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Conserved domains on  [gi|1720397514|ref|XP_030103946|]
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anaphase-promoting complex subunit 1 isoform X1 [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 ...
497-867 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 1720397514  497 SELVQTCLQAIKFILPKEVAIQVLVKWYNVHSAPGGPSCHSEWSLFVICLLNMMGYNTDRLAWTRSFDFEGSLSPVIAPK 576
Cdd:pfam20518    1 SELVQTCLQAIKFILPKEIAVQMLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  577 KARPSDTGSDEDWEYLLNSEYHRNVESHLLNKSLCLTALEVSNAKDEDFSQNLSLDSSTLLFAHIPAIFFVLHLVYEELK 656
Cdd:pfam20518   81 KARPSETGSDDDWEYLLNSDYHQNVESHLLNRSLCLSPSEASQMKDEDFSQNLSLDSSTLLFTHIPAIFFVLHLVYEELK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  657 LNTLMGEGICSLIDLLVQLARDLKLDSYLDHYYRDSPTLVKTTGQVCTIDQGQMGFMHHPPFFTSEPPSIYQWVSSCLKG 736
Cdd:pfam20518  161 LNTLMGEGICSLVELLVQLARDLKLGPYVDHYYRDYPTLVRTTGQVCTIDPGQTGFMHHPSFFTSEPPSIYQWVSSCLKG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  737 EGMPPYPYLPGICERSRLVVLSIALYTLGDESCVSDETCQYLSKVTSTPQKPQAEQEENRFTFRHSASVSVLAERLVVWM 816
Cdd:pfam20518  241 EGMPPYPYLPGICERSRLVVLSIALYILGDESLVSDESSQYLTRITIAPQKLQVEQEENRFSFRHSTSVSSLAERLVVWM 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720397514  817 ASVGFTLRDLETLPFGIALPIRDAIYHCREQPDSDWSEAVCLLIGRQDLSK 867
Cdd:pfam20518  321 TNVGFTLRDLETLPFGIALPIRDAIYHCREQPASDWPEAVCLLIGRQDLSK 371
APC1_C pfam18122
Anaphase-promoting complex sub unit 1 C-terminal domain; This is the C-terminal domain of ...
1621-1777 2.19e-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: 169.85  E-value: 2.19e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514 1621 SSFTSDPALLSFAEYFCKPTVSMGPKQEILDLFSSILYECVAQETPEMLPAYIAMDQALRSLKKRDMSDTSDLWQIKLIL 1700
Cdd:pfam18122    1 KSFSSDPSLLAFADYFCTPSSNTEAEVDFAAFCSSVLLECLTQDKPELLPTYLALYSAIQNLEASSSPASLALWQLRLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514 1701 EFFSSRSHQDRQHTYPKRGLFINSEFLPVVKCTVDATLDQWLQAGGDVcVHAYLSGQ---PVEKSQLNMLACFLVYHSVP 1777
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 ...
76-241 2.46e-08

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: 57.44  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514   76 SSHEVPPSLPREPLPTMFSMLHPLDEITPLVCKSGSLFGSSRVQ------YVVDPAVKIVF---------LNIDPSIVM- 139
Cdd:pfam12859   93 DMWDPPPEDSDSDLPRLFSLTDPLSELGLVVTSSQSSRSSSPRRdsspqpEFLDPAEEILYvsdldestiWTSDPLPLVv 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  140 TYDAVQNVHSVWTLRRVKPEEENAVLKFPEQA-------GTLQNATTSSSLTAHLRSlSKGESPVASPFQNYSSIHSQSR 212
Cdd:pfam12859  173 TLNRETSQYTIWRAEYLESESESSSSKKRKRSrrrssfmGMATGATTPVARPSNLRE-SFGPLSGKRPRSSESHSDEKDE 251
                          170       180
                   ....*....|....*....|....*....
gi 1720397514  213 STSSPSLHSRSPSISNMAALSRAHSPALG 241
Cdd:pfam12859  252 EDLASQLDPDFDDIGVPRRSSRRVSSLLA 280
PC_rep pfam01851
Proteasome/cyclosome repeat;
1349-1383 1.01e-03

Proteasome/cyclosome repeat;


:

Pssm-ID: 460361 [Multi-domain]  Cd Length: 35  Bit Score: 38.17  E-value: 1.01e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720397514 1349 GACLSLGFRFAGSENLSAFSCLHKFAKDFMNYLSA 1383
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 ...
497-867 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 1720397514  497 SELVQTCLQAIKFILPKEVAIQVLVKWYNVHSAPGGPSCHSEWSLFVICLLNMMGYNTDRLAWTRSFDFEGSLSPVIAPK 576
Cdd:pfam20518    1 SELVQTCLQAIKFILPKEIAVQMLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  577 KARPSDTGSDEDWEYLLNSEYHRNVESHLLNKSLCLTALEVSNAKDEDFSQNLSLDSSTLLFAHIPAIFFVLHLVYEELK 656
Cdd:pfam20518   81 KARPSETGSDDDWEYLLNSDYHQNVESHLLNRSLCLSPSEASQMKDEDFSQNLSLDSSTLLFTHIPAIFFVLHLVYEELK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  657 LNTLMGEGICSLIDLLVQLARDLKLDSYLDHYYRDSPTLVKTTGQVCTIDQGQMGFMHHPPFFTSEPPSIYQWVSSCLKG 736
Cdd:pfam20518  161 LNTLMGEGICSLVELLVQLARDLKLGPYVDHYYRDYPTLVRTTGQVCTIDPGQTGFMHHPSFFTSEPPSIYQWVSSCLKG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  737 EGMPPYPYLPGICERSRLVVLSIALYTLGDESCVSDETCQYLSKVTSTPQKPQAEQEENRFTFRHSASVSVLAERLVVWM 816
Cdd:pfam20518  241 EGMPPYPYLPGICERSRLVVLSIALYILGDESLVSDESSQYLTRITIAPQKLQVEQEENRFSFRHSTSVSSLAERLVVWM 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720397514  817 ASVGFTLRDLETLPFGIALPIRDAIYHCREQPDSDWSEAVCLLIGRQDLSK 867
Cdd:pfam20518  321 TNVGFTLRDLETLPFGIALPIRDAIYHCREQPASDWPEAVCLLIGRQDLSK 371
APC1_C pfam18122
Anaphase-promoting complex sub unit 1 C-terminal domain; This is the C-terminal domain of ...
1621-1777 2.19e-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: 169.85  E-value: 2.19e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514 1621 SSFTSDPALLSFAEYFCKPTVSMGPKQEILDLFSSILYECVAQETPEMLPAYIAMDQALRSLKKRDMSDTSDLWQIKLIL 1700
Cdd:pfam18122    1 KSFSSDPSLLAFADYFCTPSSNTEAEVDFAAFCSSVLLECLTQDKPELLPTYLALYSAIQNLEASSSPASLALWQLRLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514 1701 EFFSSRSHQDRQHTYPKRGLFINSEFLPVVKCTVDATLDQWLQAGGDVcVHAYLSGQ---PVEKSQLNMLACFLVYHSVP 1777
Cdd:pfam18122   81 EFYGSLYFLRFSGRGESREPLIRSSFLLSLKSRVDAKLDEWLKEGSNL-LRRYLRGGgdgSSDSSLLRMLAAYLVFYDIP 159
ANAPC1 pfam12859
Anaphase-promoting complex subunit 1 WD40 beta-propeller domain; Apc1 is the largest of the ...
76-241 2.46e-08

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: 57.44  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514   76 SSHEVPPSLPREPLPTMFSMLHPLDEITPLVCKSGSLFGSSRVQ------YVVDPAVKIVF---------LNIDPSIVM- 139
Cdd:pfam12859   93 DMWDPPPEDSDSDLPRLFSLTDPLSELGLVVTSSQSSRSSSPRRdsspqpEFLDPAEEILYvsdldestiWTSDPLPLVv 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  140 TYDAVQNVHSVWTLRRVKPEEENAVLKFPEQA-------GTLQNATTSSSLTAHLRSlSKGESPVASPFQNYSSIHSQSR 212
Cdd:pfam12859  173 TLNRETSQYTIWRAEYLESESESSSSKKRKRSrrrssfmGMATGATTPVARPSNLRE-SFGPLSGKRPRSSESHSDEKDE 251
                          170       180
                   ....*....|....*....|....*....
gi 1720397514  213 STSSPSLHSRSPSISNMAALSRAHSPALG 241
Cdd:pfam12859  252 EDLASQLDPDFDDIGVPRRSSRRVSSLLA 280
PC_rep pfam01851
Proteasome/cyclosome repeat;
1349-1383 1.01e-03

Proteasome/cyclosome repeat;


Pssm-ID: 460361 [Multi-domain]  Cd Length: 35  Bit Score: 38.17  E-value: 1.01e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720397514 1349 GACLSLGFRFAGSENLSAFSCLHKFAKDFMNYLSA 1383
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 ...
497-867 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 1720397514  497 SELVQTCLQAIKFILPKEVAIQVLVKWYNVHSAPGGPSCHSEWSLFVICLLNMMGYNTDRLAWTRSFDFEGSLSPVIAPK 576
Cdd:pfam20518    1 SELVQTCLQAIKFILPKEIAVQMLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  577 KARPSDTGSDEDWEYLLNSEYHRNVESHLLNKSLCLTALEVSNAKDEDFSQNLSLDSSTLLFAHIPAIFFVLHLVYEELK 656
Cdd:pfam20518   81 KARPSETGSDDDWEYLLNSDYHQNVESHLLNRSLCLSPSEASQMKDEDFSQNLSLDSSTLLFTHIPAIFFVLHLVYEELK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  657 LNTLMGEGICSLIDLLVQLARDLKLDSYLDHYYRDSPTLVKTTGQVCTIDQGQMGFMHHPPFFTSEPPSIYQWVSSCLKG 736
Cdd:pfam20518  161 LNTLMGEGICSLVELLVQLARDLKLGPYVDHYYRDYPTLVRTTGQVCTIDPGQTGFMHHPSFFTSEPPSIYQWVSSCLKG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  737 EGMPPYPYLPGICERSRLVVLSIALYTLGDESCVSDETCQYLSKVTSTPQKPQAEQEENRFTFRHSASVSVLAERLVVWM 816
Cdd:pfam20518  241 EGMPPYPYLPGICERSRLVVLSIALYILGDESLVSDESSQYLTRITIAPQKLQVEQEENRFSFRHSTSVSSLAERLVVWM 320
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720397514  817 ASVGFTLRDLETLPFGIALPIRDAIYHCREQPDSDWSEAVCLLIGRQDLSK 867
Cdd:pfam20518  321 TNVGFTLRDLETLPFGIALPIRDAIYHCREQPASDWPEAVCLLIGRQDLSK 371
APC1_C pfam18122
Anaphase-promoting complex sub unit 1 C-terminal domain; This is the C-terminal domain of ...
1621-1777 2.19e-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: 169.85  E-value: 2.19e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514 1621 SSFTSDPALLSFAEYFCKPTVSMGPKQEILDLFSSILYECVAQETPEMLPAYIAMDQALRSLKKRDMSDTSDLWQIKLIL 1700
Cdd:pfam18122    1 KSFSSDPSLLAFADYFCTPSSNTEAEVDFAAFCSSVLLECLTQDKPELLPTYLALYSAIQNLEASSSPASLALWQLRLIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514 1701 EFFSSRSHQDRQHTYPKRGLFINSEFLPVVKCTVDATLDQWLQAGGDVcVHAYLSGQ---PVEKSQLNMLACFLVYHSVP 1777
Cdd:pfam18122   81 EFYGSLYFLRFSGRGESREPLIRSSFLLSLKSRVDAKLDEWLKEGSNL-LRRYLRGGgdgSSDSSLLRMLAAYLVFYDIP 159
ANAPC1 pfam12859
Anaphase-promoting complex subunit 1 WD40 beta-propeller domain; Apc1 is the largest of the ...
76-241 2.46e-08

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: 57.44  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514   76 SSHEVPPSLPREPLPTMFSMLHPLDEITPLVCKSGSLFGSSRVQ------YVVDPAVKIVF---------LNIDPSIVM- 139
Cdd:pfam12859   93 DMWDPPPEDSDSDLPRLFSLTDPLSELGLVVTSSQSSRSSSPRRdsspqpEFLDPAEEILYvsdldestiWTSDPLPLVv 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397514  140 TYDAVQNVHSVWTLRRVKPEEENAVLKFPEQA-------GTLQNATTSSSLTAHLRSlSKGESPVASPFQNYSSIHSQSR 212
Cdd:pfam12859  173 TLNRETSQYTIWRAEYLESESESSSSKKRKRSrrrssfmGMATGATTPVARPSNLRE-SFGPLSGKRPRSSESHSDEKDE 251
                          170       180
                   ....*....|....*....|....*....
gi 1720397514  213 STSSPSLHSRSPSISNMAALSRAHSPALG 241
Cdd:pfam12859  252 EDLASQLDPDFDDIGVPRRSSRRVSSLLA 280
PC_rep pfam01851
Proteasome/cyclosome repeat;
1349-1383 1.01e-03

Proteasome/cyclosome repeat;


Pssm-ID: 460361 [Multi-domain]  Cd Length: 35  Bit Score: 38.17  E-value: 1.01e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720397514 1349 GACLSLGFRFAGSENLSAFSCLHKFAKDFMNYLSA 1383
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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