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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568943265  134 CCISYFTKGEYILVGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCRVKPDSNYVVVGCQDGTISFYQL 200
Cdd:cd00200    97 SSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunit. It is a heptameric complex that can polymerize into a cage to deform the membrane into a bud. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. This model corresponds to the WD-associated region (WDAD) found in coatomer subunits alpha, beta, and beta' and is composed of a beta-propeller and an alpha-solenoid. The WD40 domain is 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. It 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 the GH and WD lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet. 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. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands allowing them to bind either stably or reversibly.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265  481 KEAYQIACLGVTDADWRELAMEALEGLEFETARKAFTRVQDLRYLELISSIE----------ERKKRGETNNDLFladvF 550
Cdd:cd22938   353 KIAYQLAHFVKDEKKWFSLALECGSKCNFELALEAAKAANDWEKLGLLALLQgnhqivemlaQRAENFGKNNKAF----F 428

                          90
                  ....*....|....*....
gi 568943265  551 SY--QGKFHEAAKLYKRSG 567
Cdd:cd22938   429 LYliTGKLRKMMKLLIIRK 447

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568943265  134 CCISYFTKGEYILVGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCRVKPDSNYVVVGCQDGTISFYQL 200
Cdd:cd00200    97 SSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265  544 LFLADVFSYQGKFHEAAKLYKRSghenLALDMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNINEPKAA---VEM 620
Cdd:COG2956    46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265  621 YISAGEHAKAIEisgshgwvdmlidIARKLDKAErepllmcacyfkkldspGYAAETYLKIGdlkslvQLYVDTKRWDEA 700
Cdd:COG2956   120 YEQEGDWEKAIE-------------VLERLLKLG-----------------PENAHAYCELA------ELYLEQGDYDEA 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568943265  701 FALGEK----HPEFkDDVYVPYAQWLAENDRFEEAQKAFHKAGRQ-GEAVRVLEQLTHNAVVESRFNDAAYYY 768
Cdd:COG2956   164 IEALEKalklDPDC-ARALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL 235

Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunit. It is a heptameric complex that can polymerize into a cage to deform the membrane into a bud. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. This model corresponds to the WD-associated region (WDAD) found in coatomer subunits alpha, beta, and beta' and is composed of a beta-propeller and an alpha-solenoid. The WD40 domain is 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. It 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 the GH and WD lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet. 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. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands allowing them to bind either stably or reversibly.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265  481 KEAYQIACLGVTDADWRELAMEALEGLEFETARKAFTRVQDLRYLELISSIE----------ERKKRGETNNDLFladvF 550
Cdd:cd22938   353 KIAYQLAHFVKDEKKWFSLALECGSKCNFELALEAAKAANDWEKLGLLALLQgnhqivemlaQRAENFGKNNKAF----F 428

                          90
                  ....*....|....*....
gi 568943265  551 SY--QGKFHEAAKLYKRSG 567
Cdd:cd22938   429 LYliTGKLRKMMKLLIIRK 447

WD domain, G-beta repeat;

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568943265   161 GVRLGTVGEQNSWVWTCRVKPDSNYVVVGCQDGTISFY 198
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568943265  134 CCISYFTKGEYILVGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCRVKPDSNYVVVGCQDGTISFYQL 200
Cdd:cd00200    97 SSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265   91 SPrDGNseehndILAVADWGQKLSFYQL-SGKQIGKDRPLNFDPCCISYFTKGEYILVGGSDKQVSLF-TKDGVRLGTVG 168
Cdd:COG2319   297 SP-DGK------LLASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLT 369

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568943265  169 EQNSWVWTCRVKPDSNYVVVGCQDGTISFYQL 200
Cdd:COG2319   370 GHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568943265  135 CISYFTKGEYILVGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCRVKPDSNYVVVGCQDGTISFYQL 200
Cdd:cd00200   182 SVAFSPDGEKLLSSSSDGTIKLWdLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL 248

Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265  684 LKSLVQLYVDTKRWDEAFALGEK----HPEFKD-DVYVPYAQWLAENDRFEEAQKAFHKA-------------------- 738
Cdd:COG4700   127 LLGLAQALFELGRYAEALETLEKliakNPDFKSsDAHLLYARALEALGDLEAAEAELEALarrysgpearyryakflarq 206

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568943265  739 GRQGEAVRVLEQLTHNAVVESRFNDAAYYYWM 770
Cdd:COG4700   207 GRTAEAKELLEEILDEAKHMPKHYRRLNREWI 238

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265   560 AKLYKRSGHENLALDMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARninEPKAAVEM----YI 622
Cdd:TIGR02917  540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265   623 SAGEHAKAIEIsgshgwvdmlidiARKLdkAEREP------LLMCACYFKKLDSPGyaAETYLKIG-DLKS--------L 687
Cdd:TIGR02917  613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLKRAlELKPdnteaqigL 675

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265   688 VQLYVDTKRWDEAFALG----EKHPE------FKDDVYVPYAQWLAENDRFEEAQK-------------AFHKAGRQGEA 744
Cdd:TIGR02917  676 AQLLLAAKRTESAKKIAkslqKQHPKaalgfeLEGDLYLRQKDYPAAIQAYRKALKrapssqnaiklhrALLASGNTAEA 755

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265   745 VRVLEQ-LTHNAvvesrfNDAAYYYwMLSMQCLDMAQADPAQKdamldkfhHFQHLAELY 803
Cdd:TIGR02917  756 VKTLEAwLKTHP------NDAVLRT-ALAELYLAQKDYDKAIK--------HYQTVVKKA 800

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265  619 EMYISAGEHAKAIEI-------SGSHGWVdmLIDIAR------KLDKAERepllmcacYFKKL-DSPGYAAETYLKigdl 684
Cdd:COG2956    50 NLYRRRGEYDRAIRIhqkllerDPDRAEA--LLELAQdylkagLLDRAEE--------LLEKLlELDPDDAEALRL---- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265  685 ksLVQLYVDTKRWDEAFALGEK----HPEfKDDVYVPYAQWLAENDRFEEAQKAFHKA-GRQGEAVRVLEQLTHNAVVES 759
Cdd:COG2956   116 --LAEIYEQEGDWEKAIEVLERllklGPE-NAHAYCELAELYLEQGDYDEAIEALEKAlKLDPDCARALLLLAELYLEQG 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568943265  760 RFNDAAYYYwmlsmqcLDMAQADPAQKDAMLdkfhhfqHLAELYH 804
Cdd:COG2956   193 DYEEAIAAL-------ERALEQDPDYLPALP-------RLAELYE 223

Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunit. It is a heptameric complex that can polymerize into a cage to deform the membrane into a bud. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. This model corresponds to the WD-associated region (WDAD) found in coatomer subunits alpha, beta, and beta' and is composed of a beta-propeller and an alpha-solenoid. The WD40 domain is 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. It 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 the GH and WD lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet. 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. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands allowing them to bind either stably or reversibly.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943265  481 KEAYQIACLGVTDADWRELAMEALEGLEFETARKAFTRVQDLRYLELISSIE----------ERKKRGETNNDLFladvF 550
Cdd:cd22938   353 KIAYQLAHFVKDEKKWFSLALECGSKCNFELALEAAKAANDWEKLGLLALLQgnhqivemlaQRAENFGKNNKAF----F 428

                          90
                  ....*....|....*....
gi 568943265  551 SY--QGKFHEAAKLYKRSG 567
Cdd:cd22938   429 LYliTGKLRKMMKLLIIRK 447

WD domain, G-beta repeat;

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568943265   161 GVRLGTVGEQNSWVWTCRVKPDSNYVVVGCQDGTISFY 198
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38