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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 2344894   46 DWISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22155   1 DWTLLPDDTVLGLFGLLNYRDRASLASVCRAWRALGSSHSLW 42

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2344894  143 KKITDATLS-MIVARHEALESLQLgpDFCERItsDAIKAVAFCCPKLKKLRLSGIRDVTSEAIEALAKHCPQLNDLGFLD 221
Cdd:cd09293  12 GQITQSNISqLLRILHSGLEWLEL--YMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRA 87

                ....
gi 2344894  222 CLNI 225
Cdd:cd09293  88 CENI 91

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 2344894   46 DWISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22155   1 DWTLLPDDTVLGLFGLLNYRDRASLASVCRAWRALGSSHSLW 42

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2344894    599 NNNNAAVGQEAGALEALVQLTKSPHEGVRQEAAGALWNLS 638
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40

cellulose synthase-interactive protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2344894    611 ALEALVQLTKSPHEGVRQEAAGALWNLsFDDKN--RESISVAGGVEALVALAQSCSNASTGLQERAAGALWgLSVSEANS 688
Cdd:PLN03200  610 ALRTLIQLLSSSKEETQEKAASVLADI-FSSRQdlCESLATDEIINPCIKLLTNNTEAVATQSARALAALS-RSIKENRK 687

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2344894    689 VAIGREGGVPPLIALARSEAEDVHETAAGALWNLAFNPGNALRIVEEGGVPAL 741
Cdd:PLN03200  688 VSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANLLSDPEVAAEALAEDIILPL 740

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2344894  143 KKITDATLS-MIVARHEALESLQLgpDFCERItsDAIKAVAFCCPKLKKLRLSGIRDVTSEAIEALAKHCPQLNDLGFLD 221
Cdd:cd09293  12 GQITQSNISqLLRILHSGLEWLEL--YMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRA 87

                ....
gi 2344894  222 CLNI 225
Cdd:cd09293  88 CENI 91

cellulose synthase-interactive protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2344894    388 NEGAALLLNLMQSSQEDVQERSATGLA-TFVVVDDENASIDCgraeavmkDGGIRLLLELAKSWREGLQSEAAKAIANL- 465
Cdd:PLN03200  608 NDALRTLIQLLSSSKEETQEKAASVLAdIFSSRQDLCESLAT--------DEIINPCIKLLTNNTEAVATQSARALAALs 679

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2344894    466 -SVNANIAKSVAEEGGIKILAGLAKSMNRLVAEEAAGGLWNL 506
Cdd:PLN03200  680 rSIKENRKVSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANL 721

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 2344894   46 DWISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22155   1 DWTLLPDDTVLGLFGLLNYRDRASLASVCRAWRALGSSHSLW 42

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2344894    599 NNNNAAVGQEAGALEALVQLTKSPHEGVRQEAAGALWNLS 638
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2344894    684 SEANSVAIGREGGVPPLIALARSEAEDVHETAAGALWNLA 723
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40

cellulose synthase-interactive protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2344894    611 ALEALVQLTKSPHEGVRQEAAGALWNLsFDDKN--RESISVAGGVEALVALAQSCSNASTGLQERAAGALWgLSVSEANS 688
Cdd:PLN03200  610 ALRTLIQLLSSSKEETQEKAASVLADI-FSSRQdlCESLATDEIINPCIKLLTNNTEAVATQSARALAALS-RSIKENRK 687

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2344894    689 VAIGREGGVPPLIALARSEAEDVHETAAGALWNLAFNPGNALRIVEEGGVPAL 741
Cdd:PLN03200  688 VSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANLLSDPEVAAEALAEDIILPL 740

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2344894  143 KKITDATLS-MIVARHEALESLQLgpDFCERItsDAIKAVAFCCPKLKKLRLSGIRDVTSEAIEALAKHCPQLNDLGFLD 221
Cdd:cd09293  12 GQITQSNISqLLRILHSGLEWLEL--YMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRA 87

                ....
gi 2344894  222 CLNI 225
Cdd:cd09293  88 CENI 91

A Receptor for Ubiquitination Targets;

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2344894      50 LPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFW 38

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 2344894   47 WISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22114   1 WDSLPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 2344894   45 VDWISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22179   1 LDWGNLPHHVVLHIFQYLPLVDRARASSVCRRWNEVFHIPDLW 43

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2344894     47 WISLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLW 41

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.

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2344894     690 AIGREGGVPPLIALARSEAEDVHETAAGALWNLAF 724
Cdd:smart00185   7 AVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41

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.

                        10        20        30
                ....*....|....*....|....*....|....*...
gi 2344894   50 LPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLW 87
Cdd:cd22156   5 LPEDVLMQILRLLGPKDAAKLCLVCKSWRYLVSDNRLW 42

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 2344894   50 LPYDTVLQLFTCLNYRDRASLAS-TCKTWRCLGASSCLWTSLDLR 93
Cdd:cd22092   5 LPDSILLKIFSYLSLQERCLSASlVCKYWRDLCLDSQFWKQIDLS 49

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 2344894   49 SLPYDTVLQLFTCLNYRDRASLASTCKTWRCLGASSCLWT 88
Cdd:cd22124   3 LLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42

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.

                        10        20        30
                ....*....|....*....|....*....|..
gi 2344894   46 DWISLPYDTVLQLFTCLNYRDRASLASTCKTW 77
Cdd:cd22116   1 DWGNLPSDIILHIFQYLPLLDRAHASLVCRLW 32