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Conserved domains on  [gi|526253060|ref|NP_001267475|]
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intraflagellar transport protein 122 homolog isoform 7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
19-141 2.25e-08

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.61  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   19 IERPGGSLSPIWSICWNPSreerNDILAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSL 97
Cdd:COG2319   281 LRTLTGHSGGVNSVAFSPD----GKLLASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 526253060   98 F-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 141
Cdd:COG2319   357 WdLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 485-735 1.06e-05

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: 48.19  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  485 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 561
Cdd:COG2956    46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  562 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 641
Cdd:COG2956   120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  642 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 720
Cdd:COG2956   171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242

                         250
                  ....*....|....*
gi 526253060  721 QDPAQKDtMLGKFYH 735
Cdd:COG2956   243 PSDDLLL-ALADLLE 256
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
19-141 2.25e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.61  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   19 IERPGGSLSPIWSICWNPSreerNDILAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSL 97
Cdd:COG2319   281 LRTLTGHSGGVNSVAFSPD----GKLLASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 526253060   98 F-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 141
Cdd:COG2319   357 WdLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 24-142 2.37e-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: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   24 GSLSPIWSICWNPSreerNDILAVADWGQKVSFYQLSGKQIGKDRALNFDP-CCISYFTKGEYILLGGSDKQVSLF-TKD 101
Cdd:cd00200     7 GHTGGVTCVAFSPD----GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPvRDVAASADGTYLASGSSDKTIRLWdLET 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 526253060  102 GVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQLI 142
Cdd:cd00200    83 GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE 123
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 485-735 1.06e-05

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: 48.19  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  485 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 561
Cdd:COG2956    46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  562 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 641
Cdd:COG2956   120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  642 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 720
Cdd:COG2956   171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242

                         250
                  ....*....|....*
gi 526253060  721 QDPAQKDtMLGKFYH 735
Cdd:COG2956   243 PSDDLLL-ALADLLE 256
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 501-709 1.78e-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: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   501 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 563
Cdd:TIGR02917  540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   564 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 637
Cdd:TIGR02917  613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526253060   638 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 709
Cdd:TIGR02917  663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
19-141 2.25e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.61  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   19 IERPGGSLSPIWSICWNPSreerNDILAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSL 97
Cdd:COG2319   281 LRTLTGHSGGVNSVAFSPD----GKLLASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 526253060   98 F-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 141
Cdd:COG2319   357 WdLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
24-141 4.44e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.46  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   24 GSLSPIWSICWNPSreerNDILAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKD 101
Cdd:COG2319   202 GHTGAVRSVAFSPD----GKLLASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWdLAT 277

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 526253060  102 GVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 141
Cdd:COG2319   278 GELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 24-142 2.37e-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: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   24 GSLSPIWSICWNPSreerNDILAVADWGQKVSFYQLSGKQIGKDRALNFDP-CCISYFTKGEYILLGGSDKQVSLF-TKD 101
Cdd:cd00200     7 GHTGGVTCVAFSPD----GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPvRDVAASADGTYLASGSSDKTIRLWdLET 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 526253060  102 GVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQLI 142
Cdd:cd00200    83 GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE 123
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 485-735 1.06e-05

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: 48.19  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  485 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 561
Cdd:COG2956    46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  562 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 641
Cdd:COG2956   120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  642 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 720
Cdd:COG2956   171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242

                         250
                  ....*....|....*
gi 526253060  721 QDPAQKDtMLGKFYH 735
Cdd:COG2956   243 PSDDLLL-ALADLLE 256
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 27-141 1.27e-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: 48.10  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   27 SPIWSICWNPSreerNDILAVADWGQKVSFYQLSGKQI-----GKDRALNfdpcCISYFTKGEYILLGGSDKQVSLF-TK 100
Cdd:cd00200   136 DWVNSVAFSPD----GTFVASSSQDGTIKLWDLRTGKCvatltGHTGEVN----SVAFSPDGEKLLSSSSDGTIKLWdLS 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 526253060  101 DGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 141
Cdd:cd00200   208 TGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL 248
WD40 COG2319
WD40 repeat [General function prediction only];
21-141 2.49e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 47.98  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   21 RPGGSLSPIWSICWNPSreerNDILAVADWGQKVSFYQL-SGKQI-------GKDRALNFDPccisyftKGEYILLGGSD 92
Cdd:COG2319   115 TLTGHTGAVRSVAFSPD----GKTLASGSADGTVRLWDLaTGKLLrtltghsGAVTSVAFSP-------DGKLLASGSDD 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 526253060   93 KQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 141
Cdd:COG2319   184 GTVRLWdLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 75-141 2.58e-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: 2.58e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526253060   75 CCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 141
Cdd:cd00200    97 SSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
625-711 1.69e-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: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  625 LKSLVQLHVETQRWDEAFALGEK----HPEFKD-DIYMPYAQWLAENDRFEEAQKAFHKA-------------------- 679
Cdd:COG4700   127 LLGLAQALFELGRYAEALETLEKliakNPDFKSsDAHLLYARALEALGDLEAAEAELEALarrysgpearyryakflarq 206

                          90       100       110
                  ....*....|....*....|....*....|..
gi 526253060  680 GRQREAVQVLEQLTNNAVAESRFNDAAYYYWM 711
Cdd:COG4700   207 GRTAEAKELLEEILDEAKHMPKHYRRLNREWI 238
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 501-709 1.78e-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: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   501 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 563
Cdd:TIGR02917  540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   564 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 637
Cdd:TIGR02917  613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526253060   638 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 709
Cdd:TIGR02917  663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 27-140 3.36e-03

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: 40.78  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060   27 SPIWSICWNPSREErndiLAVADWGQKVSFYQLSGKQ-----IGKDRALNfdpcCISYFTKGEYILLGGSDKQVSLF-TK 100
Cdd:cd00200   178 GEVNSVAFSPDGEK----LLSSSSDGTIKLWDLSTGKclgtlRGHENGVN----SVAFSPDGYLLASGSEDGTIRVWdLR 249

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 526253060  101 DGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQ 140
Cdd:cd00200   250 TGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 560-750 3.73e-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: 40.48  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  560 EMYISAGEHVKAIEIC-------GDHGWVdmLIDIAR------KLDKAEreplllcATYLKKLDSPGYAAETYLKmgdlk 626
Cdd:COG2956    50 NLYRRRGEYDRAIRIHqkllerdPDRAEA--LLELAQdylkagLLDRAE-------ELLEKLLELDPDDAEALRL----- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  627 sLVQLHVETQRWDEAFALGEK----HPEfKDDIYMPYAQWLAENDRFEEAQKAFHKA-GRQREAVQVLEQLTNNAVAESR 701
Cdd:COG2956   116 -LAEIYEQEGDWEKAIEVLERllklGPE-NAHAYCELAELYLEQGDYDEAIEALEKAlKLDPDCARALLLLAELYLEQGD 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 526253060  702 FNDAAYYYwmlsMQCLDIAQDPAQKDTMLGKFYH----FQRLAELYHGYHAIH 750
Cdd:COG2956   194 YEEAIAAL----ERALEQDPDYLPALPRLAELYEklgdPEEALELLRKALELD 242
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 586-814 8.73e-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: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  586 DIARKLDKAEREPLLLCATYLKKLDSPGYAAETYLKMGDLKSLVQLHVETQRWDEAFALGEKHPEFKDDIYMPYAQW--- 662
Cdd:COG3914    42 GLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLgnl 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  663 LAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIAQDPAQKDTMLGKFY------- 734
Cdd:COG3914   122 LLALGRLEEALAALRRALALNpDFAEAYLNLGEALRRLGRLEEAIAAL----RRALELDPDNAEALNNLGNALqdlgrle 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253060  735 ----HFQRLAEL-------YHGYHAIHRHTEDPFSVHRPE--------TLFNISRFLLHSLPKDTPSGISKVKILFTLAK 795
Cdd:COG3914   198 eaiaAYRRALELdpdnadaHSNLLFALRQACDWEVYDRFEellaalarGPSELSPFALLYLPDDDPAELLALARAWAQLV 277

                         250       260
                  ....*....|....*....|..
gi 526253060  796 QSKALGAYRLARHAYD---KLR 814
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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