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Conserved domains on  [gi|228008323|ref|NP_032595|]
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anaphase-promoting complex subunit 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Apc1_MidN super family cl48671
Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the ...
615-985 0e+00

Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Apc1 consists of a N-terminal WD40 beta-propeller domain, followed by the middle domain (Mid-N), a PC domain and the C-terminal domain (MidC). This entry represents the middle domain of Apc1, MidN (also referred to as the first helical domain), that coaleses with the C-terminal domain to form Apc1Mid that connects Apc1WD40 with Apc1PC. Apc1Mid consists of an alpha-solenoid capped by a beta-sandwich.


The actual alignment was detected with superfamily member pfam20518:

Pssm-ID: 466667  Cd Length: 371  Bit Score: 709.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   615 SELVQTCLQAIKFILPKEVAIQVLVKWYNVHSAPGGPSCHSEWSLFVICLLNMMGYNTDRLAWTRSFDFEGSLSPVIAPK 694
Cdd:pfam20518    1 SELVQTCLQAIKFILPKEIAVQMLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   695 KARPSDTGSDEDWEYLLNSEYHRNVESHLLNKSLCLTALEVSNAKDEDFSQNLSLDSSTLLFAHIPAIFFVLHLVYEELK 774
Cdd:pfam20518   81 KARPSETGSDDDWEYLLNSDYHQNVESHLLNRSLCLSPSEASQMKDEDFSQNLSLDSSTLLFTHIPAIFFVLHLVYEELK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   775 LNTLMGEGICSLIDLLVQLARDLKLDSYLDHYYRDSPTLVKTTGQVCTIDQGQMGFMHHPPFFTSEPPSIYQWVSSCLKG 854
Cdd:pfam20518  161 LNTLMGEGICSLVELLVQLARDLKLGPYVDHYYRDYPTLVRTTGQVCTIDPGQTGFMHHPSFFTSEPPSIYQWVSSCLKG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   855 EGMPPYPYLPGICERSRLVVLSIALYTLGDESCVSDETCQYLSKVTSTPQKPQAEQEENRFTFRHSASVSVLAERLVVWM 934
Cdd:pfam20518  241 EGMPPYPYLPGICERSRLVVLSIALYILGDESLVSDESSQYLTRITIAPQKLQVEQEENRFSFRHSTSVSSLAERLVVWM 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 228008323   935 ASVGFTLRDLETLPFGIALPIRDAIYHCREQPDSDWSEAVCLLIGRQDLSK 985
Cdd:pfam20518  321 TNVGFTLRDLETLPFGIALPIRDAIYHCREQPASDWPEAVCLLIGRQDLSK 371
Apc1_N pfam19521
Anaphase-promoting complex subunit 1 N-terminal; The anaphase-promoting complex subunit 1 ...
1-136 1.17e-94

Anaphase-promoting complex subunit 1 N-terminal; The anaphase-promoting complex subunit 1 (Apc1) is the largest scaffolding subunit that constitutes anaphase-promoting complex/cyclosome (APC/C), the crucial RING E3 ubiquitin ligase that controls cell cycle processes like sister chromatid segregation, cytokinesis and the initiation of chromosome replication. This domain represents the Apc1 N-terminal region that is rich in beta-strands and regulatory phosphorylation sites. It contains WD40 repeats and is essential for APC/C catalytic activity as it mediates the coactivator-induced conformational change of the APC/C which promotes UbcH10 binding.


:

Pssm-ID: 437353  Cd Length: 136  Bit Score: 301.50  E-value: 1.17e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323     1 MSNFSEERATMIAAGDLQEFVPFGRDHCKHHPNALNLQLRQLQPASELWSSDGAAGLVGSLQEVTIHEKQKESWQLRKGV 80
Cdd:pfam19521    1 MSVVYEERATMIAAGDLQEFVPFGREHCKNHPNALNLQLRQLQPASELWSSDGAAGLVGSLQEVTIHERQKESWQLRKGV 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 228008323    81 SEIGDAADYDEELYVAGNMVIWSKGSKSQALAVYKAFTVDSTVQQALWCDFIISQD 136
Cdd:pfam19521   81 SDVGDEVEYDEELYVAGNMVIWSKGSKTQASAVYKAFTVDSPVQQALWCDFTVPQE 136
APC1_C pfam18122
Anaphase-promoting complex sub unit 1 C-terminal domain; This is the C-terminal domain of ...
1739-1895 2.17e-48

Anaphase-promoting complex sub unit 1 C-terminal domain; This is the C-terminal domain of chain A, also known as sub-unit 1, found in anaphase-promoting complex (APC/C) present in Homo sapiens. APC/C is an ubiquitin ligase that controls chromosome segregation and mitotic exit.


:

Pssm-ID: 465659  Cd Length: 159  Bit Score: 170.24  E-value: 2.17e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323  1739 SSFTSDPALLSFAEYFCKPTVSMGPKQEILDLFSSILYECVAQETPEMLPAYIAMDQALRSLKKRDMSDTSDLWQIKLIL 1818
Cdd:pfam18122    1 KSFSSDPSLLAFADYFCTPSSNTEAEVDFAAFCSSVLLECLTQDKPELLPTYLALYSAIQNLEASSSPASLALWQLRLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323  1819 EFFSSRSHQDRQHTYPKRGLFINSEFLPVVKCTVDATLDQWLQAGGDVcVHAYLSGQ---PVEKSQLNMLACFLVYHSVP 1895
Cdd:pfam18122   81 EFYGSLYFLRFSGRGESREPLIRSSFLLSLKSRVDAKLDEWLKEGSNL-LRRYLRGGgdgSSDSSLLRMLAAYLVFYDIP 159
ANAPC1 super family cl15124
Anaphase-promoting complex subunit 1 WD40 beta-propeller domain; Apc1 is the largest of the ...
151-359 7.12e-13

Anaphase-promoting complex subunit 1 WD40 beta-propeller domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Infection of human fibroblasts with human cytomegalovirus (HCMV) leads to cell cycle dysregulation, which is associated with the inactivation of the anaphase-promoting complex. Apc1 consists of a N-terminal WD40 beta-propeller domain, a middle domain (Mid-N), a PC domain and a C-terminal domain (Mid-C) that coalesces with Mid-N to form Apc1Mid which connects Apc1-WD40 with Apc1-PC and comprises an alpha-solenoid capped by a beta-sandwich. The N-terminal domain is essential for APC/C catalytic activity as it mediates the coactivator-induced conformational change of the APC/C which promotes UbcH10 binding.


The actual alignment was detected with superfamily member pfam12859:

Pssm-ID: 463732  Cd Length: 295  Bit Score: 71.31  E-value: 7.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   151 ICILQSSCMNMHSIDGKDYIASLPFQVANVWATKYGLLFERCSSS-HEVPPSLPREP----------------------- 206
Cdd:pfam12859    2 LVVFLKTQAHIYFLSGESHVVPLPFEVESAFPAPRGLLLQRKLEEdERSSLKFPAAPpnsfvssqsspldrsrkslgnpr 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   207 ------------------------LPTMFSMLHPLDEITPLVCKSGSLFGSSRVQ------YVVDPAVKIVF-------- 248
Cdd:pfam12859   82 rssltlsstlgdmwdpppedsdsdLPRLFSLTDPLSELGLVVTSSQSSRSSSPRRdsspqpEFLDPAEEILYvsdldest 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   249 -LNIDPSIVM-TYDAVQNVHSVWTLRRVKPEEENAVLKFPEQA-------GTLQNATTSSSLTAHLRSlSKGESPVASPF 319
Cdd:pfam12859  162 iWTSDPLPLVvTLNRETSQYTIWRAEYLESESESSSSKKRKRSrrrssfmGMATGATTPVARPSNLRE-SFGPLSGKRPR 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 228008323   320 QNYSSIHSQSRSTSSPSLHSRSPSISNMAALSRAHSPALG 359
Cdd:pfam12859  241 SSESHSDEKDEEDLASQLDPDFDDIGVPRRSSRRVSSLLA 280
PC_rep pfam01851
Proteasome/cyclosome repeat;
1467-1501 1.13e-03

Proteasome/cyclosome repeat;


:

Pssm-ID: 460361 [Multi-domain]  Cd Length: 35  Bit Score: 38.17  E-value: 1.13e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 228008323  1467 GACLSLGFRFAGSENLSAFSCLHKFAKDFMNYLSA 1501
Cdd:pfam01851    1 GAALALGLIHAGSGNEEALDLLLPYLSDTSAESRA 35
 
Name Accession Description Interval E-value
Apc1_MidN pfam20518
Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the ...
615-985 0e+00

Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Apc1 consists of a N-terminal WD40 beta-propeller domain, followed by the middle domain (Mid-N), a PC domain and the C-terminal domain (MidC). This entry represents the middle domain of Apc1, MidN (also referred to as the first helical domain), that coaleses with the C-terminal domain to form Apc1Mid that connects Apc1WD40 with Apc1PC. Apc1Mid consists of an alpha-solenoid capped by a beta-sandwich.


Pssm-ID: 466667  Cd Length: 371  Bit Score: 709.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   615 SELVQTCLQAIKFILPKEVAIQVLVKWYNVHSAPGGPSCHSEWSLFVICLLNMMGYNTDRLAWTRSFDFEGSLSPVIAPK 694
Cdd:pfam20518    1 SELVQTCLQAIKFILPKEIAVQMLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   695 KARPSDTGSDEDWEYLLNSEYHRNVESHLLNKSLCLTALEVSNAKDEDFSQNLSLDSSTLLFAHIPAIFFVLHLVYEELK 774
Cdd:pfam20518   81 KARPSETGSDDDWEYLLNSDYHQNVESHLLNRSLCLSPSEASQMKDEDFSQNLSLDSSTLLFTHIPAIFFVLHLVYEELK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   775 LNTLMGEGICSLIDLLVQLARDLKLDSYLDHYYRDSPTLVKTTGQVCTIDQGQMGFMHHPPFFTSEPPSIYQWVSSCLKG 854
Cdd:pfam20518  161 LNTLMGEGICSLVELLVQLARDLKLGPYVDHYYRDYPTLVRTTGQVCTIDPGQTGFMHHPSFFTSEPPSIYQWVSSCLKG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   855 EGMPPYPYLPGICERSRLVVLSIALYTLGDESCVSDETCQYLSKVTSTPQKPQAEQEENRFTFRHSASVSVLAERLVVWM 934
Cdd:pfam20518  241 EGMPPYPYLPGICERSRLVVLSIALYILGDESLVSDESSQYLTRITIAPQKLQVEQEENRFSFRHSTSVSSLAERLVVWM 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 228008323   935 ASVGFTLRDLETLPFGIALPIRDAIYHCREQPDSDWSEAVCLLIGRQDLSK 985
Cdd:pfam20518  321 TNVGFTLRDLETLPFGIALPIRDAIYHCREQPASDWPEAVCLLIGRQDLSK 371
Apc1_N pfam19521
Anaphase-promoting complex subunit 1 N-terminal; The anaphase-promoting complex subunit 1 ...
1-136 1.17e-94

Anaphase-promoting complex subunit 1 N-terminal; The anaphase-promoting complex subunit 1 (Apc1) is the largest scaffolding subunit that constitutes anaphase-promoting complex/cyclosome (APC/C), the crucial RING E3 ubiquitin ligase that controls cell cycle processes like sister chromatid segregation, cytokinesis and the initiation of chromosome replication. This domain represents the Apc1 N-terminal region that is rich in beta-strands and regulatory phosphorylation sites. It contains WD40 repeats and is essential for APC/C catalytic activity as it mediates the coactivator-induced conformational change of the APC/C which promotes UbcH10 binding.


Pssm-ID: 437353  Cd Length: 136  Bit Score: 301.50  E-value: 1.17e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323     1 MSNFSEERATMIAAGDLQEFVPFGRDHCKHHPNALNLQLRQLQPASELWSSDGAAGLVGSLQEVTIHEKQKESWQLRKGV 80
Cdd:pfam19521    1 MSVVYEERATMIAAGDLQEFVPFGREHCKNHPNALNLQLRQLQPASELWSSDGAAGLVGSLQEVTIHERQKESWQLRKGV 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 228008323    81 SEIGDAADYDEELYVAGNMVIWSKGSKSQALAVYKAFTVDSTVQQALWCDFIISQD 136
Cdd:pfam19521   81 SDVGDEVEYDEELYVAGNMVIWSKGSKTQASAVYKAFTVDSPVQQALWCDFTVPQE 136
APC1_C pfam18122
Anaphase-promoting complex sub unit 1 C-terminal domain; This is the C-terminal domain of ...
1739-1895 2.17e-48

Anaphase-promoting complex sub unit 1 C-terminal domain; This is the C-terminal domain of chain A, also known as sub-unit 1, found in anaphase-promoting complex (APC/C) present in Homo sapiens. APC/C is an ubiquitin ligase that controls chromosome segregation and mitotic exit.


Pssm-ID: 465659  Cd Length: 159  Bit Score: 170.24  E-value: 2.17e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323  1739 SSFTSDPALLSFAEYFCKPTVSMGPKQEILDLFSSILYECVAQETPEMLPAYIAMDQALRSLKKRDMSDTSDLWQIKLIL 1818
Cdd:pfam18122    1 KSFSSDPSLLAFADYFCTPSSNTEAEVDFAAFCSSVLLECLTQDKPELLPTYLALYSAIQNLEASSSPASLALWQLRLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323  1819 EFFSSRSHQDRQHTYPKRGLFINSEFLPVVKCTVDATLDQWLQAGGDVcVHAYLSGQ---PVEKSQLNMLACFLVYHSVP 1895
Cdd:pfam18122   81 EFYGSLYFLRFSGRGESREPLIRSSFLLSLKSRVDAKLDEWLKEGSNL-LRRYLRGGgdgSSDSSLLRMLAAYLVFYDIP 159
ANAPC1 pfam12859
Anaphase-promoting complex subunit 1 WD40 beta-propeller domain; Apc1 is the largest of the ...
151-359 7.12e-13

Anaphase-promoting complex subunit 1 WD40 beta-propeller domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Infection of human fibroblasts with human cytomegalovirus (HCMV) leads to cell cycle dysregulation, which is associated with the inactivation of the anaphase-promoting complex. Apc1 consists of a N-terminal WD40 beta-propeller domain, a middle domain (Mid-N), a PC domain and a C-terminal domain (Mid-C) that coalesces with Mid-N to form Apc1Mid which connects Apc1-WD40 with Apc1-PC and comprises an alpha-solenoid capped by a beta-sandwich. The N-terminal domain is essential for APC/C catalytic activity as it mediates the coactivator-induced conformational change of the APC/C which promotes UbcH10 binding.


Pssm-ID: 463732  Cd Length: 295  Bit Score: 71.31  E-value: 7.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   151 ICILQSSCMNMHSIDGKDYIASLPFQVANVWATKYGLLFERCSSS-HEVPPSLPREP----------------------- 206
Cdd:pfam12859    2 LVVFLKTQAHIYFLSGESHVVPLPFEVESAFPAPRGLLLQRKLEEdERSSLKFPAAPpnsfvssqsspldrsrkslgnpr 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   207 ------------------------LPTMFSMLHPLDEITPLVCKSGSLFGSSRVQ------YVVDPAVKIVF-------- 248
Cdd:pfam12859   82 rssltlsstlgdmwdpppedsdsdLPRLFSLTDPLSELGLVVTSSQSSRSSSPRRdsspqpEFLDPAEEILYvsdldest 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   249 -LNIDPSIVM-TYDAVQNVHSVWTLRRVKPEEENAVLKFPEQA-------GTLQNATTSSSLTAHLRSlSKGESPVASPF 319
Cdd:pfam12859  162 iWTSDPLPLVvTLNRETSQYTIWRAEYLESESESSSSKKRKRSrrrssfmGMATGATTPVARPSNLRE-SFGPLSGKRPR 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 228008323   320 QNYSSIHSQSRSTSSPSLHSRSPSISNMAALSRAHSPALG 359
Cdd:pfam12859  241 SSESHSDEKDEEDLASQLDPDFDDIGVPRRSSRRVSSLLA 280
PC_rep pfam01851
Proteasome/cyclosome repeat;
1467-1501 1.13e-03

Proteasome/cyclosome repeat;


Pssm-ID: 460361 [Multi-domain]  Cd Length: 35  Bit Score: 38.17  E-value: 1.13e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 228008323  1467 GACLSLGFRFAGSENLSAFSCLHKFAKDFMNYLSA 1501
Cdd:pfam01851    1 GAALALGLIHAGSGNEEALDLLLPYLSDTSAESRA 35
 
Name Accession Description Interval E-value
Apc1_MidN pfam20518
Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the ...
615-985 0e+00

Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Apc1 consists of a N-terminal WD40 beta-propeller domain, followed by the middle domain (Mid-N), a PC domain and the C-terminal domain (MidC). This entry represents the middle domain of Apc1, MidN (also referred to as the first helical domain), that coaleses with the C-terminal domain to form Apc1Mid that connects Apc1WD40 with Apc1PC. Apc1Mid consists of an alpha-solenoid capped by a beta-sandwich.


Pssm-ID: 466667  Cd Length: 371  Bit Score: 709.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   615 SELVQTCLQAIKFILPKEVAIQVLVKWYNVHSAPGGPSCHSEWSLFVICLLNMMGYNTDRLAWTRSFDFEGSLSPVIAPK 694
Cdd:pfam20518    1 SELVQTCLQAIKFILPKEIAVQMLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   695 KARPSDTGSDEDWEYLLNSEYHRNVESHLLNKSLCLTALEVSNAKDEDFSQNLSLDSSTLLFAHIPAIFFVLHLVYEELK 774
Cdd:pfam20518   81 KARPSETGSDDDWEYLLNSDYHQNVESHLLNRSLCLSPSEASQMKDEDFSQNLSLDSSTLLFTHIPAIFFVLHLVYEELK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   775 LNTLMGEGICSLIDLLVQLARDLKLDSYLDHYYRDSPTLVKTTGQVCTIDQGQMGFMHHPPFFTSEPPSIYQWVSSCLKG 854
Cdd:pfam20518  161 LNTLMGEGICSLVELLVQLARDLKLGPYVDHYYRDYPTLVRTTGQVCTIDPGQTGFMHHPSFFTSEPPSIYQWVSSCLKG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   855 EGMPPYPYLPGICERSRLVVLSIALYTLGDESCVSDETCQYLSKVTSTPQKPQAEQEENRFTFRHSASVSVLAERLVVWM 934
Cdd:pfam20518  241 EGMPPYPYLPGICERSRLVVLSIALYILGDESLVSDESSQYLTRITIAPQKLQVEQEENRFSFRHSTSVSSLAERLVVWM 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 228008323   935 ASVGFTLRDLETLPFGIALPIRDAIYHCREQPDSDWSEAVCLLIGRQDLSK 985
Cdd:pfam20518  321 TNVGFTLRDLETLPFGIALPIRDAIYHCREQPASDWPEAVCLLIGRQDLSK 371
Apc1_N pfam19521
Anaphase-promoting complex subunit 1 N-terminal; The anaphase-promoting complex subunit 1 ...
1-136 1.17e-94

Anaphase-promoting complex subunit 1 N-terminal; The anaphase-promoting complex subunit 1 (Apc1) is the largest scaffolding subunit that constitutes anaphase-promoting complex/cyclosome (APC/C), the crucial RING E3 ubiquitin ligase that controls cell cycle processes like sister chromatid segregation, cytokinesis and the initiation of chromosome replication. This domain represents the Apc1 N-terminal region that is rich in beta-strands and regulatory phosphorylation sites. It contains WD40 repeats and is essential for APC/C catalytic activity as it mediates the coactivator-induced conformational change of the APC/C which promotes UbcH10 binding.


Pssm-ID: 437353  Cd Length: 136  Bit Score: 301.50  E-value: 1.17e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323     1 MSNFSEERATMIAAGDLQEFVPFGRDHCKHHPNALNLQLRQLQPASELWSSDGAAGLVGSLQEVTIHEKQKESWQLRKGV 80
Cdd:pfam19521    1 MSVVYEERATMIAAGDLQEFVPFGREHCKNHPNALNLQLRQLQPASELWSSDGAAGLVGSLQEVTIHERQKESWQLRKGV 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 228008323    81 SEIGDAADYDEELYVAGNMVIWSKGSKSQALAVYKAFTVDSTVQQALWCDFIISQD 136
Cdd:pfam19521   81 SDVGDEVEYDEELYVAGNMVIWSKGSKTQASAVYKAFTVDSPVQQALWCDFTVPQE 136
APC1_C pfam18122
Anaphase-promoting complex sub unit 1 C-terminal domain; This is the C-terminal domain of ...
1739-1895 2.17e-48

Anaphase-promoting complex sub unit 1 C-terminal domain; This is the C-terminal domain of chain A, also known as sub-unit 1, found in anaphase-promoting complex (APC/C) present in Homo sapiens. APC/C is an ubiquitin ligase that controls chromosome segregation and mitotic exit.


Pssm-ID: 465659  Cd Length: 159  Bit Score: 170.24  E-value: 2.17e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323  1739 SSFTSDPALLSFAEYFCKPTVSMGPKQEILDLFSSILYECVAQETPEMLPAYIAMDQALRSLKKRDMSDTSDLWQIKLIL 1818
Cdd:pfam18122    1 KSFSSDPSLLAFADYFCTPSSNTEAEVDFAAFCSSVLLECLTQDKPELLPTYLALYSAIQNLEASSSPASLALWQLRLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323  1819 EFFSSRSHQDRQHTYPKRGLFINSEFLPVVKCTVDATLDQWLQAGGDVcVHAYLSGQ---PVEKSQLNMLACFLVYHSVP 1895
Cdd:pfam18122   81 EFYGSLYFLRFSGRGESREPLIRSSFLLSLKSRVDAKLDEWLKEGSNL-LRRYLRGGgdgSSDSSLLRMLAAYLVFYDIP 159
ANAPC1 pfam12859
Anaphase-promoting complex subunit 1 WD40 beta-propeller domain; Apc1 is the largest of the ...
151-359 7.12e-13

Anaphase-promoting complex subunit 1 WD40 beta-propeller domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Infection of human fibroblasts with human cytomegalovirus (HCMV) leads to cell cycle dysregulation, which is associated with the inactivation of the anaphase-promoting complex. Apc1 consists of a N-terminal WD40 beta-propeller domain, a middle domain (Mid-N), a PC domain and a C-terminal domain (Mid-C) that coalesces with Mid-N to form Apc1Mid which connects Apc1-WD40 with Apc1-PC and comprises an alpha-solenoid capped by a beta-sandwich. The N-terminal domain is essential for APC/C catalytic activity as it mediates the coactivator-induced conformational change of the APC/C which promotes UbcH10 binding.


Pssm-ID: 463732  Cd Length: 295  Bit Score: 71.31  E-value: 7.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   151 ICILQSSCMNMHSIDGKDYIASLPFQVANVWATKYGLLFERCSSS-HEVPPSLPREP----------------------- 206
Cdd:pfam12859    2 LVVFLKTQAHIYFLSGESHVVPLPFEVESAFPAPRGLLLQRKLEEdERSSLKFPAAPpnsfvssqsspldrsrkslgnpr 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   207 ------------------------LPTMFSMLHPLDEITPLVCKSGSLFGSSRVQ------YVVDPAVKIVF-------- 248
Cdd:pfam12859   82 rssltlsstlgdmwdpppedsdsdLPRLFSLTDPLSELGLVVTSSQSSRSSSPRRdsspqpEFLDPAEEILYvsdldest 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008323   249 -LNIDPSIVM-TYDAVQNVHSVWTLRRVKPEEENAVLKFPEQA-------GTLQNATTSSSLTAHLRSlSKGESPVASPF 319
Cdd:pfam12859  162 iWTSDPLPLVvTLNRETSQYTIWRAEYLESESESSSSKKRKRSrrrssfmGMATGATTPVARPSNLRE-SFGPLSGKRPR 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 228008323   320 QNYSSIHSQSRSTSSPSLHSRSPSISNMAALSRAHSPALG 359
Cdd:pfam12859  241 SSESHSDEKDEEDLASQLDPDFDDIGVPRRSSRRVSSLLA 280
PC_rep pfam01851
Proteasome/cyclosome repeat;
1467-1501 1.13e-03

Proteasome/cyclosome repeat;


Pssm-ID: 460361 [Multi-domain]  Cd Length: 35  Bit Score: 38.17  E-value: 1.13e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 228008323  1467 GACLSLGFRFAGSENLSAFSCLHKFAKDFMNYLSA 1501
Cdd:pfam01851    1 GAALALGLIHAGSGNEEALDLLLPYLSDTSAESRA 35
 
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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