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Conserved domains on  [gi|526253058|ref|NP_001267474|]
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intraflagellar transport protein 122 homolog isoform 6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 super family cl43672
WD40 repeat [General function prediction only];
103-200 5.16e-06

WD40 repeat [General function prediction only];


The actual alignment was detected with superfamily member COG2319:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 50.29  E-value: 5.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  103 ILAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAK 180
Cdd:COG2319   218 LLASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWdLATGELLRTLTGHSGGVNSVAFS 297

                          90       100
                  ....*....|....*....|
gi 526253058  181 PDSNYVVVGCQDGTISFYQL 200
Cdd:COG2319   298 PDGKLLASGSDDGTVRLWDL 317
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 544-794 8.57e-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: 48.57  E-value: 8.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  544 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 620
Cdd:COG2956    46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  621 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 700
Cdd:COG2956   120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  701 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 779
Cdd:COG2956   171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242

                         250
                  ....*....|....*
gi 526253058  780 QDPAQKDtMLGKFYH 794
Cdd:COG2956   243 PSDDLLL-ALADLLE 256
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
103-200 5.16e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 50.29  E-value: 5.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  103 ILAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAK 180
Cdd:COG2319   218 LLASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWdLATGELLRTLTGHSGGVNSVAFS 297

                          90       100
                  ....*....|....*....|
gi 526253058  181 PDSNYVVVGCQDGTISFYQL 200
Cdd:COG2319   298 PDGKLLASGSDDGTVRLWDL 317
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 544-794 8.57e-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: 48.57  E-value: 8.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  544 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 620
Cdd:COG2956    46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  621 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 700
Cdd:COG2956   120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  701 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 779
Cdd:COG2956   171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242

                         250
                  ....*....|....*
gi 526253058  780 QDPAQKDtMLGKFYH 794
Cdd:COG2956   243 PSDDLLL-ALADLLE 256
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 134-200 2.75e-05

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: 47.33  E-value: 2.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526253058  134 CCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 200
Cdd:cd00200    97 SSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 560-768 1.89e-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: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058   560 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 622
Cdd:TIGR02917  540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058   623 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 696
Cdd:TIGR02917  613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526253058   697 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 768
Cdd:TIGR02917  663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
103-200 5.16e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 50.29  E-value: 5.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  103 ILAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAK 180
Cdd:COG2319   218 LLASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWdLATGELLRTLTGHSGGVNSVAFS 297

                          90       100
                  ....*....|....*....|
gi 526253058  181 PDSNYVVVGCQDGTISFYQL 200
Cdd:COG2319   298 PDGKLLASGSDDGTVRLWDL 317
WD40 COG2319
WD40 repeat [General function prediction only];
103-200 8.11e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 49.52  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  103 ILAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAK 180
Cdd:COG2319   302 LLASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGAVTSVAFS 381

                          90       100
                  ....*....|....*....|
gi 526253058  181 PDSNYVVVGCQDGTISFYQL 200
Cdd:COG2319   382 PDGRTLASGSADGTVRLWDL 401
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 544-794 8.57e-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: 48.57  E-value: 8.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  544 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 620
Cdd:COG2956    46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  621 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 700
Cdd:COG2956   120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  701 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 779
Cdd:COG2956   171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242

                         250
                  ....*....|....*
gi 526253058  780 QDPAQKDtMLGKFYH 794
Cdd:COG2956   243 PSDDLLL-ALADLLE 256
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 134-200 2.75e-05

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: 47.33  E-value: 2.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526253058  134 CCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 200
Cdd:cd00200    97 SSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 135-200 1.29e-04

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: 45.02  E-value: 1.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526253058  135 CISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 200
Cdd:cd00200   182 SVAFSPDGEKLLSSSSDGTIKLWdLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL 248
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
684-770 1.56e-04

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


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 44.49  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  684 LKSLVQLHVETQRWDEAFALGEK----HPEFKD-DIYMPYAQWLAENDRFEEAQKAFHKA-------------------- 738
Cdd:COG4700   127 LLGLAQALFELGRYAEALETLEKliakNPDFKSsDAHLLYARALEALGDLEAAEAELEALarrysgpearyryakflarq 206

                          90       100       110
                  ....*....|....*....|....*....|..
gi 526253058  739 GRQREAVQVLEQLTNNAVAESRFNDAAYYYWM 770
Cdd:COG4700   207 GRTAEAKELLEEILDEAKHMPKHYRRLNREWI 238
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 560-768 1.89e-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: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058   560 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 622
Cdd:TIGR02917  540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058   623 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 696
Cdd:TIGR02917  613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526253058   697 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 768
Cdd:TIGR02917  663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 135-201 2.47e-04

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: 44.25  E-value: 2.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526253058  135 CISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQLI 201
Cdd:cd00200    56 DVAASADGTYLASGSSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE 123
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 134-200 4.29e-04

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: 43.48  E-value: 4.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526253058  134 CCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 200
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKVWdLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
WD40 COG2319
WD40 repeat [General function prediction only];
103-200 1.73e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.21  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  103 ILAVADWGQKVSFYQL-SGKQI-------GKDRALNFDPccisyftKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSW 173
Cdd:COG2319   134 TLASGSADGTVRLWDLaTGKLLrtltghsGAVTSVAFSP-------DGKLLASGSDDGTVRLWdLATGKLLRTLTGHTGA 206

                          90       100
                  ....*....|....*....|....*..
gi 526253058  174 VWTCQAKPDSNYVVVGCQDGTISFYQL 200
Cdd:COG2319   207 VRSVAFSPDGKLLASGSADGTVRLWDL 233
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 619-809 3.21e-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: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  619 EMYISAGEHVKAIEIC-------GDHGWVdmLIDIAR------KLDKAEreplllcATYLKKLDSPGYAAETYLKmgdlk 685
Cdd:COG2956    50 NLYRRRGEYDRAIRIHqkllerdPDRAEA--LLELAQdylkagLLDRAE-------ELLEKLLELDPDDAEALRL----- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  686 sLVQLHVETQRWDEAFALGEK----HPEfKDDIYMPYAQWLAENDRFEEAQKAFHKA-GRQREAVQVLEQLTNNAVAESR 760
Cdd:COG2956   116 -LAEIYEQEGDWEKAIEVLERllklGPE-NAHAYCELAELYLEQGDYDEAIEALEKAlKLDPDCARALLLLAELYLEQGD 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 526253058  761 FNDAAYYYwmlsMQCLDIAQDPAQKDTMLGKFYH----FQRLAELYHGYHAIH 809
Cdd:COG2956   194 YEEAIAAL----ERALEQDPDYLPALPRLAELYEklgdPEEALELLRKALELD 242
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 645-873 8.34e-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: 8.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  645 DIARKLDKAEREPLLLCATYLKKLDSPGYAAETYLKMGDLKSLVQLHVETQRWDEAFALGEKHPEFKDDIYMPYAQW--- 721
Cdd:COG3914    42 GLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLgnl 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  722 LAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIAQDPAQKDTMLGKFY------- 793
Cdd:COG3914   122 LLALGRLEEALAALRRALALNpDFAEAYLNLGEALRRLGRLEEAIAAL----RRALELDPDNAEALNNLGNALqdlgrle 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253058  794 ----HFQRLAEL-------YHGYHAIHRHTEDPFSVHRPE--------TLFNISRFLLHSLPKDTPSGISKVKILFTLAK 854
Cdd:COG3914   198 eaiaAYRRALELdpdnadaHSNLLFALRQACDWEVYDRFEellaalarGPSELSPFALLYLPDDDPAELLALARAWAQLV 277

                         250       260
                  ....*....|....*....|..
gi 526253058  855 QSKALGAYRLARHAYD---KLR 873
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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