|
Name |
Accession |
Description |
Interval |
E-value |
| WD40_3 |
pfam15911 |
WD domain, G-beta repeat; |
508-564 |
5.23e-30 |
|
WD domain, G-beta repeat;
Pssm-ID: 464937 Cd Length: 57 Bit Score: 113.07 E-value: 5.23e-30
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462598470 508 VNDYRHPVSVKKIFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWE 564
Cdd:pfam15911 1 VNEYRHSVGIKKLFPNPSGTRLVFIDEKGDGFLYNPVSDELLEIPDFPPTVKGVLWD 57
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-345 |
5.39e-12 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 69.55 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 26 GNYLAVTGADYIVKIFDRHGQK--RSEINLPGNCVAMDWDKDGDVLAVIAEKSScIYLWDANTNKTSQLDNGMRDQMSFL 103
Cdd:COG2319 90 GRLLASASADGTVRLWDLATGLllRTLTGHTGAVRSVAFSPDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVTSV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 104 LWSKVGSFLAVGTVKGNLLIYNHQTSRKIPVLGKHTKRITCGCWNAE-NLLALGGEDKMITVSN-QEGDTIRQTQVRSEP 181
Cdd:COG2319 169 AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgKLLASGSADGTVRLWDlATGKLLRTLTGHSGS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 182 SNmqfflmkmddrtSAAES----MISVVLGKKTLFFLNLNEPDNPADLEFQQDFGNIVCynWYGDGRIMIGFSCGHFV-V 256
Cdd:COG2319 249 VR------------SVAFSpdgrLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVA--FSPDGKLLASGSDDGTVrL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 257 ISTHTGELGQEIfqaRNHKDNLTSIAVSQTLNKVATCG-DNCIKiqdLVDLKDMYVILNLDEENKGLGTLSWTDDGQLLA 335
Cdd:COG2319 315 WDLATGKLLRTL---TGHTGAVRSVAFSPDGKTLASGSdDGTVR---LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLA 388
|
330
....*....|
gi 2462598470 336 LSTQRGSLHV 345
Cdd:COG2319 389 SGSADGTVRL 398
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
26-302 |
4.52e-09 |
|
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: 59.27 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 26 GNYLAVTGADYIVKIFDRHGQKRSEInLPG-----NCVamDWDKDGDVLAVIAEKSSCIyLWDANTNKTSQLDNGMRDQM 100
Cdd:cd00200 63 GTYLASGSSDKTIRLWDLETGECVRT-LTGhtsyvSSV--AFSPDGRILSSSSRDKTIK-VWDVETGKCLTTLRGHTDWV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 101 SFLLWSKVGSFLAVGTVKGNLLIYNHQTSRKIPVLGKHTKRITCGCWNAEN-LLALGGEDKMITVSN-QEGDTIRQtqvr 178
Cdd:cd00200 139 NSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGeKLLSSSSDGTIKLWDlSTGKCLGT---- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 179 sepsnmqfflmkmddrtsaaesmisvvlgkktlfflnlnepdnpadLEFQQDFGNIVCYNWygDGRIMIGFSC-GHFVVI 257
Cdd:cd00200 215 ----------------------------------------------LRGHENGVNSVAFSP--DGYLLASGSEdGTIRVW 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462598470 258 STHTGELGQEIfqaRNHKDNLTSIAVSQTLNKVATCG-DNCIKIQD 302
Cdd:cd00200 247 DLRTGECVQTL---SGHTNSVTSLAWSPDGKRLASGSaDGTIRIWD 289
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
786-1004 |
5.51e-07 |
|
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: 52.81 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 786 AIQLEFAGDYVNALAHYEKGITGDNkEHDEACLAgVAQMSIRMGDIRRGV---NQALK-HPSRV-LKRDCGAILENMKQF 860
Cdd:COG2956 15 GLNYLLNGQPDKAIDLLEEALELDP-ETVEAHLA-LGNLYRRRGEYDRAIrihQKLLErDPDRAeALLELAQDYLKAGLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 861 SEAAQLYEKGL--------YYDKAASVYIRSKNWAKVGDLL-----PHVSSPKIHLQYAKAKEADGRYKEAVVAYENA-- 925
Cdd:COG2956 93 DRAEELLEKLLeldpddaeALRLLAEIYEQEGDWEKAIEVLerllkLGPENAHAYCELAELYLEQGDYDEAIEALEKAlk 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 926 KQWQSV------IRIYLDHlNNPEKAVNIVRET-----QSLDGAKMVARFFLQLGDYGSAIQFLvmskcnNEAFTLAQQH 994
Cdd:COG2956 173 LDPDCArallllAELYLEQ-GDYEEAIAALERAleqdpDYLPALPRLAELYEKLGDPEEALELL------RKALELDPSD 245
|
250
....*....|
gi 2462598470 995 NKMEIYADII 1004
Cdd:COG2956 246 DLLLALADLL 255
|
|
| CLH |
smart00299 |
Clathrin heavy chain repeat homology; |
855-968 |
1.17e-03 |
|
Clathrin heavy chain repeat homology;
Pssm-ID: 128594 [Multi-domain] Cd Length: 140 Bit Score: 40.72 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 855 ENMKQFSEAAQLYekgLYYDKAASV-YIRSKNwakvgdllPHVSSPKIhlqYAKAKEADGrYKEAVVAYENAKQWQSVIR 933
Cdd:smart00299 39 ENPALQTKLIELY---AKYDPQKEIeRLDNKS--------NHYDIEKV---GKLCEKAKL-YEEAVELYKKDGNFKDAIV 103
|
90 100 110
....*....|....*....|....*....|....*
gi 2462598470 934 IYLDHLNNPEKAVNIVRETQSLDGAKMVARFFLQL 968
Cdd:smart00299 104 TLIEHLGNYEKAIEYFVKQNNPELWAEVLKALLDK 138
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40_3 |
pfam15911 |
WD domain, G-beta repeat; |
508-564 |
5.23e-30 |
|
WD domain, G-beta repeat;
Pssm-ID: 464937 Cd Length: 57 Bit Score: 113.07 E-value: 5.23e-30
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462598470 508 VNDYRHPVSVKKIFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWE 564
Cdd:pfam15911 1 VNEYRHSVGIKKLFPNPSGTRLVFIDEKGDGFLYNPVSDELLEIPDFPPTVKGVLWD 57
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-345 |
5.39e-12 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 69.55 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 26 GNYLAVTGADYIVKIFDRHGQK--RSEINLPGNCVAMDWDKDGDVLAVIAEKSScIYLWDANTNKTSQLDNGMRDQMSFL 103
Cdd:COG2319 90 GRLLASASADGTVRLWDLATGLllRTLTGHTGAVRSVAFSPDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVTSV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 104 LWSKVGSFLAVGTVKGNLLIYNHQTSRKIPVLGKHTKRITCGCWNAE-NLLALGGEDKMITVSN-QEGDTIRQTQVRSEP 181
Cdd:COG2319 169 AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgKLLASGSADGTVRLWDlATGKLLRTLTGHSGS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 182 SNmqfflmkmddrtSAAES----MISVVLGKKTLFFLNLNEPDNPADLEFQQDFGNIVCynWYGDGRIMIGFSCGHFV-V 256
Cdd:COG2319 249 VR------------SVAFSpdgrLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVA--FSPDGKLLASGSDDGTVrL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 257 ISTHTGELGQEIfqaRNHKDNLTSIAVSQTLNKVATCG-DNCIKiqdLVDLKDMYVILNLDEENKGLGTLSWTDDGQLLA 335
Cdd:COG2319 315 WDLATGKLLRTL---TGHTGAVRSVAFSPDGKTLASGSdDGTVR---LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLA 388
|
330
....*....|
gi 2462598470 336 LSTQRGSLHV 345
Cdd:COG2319 389 SGSADGTVRL 398
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
26-302 |
4.52e-09 |
|
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: 59.27 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 26 GNYLAVTGADYIVKIFDRHGQKRSEInLPG-----NCVamDWDKDGDVLAVIAEKSSCIyLWDANTNKTSQLDNGMRDQM 100
Cdd:cd00200 63 GTYLASGSSDKTIRLWDLETGECVRT-LTGhtsyvSSV--AFSPDGRILSSSSRDKTIK-VWDVETGKCLTTLRGHTDWV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 101 SFLLWSKVGSFLAVGTVKGNLLIYNHQTSRKIPVLGKHTKRITCGCWNAEN-LLALGGEDKMITVSN-QEGDTIRQtqvr 178
Cdd:cd00200 139 NSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGeKLLSSSSDGTIKLWDlSTGKCLGT---- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 179 sepsnmqfflmkmddrtsaaesmisvvlgkktlfflnlnepdnpadLEFQQDFGNIVCYNWygDGRIMIGFSC-GHFVVI 257
Cdd:cd00200 215 ----------------------------------------------LRGHENGVNSVAFSP--DGYLLASGSEdGTIRVW 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462598470 258 STHTGELGQEIfqaRNHKDNLTSIAVSQTLNKVATCG-DNCIKIQD 302
Cdd:cd00200 247 DLRTGECVQTL---SGHTNSVTSLAWSPDGKRLASGSaDGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
59-346 |
6.86e-09 |
|
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: 58.89 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 59 AMDWDKDGDVLAVIAEkSSCIYLWDANTNKTSQLDNGMRDQMSFLLWSKVGSFLAVGTVKGNLLIYNHQTSRKIPVLGKH 138
Cdd:cd00200 14 CVAFSPDGKLLATGSG-DGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 139 TKRITCGCWNAEN-LLALGGEDKmitvsnqegdTIRqtqvrsepsnmqfflmkmddrtsaaesmisvvlgkktlfFLNLN 217
Cdd:cd00200 93 TSYVSSVAFSPDGrILSSSSRDK----------TIK---------------------------------------VWDVE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 218 EPDNPADLEFQQDFGNIVCYNwyGDGRIMIGFSCGHFV-VISTHTGELGQEIfqaRNHKDNLTSIAVSQTLNKVATCG-D 295
Cdd:cd00200 124 TGKCLTTLRGHTDWVNSVAFS--PDGTFVASSSQDGTIkLWDLRTGKCVATL---TGHTGEVNSVAFSPDGEKLLSSSsD 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462598470 296 NCIKIQDLVDLKDMYVilnLDEENKGLGTLSWTDDGQLLALSTQRGSLHVF 346
Cdd:cd00200 199 GTIKLWDLSTGKCLGT---LRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
25-157 |
9.78e-09 |
|
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: 58.12 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 25 SGNYLAVTGADYIVKIFD-RHGQKRSEINL---PGNCVAMDWDKDgdvLAVIAEKSSCIYLWDANTNKTSQLDNGMRDQM 100
Cdd:cd00200 104 DGRILSSSSRDKTIKVWDvETGKCLTTLRGhtdWVNSVAFSPDGT---FVASSSQDGTIKLWDLRTGKCVATLTGHTGEV 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462598470 101 SFLLWSKVGSFLAVGTVKGNLLIYNHQTSRKIPVLGKHTKRITCGCWNAENLLALGG 157
Cdd:cd00200 181 NSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASG 237
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
25-162 |
3.09e-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: 56.57 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 25 SGNYLAVTGADYIVKIFDRHGQKRSEiNLPG-----NCVAmdWDKDGDVLAVIAEkSSCIYLWDANTNKTSQLDNGMRDQ 99
Cdd:cd00200 146 DGTFVASSSQDGTIKLWDLRTGKCVA-TLTGhtgevNSVA--FSPDGEKLLSSSS-DGTIKLWDLSTGKCLGTLRGHENG 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462598470 100 MSFLLWSKVGSFLAVGTVKGNLLIYNHQTSRKIPVLGKHTKRITCGCWNAE-NLLALGGEDKMI 162
Cdd:cd00200 222 VNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDgKRLASGSADGTI 285
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
786-1004 |
5.51e-07 |
|
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: 52.81 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 786 AIQLEFAGDYVNALAHYEKGITGDNkEHDEACLAgVAQMSIRMGDIRRGV---NQALK-HPSRV-LKRDCGAILENMKQF 860
Cdd:COG2956 15 GLNYLLNGQPDKAIDLLEEALELDP-ETVEAHLA-LGNLYRRRGEYDRAIrihQKLLErDPDRAeALLELAQDYLKAGLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 861 SEAAQLYEKGL--------YYDKAASVYIRSKNWAKVGDLL-----PHVSSPKIHLQYAKAKEADGRYKEAVVAYENA-- 925
Cdd:COG2956 93 DRAEELLEKLLeldpddaeALRLLAEIYEQEGDWEKAIEVLerllkLGPENAHAYCELAELYLEQGDYDEAIEALEKAlk 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 926 KQWQSV------IRIYLDHlNNPEKAVNIVRET-----QSLDGAKMVARFFLQLGDYGSAIQFLvmskcnNEAFTLAQQH 994
Cdd:COG2956 173 LDPDCArallllAELYLEQ-GDYEEAIAALERAleqdpDYLPALPRLAELYEKLGDPEEALELL------RKALELDPSD 245
|
250
....*....|
gi 2462598470 995 NKMEIYADII 1004
Cdd:COG2956 246 DLLLALADLL 255
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
673-925 |
3.06e-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: 50.50 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 673 NDEAAWNELARACLHHMEVEFAIRVYRRIgnvgivmsLEQIKGIEDYNLLAGHLAMFTNDYNLAQDLY--LASSCP--IA 748
Cdd:COG2956 40 ETVEAHLALGNLYRRRGEYDRAIRIHQKL--------LERDPDRAEALLELAQDYLKAGLLDRAEELLekLLELDPddAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 749 ALEVWQQMRRDLQHWDSALQLAKHLAP--DQIPFISKEYAIQLEFAGDYVNALAHYEKGITgDNKEHDEACLAgVAQMSI 826
Cdd:COG2956 112 ALRLLAEIYEQEGDWEKAIEVLERLLKlgPENAHAYCELAELYLEQGDYDEAIEALEKALK-LDPDCARALLL-LAELYL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 827 RMGDirrgVNQALKHPSRVLKRDcgaiLENMKQFSEAAQLYEKGLYYDKAASVYIRsknwakvgdLLPHVSSPKIHLQYA 906
Cdd:COG2956 190 EQGD----YEEAIAALERALEQD----PDYLPALPRLAELYEKLGDPEEALELLRK---------ALELDPSDDLLLALA 252
|
250
....*....|....*....
gi 2462598470 907 KAKEADGRYKEAVVAYENA 925
Cdd:COG2956 253 DLLERKEGLEAALALLERQ 271
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
719-967 |
9.92e-06 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 49.99 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 719 YNLLAGHLAMFTNDYNLAQDLYLASSCPIAALEVWQQMRRDLQHWDSALQLAKHLAPDQIPFISKEYAIQLEfAGDYVNA 798
Cdd:COG3914 19 AAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQA-LGRYEEA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 799 LAHYEKGITGDNKEHDEACLAGVAQMsiRMGDIrrgvNQALKHPSRVLKRD---------CGAILENMKQFSEAAQLYEK 869
Cdd:COG3914 98 LALYRRALALNPDNAEALFNLGNLLL--ALGRL----EEALAALRRALALNpdfaeaylnLGEALRRLGRLEEAIAALRR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 870 GLyydkaasvyirsknwakvgDLLPHvsSPKIHLQYAKAKEADGRYKEAVVAYENAKQ--------WQSVIRIYLDHLNN 941
Cdd:COG3914 172 AL-------------------ELDPD--NAEALNNLGNALQDLGRLEEAIAAYRRALEldpdnadaHSNLLFALRQACDW 230
|
250 260
....*....|....*....|....*.
gi 2462598470 942 PEKAVNIVRETQSLDGAKMVARFFLQ 967
Cdd:COG3914 231 EVYDRFEELLAALARGPSELSPFALL 256
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
784-927 |
2.01e-04 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 42.87 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 784 EYAIQLEFAGDYVNALAHYEKGITgDNKEHDEAcLAGVAQMSIRMGDIRRGV---NQALK-HP-SRVLKRDCGAILENMK 858
Cdd:COG4783 9 ALAQALLLAGDYDEAEALLEKALE-LDPDNPEA-FALLGEILLQLGDLDEAIvllHEALElDPdEPEARLNLGLALLKAG 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462598470 859 QFSEAAQLYEKGLYYDKaasvyirsknwakvgdllphvSSPKIHLQYAKAKEADGRYKEAVVAYENAKQ 927
Cdd:COG4783 87 DYDEALALLEKALKLDP---------------------EHPEAYLRLARAYRALGRPDEAIAALEKALE 134
|
|
| COG4700 |
COG4700 |
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown]; |
851-925 |
2.65e-04 |
|
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
Pssm-ID: 443735 [Multi-domain] Cd Length: 249 Bit Score: 44.10 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 851 GAILENMKQFSEAAQLYEK---GLYYD------KAASVYIRSKNWAKVGDLL-------PHVSSPKIHLQYAKAKEADGR 914
Cdd:COG4700 96 ADALLELGRYDEAIELYEEaltGIFADdphillGLAQALFELGRYAEALETLekliaknPDFKSSDAHLLYARALEALGD 175
|
90
....*....|.
gi 2462598470 915 YKEAVVAYENA 925
Cdd:COG4700 176 LEAAEAELEAL 186
|
|
| COG5290 |
COG5290 |
IkappaB kinase complex, IKAP component [Transcription]; |
836-934 |
4.81e-04 |
|
IkappaB kinase complex, IKAP component [Transcription];
Pssm-ID: 227610 [Multi-domain] Cd Length: 1243 Bit Score: 44.61 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 836 NQALKHpsrvLKRDCGAILENMKqFSEAAQLYEKGLYYDKaasvYIRSKNWAKVGDLLPHVSSPKIHLQYAKAKEADGRY 915
Cdd:COG5290 881 ESALGH----LNEDLNVIREVMK-YICRHDLYDFLLLLYR----YDGELQKFKINIFAGNLVDNLYHISAAKAYEVEGKY 951
|
90
....*....|....*....
gi 2462598470 916 KEAVVAYENAKQWQSVIRI 934
Cdd:COG5290 952 IEAHGAYDSALMWRECGSI 970
|
|
| CLH |
smart00299 |
Clathrin heavy chain repeat homology; |
855-968 |
1.17e-03 |
|
Clathrin heavy chain repeat homology;
Pssm-ID: 128594 [Multi-domain] Cd Length: 140 Bit Score: 40.72 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 855 ENMKQFSEAAQLYekgLYYDKAASV-YIRSKNwakvgdllPHVSSPKIhlqYAKAKEADGrYKEAVVAYENAKQWQSVIR 933
Cdd:smart00299 39 ENPALQTKLIELY---AKYDPQKEIeRLDNKS--------NHYDIEKV---GKLCEKAKL-YEEAVELYKKDGNFKDAIV 103
|
90 100 110
....*....|....*....|....*....|....*
gi 2462598470 934 IYLDHLNNPEKAVNIVRETQSLDGAKMVARFFLQL 968
Cdd:smart00299 104 TLIEHLGNYEKAIEYFVKQNNPELWAEVLKALLDK 138
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
793-925 |
3.86e-03 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 40.76 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598470 793 GDYVNALAHYEKGITGDNKEHDEACLAGVAQMsiRMGDIRrgvnQALKHPSRVLKRD---------CGAILENMKQFSEA 863
Cdd:COG0457 22 GRYEEAIEDYEKALELDPDDAEALYNLGLAYL--RLGRYE----EALADYEQALELDpddaealnnLGLALQALGRYEEA 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462598470 864 AQLYEKGLyydkaasvyirsknwakvgDLLPhvSSPKIHLQYAKAKEADGRYKEAVVAYENA 925
Cdd:COG0457 96 LEDYDKAL-------------------ELDP--DDAEALYNLGLALLELGRYDEAIEAYERA 136
|
|
|