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 767947136 529 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 606
Cdd:cd09293   14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947136 607 HLTAQGIGYIV-NIFSLVSIDLSG-------TDISNEAFCKSSLILEHLDVSYCsQLSDMIIKALAIYCI-NLTSLSIAG 677
Cdd:cd09293   90 NITDSGIVALAtNCPKLQTINLGRhrnghliTDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNN 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767947136 678 CPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 709
Cdd:cd09293  169 CRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202

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 767947136 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 286
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42

Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a role in spindle body duplication. They contain binding sites for calmodulin-like proteins called centrins which are present in microtubule-organizing centres.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947136  112 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNILLriqqiIYCHKLTI-ILTKWRNTARH 190
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767947136  191 KSK------KKEDELILKHelQLKKWknrlilkRAAAEES 224
Cdd:pfam08457 379 VQKlekwarDARFYFLATR--TLKKW-------RAATEES 409

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 767947136 529 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 606
Cdd:cd09293   14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947136 607 HLTAQGIGYIV-NIFSLVSIDLSG-------TDISNEAFCKSSLILEHLDVSYCsQLSDMIIKALAIYCI-NLTSLSIAG 677
Cdd:cd09293   90 NITDSGIVALAtNCPKLQTINLGRhrnghliTDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNN 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767947136 678 CPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 709
Cdd:cd09293  169 CRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202

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 767947136 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 286
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767947136  245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAID 289
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45

Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a role in spindle body duplication. They contain binding sites for calmodulin-like proteins called centrins which are present in microtubule-organizing centres.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947136  112 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNILLriqqiIYCHKLTI-ILTKWRNTARH 190
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767947136  191 KSK------KKEDELILKHelQLKKWknrlilkRAAAEES 224
Cdd:pfam08457 379 VQKlekwarDARFYFLATR--TLKKW-------RAATEES 409

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 767947136 529 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 606
Cdd:cd09293   14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947136 607 HLTAQGIGYIV-NIFSLVSIDLSG-------TDISNEAFCKSSLILEHLDVSYCsQLSDMIIKALAIYCI-NLTSLSIAG 677
Cdd:cd09293   90 NITDSGIVALAtNCPKLQTINLGRhrnghliTDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNN 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767947136 678 CPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 709
Cdd:cd09293  169 CRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202

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 767947136 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 286
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42

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 767947136 419 LDLSGCtQISVQGFRYIANsCTGIMHLTINDMPTLTDNCVKALVEKCSRITSLVFTGAPHISDCTFRALSA-CKLRKI-- 495
Cdd:cd09293   33 LELYMC-PISDPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATnCPKLQTin 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947136 496 --RFEGNKRVTDASFKFIDKNYPNLSHIYMADCKgITDSSLRSLSPL--KQLTVLNLANCVRIGDMGLKQFLDGPASMRI 571
Cdd:cd09293  111 lgRHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGcsKSLERLSLNNCRNLTDQSIPAILASNYFPNL 189

                        170
                 ....*....|....*
gi 767947136 572 RELNLSNCVRLSDAS 586
Cdd:cd09293  190 SVLEFRGCPLITDFS 204

F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) and similar proteins; DdgacFF, also called GTPase activating factor for raC protein FF, is a Rho GTPase-activating protein involved in the signal transduction pathway. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767947136 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNA 287
Cdd:cd22148    2 ISLLPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWKA 44

F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also called F-box and leucine-rich repeat protein 5, F-box protein FBL4/FBL5, or p45SKP2-like protein, is the substrate-recognition component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 767947136 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 285
Cdd:cd22118    1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41

dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar proteins; AK5 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 5, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. It also displays broad nucleoside diphosphate kinase activity. AK5 contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.

                         10        20        30
                 ....*....|....*....|....*....|...
gi 767947136  12 KNYFKENYIPQVCEALLCGILVTCPEDPLRYLE 44
Cdd:cd22978    5 KDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLE 37

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 767947136 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 285
Cdd:cd22123    1 LDQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLW 41

F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, also called F-box and WD-40 domain-containing protein 5, is the substrate-recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767947136 246 SLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 285
Cdd:cd22132    2 PLLPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLW 41

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 767947136 246 SLLPERAILQIFFYLSLKDVIICGQVNHAW 275
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRW 30

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        40
                 ....*....|....*....|....*....|....*....|...
gi 767947136 243 CDISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 285
Cdd:cd22178    1 VDWGNLLQDIILQIFQYLPLLDRAHASQVCRNWNQVFHMPDLW 43

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 767947136 639 KSSLILEHLdvsycSQLSDMIIKAL-AIYCINLTSLSIAGCPKItDSAMEMLSAkCHYLHILDISGCVLLTDQILEDLQI 717
Cdd:cd09293    3 PLLFILHKL-----GQITQSNISQLlRILHSGLEWLELYMCPIS-DPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQ 75

                         90
                 ....*....|....*..
gi 767947136 718 GCKQLRILKMQYCTNIS 734
Cdd:cd09293   76 SCPNLQVLDLRACENIT 92