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 313851009   9 PRLRSYFRDKYIPQICEALLCGLLVTCPEDPLKYLEHMILAI 50
Cdd:cd22977    2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 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        40
                 ....*....|....*....|....*....|....*....|..
gi 313851009 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWN 281
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42

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 313851009   9 PRLRSYFRDKYIPQICEALLCGLLVTCPEDPLKYLEHMILAI 50
Cdd:cd22977    2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 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 313851009 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWN 281
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851009 536 QLTVLNLtNCIRIGDIGLKHFFDG-PASIRLRELNLTNCSLlGDSSVIRLSE---RCPNLHYLNLRNcEHLTDLAIEYIA 611
Cdd:COG5238  181 SVETVYL-GCNQIGDEGIEELAEAlTQNTTVTTLWLKRNPI-GDEGAEILAEalkGNKSLTTLDLSN-NQIGDEGVIALA 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851009 612 SML----SLISVDLSGTLISNEGM----TILSRHRKLREVSVSDcVNITDFGIRAYCKT---SLLLEHLDVSYCsQLTDD 680
Cdd:COG5238  258 EALknntTVETLYLSGNQIGAEGAialaKALQGNTTLTSLDLSV-NRIGDEGAIALAEGlqgNKTLHTLNLAYN-GIGAQ 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851009 681 ----IIKTIAIFcTRITSLNIAGcPKITDAGMEILsarCHY------LHILDISGcIQLTDQ----IIQDLQIGckQLRI 746
Cdd:COG5238  336 gaiaLAKALQEN-TTLHSLDLSD-NQIGDEGAIAL---AKYlegnttLRELNLGK-NNIGKQgaeaLIDALQTN--RLHT 407

                 ...
gi 313851009 747 LKM 749
Cdd:COG5238  408 LIL 410

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

                           10        20
                   ....*....|....*....|....*
gi 313851009   588 CPNLHYLNLRNCEHLTDLAIEYIAS 612
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAK 25

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851009 306 NVLRLNFRGCDFrTKTLKAVSHCKNLQELNVSDCQsftdesMRHISE---GCPGVLYLNLSNTTITNrtmrlLPRYF--- 379
Cdd:COG4886  137 NLKELDLSNNQL-TDLPEPLGNLTNLKSLDLSNNQ------LTDLPEelgNLTNLKELDLSNNQITD-----LPEPLgnl 204

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313851009 380 HNLQNLSLAYCrKFTD--------KGLQYLNLGN----------GCHKLIYLDLSGcTQIS 422
Cdd:COG4886  205 TNLEELDLSGN-QLTDlpeplanlTNLETLDLSNnqltdlpelgNLTNLEELDLSN-NQLT 263

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 313851009   9 PRLRSYFRDKYIPQICEALLCGLLVTCPEDPLKYLEHMILAI 50
Cdd:cd22977    2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 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 313851009 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWN 281
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 313851009 431 SSCTGIVHLTINDMPTLTDNCVKVLVEKCPRISSVVLIGSPHISDSAFKALS-SCDLKKI----RFEGNKRISDACFKSI 505
Cdd:cd09293   49 SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALAtNCPKLQTinlgRHRNGHLITDVSLSAL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851009 506 DRNYPGINHIYMVDCKgltdsslkslsllkqltvlnltncirIGDIGLKHFFDGpASIRLRELNLTNCSLLGDSSV--IR 583
Cdd:cd09293  129 GKNCTFLQTVGFAGCD--------------------------VTDKGVWELASG-CSKSLERLSLNNCRNLTDQSIpaIL 181

                        170       180
                 ....*....|....*....|..
gi 313851009 584 LSERCPNLHYLNLRNCEHLTDL 605
Cdd:cd09293  182 ASNYFPNLSVLEFRGCPLITDF 203

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 313851009 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLW 280
Cdd:cd22118    1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41

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 313851009 360 LNLSNTTITNRTMRLLPRYFHNLQNLS-LAYCRKFT---DKGLQYL--NLGNGChKLIYLDLSGC--TQISVQGFRNIAS 431
Cdd:cd00116   28 LRLEGNTLGEEAAKALASALRPQPSLKeLCLSLNETgriPRGLQSLlqGLTKGC-GLQELDLSDNalGPDGCGVLESLLR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851009 432 SCT-GIVHLTINDM-PTLTDNCVKVLVEKCPRISSVVLIGSPHISDSAF---KALSS-CDLKKIRFeGNKRISDacfksi 505
Cdd:cd00116  107 SSSlQELKLNNNGLgDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEalaKALRAnRDLKELNL-ANNGIGD------ 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313851009 506 drnyPGINHIymvdCKGLTDSSlkslsllkQLTVLNLTNCIrIGDIGLKHFFDGPASIR-LRELNLTNCsLLGDSSVIRL 584
Cdd:cd00116  180 ----AGIRAL----AEGLKANC--------NLEVLDLNNNG-LTDEGASALAETLASLKsLEVLNLGDN-NLTDAGAAAL 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313851009 585 SE--RCPN--LHYLNLRNCeHLTDLA----IEYIASMLSLISVDLSGTLISNEGMTIL--SRHRKLRE 642
Cdd:cd00116  242 ASalLSPNisLLTLSLSCN-DITDDGakdlAEVLAEKESLLELDLRGNKFGEEGAQLLaeSLLEPGNE 308

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 313851009  12 RSYFRDKYIPQICEALLCGLLVTCPEDPLKYLE 44
Cdd:cd22978    5 KDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLE 37

F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, also called F-box and WD-40 domain-containing protein 8, or F-box only protein 29 (FBXO29), is the substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as GORASP1, IRS1, MAP4K1/HPK1. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 313851009 238 FDISvLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWNSI 283
Cdd:cd22134    3 FDIQ-LPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLWYRI 47

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
                 ....*....|....*....|....*....|....*...
gi 313851009 243 LPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLW 280
Cdd:cd22132    4 LPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLW 41

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 313851009 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLW 280
Cdd:cd22147    2 LSALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELW 42

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

                           10        20
                   ....*....|....*....|....*.
gi 313851009   328 CKNLQELNVSDCQSFTDESMRHISEG 353
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26

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 313851009 241 SVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQ 275
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 313851009  564 RLRELNLTNCSLlgdsSVIRLSERCPNLHYLNLRNCEHLTDL 605
Cdd:pfam12799   2 NLEVLDLSNNQI----TDIPPLAKLPNLETLDLSGNNKITDL 39

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 313851009 241 SVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWNSIDFS 286
Cdd:cd22104    2 ANLPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSLRLH 47

F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and similar proteins; ScCDC4 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 is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. 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 313851009 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLW 280
Cdd:cd22141    1 IGNLPFEISLKIFNYLQFEDLLNSLGVSKKWNKIIRNTALW 41