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 568990536 250 CTQLTHLYLRRCVRLtDEGLRYLvIYCTSIKELSVSDCRFVSDFGLREIAKLESRLRYLSIAHCGRITDVGIRYVAKYCS 329
Cdd:cd09293   27 HSGLEWLELYMCPIS-DPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 330 KLRYLN---ARGCEGITDHGVEYLAKNCTKLKSLDIGKCPlVSDTGLESLALNCF-NLKRLSLKSCESITGQGL-QIVAA 404
Cdd:cd09293  105 KLQTINlgrHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSkSLERLSLNNCRNLTDQSIpAILAS 183

                        170
                 ....*....|....
gi 568990536 405 NCF-DLQMLNVQDC 417
Cdd:cd09293  184 NYFpNLSVLEFRGC 197

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 568990536 138 CLMLETVIVSGCRRLTDRGLYTIAQCCPELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSGCSKvtCISLTreasikl 217
Cdd:cd09293   51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRN--GHLIT------- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 218 splhgkqisiryldmtdcfvleDEGLHTIAAHCTQLTHLYLRRCvRLTDEGLRYLVIYC-TSIKELSVSDCRFVSDFGLR 296
Cdd:cd09293  122 ----------------------DVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIP 178

                        170       180
                 ....*....|....*....|....*
gi 568990536 297 EIAKLES--RLRYLSIAHCGRITDV 319
Cdd:cd09293  179 AILASNYfpNLSVLEFRGCPLITDF 203

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 568990536 250 CTQLTHLYLRRCVRLtDEGLRYLvIYCTSIKELSVSDCRFVSDFGLREIAKLESRLRYLSIAHCGRITDVGIRYVAKYCS 329
Cdd:cd09293   27 HSGLEWLELYMCPIS-DPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 330 KLRYLN---ARGCEGITDHGVEYLAKNCTKLKSLDIGKCPlVSDTGLESLALNCF-NLKRLSLKSCESITGQGL-QIVAA 404
Cdd:cd09293  105 KLQTINlgrHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSkSLERLSLNNCRNLTDQSIpAILAS 183

                        170
                 ....*....|....
gi 568990536 405 NCF-DLQMLNVQDC 417
Cdd:cd09293  184 NYFpNLSVLEFRGC 197

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 568990536 138 CLMLETVIVSGCRRLTDRGLYTIAQCCPELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSGCSKvtCISLTreasikl 217
Cdd:cd09293   51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRN--GHLIT------- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 218 splhgkqisiryldmtdcfvleDEGLHTIAAHCTQLTHLYLRRCvRLTDEGLRYLVIYC-TSIKELSVSDCRFVSDFGLR 296
Cdd:cd09293  122 ----------------------DVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIP 178

                        170       180
                 ....*....|....*....|....*
gi 568990536 297 EIAKLES--RLRYLSIAHCGRITDV 319
Cdd:cd09293  179 AILASNYfpNLSVLEFRGCPLITDF 203

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 164 CPELRRLEVSGCYNISNeavfdvvslCPNLEHLDVSGCsKVTCISLTreasikLSPLHgkqiSIRYLDMTDCfvledeGL 243
Cdd:COG4886   95 LTNLTELDLSGNEELSN---------LTNLESLDLSGN-QLTDLPEE------LANLT----NLKELDLSNN------QL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 244 HTIA---AHCTQLTHLYLRRCvRLTDegLRYLVIYCTSIKELSVSDCRfVSDFGLrEIAKLeSRLRYLSIAHCgRITDVG 320
Cdd:COG4886  149 TDLPeplGNLTNLKSLDLSNN-QLTD--LPEELGNLTNLKELDLSNNQ-ITDLPE-PLGNL-TNLEELDLSGN-QLTDLP 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 321 IRYVAkyCSKLRYLNARGCEgITDhgVEYLAkNCTKLKSLDIGKCPLvSD-------TGLESLALNCFNLKRLSLKSCES 393
Cdd:COG4886  222 EPLAN--LTNLETLDLSNNQ-LTD--LPELG-NLTNLEELDLSNNQL-TDlpplanlTNLKTLDLSNNQLTDLKLKELEL 294

                        250
                 ....*....|..
gi 568990536 394 ITGQGLQIVAAN 405
Cdd:COG4886  295 LLGLNSLLLLLL 306

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

                           10        20
                   ....*....|....*....|....*.
gi 568990536   328 CSKLRYLNARGCEGITDHGVEYLAKN 353
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26

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

                           10        20
                   ....*....|....*....|....*
gi 568990536   190 CPNLEHLDVSGCSKVTCISLTREAS 214
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAK 25

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 568990536 250 CTQLTHLYLRRCVRLtDEGLRYLvIYCTSIKELSVSDCRFVSDFGLREIAKLESRLRYLSIAHCGRITDVGIRYVAKYCS 329
Cdd:cd09293   27 HSGLEWLELYMCPIS-DPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 330 KLRYLN---ARGCEGITDHGVEYLAKNCTKLKSLDIGKCPlVSDTGLESLALNCF-NLKRLSLKSCESITGQGL-QIVAA 404
Cdd:cd09293  105 KLQTINlgrHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSkSLERLSLNNCRNLTDQSIpAILAS 183

                        170
                 ....*....|....
gi 568990536 405 NCF-DLQMLNVQDC 417
Cdd:cd09293  184 NYFpNLSVLEFRGC 197

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 568990536 162 QCCPELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSGCSKVTcisltreasiklsplhgkqisiryldmtdcfvleDE 241
Cdd:cd09293   49 SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENIT----------------------------------DS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 242 GLHTIAAHCTQLTHLYLRR---CVRLTDEGLRYLVIYCTSIKELSVSDCrFVSDFGLREIAKLESR-LRYLSIAHCGRIT 317
Cdd:cd09293   95 GIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSKsLERLSLNNCRNLT 173

                        170       180       190
                 ....*....|....*....|....*....|
gi 568990536 318 DVGIRYV--AKYCSKLRYLNARGCEGITDH 345
Cdd:cd09293  174 DQSIPAIlaSNYFPNLSVLEFRGCPLITDF 203

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 568990536 138 CLMLETVIVSGCRRLTDRGLYTIAQCCPELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSGCSKvtCISLTreasikl 217
Cdd:cd09293   51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRN--GHLIT------- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 218 splhgkqisiryldmtdcfvleDEGLHTIAAHCTQLTHLYLRRCvRLTDEGLRYLVIYC-TSIKELSVSDCRFVSDFGLR 296
Cdd:cd09293  122 ----------------------DVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIP 178

                        170       180
                 ....*....|....*....|....*
gi 568990536 297 EIAKLES--RLRYLSIAHCGRITDV 319
Cdd:cd09293  179 AILASNYfpNLSVLEFRGCPLITDF 203

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 568990536  67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22123    1 LDQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLWR 42

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 164 CPELRRLEVSGCYNISNeavfdvvslCPNLEHLDVSGCsKVTCISLTreasikLSPLHgkqiSIRYLDMTDCfvledeGL 243
Cdd:COG4886   95 LTNLTELDLSGNEELSN---------LTNLESLDLSGN-QLTDLPEE------LANLT----NLKELDLSNN------QL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 244 HTIA---AHCTQLTHLYLRRCvRLTDegLRYLVIYCTSIKELSVSDCRfVSDFGLrEIAKLeSRLRYLSIAHCgRITDVG 320
Cdd:COG4886  149 TDLPeplGNLTNLKSLDLSNN-QLTD--LPEELGNLTNLKELDLSNNQ-ITDLPE-PLGNL-TNLEELDLSGN-QLTDLP 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 321 IRYVAkyCSKLRYLNARGCEgITDhgVEYLAkNCTKLKSLDIGKCPLvSD-------TGLESLALNCFNLKRLSLKSCES 393
Cdd:COG4886  222 EPLAN--LTNLETLDLSNNQ-LTD--LPELG-NLTNLEELDLSNNQL-TDlpplanlTNLKTLDLSNNQLTDLKLKELEL 294

                        250
                 ....*....|..
gi 568990536 394 ITGQGLQIVAAN 405
Cdd:COG4886  295 LLGLNSLLLLLL 306

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 568990536  67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLW 107
Cdd:cd22118    1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 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        40
                 ....*....|....*....|....*....|....*....|..
gi 568990536  67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22115    4 NKKLPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNWQ 45

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 166 ELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSGCSKVTciSLTREASIKLSplhGKQISirylDMTDCFvledeglht 245
Cdd:COG4886   71 LLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS--NLTNLESLDLS---GNQLT----DLPEEL--------- 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 246 iaAHCTQLTHLYLRRCvRLTD--EGLRYLviycTSIKELSVSDCRfVSDFGlREIAKLeSRLRYLSIAHCgRITDvgIRY 323
Cdd:COG4886  133 --ANLTNLKELDLSNN-QLTDlpEPLGNL----TNLKSLDLSNNQ-LTDLP-EELGNL-TNLKELDLSNN-QITD--LPE 199

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568990536 324 VAKYCSKLRYLNARGCEgITDHGVEyLAkNCTKLKSLDIGKCPLvsdTGLESLAlNCFNLKRLSL 388
Cdd:COG4886  200 PLGNLTNLEELDLSGNQ-LTDLPEP-LA-NLTNLETLDLSNNQL---TDLPELG-NLTNLEELDL 257

F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; The JHDM family includes F-box/LRR-repeat proteins FBXL10, FBXL11 and FBXL19. FBXL10 is also called lysine-specific demethylase 2B (KDM2B), CXXC-type zinc finger protein 2 (CXXC2), F-box and leucine-rich repeat protein 10 (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. FBXL11, also called KDM2A, CXXC8, F-box and leucine-rich repeat protein 11, F-box protein FBL7, F-box protein Lilina, JmjC domain-containing histone demethylation protein 1A (JHDM1A), or [Histone-H3]-lysine-36 demethylase 1A, is a histone H3 lysine 36 (H3K36) demethylase that regulates epithelial mesenchymal transition (EMT) and the metastasis of ovarian cancer. It plays an essential role in embryonic development and homeostasis by regulating cell proliferation and survival. FBXL11 may also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. It associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. It is required to sustain centromeric integrity and genomic stability, particularly during mitosis. FBXL19, also called F-box and leucine-rich repeat protein 19, is the substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It acts as a CpG island-binding protein in mouse embryonic stem (ES) cells and has been shown to associate with the CDK-Mediator complex. It promotes H2Bub1 at the promoters of CpG island-containing genes by interacting with RNF20. 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 568990536  70 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRT 109
Cdd:cd22122    4 LPREVWLPVFQYLSPKDLCVCMRVCKTWNRWCCDPSLWKR 43

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 568990536  68 DRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLA 101
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELA 34

F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called FBX33, 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. It exerts similar functions as F-box involved in polyQ pathogenesis (FipoQ) in modulating the ubiquitination and solubility of expanded SCA3-polyQ proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568990536  68 DRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIRL 112
Cdd:cd22104    2 ANLPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSLRL 46

A Receptor for Ubiquitination Targets;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568990536    70 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 110
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 (FBXO3); This subfamily corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 3 (FBXO3). FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex, that mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). 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 568990536  70 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIR 111
Cdd:cd22139    4 LPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQIC 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 568990536  67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22147    2 LSALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWK 43

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 568990536  65 ASIDRLPDHSMVQIFSFLPTNQL-CRCARVCRRWYNLAWDPRLWRT 109
Cdd:cd22168    2 LTISDLPEDVLLEILSLVPARDLiLSCRLVCSRWRDLVDLPTLWKR 47

F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called FBX18, or F-box DNA helicase 1 (FBH1), is a 3'-5' DNA helicase and the substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568990536  66 SIDRLPDHSMVQIFSFLPTNQLCR-CARVCRRWYNLAWDP 104
Cdd:cd22095    1 HIQQLPEELLRNIFAFLPAEDLYQnISLVCRHWRDIVSDP 40

F-box domain found in F-box only protein 39 (FBXO39) and similar proteins; FBXO39, also called FBX39, likely functions as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a cancer/testis antigen from colon cancer patients by serological analysis of recombinant cDNA expression libraries (SEREX). 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 568990536  70 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRT 109
Cdd:cd22108    4 LPDVCLRHVFRWLGDRDRSRAALVCKRWNQAMYSPALWRS 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 568990536  67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLW 107
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLW 41

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 249 HCTQLTHLYL-----------RRCVRLTD-----------EGLRylviYCTSIKELSVS----DCRFVSDFGLREIAKLE 302
Cdd:cd21340   44 FLTNLTHLYLqnnqiekienlENLVNLKKlylggnrisvvEGLE----NLTNLEELHIEnqrlPPGEKLTFDPRSLAALS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 303 SRLRYLSIAHCgRITDvgIRYVAkYCSKLRYLNARGCEgITDHG-VEYLAKNCTKLKSLDIGKCPLVSDTGL-ESLALNC 380
Cdd:cd21340  120 NSLRVLNISGN-NIDS--LEPLA-PLRNLEQLDASNNQ-ISDLEeLLDLLSSWPSLRELDLTGNPVCKKPKYrDKIILAS 194

                 ....*....
gi 568990536 381 FNLKRLSLK 389
Cdd:cd21340  195 KSLEVLDGK 203

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

                           10        20
                   ....*....|....*....|....*.
gi 568990536   328 CSKLRYLNARGCEGITDHGVEYLAKN 353
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990536 275 YCTSIKELSVSDCRfvsdfglrEIAKLESrLRYLSIAHCgRITDVGIRyvAKYCSKLRYLNARGCEgITDHGvEYLAkNC 354
Cdd:COG4886   94 DLTNLTELDLSGNE--------ELSNLTN-LESLDLSGN-QLTDLPEE--LANLTNLKELDLSNNQ-LTDLP-EPLG-NL 158

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568990536 355 TKLKSLDIGKCPLvsdTGLESLALNCFNLKRLSLKSCEsITGQGLQIvaANCFDLQMLNVQDCEVS 420
Cdd:COG4886  159 TNLKSLDLSNNQL---TDLPEELGNLTNLKELDLSNNQ-ITDLPEPL--GNLTNLEELDLSGNQLT 218

F-box domain found in F-box only protein 9 (FBXO9) and similar proteins; FBXO9, also called FBX9, cross-immune reaction antigen 1, renal carcinoma antigen NY-REN-57, or VCIA1, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. FBXO9 acts as an E3 ubiquitin ligase that regulates the stability and activity of peroxisome proliferator-activated receptor gamma (PPARgamma) through ubiquitination. It is also required for adipocyte differentiation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568990536  67 IDRLPDHSMVQIF----SFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22089    3 ISALPSEILLYILrwvvSDLDLRSLEQLSLVCRKFYLLARDPSIWR 48

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 568990536  78 IFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22172   17 IFSFLDPRSLCRCAQVCWYWKYLTELDQLWM 47

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 568990536  69 RLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIR 111
Cdd:cd20090    4 DLPDDLLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRRIA 46

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 568990536  67 IDRLPDHSMVQIFSFL-PTNQLCRCARVCRRWYNLA 101
Cdd:cd22110    1 INDLPEEILEYILSYLsPYGDLKSAALVCKRWHRII 36

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 568990536  67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 110
Cdd:cd22093    1 IERLPSEILLKILSYLDASSLLCISCVNKLFYQLANDNALWRKL 44

F-box domain found in F-box/WD repeat-containing proteins, FBXW1A, FBXW1B and similar proteins; FBXW1A, also called E3RSIkappaB, epididymis tissue protein Li 2a, F-box and WD repeats protein beta-TrCP, or pIkappaBalpha-E3 receptor subunit, 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 CTNNB1, NFKBIA, NFKBIB and NFKBIE, as well as phosphorylated NFKB1, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. FBXW1B, also called F-box/WD repeat-containing protein 11 (FBXW11), F-box and WD repeats protein beta-TrCP2, or homologous to Slimb protein (HOS), is the substrate-recognition component of an SCF E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as IFNAR1, CEP68 and CDC25A, as well as phosphorylated CTNNB1, NFKBIA, PER1 and PER2. 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 568990536  72 DHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22130   14 DHIAENILSYLDAKSLCAAELVCKEWYRVIADGMLWK 50

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 568990536  78 IFSFLPTNQLCRCARVCRRWYNLAWDPRLW 107
Cdd:cd22180   14 VFSYLSHRDLCVCMRVCRTWNRWCCDKRLW 43

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 568990536  70 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLW 107
Cdd:cd22094    6 LPRFLSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELW 43

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 568990536  67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIRL 112
Cdd:cd22106    1 LVRLPDKLLLYIISYLDLEDIARLSQTSKRFKKLCNSDELWEKIYM 46

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

                           10        20
                   ....*....|....*....|....*.
gi 568990536   250 CTQLTHLYLRRCVRLTDEGLRYLVIY 275
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26

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

                           10        20
                   ....*....|....*....|....
gi 568990536   304 RLRYLSIAHCGRITDVGIRYVAKY 327
Cdd:smart00367   3 NLRELDLSGCTNITDEGLQALAKG 26