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 229462981 411 CPGLLRYTAYRCKQLsdTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMIVIAKGCL 490
Cdd:cd09293   27 HSGLEWLELYMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462981 491 KLQRI---YMQENKLVTDQSVKAFAEHCPELQYVGFMGCSVTSKGVIHLT--KLRNLSSLDLRHITELDNETVMEIVK-- 563
Cdd:cd09293  105 KLQTInlgRHRNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAsgCSKSLERLSLNNCRNLTDQSIPAILAsn 184

                        170
                 ....*....|
gi 229462981 564 RCKNLSSLNL 573
Cdd:cd09293  185 YFPNLSVLEF 194

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 229462981 411 CPGLLRYTAYRCKQLsdTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMIVIAKGCL 490
Cdd:cd09293   27 HSGLEWLELYMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462981 491 KLQRI---YMQENKLVTDQSVKAFAEHCPELQYVGFMGCSVTSKGVIHLT--KLRNLSSLDLRHITELDNETVMEIVK-- 563
Cdd:cd09293  105 KLQTInlgRHRNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAsgCSKSLERLSLNNCRNLTDQSIPAILAsn 184

                        170
                 ....*....|
gi 229462981 564 RCKNLSSLNL 573
Cdd:cd09293  185 YFPNLSVLEF 194

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 229462981  321 INQLPPSILLKIFSNLSLDERClSASLVCKYWRDLCLDFQFWKQLD 366
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLL-RLALVCRRWRELASDDSLWRRLC 45

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 229462981 547 LRHITELDNETVMEIvkRCKNLSSLNL--C------LNWIINdrcveviakeGQNLKELYLVSCK-ITDYALIAIGRYSM 617
Cdd:cd09293   11 LGQITQSNISQLLRI--LHSGLEWLELymCpisdppLDQLSN----------CNKLKKLILPGSKlIDDEGLIALAQSCP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 229462981 618 TIETVDVGWCKEITDQGATLIAQSSKSLRYLGLMRCDKVNEVT 660
Cdd:cd09293   79 NLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRNGHLIT 121

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 229462981 411 CPGLLRYTAYRCKQLsdTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMIVIAKGCL 490
Cdd:cd09293   27 HSGLEWLELYMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462981 491 KLQRI---YMQENKLVTDQSVKAFAEHCPELQYVGFMGCSVTSKGVIHLT--KLRNLSSLDLRHITELDNETVMEIVK-- 563
Cdd:cd09293  105 KLQTInlgRHRNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAsgCSKSLERLSLNNCRNLTDQSIPAILAsn 184

                        170
                 ....*....|
gi 229462981 564 RCKNLSSLNL 573
Cdd:cd09293  185 YFPNLSVLEF 194

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 229462981 461 SKCRELKDIHFGQCYKISDEGMIVIAKGCLKLQRIYMQENKLVTDQSVKAFAEHCPELQyvgfmgcsvtskgVIHLTKLR 540
Cdd:cd09293   49 SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQ-------------TINLGRHR 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229462981 541 NLSSldlrhITELdneTVMEIVKRCKNLSSLNL--CLnwiINDRCV-EVIAKEGQNLKELYLVSC-KITDYALIAI 612
Cdd:cd09293  116 NGHL-----ITDV---SLSALGKNCTFLQTVGFagCD---VTDKGVwELASGCSKSLERLSLNNCrNLTDQSIPAI 180

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 229462981  321 INQLPPSILLKIFSNLSLDERClSASLVCKYWRDLCLDFQFWKQLD 366
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLL-RLALVCRRWRELASDDSLWRRLC 45

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462981 453 DEGLKQLGSKCRELKDIHFG----QCYKISDEGMIVIAKGCLK---LQRIYMQENKlVTDQSVKAFAEH---CPELQYVG 522
Cdd:COG5238  164 RLGLLAAISMAKALQNNSVEtvylGCNQIGDEGIEELAEALTQnttVTTLWLKRNP-IGDEGAEILAEAlkgNKSLTTLD 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462981 523 FMGCSVTSKGVI----HLTKLRNLSSLDL--RHITELDNETVMEIVKRCKNLSSLNLCLNwIINDRCVEVIAK---EGQN 593
Cdd:COG5238  243 LSNNQIGDEGVIalaeALKNNTTVETLYLsgNQIGAEGAIALAKALQGNTTLTSLDLSVN-RIGDEGAIALAEglqGNKT 321

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229462981 594 LKELYLVSCKITDYALIAIG---RYSMTIETVDVGwCKEITDQGATLIAQS---SKSLRYLGLMRcDKVNEVTVEQLVQ 666
Cdd:COG5238  322 LHTLNLAYNGIGAQGAIALAkalQENTTLHSLDLS-DNQIGDEGAIALAKYlegNTTLRELNLGK-NNIGKQGAEALID 398

A Receptor for Ubiquitination Targets;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 229462981   324 LPPSILLKIFSNLSLDERClSASLVCKYWRDLCLDFQFWKQL 365
Cdd:smart00256   1 LPDEILEEILSKLDPKDLL-RLRKVSRKWRSLIDSHDFWFKL 41

F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called FBX18, or F-box DNA helicase 1 (FBH1), is a 3'-5' DNA helicase and the substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks. 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 229462981 321 INQLPPSILLKIFSNLSLDERCLSASLVCKYWRDLCLD--FQFWKQL 365
Cdd:cd22095    2 IQQLPEELLRNIFAFLPAEDLYQNISLVCRHWRDIVSDplFIPWKKL 48

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 229462981 322 NQLPPSILLKIFSNLSLDERClSASLVCKYWRDLC 356
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLL-RLSLVCKRWRELA 34

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        40
                 ....*....|....*....|....*....|....*....|..
gi 229462981 324 LPPSILLKIFSNLSLDErCLSASLVCKYWRDLCLDFQFWKQL 365
Cdd:cd22132    4 LPDSLLLHIFSYLSPKD-LLAAGQVCKQWYRVSRDEFLWKEL 44

F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also called F-box and leucine-rich repeat protein 5, F-box protein FBL4/FBL5, or p45SKP2-like protein, is the substrate-recognition component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. 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 229462981 321 INQLPPSILLKIFSNLSLDERCLSASlVCKYWRDLCLDFQFW 362
Cdd:cd22118    1 ISSLPPEIMLKIFSYLNPQDLCRCAQ-VCTKWSQLARDGSLW 41

F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also called F-box and leucine-rich repeat protein 4, or F-box protein FBL4/FBL5, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It serves as a clock output molecule that regulates sleep through promotion of rhythmic degradation of the GABA(A) receptor. Biallelic pathogenic variants in FBXL4 are associated with an encephalopathic mtDNA maintenance defect syndrome that is a multi-system disease characterized by lactic acidemia, developmental delay, and hypotonia. 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 229462981 324 LPPSILLKIFSNLSLDERClSASLVCKYWRDLCLDFQFWKQLDL 367
Cdd:cd22117    4 LPYELIQLILSYLDLPSLC-RLSQTCKLFRKHCYDPLLWKELNL 46

F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) and similar proteins; The family includes FBXL2 and FBXL30. FBXL2, also called F-box and leucine-rich repeat protein 2, or F-box protein FBL2/FBL3, is a calcium-activated substrate-recognition component of an SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin. FBXL20, also called SCRAPPER, F-box and leucine-rich repeat protein 20, or F-box/LRR-repeat protein 2-like, is a component of a synapse-localized SCF-type E3 ubiquitin ligase which regulates neural transmission. It is widely expressed in the central nervous system and plays an important role in the ubiquitin-dependent degradation of regulating synaptic membrane exocytosis 1 (RIM1), which is an important factor in the release of synaptic vesicles. It may also mediate the ubiquitin degradation of E-cadherin resulting in an increased invasive ability of malignant cells. 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 229462981 321 INQLPPSILLKIFSNLSLDERCLSASlVCKYWRDLCLDFQFWK 363
Cdd:cd22115    4 NKKLPKELLLRIFSFLDVVTLCRCAQ-VSKYWNVLALDGSNWQ 45

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 19 (AtSKIP19) and similar proteins; AtSKIP19, also called F-box protein SKIP19, or F-box/LRR-repeat protein 20 (FBL20), is a component of SCF (SPK1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with CUL1 and SPK1B/ASK2. 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 229462981 323 QLPPSILLKIFSNLSLDERCLSASLVCKYWRDLCLDFQFWKQLD 366
Cdd:cd22164    4 DLPDDLTASILSRLGAIDILTNAQKVCKLWRRICKDPSMWRVID 47

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 229462981 322 NQLPPSILLKIFSNLSLDErCLSASLVCKYWRDLCLDFQFW 362
Cdd:cd22114    2 DSLPDELLLGIFSCLCLPD-LLKVSQVCKRWYRLASDESLW 41

F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also called F-box and leucine-rich repeat protein 7, or F-box protein FBL6/FBL7, 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 Aurora kinase A (AURKA) during mitosis, causing mitotic arrest. 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 229462981 321 INQLPPSILLKIFSNLSLDERCLSAsLVCKYWRDLCLDFQFWKQL 365
Cdd:cd22120    1 FDRLPDDVILQIFSHLPTNQLCRCA-RVCRRWYNLAWDPRLWTTI 44

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 229462981 324 LPPSILLKIFSNLSLDErCLSASLVCKYWRDLCLDFQFWK 363
Cdd:cd22148    5 LPEHLALKILSYLSPKE-LLIASQVSKTWRRLASSNELWK 43

F-box domain found in F-box only protein 8 (FBXO8) and similar proteins; FBXO8, also called FBX8, or F-box/SEC7 protein FBS, is a novel component of F-box proteins which contains an F-box domain and a putative Sec7 domain. FBX8 was originally identified as a Skp1-binding protein. It is involved in the ubiquitin-dependent proteolytic pathway. It acts as a metastasis suppressor that functions through mTOR signaling pathway. FBXO8 may promote the activation of ADP-ribosylation factor (ARF) through replacement of GDP with GTP. 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 229462981 318 TPDINQLPPSILLKIFSNLSLDERCLsASLVckyWRDLCLDFQFWKQL 365
Cdd:cd22088    1 FPDLEELPPELSLTVLSHLNATDLCL-ASCV---WQDLANDELLWQGL 44

F-box domain found in F-box only protein 9 (FBXO9) and similar proteins; FBXO9, also called FBX9, cross-immune reaction antigen 1, renal carcinoma antigen NY-REN-57, or VCIA1, 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 TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. FBXO9 acts as an E3 ubiquitin ligase that regulates the stability and activity of peroxisome proliferator-activated receptor gamma (PPARgamma) through ubiquitination. It is also required for adipocyte differentiation. 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 229462981 321 INQLPPSILLKIFSNL--SLDERCLSA-SLVCKYWRDLCLDFQFWKQL 365
Cdd:cd22089    3 ISALPSEILLYILRWVvsDLDLRSLEQlSLVCRKFYLLARDPSIWRLA 50

F-box domain found in F-box only protein 28 (FBXO28) and similar proteins; FBXO28, also called FBX28, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It promotes mitotic progression and regulates topoisomerase IIalpha-dependent DNA decatenation. FBXO28 plays a crucial role in the pathogenesis of the 1q41q42 microdeletion syndrome. 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 229462981 321 INQLPPSILLKIFSNLSLDErcLSAS-LVCKYWRDLC---LDFQFWK 363
Cdd:cd22100    1 LLELPDEIIEKILSYLSYDE--ISKLrLVCRRFNEVCqriLNQGFKK 45

F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called FBX10, or PRMT11, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The SCF(FBXO10) complex mediates ubiquitination and degradation of BCL2, an anti-apoptotic protein, thereby playing a role in apoptosis by controlling the stability of BCL2. It also associates with the receptor for advanced glycation end products (RAGE) to mediate its ubiquitination and degradation. 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        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 229462981 320 DINQLPPSILLKIFSNLSLDERClSASLVCKYWRDLC--LDFQFWKQLDLS 368
Cdd:cd22090    1 EVTGLPLELWRLILAYLPVRDLC-RCCQVCRAWYELIlsLDSTRWKQLYLG 50

F-box domain found in Saccharomyces cerevisiae protein Digs into agar protein 2 (ScDIA2) and similar proteins; ScDIA2 is a replication origin-binding protein that plays a role in regulating DNA replication. It is a component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target 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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 229462981 321 INQLPPSILLKIFSNLSLDErCLSASLVCKYWRDLCLDF-QFWKQLDL 367
Cdd:cd22142    2 WENLPLDILPLIFQKFSTKE-LITLSHVCSSWRAKILDFpHLWKTVEL 48

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). 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 229462981 321 INQLPPSILLKIFSNLS-LDERcLSASLVCKYWRDL 355
Cdd:cd22159    1 IDLLPDEILELIFSYLSdPWDR-NSCSLVCKRWYRL 35

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.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 229462981 319 PDINQLPPSILLKIFSNLSLDERCLsASLVCKYW 352
Cdd:cd22178    1 VDWGNLLQDIILQIFQYLPLLDRAH-ASQVCRNW 33