F-box domain found in F-box/WD repeat-containing protein 7 (FBXW7) and similar proteins; FBXW7, also called Archipelago homolog (Ago), F-box and WD-40 domain-containing protein 7, F-box protein FBX30, SEL-10, or Cdc4, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1, and probably PSEN1. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936785 184 QVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 242
Cdd:cd22133     1 QVRHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 294 KVLKGHDDhVITCLQF--CGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGV----WSSQmrDNIIISGSTDRTLKVWN 367
Cdd:cd00200     3 RTLKGHTG-GVTCVAFspDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVrdvaASAD--GTYLASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 368 AETGECIHTLYGHTSTVRCMHLHEKR--VVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQY--DGRRVVSGAYDFMV 443
Cdd:cd00200    80 LETGECVRTLTGHTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFspDGTFVASSSQDGTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 444 KVWDPETETCLHTLQGHTNRVYSLQF--DGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQ-SLTSGMELKDN-ILVSGNA 519
Cdd:cd00200   160 KLWDLRTGKCVATLTGHTGEVNSVAFspDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHEnGVNSVAFSPDGyLLASGSE 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622936785 520 DSTVKIWDIKTGQCLQTLQGpnkHQSAVTCLQF--NKNFVITSSDDGTVKLWD 570
Cdd:cd00200   240 DGTIRVWDLRTGECVQTLSG---HTNSVTSLAWspDGKRLASGSADGTIRIWD 289

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622936785 201 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 245
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622936785  530 TGQCLQTLQGpnkHQSAVTCLQFNKN--FVITSSDDGTVKLWD 570
Cdd:smart00320   1 SGELLKTLKG---HTGPVTSVAFSPDgkYLASGSDDGTIKLWD 40

A Receptor for Ubiquitination Targets;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1622936785  204 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREK 244
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 285 WRRGELKSPKVLKGHDDHViTCLQF--CGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWSSQMRDN--IIISGSTD 360
Cdd:COG2319   105 WDLATGLLLRTLTGHTGAV-RSVAFspDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDgkLLASGSDD 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 361 RTLKVWNAETGECIHTLYGHTSTVRCMHLH--EKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQY--DGRRVVS 436
Cdd:COG2319   184 GTVRLWDLATGKLLRTLTGHTGAVRSVAFSpdGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFspDGRLLAS 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 437 GAYDFMVKVWDPETETCLHTLQGHTNRVYSLQF--DGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMEL--KDN 512
Cdd:COG2319   264 GSADGTVRLWDLATGELLRTLTGHSGGVNSVAFspDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGK 343

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936785 513 ILVSGNADSTVKIWDIKTGQCLQTLQGpnkHQSAVTCLQFNKN--FVITSSDDGTVKLWDLKT 573
Cdd:COG2319   344 TLASGSDDGTVRLWDLATGELLRTLTG---HTGAVTSVAFSPDgrTLASGSADGTVRLWDLAT 403

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 373 CIHTLYGHTSTVRCMHLHE--KRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQY--DGRRVVSGAYDFMVKVWDP 448
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAsaDGTYLASGSSDKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 449 ETETCLHTLQGHTNRVYSLQFDGIH--VVSGSLDTSIRVWDVETGNCIHTLTGHQSltSGMELK----DNILVSGNADST 522
Cdd:cd00200    81 ETGECVRTLTGHTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLTTLRGHTD--WVNSVAfspdGTFVASSSQDGT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 523 VKIWDIKTGQCLQTLQGpnkHQSAVTCLQF--NKNFVITSSDDGTVKLWDLKTGEFIRNLVtlesgGSGGVVWRIRASNT 600
Cdd:cd00200   159 IKLWDLRTGKCVATLTG---HTGEVNSVAFspDGEKLLSSSSDGTIKLWDLSTGKCLGTLR-----GHENGVNSVAFSPD 230

                         250
                  ....*....|..
gi 1622936785 601 KLVCAVGSRNGT 612
Cdd:cd00200   231 GYLLASGSEDGT 242

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 430 DGRRVVSGAYDFMVKVWDPETETCLHTLQGHTNRVYSLQF--DGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGM 507
Cdd:COG2319     5 DGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAAspDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 508 ELK--DNILVSGNADSTVKIWDIKTGQCLQTLQGpnkHQSAVTCLQFNKN--FVITSSDDGTVKLWDLKTGEFIRNLVtl 583
Cdd:COG2319    85 AFSpdGRLLASASADGTVRLWDLATGLLLRTLTG---HTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLT-- 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622936785 584 esgGSGGVVWRIRAS-NTKLVcAVGSRNGT 612
Cdd:COG2319   160 ---GHSGAVTSVAFSpDGKLL-ASGSDDGT 185

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622936785 201 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 245
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45

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        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622936785 199 DFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 245
Cdd:cd22094     1 DFTRVLPRFLSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELWLPKC 47

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        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622936785 196 FQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 245
Cdd:cd22172     1 EHIDFTRVLPRVLSLYIFSFLDPRSLCRCAQVCWYWKYLTELDQLWMPKC 50

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 1622936785 202 SLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWRE 243
Cdd:cd22132     2 PLLPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKE 43

protein SPA1-RELATED; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 312 NRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWS---SQMRDNIIISGSTDRTLKVWNAETGECIHTLyGHTSTVRCMH 388
Cdd:PLN00181  546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSidySSADPTLLASGSDDGSVKLWSINQGVSIGTI-KTKANICCVQ 624

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 389 LHE---KRVVSGSRDATLRVWDIETGQC-LHVLMGHVAAVRCVQY-DGRRVVSGAYDFMVKVWDPE------TETCLHTL 457
Cdd:PLN00181  625 FPSesgRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFvDSSTLVSSSTDNTLKLWDLSmsisgiNETPLHSF 704

                         170       180
                  ....*....|....*....|....
gi 1622936785 458 QGHTNrvySLQFDGIHVVSGSLDT 481
Cdd:PLN00181  705 MGHTN---VKNFVGLSVSDGYIAT 725

F-box domain found in F-box/WD repeat-containing protein 12 (FBXW12) and similar proteins; FBXW12, also called F-box and WD-40 domain-containing protein 12, or F-box only protein 35 (FBXO35), is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It functions as an epithelial growth suppressor. 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 1622936785 204 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 245
Cdd:cd22137     3 LPDLPMLRIFSFLDAFSLLQAAQVNKQWNKVADSDYLWRNLC 44

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        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622936785 201 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDN-LLWREKC 245
Cdd:cd22113     1 IELLPPEMSLRIFSQLDVQSLCRASQTCKTWNDLIENSdYLWRPHC 46

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 1622936785 201 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLW 241
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLW 41

F-box domain found in F-box only protein 7 (FBXO7) and similar proteins; FBXO7, also called FBX7, 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 recognizes BIRC2 and DLGAP5. FBXO7 plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PRKN to dysfunctional depolarized mitochondria. It promotes MFN1 ubiquitination. FBXO7 acts as a cell cycle regulator by enhancing cyclin D/cyclin-dependent kinase 6 (Cdk6) complex formation and stabilizing levels of p27, a cyclin-dependent kinase inhibitor. Mutations in the FBXO7 (PARK15) gene have been implicated in a juvenile form of parkinsonism called parkinsonian pyramidal syndrome (PPS), characterized by Parkinsonian symptoms and pyramidal tract signs. 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 1622936785 203 LLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 245
Cdd:cd22087     3 ALPPEIKLRILSLLDVRSLLSLSQVCRDLNSATNDQLLWRFLL 45

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622936785  530 TGQCLQTLQGpnkHQSAVTCLQFNKN--FVITSSDDGTVKLWD 570
Cdd:smart00320   1 SGELLKTLKG---HTGPVTSVAFSPDgkYLASGSDDGTIKLWD 40

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1622936785  450 TETCLHTLQGHTNRVYSLQF--DGIHVVSGSLDTSIRVWD 487
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). 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 1622936785 201 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 242
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWK 42

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 1622936785 204 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 242
Cdd:cd22115     7 LPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNWQ 45

F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It 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 1622936785 201 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCKE 247
Cdd:cd22084     1 LDDLPSDPLLNILSFLDYRDLISCSQVCRRLNQLCSHDPLWKRLCKK 47

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622936785 371 GECIHTLYGHTSTVRCMHLH--EKRVVSGSRDATLRVWD 407
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSpdGKLLASGSDDGTVKVWD 39

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 31 (AtSKIP31) and similar proteins; AtSKIP31, also called F-box protein SKIP31, is a component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with SKP1A/ASK1 and SPK1B/ASK2. 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 1622936785 204 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 242
Cdd:cd22166     4 LPPELFRHILKFLSPEDLTSCATVCRFLRGAASDESLWR 42

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        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622936785 197 QRDFISLLPKE----LALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWRE 243
Cdd:cd22130     1 QRDFISALPAKgldhIAENILSYLDAKSLCAAELVCKEWYRVIADGMLWKK 51

A Receptor for Ubiquitination Targets;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1622936785  204 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREK 244
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41

F-box domain found in F-box/WD repeat-containing protein 1B (FBXW1B) and similar proteins; 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 (SKP1-CUL1-F-box protein) 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        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622936785 197 QRDFISLLPKE----LALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWRE 243
Cdd:cd22183     1 QRDFITALPAKgldhIAENILSYLDAESLCAAELVCKEWQRVISEGMLWKK 51

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 1622936785 202 SLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 245
Cdd:cd22151     1 RKLPDDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWENAC 44

coronin; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 419 GHVAAVRCVQYDGRRVVSGAYDFMVKVWD-PE---TETCLHT---LQGHTNRVYSLQF----DGIhVVSGSLDTSIRVWD 487
Cdd:PTZ00421   76 GPIIDVAFNPFDPQKLFTASEDGTIMGWGiPEeglTQNISDPivhLQGHTKKVGIVSFhpsaMNV-LASAGADMVVNVWD 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936785 488 VETGNCIHTLTGHQSLTSGME--LKDNILVSGNADSTVKIWDIKTGQCLQTLQG--PNKHQSAVTCLQfnKNFVIT---- 559
Cdd:PTZ00421  155 VERGKAVEVIKCHSDQITSLEwnLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAhaSAKSQRCLWAKR--KDLIITlgcs 232

                         170
                  ....*....|...
gi 1622936785 560 SSDDGTVKLWDLK 572
Cdd:PTZ00421  233 KSQQRQIMLWDTR 245

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1622936785  330 TGKCLRTLVGHTGGVWSSQM--RDNIIISGSTDRTLKVWN 367
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

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 1622936785 201 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCK 246
Cdd:cd22093     1 IERLPSEILLKILSYLDASSLLCISCVNKLFYQLANDNALWRKLYS 46

F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called FBX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1), 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 DTL/CDT2, BCL6 and PRDM1/BLIMP1. 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 1622936785 204 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 242
Cdd:cd22091     4 LPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWK 42