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Conserved domains on  [gi|16554623|ref|NP_443715|]
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intraflagellar transport protein 122 homolog isoform 2 [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];
15-350 2.85e-32

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 130.80  E-value: 2.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:COG2319  123 VRSVAFSPDGK--TLASGSAdgtVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWdlaTGKLLRTL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   89 KyTHNDAIQCVSYNPITHQLASCSSSDF-GLWSPE--QKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEE 165
Cdd:COG2319  201 T-GHTGAVRSVAFSPDGKLLASGSADGTvRLWDLAtgKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGE 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  166 KVKieRPGGSLSPIWSICWNPSSRWesfwmnrenedaedvivnryiqeipstlksavyssqgseaeeeepeeeddsprdd 245
Cdd:COG2319  280 LLR--TLTGHSGGVNSVAFSPDGKL------------------------------------------------------- 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  246 nleerndiLAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSW 323
Cdd:COG2319  303 --------LASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGA 374

                        330       340
                 ....*....|....*....|....*..
gi 16554623  324 VWTCQAKPDSNYVVVGCQDGTISFYQL 350
Cdd:COG2319  375 VTSVAFSPDGRTLASGSADGTVRLWDL 401
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 694-944 4.88e-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: 49.73  E-value: 4.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  694 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 770
Cdd:COG2956   46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  771 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 850
Cdd:COG2956  120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  851 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 929
Cdd:COG2956  171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242

                        250
                 ....*....|....*
gi 16554623  930 QDPAQKDtMLGKFYH 944
Cdd:COG2956  243 PSDDLLL-ALADLLE 256
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
15-350 2.85e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 130.80  E-value: 2.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:COG2319  123 VRSVAFSPDGK--TLASGSAdgtVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWdlaTGKLLRTL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   89 KyTHNDAIQCVSYNPITHQLASCSSSDF-GLWSPE--QKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEE 165
Cdd:COG2319  201 T-GHTGAVRSVAFSPDGKLLASGSADGTvRLWDLAtgKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGE 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  166 KVKieRPGGSLSPIWSICWNPSSRWesfwmnrenedaedvivnryiqeipstlksavyssqgseaeeeepeeeddsprdd 245
Cdd:COG2319  280 LLR--TLTGHSGGVNSVAFSPDGKL------------------------------------------------------- 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  246 nleerndiLAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSW 323
Cdd:COG2319  303 --------LASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGA 374

                        330       340
                 ....*....|....*....|....*..
gi 16554623  324 VWTCQAKPDSNYVVVGCQDGTISFYQL 350
Cdd:COG2319  375 VTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 15-190 1.16e-21

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: 96.64  E-value: 1.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:cd00200   96 VSSVAFSPDGR--ILSSSSRdktIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWdlrTGKCVATL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   89 KyTHNDAIQCVSYNPITHQLASCSS-SDFGLWSP--EQKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRN-KNGE 164
Cdd:cd00200  174 T-GHTGEVNSVAFSPDGEKLLSSSSdGTIKLWDLstGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDlRTGE 252

                        170       180
                 ....*....|....*....|....*.
gi 16554623  165 EKVKIErpgGSLSPIWSICWNPSSRW 190
Cdd:cd00200  253 CVQTLS---GHTNSVTSLAWSPDGKR 275
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 42-80 9.74e-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: 51.93  E-value: 9.74e-09
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 16554623      42 DGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
43-80 4.38e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 4.38e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 16554623     43 GTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 694-944 4.88e-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: 49.73  E-value: 4.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  694 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 770
Cdd:COG2956   46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  771 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 850
Cdd:COG2956  120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  851 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 929
Cdd:COG2956  171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242

                        250
                 ....*....|....*
gi 16554623  930 QDPAQKDtMLGKFYH 944
Cdd:COG2956  243 PSDDLLL-ALADLLE 256
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 710-918 2.20e-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: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623    710 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 772
Cdd:TIGR02917  540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623    773 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 846
Cdd:TIGR02917  613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16554623    847 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 918
Cdd:TIGR02917  663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
15-350 2.85e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 130.80  E-value: 2.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:COG2319  123 VRSVAFSPDGK--TLASGSAdgtVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWdlaTGKLLRTL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   89 KyTHNDAIQCVSYNPITHQLASCSSSDF-GLWSPE--QKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEE 165
Cdd:COG2319  201 T-GHTGAVRSVAFSPDGKLLASGSADGTvRLWDLAtgKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGE 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  166 KVKieRPGGSLSPIWSICWNPSSRWesfwmnrenedaedvivnryiqeipstlksavyssqgseaeeeepeeeddsprdd 245
Cdd:COG2319  280 LLR--TLTGHSGGVNSVAFSPDGKL------------------------------------------------------- 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  246 nleerndiLAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSW 323
Cdd:COG2319  303 --------LASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGA 374

                        330       340
                 ....*....|....*....|....*..
gi 16554623  324 VWTCQAKPDSNYVVVGCQDGTISFYQL 350
Cdd:COG2319  375 VTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 15-190 1.16e-21

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: 96.64  E-value: 1.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:cd00200   96 VSSVAFSPDGR--ILSSSSRdktIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWdlrTGKCVATL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   89 KyTHNDAIQCVSYNPITHQLASCSS-SDFGLWSP--EQKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRN-KNGE 164
Cdd:cd00200  174 T-GHTGEVNSVAFSPDGEKLLSSSSdGTIKLWDLstGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDlRTGE 252

                        170       180
                 ....*....|....*....|....*.
gi 16554623  165 EKVKIErpgGSLSPIWSICWNPSSRW 190
Cdd:cd00200  253 CVQTLS---GHTNSVTSLAWSPDGKR 275
WD40 COG2319
WD40 repeat [General function prediction only];
15-350 2.77e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 98.06  E-value: 2.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   15 INDIAFKPDGTQLILAAGSR-LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGILKy 90
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGtVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWdlaTGKLLRTLT- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   91 THNDAIQCVSYNPithqlascsssdfglwspeqksvskhkssskiiccswtnDGQYLALGMFNGIISIRN-KNGEEkvkI 169
Cdd:COG2319  160 GHSGAVTSVAFSP---------------------------------------DGKLLASGSDDGTVRLWDlATGKL---L 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  170 ERPGGSLSPIWSICWNPSSRWesfwmnrenedaedvivnryiqeipstlksavyssqgseaeeeepeeeddsprddnlee 249
Cdd:COG2319  198 RTLTGHTGAVRSVAFSPDGKL----------------------------------------------------------- 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  250 rndiLAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTC 327
Cdd:COG2319  219 ----LASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWdLATGELLRTLTGHSGGVNSV 294

                        330       340
                 ....*....|....*....|...
gi 16554623  328 QAKPDSNYVVVGCQDGTISFYQL 350
Cdd:COG2319  295 AFSPDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 12-190 8.03e-20

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: 91.24  E-value: 8.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   12 EHCINDIAFKPDGTQLILAAGSRLL-VYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGI 87
Cdd:cd00200   51 TGPVRDVAASADGTYLASGSSDKTIrLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWdveTGKCLTT 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   88 LKyTHNDAIQCVSYNPiTHQLASCSSSDF--GLWSPEQKSVSKHKS--SSKIICCSWTNDGQYLALGMFNGIISIRNKNG 163
Cdd:cd00200  131 LR-GHTDWVNSVAFSP-DGTFVASSSQDGtiKLWDLRTGKCVATLTghTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208

                        170       180
                 ....*....|....*....|....*..
gi 16554623  164 EEKVKIERpgGSLSPIWSICWNPSSRW 190
Cdd:cd00200  209 GKCLGTLR--GHENGVNSVAFSPDGYL 233
WD40 COG2319
WD40 repeat [General function prediction only];
2-350 2.03e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 89.20  E-value: 2.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623    2 RAVLTWRDKAEHCINDIAFKPDGTQLILAAGSRL-LVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:COG2319   26 GALLLLLLGLAAAVASLAASPDGARLAAGAGDLTlLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   81 --TSKLEGILKYTHNDAIQCVSYNPITHQLAScSSSDFG--LWSPE--QKSVSKHKSSSKIICCSWTNDGQYLALGMFNG 154
Cdd:COG2319  106 dlATGLLLRTLTGHTGAVRSVAFSPDGKTLAS-GSADGTvrLWDLAtgKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  155 IISIRN-KNGEEkvkIERPGGSLSPIWSICWNPSSRWesfwmnrenedaedvIV----NRYIQ-------EIPSTLK--- 219
Cdd:COG2319  185 TVRLWDlATGKL---LRTLTGHTGAVRSVAFSPDGKL---------------LAsgsaDGTVRlwdlatgKLLRTLTghs 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  220 ----SAVYSSQGSeaeeeepeeeddsprddnleerndILAVADWGQKVSFYQLSGKQIGKD--------RALNFDPccis 287
Cdd:COG2319  247 gsvrSVAFSPDGR------------------------LLASGSADGTVRLWDLATGELLRTltghsggvNSVAFSP---- 298

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16554623  288 yftKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 350
Cdd:COG2319  299 ---DGKLLASGSDDGTVRLWdLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 49-350 2.01e-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: 84.31  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   49 LKGHKDTVYCVAYAKDGKRFASGSADKSVIIWTSKlEGILKYT---HNDAIQCVSYNPITHQLASCSSSDFG-LWSPEQK 124
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE-TGELLRTlkgHTGPVRDVAASADGTYLASGSSDKTIrLWDLETG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  125 SVSKHKS--SSKIICCSWTNDGQYLALGMFNGiiSIR---NKNGEEKVKIErpgGSLSPIWSICWNPSsrwesfwmnren 199
Cdd:cd00200   84 ECVRTLTghTSYVSSVAFSPDGRILSSSSRDK--TIKvwdVETGKCLTTLR---GHTDWVNSVAFSPD------------ 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  200 edaedvivnryiqeipstlksavyssqgseaeeeepeeeddsprddnleerNDILAVADWGQKVSFYQLSGKQI-----G 274
Cdd:cd00200  147 ---------------------------------------------------GTFVASSSQDGTIKLWDLRTGKCvatltG 175

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16554623  275 KDRALNfdpcCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQL 350
Cdd:cd00200  176 HTGEVN----SVAFSPDGEKLLSSSSDGTIKLWdLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL 248
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 15-189 5.56e-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: 82.77  E-value: 5.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:cd00200   12 VTCVAFSPDGK--LLATGSGdgtIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWdleTGECVRTL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   89 KyTHNDAIQCVSYNPiTHQLASCSSSD--FGLWSPEQKSVSKHKS--SSKIICCSWTNDGQYLALGMFNGIISI-RNKNG 163
Cdd:cd00200   90 T-GHTSYVSSVAFSP-DGRILSSSSRDktIKVWDVETGKCLTTLRghTDWVNSVAFSPDGTFVASSSQDGTIKLwDLRTG 167

                        170       180
                 ....*....|....*....|....*.
gi 16554623  164 EEKVKIErpgGSLSPIWSICWNPSSR 189
Cdd:cd00200  168 KCVATLT---GHTGEVNSVAFSPDGE 190
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 15-158 5.94e-16

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: 79.69  E-value: 5.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:cd00200  138 VNSVAFSPDGT--FVASSSQdgtIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWdlsTGKCLGTL 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16554623   89 KYtHNDAIQCVSYNPiTHQLASCSSSD--FGLWS--PEQKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISI 158
Cdd:cd00200  216 RG-HENGVNSVAFSP-DGYLLASGSEDgtIRVWDlrTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
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 16554623   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 9.74e-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: 51.93  E-value: 9.74e-09
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 16554623      42 DGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
43-80 4.38e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 4.38e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 16554623     43 GTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 694-944 4.88e-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: 49.73  E-value: 4.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  694 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 770
Cdd:COG2956   46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  771 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 850
Cdd:COG2956  120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  851 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIA 929
Cdd:COG2956  171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL----RKALELD 242

                        250
                 ....*....|....*
gi 16554623  930 QDPAQKDtMLGKFYH 944
Cdd:COG2956  243 PSDDLLL-ALADLLE 256
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 41-80 9.58e-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: 9.58e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 16554623     41 SDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:pfam20426  112 NDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVW 151
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
834-920 1.41e-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: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  834 LKSLVQLHVETQRWDEAFALGEK----HPEFKD-DIYMPYAQWLAENDRFEEAQKAFHKA-------------------- 888
Cdd:COG4700  127 LLGLAQALFELGRYAEALETLEKliakNPDFKSsDAHLLYARALEALGDLEAAEAELEALarrysgpearyryakflarq 206

                         90       100       110
                 ....*....|....*....|....*....|..
gi 16554623  889 GRQREAVQVLEQLTNNAVAESRFNDAAYYYWM 920
Cdd:COG4700  207 GRTAEAKELLEEILDEAKHMPKHYRRLNREWI 238
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 710-918 2.20e-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: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623    710 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 772
Cdd:TIGR02917  540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623    773 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 846
Cdd:TIGR02917  613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16554623    847 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 918
Cdd:TIGR02917  663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 285-351 4.16e-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: 43.86  E-value: 4.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16554623  285 CISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQLI 351
Cdd:cd00200   56 DVAASADGTYLASGSSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE 123
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 769-959 1.94e-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: 41.64  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  769 EMYISAGEHVKAIEIC-------GDHGWVdmLIDIAR------KLDKAEreplllcATYLKKLDSPGYAAETYLKmgdlk 835
Cdd:COG2956   50 NLYRRRGEYDRAIRIHqkllerdPDRAEA--LLELAQdylkagLLDRAE-------ELLEKLLELDPDDAEALRL----- 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  836 sLVQLHVETQRWDEAFALGEK----HPEfKDDIYMPYAQWLAENDRFEEAQKAFHKA-GRQREAVQVLEQLTNNAVAESR 910
Cdd:COG2956  116 -LAEIYEQEGDWEKAIEVLERllklGPE-NAHAYCELAELYLEQGDYDEAIEALEKAlKLDPDCARALLLLAELYLEQGD 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16554623  911 FNDAAYYYwmlsMQCLDIAQDPAQKDTMLGKFYH----FQRLAELYHGYHAIH 959
Cdd:COG2956  194 YEEAIAAL----ERALEQDPDYLPALPRLAELYEklgdPEEALELLRKALELD 242
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 795-1023 9.34e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 40.36  E-value: 9.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  795 DIARKLDKAEREPLLLCATYLKKLDSPGYAAETYLKMGDLKSLVQLHVETQRWDEAFALGEKHPEFKDDIYMPYAQW--- 871
Cdd:COG3914   42 GLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLgnl 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  872 LAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYYwmlsMQCLDIAQDPAQKDTMLGKFY------- 943
Cdd:COG3914  122 LLALGRLEEALAALRRALALNpDFAEAYLNLGEALRRLGRLEEAIAAL----RRALELDPDNAEALNNLGNALqdlgrle 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554623  944 ----HFQRLAEL-------YHGYHAIHRHTEDPFSVHRPE--------TLFNISRFLLHSLPKDTPSGISKVKILFTLAK 1004
Cdd:COG3914  198 eaiaAYRRALELdpdnadaHSNLLFALRQACDWEVYDRFEellaalarGPSELSPFALLYLPDDDPAELLALARAWAQLV 277

                        250       260
                 ....*....|....*....|..
gi 16554623 1005 QSKALGAYRLARHAYD---KLR 1023
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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