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Conserved domains on  [gi|2462591261|ref|XP_054203200|]
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intraflagellar transport protein 122 homolog isoform X6 [Homo sapiens]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 18610525)

WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; similar to 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

CATH:  2.130.10.10
Gene Ontology:  GO:0005515
SCOP:  4002744

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
15-239 8.51e-26

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 111.16  E-value: 8.51e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   15 INDIAFKPDGTQLilAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDG-------------LWSPE--QKSVSK 76
Cdd:COG2319    165 VTSVAFSPDGKLL--ASGSDdgtVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGkllasgsadgtvrLWDLAtgKLLRTL 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   77 HKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEEKVKieRPGGSLSPIWSICWNPSreerNDILAVADWGQKVSFYQ 156
Cdd:COG2319    243 TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR--TLTGHSGGVNSVAFSPD----GKLLASGSDDGTVRLWD 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  157 L-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTI 234
Cdd:COG2319    317 LaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTV 396

                   ....*
gi 2462591261  235 SFYQL 239
Cdd:COG2319    397 RLWDL 401
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
565-815 7.06e-06

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


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.96  E-value: 7.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  565 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 641
Cdd:COG2956     46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  642 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 721
Cdd:COG2956    120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  722 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 800
Cdd:COG2956    171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242
                          250
                   ....*....|....*
gi 2462591261  801 QDPAQKDtMLGKFYH 815
Cdd:COG2956    243 PSDDLLL-ALADLLE 256
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
15-239 8.51e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 111.16  E-value: 8.51e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   15 INDIAFKPDGTQLilAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDG-------------LWSPE--QKSVSK 76
Cdd:COG2319    165 VTSVAFSPDGKLL--ASGSDdgtVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGkllasgsadgtvrLWDLAtgKLLRTL 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   77 HKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEEKVKieRPGGSLSPIWSICWNPSreerNDILAVADWGQKVSFYQ 156
Cdd:COG2319    243 TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR--TLTGHSGGVNSVAFSPD----GKLLASGSDDGTVRLWD 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  157 L-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTI 234
Cdd:COG2319    317 LaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTV 396

                   ....*
gi 2462591261  235 SFYQL 239
Cdd:COG2319    397 RLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
12-239 1.10e-13

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 72.75  E-value: 1.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   12 EHCINDIAFKPDGTQLILAAGSRLL-VYDTSDGTLLQPLKGHKDTVYcvayakdglwspeqksvskhkssskiiCCSWTN 90
Cdd:cd00200     51 TGPVRDVAASADGTYLASGSSDKTIrLWDLETGECVRTLTGHTSYVS---------------------------SVAFSP 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   91 DGQYLALGMFNGiiSIR---NKNGEEKVKIErpgGSLSPIWSICWNPSreerNDILAVADWGQKVSFYQLSGKQI----- 162
Cdd:cd00200    104 DGRILSSSSRDK--TIKvwdVETGKCLTTLR---GHTDWVNSVAFSPD----GTFVASSSQDGTIKLWDLRTGKCvatlt 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591261  163 GKDRALNfdpcCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 239
Cdd:cd00200    175 GHTGEVN----SVAFSPDGEKLLSSSSDGTIKLWdLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL 248
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
565-815 7.06e-06

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.96  E-value: 7.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  565 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 641
Cdd:COG2956     46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  642 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 721
Cdd:COG2956    120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  722 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 800
Cdd:COG2956    171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242
                          250
                   ....*....|....*
gi 2462591261  801 QDPAQKDtMLGKFYH 815
Cdd:COG2956    243 PSDDLLL-ALADLLE 256
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
581-789 1.93e-04

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.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 45.46  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  581 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 643
Cdd:TIGR02917  540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  644 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 717
Cdd:TIGR02917  613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462591261  718 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 789
Cdd:TIGR02917  663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
15-239 8.51e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 111.16  E-value: 8.51e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   15 INDIAFKPDGTQLilAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDG-------------LWSPE--QKSVSK 76
Cdd:COG2319    165 VTSVAFSPDGKLL--ASGSDdgtVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGkllasgsadgtvrLWDLAtgKLLRTL 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   77 HKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEEKVKieRPGGSLSPIWSICWNPSreerNDILAVADWGQKVSFYQ 156
Cdd:COG2319    243 TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR--TLTGHSGGVNSVAFSPD----GKLLASGSDDGTVRLWD 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  157 L-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTI 234
Cdd:COG2319    317 LaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTV 396

                   ....*
gi 2462591261  235 SFYQL 239
Cdd:COG2319    397 RLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
15-239 4.48e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.07  E-value: 4.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDG-------------LWSPE--QKSVSK 76
Cdd:COG2319    123 VRSVAFSPDGK--TLASGSAdgtVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGkllasgsddgtvrLWDLAtgKLLRTL 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   77 HKSSSKIICCSWTNDGQYLALGMFNGIISIRN-KNGEEkvkIERPGGSLSPIWSICWNPSreerNDILAVADWGQKVSFY 155
Cdd:COG2319    201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDlATGKL---LRTLTGHSGSVRSVAFSPD----GRLLASGSADGTVRLW 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  156 QLSGKQIGKD--------RALNFDPccisyftKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVV 226
Cdd:COG2319    274 DLATGELLRTltghsggvNSVAFSP-------DGKLLASGSDDGTVRLWdLATGKLLRTLTGHTGAVRSVAFSPDGKTLA 346
                          250
                   ....*....|...
gi 2462591261  227 VGCQDGTISFYQL 239
Cdd:COG2319    347 SGSDDGTVRLWDL 359
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
12-239 1.10e-13

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 72.75  E-value: 1.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   12 EHCINDIAFKPDGTQLILAAGSRLL-VYDTSDGTLLQPLKGHKDTVYcvayakdglwspeqksvskhkssskiiCCSWTN 90
Cdd:cd00200     51 TGPVRDVAASADGTYLASGSSDKTIrLWDLETGECVRTLTGHTSYVS---------------------------SVAFSP 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   91 DGQYLALGMFNGiiSIR---NKNGEEKVKIErpgGSLSPIWSICWNPSreerNDILAVADWGQKVSFYQLSGKQI----- 162
Cdd:cd00200    104 DGRILSSSSRDK--TIKvwdVETGKCLTTLR---GHTDWVNSVAFSPD----GTFVASSSQDGTIKLWDLRTGKCvatlt 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591261  163 GKDRALNfdpcCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 239
Cdd:cd00200    175 GHTGEVN----SVAFSPDGEKLLSSSSDGTIKLWdLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL 248
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
15-248 4.78e-11

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 65.05  E-value: 4.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCvayakdglwspeqksvskhkssskiicCSWTND 91
Cdd:cd00200     12 VTCVAFSPDGK--LLATGSGdgtIKVWDLETGELLRTLKGHTGPVRD---------------------------VAASAD 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   92 GQYLALGMFNGIISIRNKNGEEKVKIERpgGSLSPIWSICWNPSREerndILAVADWGQKVSFYQL-SGKQIGKDRALNF 170
Cdd:cd00200     63 GTYLASGSSDKTIRLWDLETGECVRTLT--GHTSYVSSVAFSPDGR----ILSSSSRDKTIKVWDVeTGKCLTTLRGHTD 136
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591261  171 DPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQLIFSTVHGLY 248
Cdd:cd00200    137 WVNSVAFSPDGTFVASSSQDGTIKLWdLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTL 215
WD40 COG2319
WD40 repeat [General function prediction only];
15-159 9.64e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.85  E-value: 9.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   15 INDIAFKPDGTQLilAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAyakdglWSPeqksvskhkssskiiccswtnD 91
Cdd:COG2319    291 VNSVAFSPDGKLL--ASGSDdgtVRLWDLATGKLLRTLTGHTGAVRSVA------FSP---------------------D 341
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591261   92 GQYLALGMFNGIISIRNKNGEEKVKIERpgGSLSPIWSICWNPSreerNDILAVADWGQKVSFYQLSG 159
Cdd:COG2319    342 GKTLASGSDDGTVRLWDLATGELLRTLT--GHTGAVTSVAFSPD----GRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
12-106 4.79e-08

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 55.80  E-value: 4.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261   12 EHCINDIAFKPDGTQLILAAGSR-LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGLW---------------SPEQKSVS 75
Cdd:cd00200    177 TGEVNSVAFSPDGEKLLSSSSDGtIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLlasgsedgtirvwdlRTGECVQT 256
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462591261   76 KHKSSSKIICCSWTNDGQYLALGMFNGIISI 106
Cdd:cd00200    257 LSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
122-240 2.91e-07

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 53.49  E-value: 2.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  122 GSLSPIWSICWNPSreerNDILAVADWGQKVSFYQLSGKQIGKDRALNFDP-CCISYFTKGEYILLGGSDKQVSLF-TKD 199
Cdd:cd00200      7 GHTGGVTCVAFSPD----GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPvRDVAASADGTYLASGSSDKTIRLWdLET 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2462591261  200 GVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQLI 240
Cdd:cd00200     83 GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE 123
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
565-815 7.06e-06

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.96  E-value: 7.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  565 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 641
Cdd:COG2956     46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  642 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 721
Cdd:COG2956    120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  722 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 800
Cdd:COG2956    171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242
                          250
                   ....*....|....*
gi 2462591261  801 QDPAQKDtMLGKFYH 815
Cdd:COG2956    243 PSDDLLL-ALADLLE 256
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
705-791 1.45e-04

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


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 44.87  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  705 LKSLVQLHVETQRWDEAFALGEK----HPEFKD-DIYMPYAQWLAENDRFEEAQKAFHKA-------------------- 759
Cdd:COG4700    127 LLGLAQALFELGRYAEALETLEKliakNPDFKSsDAHLLYARALEALGDLEAAEAELEALarrysgpearyryakflarq 206
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462591261  760 GRQREAVQVLEQLTNNAVAESRFNDAAYYYWM 791
Cdd:COG4700    207 GRTAEAKELLEEILDEAKHMPKHYRRLNREWI 238
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
581-789 1.93e-04

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.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 45.46  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  581 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 643
Cdd:TIGR02917  540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  644 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 717
Cdd:TIGR02917  613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462591261  718 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 789
Cdd:TIGR02917  663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
640-830 2.87e-03

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.87  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  640 EMYISAGEHVKAIEIC-------GDHGWVdmLIDIAR------KLDKAEreplllcATYLKKLDSPGYAAETYLKmgdlk 706
Cdd:COG2956     50 NLYRRRGEYDRAIRIHqkllerdPDRAEA--LLELAQdylkagLLDRAE-------ELLEKLLELDPDDAEALRL----- 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  707 sLVQLHVETQRWDEAFALGEK----HPEfKDDIYMPYAQWLAENDRFEEAQKAFHKA-GRQREAVQVLEQLTNNAVAESR 781
Cdd:COG2956    116 -LAEIYEQEGDWEKAIEVLERllklGPE-NAHAYCELAELYLEQGDYDEAIEALEKAlKLDPDCARALLLLAELYLEQGD 193
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462591261  782 FNDAAYYYwmlsMQCLDIAQDPAQKDTMLGKFYH----FQRLAELYHGYHAIH 830
Cdd:COG2956    194 YEEAIAAL----ERALEQDPDYLPALPRLAELYEklgdPEEALELLRKALELD 242
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
666-894 9.44e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.98  E-value: 9.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  666 DIARKLDKAEREPLLLCATYLKKLDSPGYAAETYLKMGDLKSLVQLHVETQRWDEAFALGEKHPEFKDDIYMPYAQW--- 742
Cdd:COG3914     42 GLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLgnl 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  743 LAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIAQDPAQKDTMLGKFY------- 814
Cdd:COG3914    122 LLALGRLEEALAALRRALALNpDFAEAYLNLGEALRRLGRLEEAIAAL----RRALELDPDNAEALNNLGNALqdlgrle 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591261  815 ----HFQRLAEL-------YHGYHAIHRHTEDPFSVHRPE--------TLFNISRFLLHSLPKDTPSGISKVKILFTLAK 875
Cdd:COG3914    198 eaiaAYRRALELdpdnadaHSNLLFALRQACDWEVYDRFEellaalarGPSELSPFALLYLPDDDPAELLALARAWAQLV 277
                          250       260
                   ....*....|....*....|..
gi 2462591261  876 QSKALGAYRLARHAYD---KLR 894
Cdd:COG3914    278 AAAAAPELPPPPNPRDpdrKLR 299
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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