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 2462613032 496 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 573
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613032 574 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 652
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462613032 653 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 704
Cdd:cd09293   148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 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 2462613032 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 2462613032 112 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNMLLriqqiIYCHKLTI-ILTKWRNTARH 190
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462613032 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 2462613032 496 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 573
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613032 574 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 652
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462613032 653 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 704
Cdd:cd09293   148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 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 2462613032 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 286
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613032 279 TQLNSLWNAIDFSSVKNVIPDKYIVSTLQRWRLNVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDesmrhise 358
Cdd:COG4886    40 LSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN-------- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613032 359 gCPGVLCLNLSNTTITNRTMRLlpRHFHNLQNLSLAYCRrFTD--------KGLQYLNLGN-----------GCHKLIYL 419
Cdd:COG4886   112 -LTNLESLDLSGNQLTDLPEEL--ANLTNLKELDLSNNQ-LTDlpeplgnlTNLKSLDLSNnqltdlpeelgNLTNLKEL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613032 420 DLSGCtqalvekcsRITSLvftgAPHISDCTfralsacKLRKIRFEGNKrVTDASFKFidKNYPNLSHIYMADCKgITDs 499
Cdd:COG4886   188 DLSNN---------QITDL----PEPLGNLT-------NLEELDLSGNQ-LTDLPEPL--ANLTNLETLDLSNNQ-LTD- 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613032 500 sLRSLSPLKQLTVLNLANCvRIGDMGLKQFLDgpasmRIRELNLSNCvRLSDASVMKLSERCPNLNYLSLRNCEHLTAQG 579
Cdd:COG4886   243 -LPELGNLTNLEELDLSNN-QLTDLPPLANLT-----NLKTLDLSNN-QLTDLKLKELELLLGLNSLLLLLLLLNLLELL 314

                         330       340
                  ....*....|....*....|....*.
gi 2462613032 580 IGYIVNIFSLVSIDLSGTDISNEGLN 605
Cdd:COG4886   315 ILLLLLTTLLLLLLLLKGLLVTLTTL 340

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 2462613032 112 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNMLLriqqiIYCHKLTI-ILTKWRNTARH 190
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462613032 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 2462613032 496 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 573
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613032 574 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 652
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462613032 653 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 704
Cdd:cd09293   148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202

dimerization/docking (D/D) 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 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It 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        40
                  ....*....|....*....|....*....|....*....|...
gi 2462613032   8 NPRLKNYFKENYIPQVCEALLCGILVTCPEDPLRYLEGMIMVI 50
Cdd:cd22977     1 DPELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 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 2462613032 312 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPgvlclnlsnttitnrtmrllprhfhNLQNL 391
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCP-------------------------NLQVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613032 392 SLAYCRRFTDKGLQYLNLgnGCHKLIYLDLSGctqalVEKCSRItslvftgaphisdctfralsacklrkirfegnkrvT 471
Cdd:cd09293    84 DLRACENITDSGIVALAT--NCPKLQTINLGR-----HRNGHLI-----------------------------------T 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613032 472 DASFKFIDKNYPNLSHIYMADCKgITDSSLRSLSplkqltvlnlANCvrigdmglkqfldgpaSMRIRELNLSNCVRLSD 551
Cdd:cd09293   122 DVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELA----------SGC----------------SKSLERLSLNNCRNLTD 174

                         250       260
                  ....*....|....*....|....*..
gi 2462613032 552 ASVMKL--SERCPNLNYLSLRNCEHLT 576
Cdd:cd09293   175 QSIPAIlaSNYFPNLSVLEFRGCPLIT 201

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 2462613032 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 2462613032 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 2462613032  12 KNYFKENYIPQVCEALLCGILVTCPEDPLRYLE 44
Cdd:cd22978     5 KDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLE 37

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613032 360 CPGVLCLNLSNTTITNRTMRLLPR--HFHNLQNLSLAYCR------RFTDKGLQYLNlgngcHKLIYLDLSGCTqaLVEK 431
Cdd:cd00116    80 GCGLQELDLSDNALGPDGCGVLESllRSSSLQELKLNNNGlgdrglRLLAKGLKDLP-----PALEKLVLGRNR--LEGA 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613032 432 CSRITSLVFtgaPHIsdctfralsaCKLRKIRFeGNKRVTDASFKFID---KNYPNLSHIYMADCkGITDSSLRSLS--- 505
Cdd:cd00116   153 SCEALAKAL---RAN----------RDLKELNL-ANNGIGDAGIRALAeglKANCNLEVLDLNNN-GLTDEGASALAetl 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462613032 506 -PLKQLTVLNLANCVrIGDMGLKQFLDG--PASMRIRELNLSNCvRLSDASVMKLSERCPN---LNYLSLR 570
Cdd:cd00116   218 aSLKSLEVLNLGDNN-LTDAGAAALASAllSPNISLLTLSLSCN-DITDDGAKDLAEVLAEkesLLELDLR 286

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 2462613032 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 2462613032 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 2462613032 243 CDISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 285
Cdd:cd22178     1 VDWGNLLQDIILQIFQYLPLLDRAHASQVCRNWNQVFHMPDLW 43

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

                           10        20
                   ....*....|....*....|....*
gi 2462613032  611 KKLKELSVSECYRITDDGIQAFCKS 635
Cdd:smart00367   2 PNLRELDLSGCTNITDEGLQALAKG 26