHRL-NWQRVWTLSP-DKEDLEVTSLAWRPDGKLLAVGYSDG-TVRLLDAENGKIVHHFS 77

                          90
                  ....*....|....
gi 557948106  106 VEAP-VSCMHWMEV 118
Cdd:pfam12894  78 AGSDlITCLGWGEN 91
WD40 COG2319
WD40 repeat [General function prediction only];
26-105 2.02e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 47.60  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  26 LVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENtgkEVTCLAWRPDGKLLAFALADtKKIVLCDVEKPESLHSFS 105
Cdd:COG2319  168 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTG---AVRSVAFSPDGKLLASGSAD-GTVRLWDLATGKLLRTLT 243
WD40 COG2319
WD40 repeat [General function prediction only];
22-105 6.24e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.06  E-value: 6.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  22 EIIFLVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENTgkeVTCLAWRPDGKLLAFALADtKKIVLCDVEKPESL 101
Cdd:COG2319  248 SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGG---VNSVAFSPDGKLLASGSDD-GTVRLWDLATGKLL 323


                 ....
gi 557948106 102 HSFS 105
Cdd:COG2319  324 RTLT 327
WD40 COG2319
WD40 repeat [General function prediction only];
26-105 6.63e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.06  E-value: 6.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  26 LVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENtgkEVTCLAWRPDGKLLAFALADtKKIVLCDVEKPESLHSFS 105
Cdd:COG2319  210 VAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSG---SVRSVAFSPDGRLLASGSAD-GTVRLWDLATGELLRTLT 285
WD40 COG2319
WD40 repeat [General function prediction only];
26-115 3.27e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 43.75  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  26 LVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENTgkeVTCLAWRPDGKLLAFALADtKKIVLCDVEKPESLHSFS 105
Cdd:COG2319  126 VAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGA---VTSVAFSPDGKLLASGSDD-GTVRLWDLATGKLLRTLT 201

                         90
                 ....*....|.
gi 557948106 106 V-EAPVSCMHW 115
Cdd:COG2319  202 GhTGAVRSVAF 212
WD40 COG2319
WD40 repeat [General function prediction only];
26-105 5.56e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.98  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  26 LVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENTgkeVTCLAWRPDGKLLAFALADtKKIVLCDVEKPESLHSFS 105
Cdd:COG2319  294 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGA---VRSVAFSPDGKTLASGSDD-GTVRLWDLATGELLRTLT 369
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 26-115 2.01e-03

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 41.17  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  26 LVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENTgkeVTCLAWRPDGKLLAFALADtKKIVLCDVEKPESLHSFS 105
Cdd:cd00200  183 VAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENG---VNSVAFSPDGYLLASGSED-GTIRVWDLRTGECVQTLS 258

                         90
                 ....*....|.
gi 557948106 106 -VEAPVSCMHW 115
Cdd:cd00200  259 gHTNSVTSLAW 269
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 26-97 4.26e-03

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 40.79  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106   26 LVWSPKRDLIALANTAGEVLLHRLAS-----------FHRVWSFppnentgkevtclAWRPDGKLLAFALADT---KKIV 91
Cdd:COG4946   394 PVWSPDGKKIAFTDNRGRLWVVDLASgkvrkvdtdgyGDGISDL-------------AWSPDSKWLAYSKPGPnqlSQIF 460


                  ....*.
gi 557948106   92 LCDVEK 97
Cdd:COG4946   461 LYDVET 466
WD40 COG2319
WD40 repeat [General function prediction only];
23-105 5.11e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.89  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948106  23 IIFLVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENTgkeVTCLAWRPDGKLLAFALADtKKIVLCDVEKPESLH 102
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGA---VRSVAFSPDGKTLASGSAD-GTVRLWDLATGKLLR 156


                 ...
gi 557948106 103 SFS 105
Cdd:COG2319  157 TLT 159
 
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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