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 2228568566 228 TGLRLLNLSFCGgISDAGLLHLSHMGSLRSLNLRSCDNISDTGIMHLAMGSLRLSGLDVSFCDKVGDQSLAYIAQGLDGL 307
Cdd:cd09293    28 SGLEWLELYMCP-ISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568566 308 KSLSL---CSCH-ISDDGINRMVRQMHGLRTLNIGQCvRITDKGL-ELIAEHLSQLTGIDLYGCTRITKRGLERI---TQ 379
Cdd:cd09293   107 QTINLgrhRNGHlITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAIlasNY 185

                         170
                  ....*....|....*..
gi 2228568566 380 LPCLKVLNL-GLWQMTD 395
Cdd:cd09293   186 FPNLSVLEFrGCPLITD 202

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 2228568566 228 TGLRLLNLSFCGgISDAGLLHLSHMGSLRSLNLRSCDNISDTGIMHLAMGSLRLSGLDVSFCDKVGDQSLAYIAQGLDGL 307
Cdd:cd09293    28 SGLEWLELYMCP-ISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568566 308 KSLSL---CSCH-ISDDGINRMVRQMHGLRTLNIGQCvRITDKGL-ELIAEHLSQLTGIDLYGCTRITKRGLERI---TQ 379
Cdd:cd09293   107 QTINLgrhRNGHlITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAIlasNY 185

                         170
                  ....*....|....*..
gi 2228568566 380 LPCLKVLNL-GLWQMTD 395
Cdd:cd09293   186 FPNLSVLEFrGCPLITD 202

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2228568566   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWR 42

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568566  74 QILSLRRSLSYVIQGMANIESLNLSGCyNLTDngLGHAFVQeIGSLRALNLSLCkQITD--SSLGRiaqyLKGLEVLELG 151
Cdd:COG4886    97 NLTELDLSGNEELSNLTNLESLDLSGN-QLTD--LPEELAN-LTNLKELDLSNN-QLTDlpEPLGN----LTNLKSLDLS 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568566 152 GCsNITNTGLLLiaWGLQRLKSLNLRSCRhLSDVGiGHLAGMTRsaaegclgLEQLTLQDCQkLTDLSLKhISRgLTGLR 231
Cdd:COG4886   168 NN-QLTDLPEEL--GNLTNLKELDLSNNQ-ITDLP-EPLGNLTN--------LEELDLSGNQ-LTDLPEP-LAN-LTNLE 231

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2228568566 232 LLNLSFCgGISDagLLHLSHMGSLRSLNLRSCdNISD 268
Cdd:COG4886   232 TLDLSNN-QLTD--LPELGNLTNLEELDLSNN-QLTD 264

A Receptor for Ubiquitination Targets;

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2228568566    8 LFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 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 2228568566 228 TGLRLLNLSFCGgISDAGLLHLSHMGSLRSLNLRSCDNISDTGIMHLAMGSLRLSGLDVSFCDKVGDQSLAYIAQGLDGL 307
Cdd:cd09293    28 SGLEWLELYMCP-ISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568566 308 KSLSL---CSCH-ISDDGINRMVRQMHGLRTLNIGQCvRITDKGL-ELIAEHLSQLTGIDLYGCTRITKRGLERI---TQ 379
Cdd:cd09293   107 QTINLgrhRNGHlITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAIlasNY 185

                         170
                  ....*....|....*..
gi 2228568566 380 LPCLKVLNL-GLWQMTD 395
Cdd:cd09293   186 FPNLSVLEFrGCPLITD 202

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 2228568566  82 LSYVIQGMANIESLNLSGCYNLTDNGLgHAFVQEIGSLRALNLSL---CKQITDSSLGRIAQYLKGLEVLELGGCsNITN 158
Cdd:cd09293    70 LIALAQSCPNLQVLDLRACENITDSGI-VALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2228568566 159 TGLLLIAWG-LQRLKSLNLRSCRHLSDVGIGHLAGMTrsaaeGCLGLEQLTLQDCQKLTDLS 219
Cdd:cd09293   148 KGVWELASGcSKSLERLSLNNCRNLTDQSIPAILASN-----YFPNLSVLEFRGCPLITDFS 204

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 2228568566   6 SCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAA 39
Cdd:cd22121     1 NALPEEILVHIFRHLSLRDRYAAAQVCKHWREAA 34

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 2228568566 122 LNLSLCKQITDSSLGRIAQ----YLKGLEVLELGGcsniTNTGLLLIAWGLQRLKSLNLRSCRHLSDVGIGHLaGMTRSA 197
Cdd:COG5238   119 LRRIMAKTLEDSLILYLALprriNLIQVLKDPLGG----NAVHLLGLAARLGLLAAISMAKALQNNSVETVYL-GCNQIG 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568566 198 AEGCLGL-EQLTLQDCQKLTDLSLKHIS-----------RGLTGLRLLNLSFcGGISDAGLL----HLSHMGSLRSLNLr 261
Cdd:COG5238   194 DEGIEELaEALTQNTTVTTLWLKRNPIGdegaeilaealKGNKSLTTLDLSN-NQIGDEGVIalaeALKNNTTVETLYL- 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568566 262 SCDNISDTGIMHLA---MGSLRLSGLDVSFcDKVGDQSLAYIAQGLDG---LKSLSLCSCHISDDGINRMVRQMHGLRTL 335
Cdd:COG5238   272 SGNQIGAEGAIALAkalQGNTTLTSLDLSV-NRIGDEGAIALAEGLQGnktLHTLNLAYNGIGAQGAIALAKALQENTTL 350

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2228568566 336 NIGQCV--RITDKGLELIAEHL---SQLTGIDLyGCTRITKRGLERIT---QLPCLKVLNLGLWQMTDSEKVR 400
Cdd:COG5238   351 HSLDLSdnQIGDEGAIALAKYLegnTTLRELNL-GKNNIGKQGAEALIdalQTNRLHTLILDGNLIGAEAQQR 422

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 2228568566  11 ELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWRGV 48
Cdd:cd22109     9 DALFCVFSYLDTKSLLRCAEVCREWRDVSRHPALWQRV 46

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 2228568566 113 VQEIGSLRALNLSLcKQITDSSLGRIAQYLKG---LEVLELGGcSNITNTGLLLIAWGLQRLKslNLRSCrHLSDVGIGh 189
Cdd:COG5238   232 LKGNKSLTTLDLSN-NQIGDEGVIALAEALKNnttVETLYLSG-NQIGAEGAIALAKALQGNT--TLTSL-DLSVNRIG- 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568566 190 lagmtrsaAEGCLGLEQlTLQDCQKLTDLSLKHISRGLTGLRLL-----------NLSFCGG-ISDAGLLHLSH----MG 253
Cdd:COG5238   306 --------DEGAIALAE-GLQGNKTLHTLNLAYNGIGAQGAIALakalqenttlhSLDLSDNqIGDEGAIALAKylegNT 376

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2228568566 254 SLRSLNLRScDNISDTGIMHLAMGSL--RLSGLDVSFCDkVGDQSLAYIAQGLDGLKSL 310
Cdd:COG5238   377 TLRELNLGK-NNIGKQGAEALIDALQtnRLHTLILDGNL-IGAEAQQRLEQLLERIKSV 433

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 2228568566   6 SCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAY 40
Cdd:cd09917     1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35

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 2228568566   6 SCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22151     1 RKLPDDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWE 41

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
                  ....*....|....*....|....*....|...
gi 2228568566   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRD 37
Cdd:cd22113     1 IELLPPEMSLRIFSQLDVQSLCRASQTCKTWND 33

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
                  ....*....|....*....|....*....|....
gi 2228568566   4 HISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRD 37
Cdd:cd22090     1 EVTGLPLELWRLILAYLPVRDLCRCCQVCRAWYE 34

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 2228568566   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22147     2 LSALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWK 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 2228568566   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLW 41

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 2228568566  67 ARGIRRVQILSLRR----------SLSYVIQGMANIESLNLSGCyNLTDNGLgHAFVQEIG-SLRALNLSLCKQITDSSL 135
Cdd:cd09293   100 ATNCPKLQTINLGRhrnghlitdvSLSALGKNCTFLQTVGFAGC-DVTDKGV-WELASGCSkSLERLSLNNCRNLTDQSI 177

                          90       100
                  ....*....|....*....|....*
gi 2228568566 136 GRI--AQYLKGLEVLELGGCSNITN 158
Cdd:cd09293   178 PAIlaSNYFPNLSVLEFRGCPLITD 202

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 2228568566   8 LFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22178     6 LLQDIILQIFQYLPLLDRAHASQVCRNWNQVFHMPDLW 43

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 2228568566   8 LFPELLAM-IFGYLDVRDKGRAAQVCTAWRDAAYHKSVWRG 47
Cdd:cd22173     5 VLPRFLSLyIFSFLDPRSLCRAAQVSWHWKFLAEQDCLWMP 45

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 2228568566   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22133    18 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59

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
                  ....*....|....*....|....*....|....*...
gi 2228568566   9 FPELLAM-IFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22094     6 LPRFLSLyIFSYLDPRSLCRAAQVSWYWKFLCESDELW 43

A Receptor for Ubiquitination Targets;

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2228568566    8 LFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39