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Conserved domains on  [gi|1063706825|ref|NP_001325003|]
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ARABIDILLO-1 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
F-box_AtADLO1-like cd22155
F-box domain found in Arabidopsis thaliana protein ARABIDILLO 1 (AtADLO1) and similar proteins; ...
46-87 1.20e-20

F-box domain found in Arabidopsis thaliana protein ARABIDILLO 1 (AtADLO1) and similar proteins; AtADLO1, also called F-box only protein 5 (FBX5), promotes lateral root initiation and development, independently of auxin (IAA) and abscisic acid (ABA). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


:

Pssm-ID: 438926  Cd Length: 42  Bit Score: 85.70  E-value: 1.20e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1063706825  46 DWISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22155     1 DWTLLPDDTVLGLFGLLNYRDRASLASVCRAWRALGSSHSLW 42
HEAT COG1413
HEAT repeat [General function prediction only];
608-762 2.27e-07

HEAT repeat [General function prediction only];


:

Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 50.78  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825 608 EAGALEALVQLTKSPHEGVRQEAAGALWNLsfddknresisvaGGVEALVALAQSCSNASTGLQERAAGALwglsvsean 687
Cdd:COG1413    14 DPAAVPALIAALADEDPDVRAAAARALGRL-------------GDPRAVPALLEALKDPDPEVRAAAAEAL--------- 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063706825 688 sVAIGREGGVPPLIALARSEAEDVHETAAGALWNLAfnpgnalrivEEGGVPALVHLCSSSVSKMaRFMAALALA 762
Cdd:COG1413    72 -GRIGDPEAVPALIAALKDEDPEVRRAAAEALGRLG----------DPAAVPALLEALKDPDWEV-RRAAARALG 134
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
143-225 4.86e-06

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 48.86  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825 143 KKITDATLS-MIVARHEALESLQLgpDFCERItsDAIKAVAFCCPKLKKLRLSGIRDVTSEAIEALAKHCPQLNDLGFLD 221
Cdd:cd09293    12 GQITQSNISqLLRILHSGLEWLEL--YMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRA 87

                  ....
gi 1063706825 222 CLNI 225
Cdd:cd09293    88 CENI 91
PLN03200 super family cl33659
cellulose synthase-interactive protein; Provisional
388-506 4.21e-04

cellulose synthase-interactive protein; Provisional


The actual alignment was detected with superfamily member PLN03200:

Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 44.32  E-value: 4.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825  388 NEGAALLLNLMQSSQEDVQERSATGLA-TFVVVDDENASIDCgraeavmkDGGIRLLLELAKSWREGLQSEAAKAIANL- 465
Cdd:PLN03200   608 NDALRTLIQLLSSSKEETQEKAASVLAdIFSSRQDLCESLAT--------DEIINPCIKLLTNNTEAVATQSARALAALs 679
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1063706825  466 -SVNANIAKSVAEEGGIKILAGLAKSMNRLVAEEAAGGLWNL 506
Cdd:PLN03200   680 rSIKENRKVSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANL 721
 
Name Accession Description Interval E-value
F-box_AtADLO1-like cd22155
F-box domain found in Arabidopsis thaliana protein ARABIDILLO 1 (AtADLO1) and similar proteins; ...
46-87 1.20e-20

F-box domain found in Arabidopsis thaliana protein ARABIDILLO 1 (AtADLO1) and similar proteins; AtADLO1, also called F-box only protein 5 (FBX5), promotes lateral root initiation and development, independently of auxin (IAA) and abscisic acid (ABA). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438926  Cd Length: 42  Bit Score: 85.70  E-value: 1.20e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1063706825  46 DWISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22155     1 DWTLLPDDTVLGLFGLLNYRDRASLASVCRAWRALGSSHSLW 42
HEAT COG1413
HEAT repeat [General function prediction only];
608-762 2.27e-07

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 50.78  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825 608 EAGALEALVQLTKSPHEGVRQEAAGALWNLsfddknresisvaGGVEALVALAQSCSNASTGLQERAAGALwglsvsean 687
Cdd:COG1413    14 DPAAVPALIAALADEDPDVRAAAARALGRL-------------GDPRAVPALLEALKDPDPEVRAAAAEAL--------- 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063706825 688 sVAIGREGGVPPLIALARSEAEDVHETAAGALWNLAfnpgnalrivEEGGVPALVHLCSSSVSKMaRFMAALALA 762
Cdd:COG1413    72 -GRIGDPEAVPALIAALKDEDPEVRRAAAEALGRLG----------DPAAVPALLEALKDPDWEV-RRAAARALG 134
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
599-638 4.41e-07

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 47.06  E-value: 4.41e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1063706825 599 NNNNAAVGQEAGALEALVQLTKSPHEGVRQEAAGALWNLS 638
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
F-box-like pfam12937
F-box-like; This is an F-box-like family.
47-91 5.27e-07

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 47.09  E-value: 5.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1063706825  47 WISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLWTSLD 91
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
611-741 1.15e-06

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 52.80  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825  611 ALEALVQLTKSPHEGVRQEAAGALWNLsFDDKN--RESISVAGGVEALVALAQSCSNASTGLQERAAGALWgLSVSEANS 688
Cdd:PLN03200   610 ALRTLIQLLSSSKEETQEKAASVLADI-FSSRQdlCESLATDEIINPCIKLLTNNTEAVATQSARALAALS-RSIKENRK 687
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1063706825  689 VAIGREGGVPPLIALARSEAEDVHETAAGALWNLAFNPGNALRIVEEGGVPAL 741
Cdd:PLN03200   688 VSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANLLSDPEVAAEALAEDIILPL 740
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
599-639 3.77e-06

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 44.34  E-value: 3.77e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1063706825  599 NNNNAAVGQEAGALEALVQLTKSPHEGVRQEAAGALWNLSF 639
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
143-225 4.86e-06

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 48.86  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825 143 KKITDATLS-MIVARHEALESLQLgpDFCERItsDAIKAVAFCCPKLKKLRLSGIRDVTSEAIEALAKHCPQLNDLGFLD 221
Cdd:cd09293    12 GQITQSNISqLLRILHSGLEWLEL--YMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRA 87

                  ....
gi 1063706825 222 CLNI 225
Cdd:cd09293    88 CENI 91
FBOX smart00256
A Receptor for Ubiquitination Targets;
50-87 2.15e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 42.42  E-value: 2.15e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1063706825   50 LPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFW 38
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
388-506 4.21e-04

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 44.32  E-value: 4.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825  388 NEGAALLLNLMQSSQEDVQERSATGLA-TFVVVDDENASIDCgraeavmkDGGIRLLLELAKSWREGLQSEAAKAIANL- 465
Cdd:PLN03200   608 NDALRTLIQLLSSSKEETQEKAASVLAdIFSSRQDLCESLAT--------DEIINPCIKLLTNNTEAVATQSARALAALs 679
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1063706825  466 -SVNANIAKSVAEEGGIKILAGLAKSMNRLVAEEAAGGLWNL 506
Cdd:PLN03200   680 rSIKENRKVSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANL 721
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
432-466 1.94e-03

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 36.66  E-value: 1.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1063706825 432 EAVMKDGGIRLLLELAKSWREGLQSEAAKAIANLS 466
Cdd:pfam00514   6 QAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
 
Name Accession Description Interval E-value
F-box_AtADLO1-like cd22155
F-box domain found in Arabidopsis thaliana protein ARABIDILLO 1 (AtADLO1) and similar proteins; ...
46-87 1.20e-20

F-box domain found in Arabidopsis thaliana protein ARABIDILLO 1 (AtADLO1) and similar proteins; AtADLO1, also called F-box only protein 5 (FBX5), promotes lateral root initiation and development, independently of auxin (IAA) and abscisic acid (ABA). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438926  Cd Length: 42  Bit Score: 85.70  E-value: 1.20e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1063706825  46 DWISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22155     1 DWTLLPDDTVLGLFGLLNYRDRASLASVCRAWRALGSSHSLW 42
HEAT COG1413
HEAT repeat [General function prediction only];
608-762 2.27e-07

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 50.78  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825 608 EAGALEALVQLTKSPHEGVRQEAAGALWNLsfddknresisvaGGVEALVALAQSCSNASTGLQERAAGALwglsvsean 687
Cdd:COG1413    14 DPAAVPALIAALADEDPDVRAAAARALGRL-------------GDPRAVPALLEALKDPDPEVRAAAAEAL--------- 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063706825 688 sVAIGREGGVPPLIALARSEAEDVHETAAGALWNLAfnpgnalrivEEGGVPALVHLCSSSVSKMaRFMAALALA 762
Cdd:COG1413    72 -GRIGDPEAVPALIAALKDEDPEVRRAAAEALGRLG----------DPAAVPALLEALKDPDWEV-RRAAARALG 134
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
599-638 4.41e-07

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 47.06  E-value: 4.41e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1063706825 599 NNNNAAVGQEAGALEALVQLTKSPHEGVRQEAAGALWNLS 638
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
47-94 4.51e-07

F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called FBX33, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It exerts similar functions as F-box involved in polyQ pathogenesis (FipoQ) in modulating the ubiquitination and solubility of expanded SCA3-polyQ proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438876  Cd Length: 48  Bit Score: 47.25  E-value: 4.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1063706825  47 WISLPYDTVLQLFTCLNYRDRASLASTCKTWR-CLgASSCLWTSLDLRP 94
Cdd:cd22104     1 WANLPSVVLVHIFSYLPPRDRLRASSTCRRWReAL-FHPSLWRSLRLHL 48
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
684-723 4.63e-07

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 47.06  E-value: 4.63e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1063706825 684 SEANSVAIGREGGVPPLIALARSEAEDVHETAAGALWNLA 723
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
F-box-like pfam12937
F-box-like; This is an F-box-like family.
47-91 5.27e-07

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 47.09  E-value: 5.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1063706825  47 WISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLWTSLD 91
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
611-741 1.15e-06

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 52.80  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825  611 ALEALVQLTKSPHEGVRQEAAGALWNLsFDDKN--RESISVAGGVEALVALAQSCSNASTGLQERAAGALWgLSVSEANS 688
Cdd:PLN03200   610 ALRTLIQLLSSSKEETQEKAASVLADI-FSSRQdlCESLATDEIINPCIKLLTNNTEAVATQSARALAALS-RSIKENRK 687
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1063706825  689 VAIGREGGVPPLIALARSEAEDVHETAAGALWNLAFNPGNALRIVEEGGVPAL 741
Cdd:PLN03200   688 VSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANLLSDPEVAAEALAEDIILPL 740
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
599-639 3.77e-06

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 44.34  E-value: 3.77e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1063706825  599 NNNNAAVGQEAGALEALVQLTKSPHEGVRQEAAGALWNLSF 639
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
143-225 4.86e-06

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 48.86  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825 143 KKITDATLS-MIVARHEALESLQLgpDFCERItsDAIKAVAFCCPKLKKLRLSGIRDVTSEAIEALAKHCPQLNDLGFLD 221
Cdd:cd09293    12 GQITQSNISqLLRILHSGLEWLEL--YMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRA 87

                  ....
gi 1063706825 222 CLNI 225
Cdd:cd09293    88 CENI 91
F-box_unchar cd22138
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 ...
49-91 5.48e-06

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 (FBXO13); The family corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 13 (FBXO13). FBXO13, also called FBX13, or F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438910  Cd Length: 45  Bit Score: 44.24  E-value: 5.48e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1063706825  49 SLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLWTSLD 91
Cdd:cd22138     3 SLPVECQLKIFSFLSEVDKCLAATVCRSWSELIRSPRLWRTVD 45
FBOX smart00256
A Receptor for Ubiquitination Targets;
50-87 2.15e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 42.42  E-value: 2.15e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1063706825   50 LPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFW 38
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
104-222 4.88e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 45.78  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825 104 SLASRCVNLHYLRFRGVES-ADSLIHLKARNlievsgdyCKK--------------ITDATLSMIVARHEALESLQLGPd 168
Cdd:cd09293    72 ALAQSCPNLQVLDLRACENiTDSGIVALATN--------CPKlqtinlgrhrnghlITDVSLSALGKNCTFLQTVGFAG- 142
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706825 169 fCErITSDAIKAVAF-CCPKLKKLRLSGIRDVTSEAIEA-LAKH-CPQLNDLGFLDC 222
Cdd:cd09293   143 -CD-VTDKGVWELASgCSKSLERLSLNNCRNLTDQSIPAiLASNyFPNLSVLEFRGC 197
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
47-87 5.78e-05

F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also called S-phase kinase-associated protein 2, cyclin-A/CDK2-associated protein p45, F-box protein Skp2, or p45skp2, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. It specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438886  Cd Length: 41  Bit Score: 41.24  E-value: 5.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1063706825  47 WISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22114     1 WDSLPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
49-80 8.46e-05

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 40.51  E-value: 8.46e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1063706825  49 SLPYDTVLQLFTCLNYRDRASLASTCKTWRCL 80
Cdd:cd09917     2 DLPDEILLKILSYLDPRDLLRLSLVCKRWREL 33
F-box_FBXL21 cd22179
F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also ...
45-87 1.15e-04

F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also called F-box and leucine-rich repeat protein 21, F-box and leucine-rich repeat protein 3B (FBXL3B), or F-box/LRR-repeat protein 3B, is the substrate-recognition component of the SCF(FBXL21) E3 ubiquitin ligase complex that mainly acts in the cytosol and mediates ubiquitination of CRY proteins (CRY1 and CRY2), leading to CRY protein stabilization, and thus, is involved in circadian rhythm function. It regulates the oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438950  Cd Length: 43  Bit Score: 40.28  E-value: 1.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1063706825  45 VDWISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22179     1 LDWGNLPHHVVLHIFQYLPLVDRARASSVCRRWNEVFHIPDLW 43
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
142-311 1.42e-04

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 44.24  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825 142 CKKITDATLSMIVARHeaLESLQL-GpdfCERITSDAIKAVAFCCPKLKKLRLSGIRDVTSEAIEALAKHCPQLN--DLG 218
Cdd:cd09293    38 CPISDPPLDQLSNCNK--LKKLILpG---SKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQtiNLG 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825 219 FLD-CLNIDE---EALGK-VVSVRYLSVAG---TSNIKWSIASNNWDKLPKLTGldVSRTDIGPTAVSRFLTSS--QSLK 288
Cdd:cd09293   113 RHRnGHLITDvslSALGKnCTFLQTVGFAGcdvTDKGVWELASGCSKSLERLSL--NNCRNLTDQSIPAILASNyfPNLS 190
                         170       180
                  ....*....|....*....|...
gi 1063706825 289 VLCALNCHVLEEDESLISYNRFK 311
Cdd:cd09293   191 VLEFRGCPLITDFSRIILFKLWQ 213
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
47-87 1.70e-04

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 425796  Cd Length: 43  Bit Score: 39.83  E-value: 1.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1063706825  47 WISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLW 41
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
608-784 1.72e-04

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 45.86  E-value: 1.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825  608 EAGALEALVQLTKSPHEGVRQEAAGALWNL-SFDDKNRESISVAGGVEALVALAQScsNASTGLQERAAGALWGLSV-SE 685
Cdd:PLN03200   187 EAGGVDILVKLLSSGNSDAQANAASLLARLmMAFESSISKVLDAGAVKQLLKLLGQ--GNEVSVRAEAAGALEALSSqSK 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825  686 ANSVAIGREGGVPPLIA--LARSE-------AEDVHETAAGALWNLAfnpgnalriveeGGVPALV----HLCSS--SVS 750
Cdd:PLN03200   265 EAKQAIADAGGIPALINatVAPSKefmqgefAQALQENAMGALANIC------------GGMSALIlylgELSESprSPA 332
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1063706825  751 KMARFMAALAlaymfdgrmdeYALMIGTSSSEST 784
Cdd:PLN03200   333 PIADTLGALA-----------YALMVFDSSAEST 355
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
690-724 4.12e-04

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 38.56  E-value: 4.12e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1063706825  690 AIGREGGVPPLIALARSEAEDVHETAAGALWNLAF 724
Cdd:smart00185   7 AVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
388-506 4.21e-04

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 44.32  E-value: 4.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825  388 NEGAALLLNLMQSSQEDVQERSATGLA-TFVVVDDENASIDCgraeavmkDGGIRLLLELAKSWREGLQSEAAKAIANL- 465
Cdd:PLN03200   608 NDALRTLIQLLSSSKEETQEKAASVLAdIFSSRQDLCESLAT--------DEIINPCIKLLTNNTEAVATQSARALAALs 679
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1063706825  466 -SVNANIAKSVAEEGGIKILAGLAKSMNRLVAEEAAGGLWNL 506
Cdd:PLN03200   680 rSIKENRKVSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANL 721
F-box_AtARP8-like cd22156
F-box domain found in Arabidopsis thaliana actin-related protein 8 (AtARP8) and similar ...
50-87 1.05e-03

F-box domain found in Arabidopsis thaliana actin-related protein 8 (AtARP8) and similar proteins; AtARP8, also called F-box protein ARP8, is an F-box protein localized to the nucleolus in Arabidopsis. Unlike other plant nuclear actin-related proteins (ARPs), ARP8 is unique in having an F-box domain and an actin homology domain. It may play a role in nucleolar functions. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438927  Cd Length: 45  Bit Score: 37.74  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1063706825  50 LPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22156     5 LPEDVLMQILRLLGPKDAAKLCLVCKSWRYLVSDNRLW 42
F-box_FBXL3 cd22178
F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also ...
45-77 1.15e-03

F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also called F-box and leucine-rich repeat protein 3A, or F-box/LRR-repeat protein 3A, is the substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex that mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2, and thus, is involved in circadian rhythm function. It plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438949  Cd Length: 43  Bit Score: 37.58  E-value: 1.15e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1063706825  45 VDWISLPYDTVLQLFTCLNYRDRASLASTCKTW 77
Cdd:cd22178     1 VDWGNLLQDIILQIFQYLPLLDRAHASQVCRNW 33
F-box_FBXO13 cd22092
F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called ...
50-93 1.19e-03

F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called FBX13, F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438864  Cd Length: 49  Bit Score: 37.78  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1063706825  50 LPYDTVLQLFTCLNYRDRASLAS-TCKTWRCLGASSCLWTSLDLR 93
Cdd:cd22092     5 LPDSILLKIFSYLSLQERCLSASlVCKYWRDLCLDSQFWKQIDLS 49
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
432-466 1.94e-03

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 36.66  E-value: 1.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1063706825 432 EAVMKDGGIRLLLELAKSWREGLQSEAAKAIANLS 466
Cdd:pfam00514   6 QAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
49-88 3.26e-03

F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6, is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It is also the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438896  Cd Length: 42  Bit Score: 36.16  E-value: 3.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1063706825  49 SLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLWT 88
Cdd:cd22124     3 LLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
49-210 4.71e-03

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 39.62  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825  49 SLPYDTVLQLFTCLNYRDRA--SLASTCKtwrclgassCLwTSLDLRPHK-----FDASMAAsLASRCVNLHYLRFRGVE 121
Cdd:cd09293    76 SCPNLQVLDLRACENITDSGivALATNCP---------KL-QTINLGRHRnghliTDVSLSA-LGKNCTFLQTVGFAGCD 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706825 122 SAD----SLIHLKARNLIEVSGDYCKKITDATLSMIVARHealeslqlgpdfceritsdaikavafCCPKLKKLRLSG-- 195
Cdd:cd09293   145 VTDkgvwELASGCSKSLERLSLNNCRNLTDQSIPAILASN--------------------------YFPNLSVLEFRGcp 198
                         170
                  ....*....|....*.
gi 1063706825 196 -IRDVTSEAIEALAKH 210
Cdd:cd09293   199 lITDFSRIILFKLWQP 214
F-box_FBXL3-like cd22116
F-box domain found in F-box/LRR-repeat protein 3 (FBXL3), F-box/LRR-repeat protein 21 (FBXL21) ...
46-77 6.67e-03

F-box domain found in F-box/LRR-repeat protein 3 (FBXL3), F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL3, also called F-box and leucine-rich repeat protein 3A, or F-box/LRR-repeat protein 3A, is the substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex that mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2, and thus, is involved in circadian rhythm function. It plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. FBXL21, also called F-box and leucine-rich repeat protein 21, F-box and leucine-rich repeat protein 3B, or F-box/LRR-repeat protein 3B, is the substrate-recognition component of the SCF(FBXL21) E3 ubiquitin ligase complex that mainly acts in the cytosol and mediates ubiquitination of CRY proteins (CRY1 and CRY2), leading to CRY protein stabilization, and thus, is also involved in circadian rhythm function. It plays regulates the oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438888  Cd Length: 39  Bit Score: 35.19  E-value: 6.67e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1063706825  46 DWISLPYDTVLQLFTCLNYRDRASLASTCKTW 77
Cdd:cd22116     1 DWGNLPSDIILHIFQYLPLLDRAHASLVCRLW 32
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
475-507 6.91e-03

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 35.12  E-value: 6.91e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1063706825 475 VAEEGGIKILAGLAKSMNRLVAEEAAGGLWNLS 507
Cdd:pfam00514   8 VIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
 
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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