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 1958802896 406 CPGLLRYTAYRCKQLsdTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMVVIAKSCL 485
Cdd:cd09293    27 HSGLEWLELYMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802896 486 KLQRI---YMQENKLVTDQSVKAFAEHCPDLQCVGFMGCSVTSKGVIHLT--KLRNLSSLDLRHITELDNETVMEIVK-- 558
Cdd:cd09293   105 KLQTInlgRHRNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAsgCSKSLERLSLNNCRNLTDQSIPAILAsn 184

                         170
                  ....*....|
gi 1958802896 559 RCKNLSSLNL 568
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 1958802896 406 CPGLLRYTAYRCKQLsdTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMVVIAKSCL 485
Cdd:cd09293    27 HSGLEWLELYMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802896 486 KLQRI---YMQENKLVTDQSVKAFAEHCPDLQCVGFMGCSVTSKGVIHLT--KLRNLSSLDLRHITELDNETVMEIVK-- 558
Cdd:cd09293   105 KLQTInlgRHRNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAsgCSKSLERLSLNNCRNLTDQSIPAILAsn 184

                         170
                  ....*....|
gi 1958802896 559 RCKNLSSLNL 568
Cdd:cd09293   185 YFPNLSVLEF 194

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 1958802896 299 PENPCDCHREPPPEIPDINQLPPSILLKIFSNLSLDERCLSASLVckywRDLCLDFQFWK-------QLDLSSRQQVTDE 371
Cdd:COG5238    94 WEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALP----RRINLIQVLKDplggnavHLLGLAARLGLLA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802896 372 LLEKIASRSQNIVEINISDCRSMSDSGVCVLAfkcPGLLRYTAYRCKQLSDTSI-----IAVASHCPLLQKVH----VGN 442
Cdd:COG5238   170 AISMAKALQNNSVETVYLGCNQIGDEGIEELA---EALTQNTTVTTLWLKRNPIgdegaEILAEALKGNKSLTtldlSNN 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802896 443 QdkLTDEGLKQLGSKCRELKDIH--FGQCYKISDEGMVVIAKScLK----LQRIYMQENKLvTDQSVKAFAEH---CPDL 513
Cdd:COG5238   247 Q--IGDEGVIALAEALKNNTTVEtlYLSGNQIGAEGAIALAKA-LQgnttLTSLDLSVNRI-GDEGAIALAEGlqgNKTL 322

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802896 514 QCVGFMGCSVTSKGVI----HLTKLRNLSSLDLRhITELDNETVMEIVK---RCKNLSSLNLCLNWIIND 576
Cdd:COG5238   323 HTLNLAYNGIGAQGAIalakALQENTTLHSLDLS-DNQIGDEGAIALAKyleGNTTLRELNLGKNNIGKQ 391

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 1958802896 406 CPGLLRYTAYRCKQLsdTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMVVIAKSCL 485
Cdd:cd09293    27 HSGLEWLELYMCPIS--DPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802896 486 KLQRI---YMQENKLVTDQSVKAFAEHCPDLQCVGFMGCSVTSKGVIHLT--KLRNLSSLDLRHITELDNETVMEIVK-- 558
Cdd:cd09293   105 KLQTInlgRHRNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAsgCSKSLERLSLNNCRNLTDQSIPAILAsn 184

                         170
                  ....*....|
gi 1958802896 559 RCKNLSSLNL 568
Cdd:cd09293   185 YFPNLSVLEF 194

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958802896 316 INQLPPSILLKIFSNLSLDERClSASLVCKYWRDLCLDFQFWKQLD 361
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLL-RLALVCRRWRELASDDSLWRRLC 45

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 1958802896 316 INQLPPSILLKIFSNLSLDERClSASLVCKYWRDLCLDFQFWK 358
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLL-RLSLVSKRWRSLVDSLKLWK 42

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 1958802896 316 INQLPPSILLKIFSNLSLDERCLSaSLVCKYWRDLCLDFQFWK 358
Cdd:cd22123     1 LDQLPENVLLEILSYLPVRDLLRI-SRVCKRWRRLVYDKTLWR 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 1958802896 317 NQLPPSILLKIFSNLSLDERClSASLVCKYWRDLC 351
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 1958802896 319 LPPSILLKIFSNLSLDErCLSASLVCKYWRDLCLDFQFWKQL 360
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 1958802896 316 INQLPPSILLKIFSNLSLDERCLSASlVCKYWRDLCLDFQFW 357
Cdd:cd22118     1 ISSLPPEIMLKIFSYLNPQDLCRCAQ-VCTKWSQLARDGSLW 41

F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also called F-box and leucine-rich repeat protein 8, or F-box protein FBL8, 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
                  ....*....|....*....|....*....|...
gi 1958802896 317 NQLPPSILLKIFSNLSLDERcLSASLVCKYWRD 349
Cdd:cd22121     1 NALPEEILVHIFRHLSLRDR-YAAAQVCKHWRE 32

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 1958802896 316 INQLPPSILLKIFSNLSLDERCLSASlVCKYWRDLCLDFQFWK 358
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 1958802896 318 QLPPSILLKIFSNLSLDERCLSASLVCKYWRDLCLDFQFWKQLD 361
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 1958802896 317 NQLPPSILLKIFSNLSLDErCLSASLVCKYWRDLCLDFQFW 357
Cdd:cd22114     2 DSLPDELLLGIFSCLCLPD-LLKVSQVCKRWYRLASDESLW 41

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802896 431 HCPLLQKVHVGNQDKLTDEGLKQLG---SKCRELKDIHFGQcYKISDEGMVVIA---KSCLKLQRIYMQENKLvTDQSVK 504
Cdd:cd00116   134 DLPPALEKLVLGRNRLEGASCEALAkalRANRDLKELNLAN-NGIGDAGIRALAeglKANCNLEVLDLNNNGL-TDEGAS 211

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958802896 505 AFAEHCPDLQCV---GFMGCSVTSKGVIHL--------TKLRNLsSLDLRHITELDNETVMEIVKRCKNLSSLNLCLN 571
Cdd:cd00116   212 ALAETLASLKSLevlNLGDNNLTDAGAAALasallspnISLLTL-SLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288

F-box domain found in F-box/LRR-repeat protein 16 (FBXL16) and similar proteins; FBXL16, also called F-box and leucine-rich repeat protein 16, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a repressor of one of the earliest steps in the cardiogenic lineage: FLK1+ progenitor formation. 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 1958802896 323 ILLKIFSNLSLDERCLSASlVCKYWRDLCLDFQFWK 358
Cdd:cd22127     7 FLNRLFWYFSPCERCVLAQ-VCKKWRDVLYQPKFWR 41

F-box domain found in F-box only protein 21 (FBXO21) and similar proteins; FBXO21, also called FBX21, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It facilitates Lys29-linkage and activation of ASK1 (apoptosis signal-regulating kinase 1) and promotes type I interferon production upon viral infection. It also polyubiquitylates EP300-interacting inhibitor of differentiation 1 (EID1) and is required for the efficient degradation of EID1 in both cycling and quiescent 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 1958802896 316 INQLPPSILLKIFSNLSLDERCL-SASLVCKYWRDLCLDFQFWK 358
Cdd:cd22096     1 LLELPDELLEYILCSDNLDHHDIiRLSCTCRRLREVCQSGKVWR 44

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 5 (AtSKIP5) and similar proteins; AtSKIP5, also called F-box protein SKIP5, is a component of SCF (SKP1-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with SKP1A/ASK1. 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 1958802896 316 INQLPPSILLKIFSNLS-LDERcLSASLVCKYWRDLCLDFQFW 357
Cdd:cd22163     1 INDLDDDCLMHIFSFLTpLPDR-FNAARVCKRWRALALDPRSW 42

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 1958802896 314 PDINQLPPSILLKIFSNLSLDERCLsASLVckyWRDLCLDFQFWKQL 360
Cdd:cd22088     2 PDLEELPPELSLTVLSHLNATDLCL-ASCV---WQDLANDELLWQGL 44

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
                  ....*....|....*....|....*....|....*....|...
gi 1958802896 316 INQLPPSILLKIFSNLSLDERCLSASLVCKYWRDLCLDFQFWK 358
Cdd:cd22168     4 ISDLPEDVLLEILSLVPARDLILSCRLVCSRWRDLVDLPTLWK 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 1958802896 316 INQLPPSILLKIFSnlSLDERCL-SASLVCKYWRDLCLDFQFWKQL 360
Cdd:cd22093     1 IERLPSEILLKILS--YLDASSLlCISCVNKLFYQLANDNALWRKL 44

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 1958802896 316 INQLPPSILLKIFSNLSLDERCLSASLVCKYWRDL 350
Cdd:cd22159     1 IDLLPDEILELIFSYLSDPWDRNSCSLVCKRWYRL 35