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 22748931 228 TGLRLLNLSFCGgISDAGLLHLSHMGSLRSLNLRSCDNISDTGIMHLAMGSLRLSGLDVSFCDKVGDQSLAYIAQGLDGL 307
Cdd:cd09293  28 SGLEWLELYMCP-ISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748931 308 KSLSL---CSCH-ISDDGINRMVRQMHGLRTLNIGQCvRITDKGL-ELIAEHLSQLTGIDLYGCTRITKRGLERI---TQ 379
Cdd:cd09293 107 QTINLgrhRNGHlITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAIlasNY 185

                       170       180
                ....*....|....*....|...
gi 22748931 380 LPCLKVLNL-GLWQMTDSEKEAR 401
Cdd:cd09293 186 FPNLSVLEFrGCPLITDFSRIIL 208

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 22748931 228 TGLRLLNLSFCGgISDAGLLHLSHMGSLRSLNLRSCDNISDTGIMHLAMGSLRLSGLDVSFCDKVGDQSLAYIAQGLDGL 307
Cdd:cd09293  28 SGLEWLELYMCP-ISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748931 308 KSLSL---CSCH-ISDDGINRMVRQMHGLRTLNIGQCvRITDKGL-ELIAEHLSQLTGIDLYGCTRITKRGLERI---TQ 379
Cdd:cd09293 107 QTINLgrhRNGHlITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAIlasNY 185

                       170       180
                ....*....|....*....|...
gi 22748931 380 LPCLKVLNL-GLWQMTDSEKEAR 401
Cdd:cd09293 186 FPNLSVLEFrGCPLITDFSRIIL 208

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 22748931     5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWR 42

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748931  74 QILSLRRSLSYVIQGMANIESLNLSGCyNLTDngLGHAFVQeIGSLRALNLSLCkQITD--SSLGRiaqyLKGLEVLELG 151
Cdd:COG4886  97 NLTELDLSGNEELSNLTNLESLDLSGN-QLTD--LPEELAN-LTNLKELDLSNN-QLTDlpEPLGN----LTNLKSLDLS 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748931 152 GCsNITNTGLLLiaWGLQRLKSLNLRSCRhLSDVGiGHLAGMTRsaaegclgLEQLTLQDCQkLTDLSLKhISRgLTGLR 231
Cdd:COG4886 168 NN-QLTDLPEEL--GNLTNLKELDLSNNQ-ITDLP-EPLGNLTN--------LEELDLSGNQ-LTDLPEP-LAN-LTNLE 231

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 22748931 232 LLNLSFCgGISDagLLHLSHMGSLRSLNLRSCdNISD 268
Cdd:COG4886 232 TLDLSNN-QLTD--LPELGNLTNLEELDLSNN-QLTD 264

A Receptor for Ubiquitination Targets;

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 22748931      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 22748931 228 TGLRLLNLSFCGgISDAGLLHLSHMGSLRSLNLRSCDNISDTGIMHLAMGSLRLSGLDVSFCDKVGDQSLAYIAQGLDGL 307
Cdd:cd09293  28 SGLEWLELYMCP-ISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748931 308 KSLSL---CSCH-ISDDGINRMVRQMHGLRTLNIGQCvRITDKGL-ELIAEHLSQLTGIDLYGCTRITKRGLERI---TQ 379
Cdd:cd09293 107 QTINLgrhRNGHlITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVwELASGCSKSLERLSLNNCRNLTDQSIPAIlasNY 185

                       170       180
                ....*....|....*....|...
gi 22748931 380 LPCLKVLNL-GLWQMTDSEKEAR 401
Cdd:cd09293 186 FPNLSVLEFrGCPLITDFSRIIL 208

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 22748931  82 LSYVIQGMANIESLNLSGCYNLTDNGLgHAFVQEIGSLRALNLSL---CKQITDSSLGRIAQYLKGLEVLELGGCsNITN 158
Cdd:cd09293  70 LIALAQSCPNLQVLDLRACENITDSGI-VALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22748931 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 22748931   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 22748931 122 LNLSLCKQITDSSLGRIAQ----YLKGLEVLELGGcsniTNTGLLLIAWGLQRLKSLNLRSCRHLSDVGIGHLaGMTRSA 197
Cdd:COG5238 119 LRRIMAKTLEDSLILYLALprriNLIQVLKDPLGG----NAVHLLGLAARLGLLAAISMAKALQNNSVETVYL-GCNQIG 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748931 198 AEGCLGL-EQLTLQDCQKLTDLSLKHIS-----------RGLTGLRLLNLSFcGGISDAGLL----HLSHMGSLRSLNLr 261
Cdd:COG5238 194 DEGIEELaEALTQNTTVTTLWLKRNPIGdegaeilaealKGNKSLTTLDLSN-NQIGDEGVIalaeALKNNTTVETLYL- 271

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748931 262 SCDNISDTGIMHLA---MGSLRLSGLDVSFcDKVGDQSLAYIAQGLDG---LKSLSLCSCHISDDGINRMVRQMHGLRTL 335
Cdd:COG5238 272 SGNQIGAEGAIALAkalQGNTTLTSLDLSV-NRIGDEGAIALAEGLQGnktLHTLNLAYNGIGAQGAIALAKALQENTTL 350

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22748931 336 NIGQCV--RITDKGLELIAEHL---SQLTGIDLyGCTRITKRGLERIT---QLPCLKVLNLGLWQMTDSEKEA 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 22748931  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 22748931 113 VQEIGSLRALNLSLcKQITDSSLGRIAQYLKG---LEVLELGGcSNITNTGLLLIAWGLQRLKslNLRSCrHLSDVGIGh 189
Cdd:COG5238 232 LKGNKSLTTLDLSN-NQIGDEGVIALAEALKNnttVETLYLSG-NQIGAEGAIALAKALQGNT--TLTSL-DLSVNRIG- 305

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748931 190 lagmtrsaAEGCLGLEQlTLQDCQKLTDLSLKHISRGLTGLRLL-----------NLSFCGG-ISDAGLLHLSHM----G 253
Cdd:COG5238 306 --------DEGAIALAE-GLQGNKTLHTLNLAYNGIGAQGAIALakalqenttlhSLDLSDNqIGDEGAIALAKYlegnT 376

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 22748931 254 SLRSLNLRScDNISDTGIMHLAMGSL--RLSGLDVSFCDkVGDQSLAYIAQGLDGLKSL 310
Cdd:COG5238 377 TLRELNLGK-NNIGKQGAEALIDALQtnRLHTLILDGNL-IGAEAQQRLEQLLERIKSV 433

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 22748931   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22118   1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41

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 22748931   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 22748931   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRD 37
Cdd:cd22113   1 IELLPPEMSLRIFSQLDVQSLCRASQTCKTWND 33

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 22748931  10 PELLAMIFGYLdVRDKG------RAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22119   6 PEILVKIFQFA-VATEGavpllcRLSRVCRLWREVALDPSLWT 47

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 22748931   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 22748931   5 ISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22124   1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLW 41

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
                ....*....|....*....|....*....|....*....
gi 22748931   8 LFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:cd22115   7 LPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNWQ 45

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 22748931   6 SCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22114   2 DSLPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41

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 22748931   7 CLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22134   6 QLPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLW 44

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 22748931 310 LSLCSCHISDDGINRMVR--QMHGLRTLNIGqCVRITDKGLELIAEHLSQ---LTGIDLYGcTRITKRGLERITQ----L 380
Cdd:COG5238 158 LLGLAARLGLLAAISMAKalQNNSVETVYLG-CNQIGDEGIEELAEALTQnttVTTLWLKR-NPIGDEGAEILAEalkgN 235

                        90       100
                ....*....|....*....|...
gi 22748931 381 PCLKVLNLGLWQMTDSEKEARGD 403
Cdd:COG5238 236 KSLTTLDLSNNQIGDEGVIALAE 258

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 22748931   9 FPELLAM-IFGYLDVRDKGRAAQVCTAWRDAAYHKSVW 45
Cdd:cd22094   6 LPRFLSLyIFSYLDPRSLCRAAQVSWYWKFLCESDELW 43

A Receptor for Ubiquitination Targets;

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 22748931      8 LFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWR 46
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39