Hemerythrin-like domain of FBXL5-like proteins; Human FBXL5 (F-box and leucine-rich repeat protein 5) protein plays a role in cellular iron homeostasis. It is part of an E3 ubiquitin ligase complex that targets the iron regulatory protein IRP2 for proteasomal degradation. The FBXL5's stability is regulated by iron concentration, with its iron- and oxygen-binding hemerythrin domain acting as a ligand-dependent regulatory switch.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639327   1 MHEQIENEYIIGLLQQRSQT----IYNVHSDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTRDFLPHMKEEE 76
Cdd:cd12109    50 AHEQHENEFIHPLLEKRLPGlsaaVANEHSDHDLSIMLLLELLGALRTAPEAERPAAGRQLYRALAAFVADNLPHMHEEE 129

                          90       100
                  ....*....|....*....|....*....
gi 1034639327  77 EVFQPMLMEYFTYEELKDIKKKVIAQHCS 105
Cdd:cd12109   130 TVFQPLLWEYFSDEELKAIKKAVIASHPP 158

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
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034639327 299 LCPNLEHLDLTQTDISDSAFDswsWLGCCQSLRHLDLSGCEKITDVALEKISRAL 353
Cdd:cd09293    26 LHSGLEWLELYMCPISDPPLD---QLSNCNKLKKLILPGSKLIDDEGLIALAQSC 77

Hemerythrin-like domain of FBXL5-like proteins; Human FBXL5 (F-box and leucine-rich repeat protein 5) protein plays a role in cellular iron homeostasis. It is part of an E3 ubiquitin ligase complex that targets the iron regulatory protein IRP2 for proteasomal degradation. The FBXL5's stability is regulated by iron concentration, with its iron- and oxygen-binding hemerythrin domain acting as a ligand-dependent regulatory switch.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639327   1 MHEQIENEYIIGLLQQRSQT----IYNVHSDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTRDFLPHMKEEE 76
Cdd:cd12109    50 AHEQHENEFIHPLLEKRLPGlsaaVANEHSDHDLSIMLLLELLGALRTAPEAERPAAGRQLYRALAAFVADNLPHMHEEE 129

                          90       100
                  ....*....|....*....|....*....
gi 1034639327  77 EVFQPMLMEYFTYEELKDIKKKVIAQHCS 105
Cdd:cd12109   130 TVFQPLLWEYFSDEELKAIKKAVIASHPP 158

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034639327 150 ITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWKHLY 194
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 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
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034639327 299 LCPNLEHLDLTQTDISDSAFDswsWLGCCQSLRHLDLSGCEKITDVALEKISRAL 353
Cdd:cd09293    26 LHSGLEWLELYMCPISDPPLD---QLSNCNKLKKLILPGSKLIDDEGLIALAQSC 77

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

                           10        20
                   ....*....|....*....|....*
gi 1034639327  327 CQSLRHLDLSGCEKITDVALEKISR 351
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAK 25

Uncharacterized conserved protein, contains DUF2059 domain [Function unknown];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639327  29 KLSEMLSLFEKGLKNV----KNEYEQLN--YAKQLKERLEAFTRDFLPHMKEEEEVFQPMLMEYFTYEELKDI 95
Cdd:COG3184    37 ELTGAEKMFDQMLPQLaeqlKQQLAQANpeLWKDLDEVVQEKALALAARRDELEDEMAPIYAKHFTEEELKAI 109

Hemerythrin-like domain of FBXL5-like proteins; Human FBXL5 (F-box and leucine-rich repeat protein 5) protein plays a role in cellular iron homeostasis. It is part of an E3 ubiquitin ligase complex that targets the iron regulatory protein IRP2 for proteasomal degradation. The FBXL5's stability is regulated by iron concentration, with its iron- and oxygen-binding hemerythrin domain acting as a ligand-dependent regulatory switch.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639327   1 MHEQIENEYIIGLLQQRSQT----IYNVHSDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTRDFLPHMKEEE 76
Cdd:cd12109    50 AHEQHENEFIHPLLEKRLPGlsaaVANEHSDHDLSIMLLLELLGALRTAPEAERPAAGRQLYRALAAFVADNLPHMHEEE 129

                          90       100
                  ....*....|....*....|....*....
gi 1034639327  77 EVFQPMLMEYFTYEELKDIKKKVIAQHCS 105
Cdd:cd12109   130 TVFQPLLWEYFSDEELKAIKKAVIASHPP 158

Hemerythrin family; Hemerythrin (Hr) and related proteins are found in bacteria, archaea and eukaryotes. They are non-heme diiron oxygen transport proteins. In addition to oxygen transport, members are involved in cadmium fixation and host anti-bacterial defense. They have the same "four alpha helix bundle" motif and similar active site structures. Some members, like Hr, form oligomers, the octameric form being most prevalent, while others are monomeric.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639327   2 HEQIENEYIIGLLQQRSQTIYNVHSDNKLSEMLSLFEKGLknvkneyeqlnyaKQLKERLEAFTRDFLPHMK-EEEEVFQ 80
Cdd:cd00522    37 HFQIENEYMIGLLQQRSQTIYNVHSDNHLSF*LSLFEKGL-------------KQLKERLEAFTRWLVNHIKsEDFEYKG 103

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 1034639327 150 ITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWK 191
Cdd:cd22115     4 NKKLPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNWQ 45

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 1034639327 150 ITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWKHL 193
Cdd:cd22147     2 LSALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWKRM 45

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034639327 152 HLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWK 191
Cdd:cd22138     3 SLPVECQLKIFSFLSEVDKCLAATVCRSWSELIRSPRLWR 42

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 1034639327 151 THLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTK 185
Cdd:cd09917     1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35

F-box domain found in F-box only protein 16 (FBXO16) and similar proteins; FBXO16, also called FBX16, 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 functions as a tumor suppressor by attenuating nuclear beta-catenin function. 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 1034639327 153 LPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLW 190
Cdd:cd22172     9 LPRVLSLYIFSFLDPRSLCRCAQVCWYWKYLTELDQLW 46

F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and similar proteins; This family includes FBXO16 and ECT2L. FBXO16, also called FBX16, 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 functions as a tumor suppressor by attenuating nuclear beta-catenin function. ECT2L, also called lung-specific F-box and DH domain-containing protein, or putative guanine nucleotide exchange factor LFDH, may act as a guanine nucleotide exchange factor (GEF). 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 1034639327 151 THLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWK 191
Cdd:cd22094     4 RVLPRFLSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELWL 44

F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called FBX48, is one of the paralogs of the F-box only protein 7 (FBXO7), which is the causative gene for PARK15 (also known as Parkinsonian-pyramidal disease, PPD). 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 1034639327 150 ITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTK-TGSLWKHL 193
Cdd:cd22113     1 IELLPPEMSLRIFSQLDVQSLCRASQTCKTWNDLIEnSDYLWRPH 45

F-box domain found in epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and similar proteins; ECT2L, also called lung-specific F-box and DH domain-containing protein, or putative guanine nucleotide exchange factor LFDH, may act as a guanine nucleotide exchange factor (GEF). 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 1034639327 151 THLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLW 190
Cdd:cd22173     4 TVLPRFLSLYIFSFLDPRSLCRAAQVSWHWKFLAEQDCLW 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 1034639327 150 ITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWK 191
Cdd:cd22148     2 ISLLPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWK 43

F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, also called F-box and WD-40 domain-containing protein 8, or F-box only protein 29 (FBXO29), is the substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as GORASP1, IRS1, MAP4K1/HPK1. 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 1034639327 153 LPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLW 190
Cdd:cd22134     7 LPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLW 44

F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also called F-box and leucine-rich repeat protein 12, or F-box protein FBL12, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the polyubiquitination and proteasomal degradation of calcium/calmodulin dependent protein kinase I (CAMK1) leading to disruption of cyclin D1/CDK4 complex assembly, which results in G1 cell cycle arrest in lung epithelia. It regulates T-cell differentiation in a cell-autonomous manner. 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 1034639327 150 ITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWK 191
Cdd:cd22123     1 LDQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLWR 42

F-box domain found in F-box only protein 4 (FBXO4) and similar proteins; FBXO4, also called FBX4, is a specific substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that catalyzes the ubiquitination and subsequent degradation of cyclin D1 and Trx1. It recognizes TERF1 and promotes its ubiquitination together with UBE2D1. 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 1034639327 149 GITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWKHL 193
Cdd:cd22085     2 LLNHLPIDLQLYILSFLSPHDLCQLGLTSHYWHTLVRDPLLWRYF 46

F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called FBX15, has a novel dual molecular function by controlling transcriptional repression and being part of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligases, which is essential for stress response, gliotoxin production and virulence in the opportunistic human pathogen Aspergillus fumigatus. 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 1034639327 150 ITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWKHLY 194
Cdd:cd22093     1 IERLPSEILLKILSYLDASSLLCISCVNKLFYQLANDNALWRKLY 45

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 1034639327 151 THLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWKHLY 194
Cdd:cd22132     2 PLLPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKELF 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
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034639327 299 LCPNLEHLDLTQTDISDSAFDswsWLGCCQSLRHLDLSGCEKITDVALEKISRAL 353
Cdd:cd09293    26 LHSGLEWLELYMCPISDPPLD---QLSNCNKLKKLILPGSKLIDDEGLIALAQSC 77

F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, also called dactylin, or F-box and WD-40 domain-containing protein 4, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is likely to be involved in key signaling pathways crucial for normal limb development. It may participate in Wnt signaling and act as a novel tumor suppressor that regulates important cellular processes. 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 1034639327 150 ITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWK 191
Cdd:cd20090     2 LLDLPDDLLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWR 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 1034639327 153 LPPEVMLSIFSYLNPQELCRCSQVsmkWSQLTKTGSLWKHL 193
Cdd:cd22088     7 LPPELSLTVLSHLNATDLCLASCV---WQDLANDELLWQGL 44

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 1034639327 301 PNLEHLDLTQTDISDsafdsWSWLGCCQSLRHLDLSGCEKITDV 344
Cdd:pfam12799   1 PNLEVLDLSNNQITD-----IPPLAKLPNLETLDLSGNNKITDL 39

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 1034639327 274 GTSVKTLVLAYSSAVSSKMVRQILELCPNLEHLDLTQTD-ISDSAFDSWSwlGCCQSLRHLDLS---GCEKITDVALEKI 349
Cdd:cd09293    51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACEnITDSGIVALA--TNCPKLQTINLGrhrNGHLITDVSLSAL 128

                  ..
gi 1034639327 350 SR 351
Cdd:cd09293   129 GK 130

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
                  ....*....|....*....|....*....|....*...
gi 1034639327 153 LPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLW 190
Cdd:cd22114     4 LPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41

F-box domain found in F-box/WD repeat-containing protein 7 (FBXW7) and similar proteins; FBXW7, also called Archipelago homolog (Ago), F-box and WD-40 domain-containing protein 7, F-box protein FBX30, SEL-10, or Cdc4, 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, such as cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1, and probably PSEN1. 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 1034639327 150 ITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWK 191
Cdd:cd22133    18 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59

F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, also called protein SLEEPY 1, is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to the activation of the 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 1034639327 153 LPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWKHLY 194
Cdd:cd22151     3 LPDDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWENAC 44

F-box domain found in F-box only protein 36 (FBXO36) and similar proteins; FBXO36, also called FBX36, likely functions as 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 1034639327 153 LPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLWKHLY 194
Cdd:cd22106     4 LPDKLLLYIISYLDLEDIARLSQTSKRFKKLCNSDELWEKIY 45

F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also called F-box and leucine-rich repeat protein 6, or F-box protein FBL6 (FBL6A), is 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 1034639327 150 ITHLPPEVMLSIFSYLNPQE-----LCRCSQVSMKWSQLTKTGSLWK 191
Cdd:cd22119     1 GQRLPPEILVKIFQFAVATEgavplLCRLSRVCRLWREVALDPSLWT 47

F-box domain found in F-box only proteins FBXO6, FBXO44 and similar proteins; This subfamily includes FBXO6 and FBXO44. FBXO6, also called FBX6, F-box protein that recognizes sugar chains 2 (FBS2), or F-box/G-domain protein 2 (FBG2), is a substrate-recognition component of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. It is involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins, by recognizing and binding sugar chains on unfolded glycoproteins that are retro-translocated into the cytosol and promoting their ubiquitination and subsequent degradation. FBXO6 can recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. It also recognizes sulfated glycans. FBXO6 is involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. FBXO44, also called FBXO6A, FBX44, or F-box/G-domain protein 3 (FBG3), is a substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It interacts with SKP1 and CUL1. FBXO44 mediates BRCA1 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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639327 148 TGITHLPPEVMLSIFSYLNPQEL-CRCSQVSMKWSQLTKTGSLWKH------LYPVHWARG--DWY 204
Cdd:cd22168     2 LTISDLPEDVLLEILSLVPARDLiLSCRLVCSRWRDLVDLPTLWKRkcqregFILKDWDGPpkDWK 67

F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called FBX42, or just one F-box and Kelch domain-containing protein (JFK), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It specifically recognizes p53/TP53, promoting its ubiquitination and degradation. FBXO42 is also involved in the ubiquitin-proteasome system that may play a role in the pathogenesis of Parkinson's disease (PD). 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 1034639327 150 ITHLPPEVMLSIFSYLNP-QELCRCSQVSMKWSQLTKT 186
Cdd:cd22110     1 INDLPEEILEYILSYLSPyGDLKSAALVCKRWHRIIKG 38

Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor Swiss:P80255 binds Cadmium so as to protect the organizm from toxicity. However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial Swiss:Q7WX96 is a regulator of response to NO, which suggests yet another set-up for its metal ligands. In Staphylococcus aureus P72360 has been noted to be important when the organizm switches to living in environments with low oxygen concentrations; perhaps this protein acts as an oxygen store or scavenger. This domain can bind oxygen (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043)

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639327   1 MHEQIENEYIIGLLQQRS---QTIYNVHSD--NKLSEMLSLFEKGLKNVKNEYEqlnyakqLKERLEAFTRDFLPHMKEE 75
Cdd:pfam01814  48 AHHAAEEELLFPALERRSpggEAPIEVLRKehDEIRELLEELEALLKGAEPGAA-------FAELLEALAEWLREHIAKE 120

                  ....*...
gi 1034639327  76 EEVFQPML 83
Cdd:pfam01814 121 EEVLFPLL 128

F-box domain found in F-box/LRR-repeat protein 10 (FBXL10) and similar proteins; FBXL10 is also called lysine-specific demethylase 2B (KDM2B), CXXC-type zinc finger protein 2 (CXXC2), F-box and leucine-rich repeat protein 10, F-box protein FBL10, JmjC domain-containing histone demethylation protein 1B (JHDM1B), Jumonji domain-containing EMSY-interactor methyltransferase motif protein, protein JEMMA, protein-containing CXXC domain 2, [Histone-H3]-lysine-36 demethylase 1B, or NDY1. It is a histone demethylase that catalyzes the demethylation of H3K4me3 and H3K36me2, thereby playing a central role in the histone code. It preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. FBXL10 may also serve as 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
                  ....*....|....*....|....*....|....*...
gi 1034639327 153 LPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTKTGSLW 190
Cdd:cd22180     6 MQREVWMAVFSYLSHRDLCVCMRVCRTWNRWCCDKRLW 43