|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
15-342 |
2.72e-32 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 130.80 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:COG2319 123 VRSVAFSPDGK--TLASGSAdgtVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWdlaTGKLLRTL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 89 KytswsvmsslhlhlpflglhktvrvtatdkapkgqggridclrpsvqnqpgqKHNDAIQCVSYNPITHQLASCSSSDF- 167
Cdd:COG2319 201 T----------------------------------------------------GHTGAVRSVAFSPDGKLLASGSADGTv 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 168 GLWSPE--QKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEEKVKieRPGGSLSPIWSICWNPSreerNDI 245
Cdd:COG2319 229 RLWDLAtgKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR--TLTGHSGGVNSVAFSPD----GKL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 246 LAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKP 323
Cdd:COG2319 303 LASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGAVTSVAFSP 382
|
330
....*....|....*....
gi 526253054 324 DSNYVVVGCQDGTISFYQL 342
Cdd:COG2319 383 DGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
49-341 |
3.11e-19 |
|
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: 89.70 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 49 LKGHKDTVYCVAYAKDGKRFASGSADKSVIIWTSKlEGILKYTS-------WSVMSSLHLHLPFL-GLHKTVRVTATDKa 120
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE-TGELLRTLkghtgpvRDVAASADGTYLASgSSDKTIRLWDLET- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 121 pkgqGGRIDCLRPsvqnqpgqkHNDAIQCVSYNPiTHQLASCSSSD--FGLWSPEQKSVSKHKS--SSKIICCSWTNDGQ 196
Cdd:cd00200 83 ----GECVRTLTG---------HTSYVSSVAFSP-DGRILSSSSRDktIKVWDVETGKCLTTLRghTDWVNSVAFSPDGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 197 YLALGMFNGIISI-RNKNGEEKVKIErpgGSLSPIWSICWNPSREErndiLAVADWGQKVSFYQLSGKQ-----IGKDRA 270
Cdd:cd00200 149 FVASSSQDGTIKLwDLRTGKCVATLT---GHTGEVNSVAFSPDGEK----LLSSSSDGTIKLWDLSTGKclgtlRGHENG 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526253054 271 LNfdpcCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQ 341
Cdd:cd00200 222 VN----SVAFSPDGYLLASGSEDGTIRVWdLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
42-80 |
9.32e-09 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 52.31 E-value: 9.32e-09
10 20 30
....*....|....*....|....*....|....*....
gi 526253054 42 DGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
43-80 |
4.23e-08 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 50.42 E-value: 4.23e-08
10 20 30
....*....|....*....|....*....|....*...
gi 526253054 43 GTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
686-937 |
1.59e-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: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 686 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 762
Cdd:COG2956 46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 763 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 842
Cdd:COG2956 120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 843 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 921
Cdd:COG2956 171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242
|
250
....*....|....*.
gi 526253054 922 QADPAQkdTMLGKFYH 937
Cdd:COG2956 243 PSDDLL--LALADLLE 256
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
702-910 |
2.18e-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: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 702 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 764
Cdd:TIGR02917 540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 765 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 838
Cdd:TIGR02917 613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526253054 839 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 910
Cdd:TIGR02917 663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
15-342 |
2.72e-32 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 130.80 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:COG2319 123 VRSVAFSPDGK--TLASGSAdgtVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWdlaTGKLLRTL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 89 KytswsvmsslhlhlpflglhktvrvtatdkapkgqggridclrpsvqnqpgqKHNDAIQCVSYNPITHQLASCSSSDF- 167
Cdd:COG2319 201 T----------------------------------------------------GHTGAVRSVAFSPDGKLLASGSADGTv 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 168 GLWSPE--QKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEEKVKieRPGGSLSPIWSICWNPSreerNDI 245
Cdd:COG2319 229 RLWDLAtgKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR--TLTGHSGGVNSVAFSPD----GKL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 246 LAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKP 323
Cdd:COG2319 303 LASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGAVTSVAFSP 382
|
330
....*....|....*....
gi 526253054 324 DSNYVVVGCQDGTISFYQL 342
Cdd:COG2319 383 DGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
15-342 |
4.38e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 97.29 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 15 INDIAFKPDGTQLILAAGSR-LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGILKy 90
Cdd:COG2319 81 VLSVAFSPDGRLLASASADGtVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWdlaTGKLLRTLT- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 91 tswsvmsslhlhlpflglhktvrvtatdkapkgqggridclrpsvqnqpgqKHNDAIQCVSYNPithqlascsssdfglw 170
Cdd:COG2319 160 ---------------------------------------------------GHSGAVTSVAFSP---------------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 171 speqksvskhkssskiiccswtnDGQYLALGMFNGIISIRN-KNGEEkvkIERPGGSLSPIWSICWNPSreerNDILAVA 249
Cdd:COG2319 173 -----------------------DGKLLASGSDDGTVRLWDlATGKL---LRTLTGHTGAVRSVAFSPD----GKLLASG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 250 DWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNY 327
Cdd:COG2319 223 SADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWdLATGELLRTLTGHSGGVNSVAFSPDGKL 302
|
330
....*....|....*
gi 526253054 328 VVVGCQDGTISFYQL 342
Cdd:COG2319 303 LASGSDDGTVRLWDL 317
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
49-341 |
3.11e-19 |
|
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: 89.70 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 49 LKGHKDTVYCVAYAKDGKRFASGSADKSVIIWTSKlEGILKYTS-------WSVMSSLHLHLPFL-GLHKTVRVTATDKa 120
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE-TGELLRTLkghtgpvRDVAASADGTYLASgSSDKTIRLWDLET- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 121 pkgqGGRIDCLRPsvqnqpgqkHNDAIQCVSYNPiTHQLASCSSSD--FGLWSPEQKSVSKHKS--SSKIICCSWTNDGQ 196
Cdd:cd00200 83 ----GECVRTLTG---------HTSYVSSVAFSP-DGRILSSSSRDktIKVWDVETGKCLTTLRghTDWVNSVAFSPDGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 197 YLALGMFNGIISI-RNKNGEEKVKIErpgGSLSPIWSICWNPSREErndiLAVADWGQKVSFYQLSGKQ-----IGKDRA 270
Cdd:cd00200 149 FVASSSQDGTIKLwDLRTGKCVATLT---GHTGEVNSVAFSPDGEK----LLSSSSDGTIKLWDLSTGKclgtlRGHENG 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526253054 271 LNfdpcCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQ 341
Cdd:cd00200 222 VN----SVAFSPDGYLLASGSEDGTIRVWdLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
12-238 |
2.19e-17 |
|
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: 83.92 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 12 EHCINDIAFKPDGTQLILAAGSRLL-VYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGI 87
Cdd:cd00200 51 TGPVRDVAASADGTYLASGSSDKTIrLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWdveTGKCLTT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 88 LKYTSWSVMsslhlHLPFLGLHKTVRVTATDKAPK---GQGGRIdclrpsVQNQPGqkHNDAIQCVSYNPITHQLASCSS 164
Cdd:cd00200 131 LRGHTDWVN-----SVAFSPDGTFVASSSQDGTIKlwdLRTGKC------VATLTG--HTGEVNSVAFSPDGEKLLSSSS 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526253054 165 -SDFGLWSP--EQKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRN-KNGEEKVKIErpgGSLSPIWSICWNPS 238
Cdd:cd00200 198 dGTIKLWDLstGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDlRTGECVQTLS---GHTNSVTSLAWSPD 272
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
15-164 |
7.31e-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: 70.44 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIWTSKlEGILKYT 91
Cdd:cd00200 138 VNSVAFSPDGT--FVASSSQdgtIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS-TGKCLGT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 92 swsvmssLHLHlpflglhkTVRVTATDKAPKGQ---GGRIDC------LRPSVQNQPGQKHNDAIQCVSYNPITHQLASC 162
Cdd:cd00200 215 -------LRGH--------ENGVNSVAFSPDGYllaSGSEDGtirvwdLRTGECVQTLSGHTNSVTSLAWSPDGKRLASG 279
|
..
gi 526253054 163 SS 164
Cdd:cd00200 280 SA 281
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
15-80 |
1.02e-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: 66.97 E-value: 1.02e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526253054 15 INDIAFKPDGtqLILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:cd00200 222 VNSVAFSPDG--YLLASGSEdgtIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
42-80 |
9.32e-09 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 52.31 E-value: 9.32e-09
10 20 30
....*....|....*....|....*....|....*....
gi 526253054 42 DGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
43-80 |
4.23e-08 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 50.42 E-value: 4.23e-08
10 20 30
....*....|....*....|....*....|....*...
gi 526253054 43 GTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
|
|
| NBCH_WD40 |
pfam20426 |
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ... |
41-80 |
9.52e-06 |
|
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.
Pssm-ID: 466575 [Multi-domain] Cd Length: 350 Bit Score: 49.30 E-value: 9.52e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 526253054 41 SDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:pfam20426 112 NDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVW 151
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
686-937 |
1.59e-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: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 686 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 762
Cdd:COG2956 46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 763 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 842
Cdd:COG2956 120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 843 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 921
Cdd:COG2956 171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242
|
250
....*....|....*.
gi 526253054 922 QADPAQkdTMLGKFYH 937
Cdd:COG2956 243 PSDDLL--LALADLLE 256
|
|
| COG4700 |
COG4700 |
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown]; |
826-912 |
1.38e-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: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 826 LKSLVQLHVETQRWDEAFALGEK----HPEFKD-DIYMPYAQWLAENDRFEEAQKAFHKA-------------------- 880
Cdd:COG4700 127 LLGLAQALFELGRYAEALETLEKliakNPDFKSsDAHLLYARALEALGDLEAAEAELEALarrysgpearyryakflarq 206
|
90 100 110
....*....|....*....|....*....|..
gi 526253054 881 GRQREAVQVLEQLTNNAVAESRFNDAAYYYWM 912
Cdd:COG4700 207 GRTAEAKELLEEILDEAKHMPKHYRRLNREWI 238
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
702-910 |
2.18e-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: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 702 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 764
Cdd:TIGR02917 540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 765 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 838
Cdd:TIGR02917 613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526253054 839 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 910
Cdd:TIGR02917 663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
761-946 |
3.23e-04 |
|
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: 43.95 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 761 EMYISAGEHVKAIEIC-------GDHGWVdmLIDIAR------KLDKAEreplllcATYLKKLDSPGYAAETYLKmgdlk 827
Cdd:COG2956 50 NLYRRRGEYDRAIRIHqkllerdPDRAEA--LLELAQdylkagLLDRAE-------ELLEKLLELDPDDAEALRL----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526253054 828 sLVQLHVETQRWDEAFALGEK----HPEfKDDIYMPYAQWLAENDRFEEAQKAFHKA-GRQREAVQVLEQLTNNAVAESR 902
Cdd:COG2956 116 -LAEIYEQEGDWEKAIEVLERllklGPE-NAHAYCELAELYLEQGDYDEAIEALEKAlKLDPDCARALLLLAELYLEQGD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 526253054 903 FNDAAYYYwmlsmqcLDIAQADPAQKDTMLgkfyhfqRLAELYH 946
Cdd:COG2956 194 YEEAIAAL-------ERALEQDPDYLPALP-------RLAELYE 223
|
|
|