dimerization/docking (D/D) 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 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767715   9 PRLRNYFKDNYIPQICEALLCGLLVTCPEDPLKYLESMILAI 50
Cdd:cd22977     2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767715 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWN 283
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767715 115 WKEIaipHANQEAIMAEKMDKAIAHDNFR--CQKHIFNRWFSYTVKRRERLIATLLRL-------RHLFYTQKQ-RIILA 184
Cdd:pfam15558  96 WREQ---AEDQENQRQEKLERARQEAEQRkqCQEQRLKEKEEELQALREQNSLQLQERleeachkRQLKEREEQkKVQEN 172

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958767715 185 KWKEKARHKSKKREDDLITKHELQLKkwkfKLSLEK 220
Cdd:pfam15558 173 NLSELLNHQARKVLVDCQAKAEELLR----RLSLEQ 204

dimerization/docking (D/D) 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 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767715   9 PRLRNYFKDNYIPQICEALLCGLLVTCPEDPLKYLESMILAI 50
Cdd:cd22977     2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43

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 1958767715 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWN 283
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958767715 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWNSID 286
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45

Leucine-rich repeat - CC (cysteine-containing) subfamily;

                           10        20
                   ....*....|....*....|....*.
gi 1958767715  330 CKNLQELNVSDCPSFTDESMRHISEG 355
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767715 115 WKEIaipHANQEAIMAEKMDKAIAHDNFR--CQKHIFNRWFSYTVKRRERLIATLLRL-------RHLFYTQKQ-RIILA 184
Cdd:pfam15558  96 WREQ---AEDQENQRQEKLERARQEAEQRkqCQEQRLKEKEEELQALREQNSLQLQERleeachkRQLKEREEQkKVQEN 172

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958767715 185 KWKEKARHKSKKREDDLITKHELQLKkwkfKLSLEK 220
Cdd:pfam15558 173 NLSELLNHQARKVLVDCQAKAEELLR----RLSLEQ 204

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767715 566 KLRELNLANCSLlgdtSVIRLSERCPNLHYLNLRNCEHLTDL 607
Cdd:pfam12799   2 NLEVLDLSNNQI----TDIPPLAKLPNLETLDLSGNNKITDL 39

dimerization/docking (D/D) 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 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958767715   9 PRLRNYFKDNYIPQICEALLCGLLVTCPEDPLKYLESMILAI 50
Cdd:cd22977     2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43

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 1958767715 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWN 283
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 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 1958767715 329 HCKNLQELNVSD---CPSFTDESMRHISEGCPGVLYLNLSNTTITNRTMRLLPRY-FHNLQNLSLAYCRKFTDKGLQYLN 404
Cdd:cd09293   102 NCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGcSKSLERLSLNNCRNLTDQSIPAIL 181

                          90       100
                  ....*....|....*....|....*...
gi 1958767715 405 LGNGCHKLIYLDLSGCTQIsvQGFRNIA 432
Cdd:cd09293   182 ASNYFPNLSVLEFRGCPLI--TDFSRII 207

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 1958767715 525 LTDSSLKSLSVL--KQLTVLNLTNCVRIgDIGLRQFFdgpASVKLRELNLANCSLLGDTSVIRLSERCPNLHYLNLRNCE 602
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958767715 603 HLTDLAIEYIAS---MLSLISI--DLSGTLISNES 632
Cdd:cd09293    90 NITDSGIVALATncpKLQTINLgrHRNGHLITDVS 124

dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55)-like family; The TEX55-like family includes TEX55, F-box/LRR-repeat protein 13 (FBXL13), adenylate kinase isoenzymes AK5 and AK8, as well as uncharacterized EF-hand calcium-binding domain-containing protein 10 (EFCAB10), and protein VEST-1. TEX55, also called testis-specific conserved cAMP-dependent type II PK-anchoring protein (TSCPA), is a putative A-kinase anchoring protein (AKAP) that is dispensable for male fertility. FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. AK5 and AK8 act as nucleoside monophosphate (NMP) kinases that catalyze the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Members of this family contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958767715  12 RNYFKDNYIPQICEALLCGLLVTCPEDPLKYLESMILAI 50
Cdd:cd22961     5 EEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQI 43

dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar proteins; AK5 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 5, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. It also displays broad nucleoside diphosphate kinase activity. AK5 contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958767715  12 RNYFKDNYIPQICEALLCGLLVTCPEDPLKYLESMILAI 50
Cdd:cd22978     5 KDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLEDCLEKI 43

F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) and similar proteins; DdgacFF, also called GTPase activating factor for raC protein FF, is a Rho GTPase-activating protein involved in the signal transduction pathway. 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 1958767715 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22148     2 ISLLPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELW 42

Leucine-rich repeat (LRR) protein [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767715 518 YMVDCKGLTDSSLKSLSVLKQLTVLNLTNCvRIGDIG--LRQFfdgpasVKLRELNLANCSLlgdTSVIRLSERCPNLHY 595
Cdd:COG4886    94 DLTNLTELDLSGNEELSNLTNLESLDLSGN-QLTDLPeeLANL------TNLKELDLSNNQL---TDLPEPLGNLTNLKS 163

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958767715 596 LNLRNCEhLTDLAIEyIASMLSLISIDLSGTLISN 630
Cdd:COG4886   164 LDLSNNQ-LTDLPEE-LGNLTNLKELDLSNNQITD 196

F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, also called F-box and WD-40 domain-containing protein 5, is the substrate-recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. 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 1958767715 245 LPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22132     4 LPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLW 41

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.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958767715 243 SVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQ 277
Cdd:cd09917     1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35

F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called FBX41, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a novel central nervous system (CNS)-specific F-box protein that localizes to the centrosome and the cytoplasm of neurons and promotes neuronal migration. 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 1958767715 253 IFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22109    14 VFSYLDTKSLLRCAEVCREWRDVSRHPALW 43

Leucine-rich repeat - CC (cysteine-containing) subfamily;

                           10        20
                   ....*....|....*....|....*
gi 1958767715  590 CPNLHYLNLRNCEHLTDLAIEYIAS 614
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAK 25

F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar proteins; SpPof1, also called F-box/WD repeat-containing protein pof1, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is required for the inactivation of zip1 via ubiquitination. This subfamily also includes Saccharomyces cerevisiae methionine-requiring protein 30 (ScMET30, also called E3 ubiquitin ligase complex SCF(Met30) subunit MET30), Aspergillus niger sulfur controller B (AnSCONB, also called sulfur metabolite repression control protein B) and Neurospora crassa sulfur controller 2 (NcSCON2, also called sulfur metabolite repression control protein 2). ScMET30 acts as a transcriptional inhibitor that negatively regulates the expression of sulfur amino acid biosynthesis genes. It controls cell cycle function (being required for the G1/S transition and M-phase but not the S-phase), sulfur metabolism, and methionine biosynthesis as part of the E3 ubiquitin ligase complex SCF(Met30). AnSCONB and NcSCON2 are components of the SCF (sconB/scon-2) E3 ubiquitin ligase complexes involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor. 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 1958767715 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22147     2 LSALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELW 42

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767715 115 WKEIaipHANQEAIMAEKMDKAIAHDNFR--CQKHIFNRWFSYTVKRRERLIATLLRL-------RHLFYTQKQ-RIILA 184
Cdd:pfam15558  96 WREQ---AEDQENQRQEKLERARQEAEQRkqCQEQRLKEKEEELQALREQNSLQLQERleeachkRQLKEREEQkKVQEN 172

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958767715 185 KWKEKARHKSKKREDDLITKHELQLKkwkfKLSLEK 220
Cdd:pfam15558 173 NLSELLNHQARKVLVDCQAKAEELLR----RLSLEQ 204

A Receptor for Ubiquitination Targets;

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958767715  245 LPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLWN 283
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39

F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called FBX45, or F-box/SPRY domain-containing protein 1, functions as the substrate-recognition component of E3 ubiquitin ligase complexes. It is critical for synaptogenesis, neuronal migration, and synaptic transmission. 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
                  ....*....|....*....|....*...
gi 1958767715 245 LPDQAVVQIFVYLTFKDLVSCSQVNRSW 272
Cdd:cd22111     4 LPSRVLEVIFSYLDLPDLRNCSLVCKSW 31

Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a role in spindle body duplication. They contain binding sites for calmodulin-like proteins called centrins which are present in microtubule-organizing centres.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767715 134 DKAIAHDNFRCQKHIFNRWFSYTVKRRERLIATLlrlrhLFYTQ--KQRiILAKWKEKARHKSK--KREDD----LITKH 205
Cdd:pfam08457 324 EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAAN-----EFYAPrlLQE-ALDAWRERHQHVQKleKWARDarfyFLATR 397

                  ....*....
gi 1958767715 206 elQLKKWKF 214
Cdd:pfam08457 398 --TLKKWRA 404

F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and similar proteins; ScCDC4 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 is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. 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 1958767715 242 ISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22141     1 IGNLPFEISLKIFNYLQFEDLLNSLGVSKKWNKIIRNTALW 41

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 1958767715 241 DISVLPDQAVVQIFVYLTFKDLVSCSQVNRSWMSMIQRGSLW 282
Cdd:cd22155     1 DWTLLPDDTVLGLFGLLNYRDRASLASVCRAWRALGSSHSLW 42