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Conserved domains on  [gi|578807565|ref|XP_006713754|]
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intraflagellar transport protein 122 homolog isoform X1 [Homo sapiens]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 18610525)

WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; similar to 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

CATH:  2.130.10.10
Gene Ontology:  GO:0005515
PubMed:  10322433|8090199|30069656|29026209
SCOP:  4002744

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 2.82e-32

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 130.80  E-value: 2.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:COG2319   123 VRSVAFSPDGK--TLASGSAdgtVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWdlaTGKLLRTL 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   89 KyTHNDAIQCVSYNPITHQLASCSSSDF-GLWSPE--QKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEE 165
Cdd:COG2319   201 T-GHTGAVRSVAFSPDGKLLASGSADGTvRLWDLAtgKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGE 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  166 KVKieRPGGSLSPIWSICWNPSSRWesfwmnrenedaedvivnryiqeipstlksavyssqgseaeeeepeeeddsprdd 245
Cdd:COG2319   280 LLR--TLTGHSGGVNSVAFSPDGKL------------------------------------------------------- 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  246 nleerndiLAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSW 323
Cdd:COG2319   303 --------LASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGA 374

                         330       340
                  ....*....|....*....|....*..
gi 578807565  324 VWTCQAKPDSNYVVVGCQDGTISFYQL 350
Cdd:COG2319   375 VTSVAFSPDGRTLASGSADGTVRLWDL 401
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 676-900 1.77e-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: 47.80  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  676 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 752
Cdd:COG2956    46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  753 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 832
Cdd:COG2956   120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578807565  833 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYY 900
Cdd:COG2956   171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL 235
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
15-350 2.82e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 130.80  E-value: 2.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:COG2319   123 VRSVAFSPDGK--TLASGSAdgtVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWdlaTGKLLRTL 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   89 KyTHNDAIQCVSYNPITHQLASCSSSDF-GLWSPE--QKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEE 165
Cdd:COG2319   201 T-GHTGAVRSVAFSPDGKLLASGSADGTvRLWDLAtgKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGE 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  166 KVKieRPGGSLSPIWSICWNPSSRWesfwmnrenedaedvivnryiqeipstlksavyssqgseaeeeepeeeddsprdd 245
Cdd:COG2319   280 LLR--TLTGHSGGVNSVAFSPDGKL------------------------------------------------------- 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  246 nleerndiLAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSW 323
Cdd:COG2319   303 --------LASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGA 374

                         330       340
                  ....*....|....*....|....*..
gi 578807565  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 1.21e-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: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:cd00200    96 VSSVAFSPDGR--ILSSSSRdktIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWdlrTGKCVATL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   89 KyTHNDAIQCVSYNPITHQLASCSS-SDFGLWSP--EQKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRN-KNGE 164
Cdd:cd00200   174 T-GHTGEVNSVAFSPDGEKLLSSSSdGTIKLWDLstGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDlRTGE 252

                         170       180
                  ....*....|....*....|....*.
gi 578807565  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 1.03e-08

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: 1.03e-08
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 578807565     42 DGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
43-80 4.45e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 4.45e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 578807565    43 GTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 676-900 1.77e-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: 47.80  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  676 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 752
Cdd:COG2956    46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  753 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 832
Cdd:COG2956   120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578807565  833 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYY 900
Cdd:COG2956   171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL 235
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 692-900 2.16e-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: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   692 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 754
Cdd:TIGR02917  540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   755 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 828
Cdd:TIGR02917  613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578807565   829 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 900
Cdd:TIGR02917  663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
15-350 2.82e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 130.80  E-value: 2.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:COG2319   123 VRSVAFSPDGK--TLASGSAdgtVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWdlaTGKLLRTL 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   89 KyTHNDAIQCVSYNPITHQLASCSSSDF-GLWSPE--QKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEE 165
Cdd:COG2319   201 T-GHTGAVRSVAFSPDGKLLASGSADGTvRLWDLAtgKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGE 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  166 KVKieRPGGSLSPIWSICWNPSSRWesfwmnrenedaedvivnryiqeipstlksavyssqgseaeeeepeeeddsprdd 245
Cdd:COG2319   280 LLR--TLTGHSGGVNSVAFSPDGKL------------------------------------------------------- 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  246 nleerndiLAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSW 323
Cdd:COG2319   303 --------LASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWdLATGELLRTLTGHTGA 374

                         330       340
                  ....*....|....*....|....*..
gi 578807565  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 1.21e-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: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:cd00200    96 VSSVAFSPDGR--ILSSSSRdktIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWdlrTGKCVATL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   89 KyTHNDAIQCVSYNPITHQLASCSS-SDFGLWSP--EQKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRN-KNGE 164
Cdd:cd00200   174 T-GHTGEVNSVAFSPDGEKLLSSSSdGTIKLWDLstGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDlRTGE 252

                         170       180
                  ....*....|....*....|....*.
gi 578807565  165 EKVKIErpgGSLSPIWSICWNPSSRW 190
Cdd:cd00200   253 CVQTLS---GHTNSVTSLAWSPDGKR 275
WD40 COG2319
WD40 repeat [General function prediction only];
15-350 2.72e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 98.06  E-value: 2.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   15 INDIAFKPDGTQLILAAGSR-LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGILKy 90
Cdd:COG2319    81 VLSVAFSPDGRLLASASADGtVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWdlaTGKLLRTLT- 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   91 THNDAIQCVSYNPithqlascsssdfglwspeqksvskhkssskiiccswtnDGQYLALGMFNGIISIRN-KNGEEkvkI 169
Cdd:COG2319   160 GHSGAVTSVAFSP---------------------------------------DGKLLASGSDDGTVRLWDlATGKL---L 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  170 ERPGGSLSPIWSICWNPSSRWesfwmnrenedaedvivnryiqeipstlksavyssqgseaeeeepeeeddsprddnlee 249
Cdd:COG2319   198 RTLTGHTGAVRSVAFSPDGKL----------------------------------------------------------- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  250 rndiLAVADWGQKVSFYQL-SGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTC 327
Cdd:COG2319   219 ----LASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWdLATGELLRTLTGHSGGVNSV 294

                         330       340
                  ....*....|....*....|...
gi 578807565  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 8.20e-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: 8.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   12 EHCINDIAFKPDGTQLILAAGSRLL-VYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGI 87
Cdd:cd00200    51 TGPVRDVAASADGTYLASGSSDKTIrLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWdveTGKCLTT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   88 LKyTHNDAIQCVSYNPiTHQLASCSSSDF--GLWSPEQKSVSKHKS--SSKIICCSWTNDGQYLALGMFNGIISIRNKNG 163
Cdd:cd00200   131 LR-GHTDWVNSVAFSP-DGTFVASSSQDGtiKLWDLRTGKCVATLTghTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208

                         170       180
                  ....*....|....*....|....*..
gi 578807565  164 EEKVKIERpgGSLSPIWSICWNPSSRW 190
Cdd:cd00200   209 GKCLGTLR--GHENGVNSVAFSPDGYL 233
WD40 COG2319
WD40 repeat [General function prediction only];
2-350 2.02e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 89.20  E-value: 2.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565    2 RAVLTWRDKAEHCINDIAFKPDGTQLILAAGSRL-LVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:COG2319    26 GALLLLLLGLAAAVASLAASPDGARLAAGAGDLTlLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   81 --TSKLEGILKYTHNDAIQCVSYNPITHQLAScSSSDFG--LWSPE--QKSVSKHKSSSKIICCSWTNDGQYLALGMFNG 154
Cdd:COG2319   106 dlATGLLLRTLTGHTGAVRSVAFSPDGKTLAS-GSADGTvrLWDLAtgKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDG 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  155 IISIRN-KNGEEkvkIERPGGSLSPIWSICWNPSSRWesfwmnrenedaedvIV----NRYIQ-------EIPSTLK--- 219
Cdd:COG2319   185 TVRLWDlATGKL---LRTLTGHTGAVRSVAFSPDGKL---------------LAsgsaDGTVRlwdlatgKLLRTLTghs 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  220 ----SAVYSSQGSeaeeeepeeeddsprddnleerndILAVADWGQKVSFYQLSGKQIGKD--------RALNFDPccis 287
Cdd:COG2319   247 gsvrSVAFSPDGR------------------------LLASGSADGTVRLWDLATGELLRTltghsggvNSVAFSP---- 298

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578807565  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 2.09e-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: 2.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   49 LKGHKDTVYCVAYAKDGKRFASGSADKSVIIWTSKlEGILKYT---HNDAIQCVSYNPITHQLASCSSSDFG-LWSPEQK 124
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE-TGELLRTlkgHTGPVRDVAASADGTYLASGSSDKTIrLWDLETG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  125 SVSKHKS--SSKIICCSWTNDGQYLALGMFNGiiSIR---NKNGEEKVKIErpgGSLSPIWSICWNPSsrwesfwmnren 199
Cdd:cd00200    84 ECVRTLTghTSYVSSVAFSPDGRILSSSSRDK--TIKvwdVETGKCLTTLR---GHTDWVNSVAFSPD------------ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  200 edaedvivnryiqeipstlksavyssqgseaeeeepeeeddsprddnleerNDILAVADWGQKVSFYQLSGKQI-----G 274
Cdd:cd00200   147 ---------------------------------------------------GTFVASSSQDGTIKLWDLRTGKCvatltG 175

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578807565  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 6.00e-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: 6.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:cd00200    12 VTCVAFSPDGK--LLATGSGdgtIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWdleTGECVRTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   89 KyTHNDAIQCVSYNPiTHQLASCSSSD--FGLWSPEQKSVSKHKS--SSKIICCSWTNDGQYLALGMFNGIISI-RNKNG 163
Cdd:cd00200    90 T-GHTSYVSSVAFSP-DGRILSSSSRDktIKVWDVETGKCLTTLRghTDWVNSVAFSPDGTFVASSSQDGTIKLwDLRTG 167

                         170       180
                  ....*....|....*....|....*.
gi 578807565  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 6.06e-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: 6.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   15 INDIAFKPDGTqlILAAGSR---LLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW---TSKLEGIL 88
Cdd:cd00200   138 VNSVAFSPDGT--FVASSSQdgtIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWdlsTGKCLGTL 215

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578807565   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 578807565   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 1.03e-08

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: 1.03e-08
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 578807565     42 DGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
43-80 4.45e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 4.45e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 578807565    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 9.43e-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: 9.43e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 578807565    41 SDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIW 80
Cdd:pfam20426  112 NDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVW 151
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 676-900 1.77e-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: 47.80  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  676 LFLADVFSYQGKFHEAAKLYKRSghenLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADwaRNIKEPKAA---VEM 752
Cdd:COG2956    46 LALGNLYRRRGEYDRAIRIHQKL----LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE--LDPDDAEALrllAEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  753 YISAGEHVKAIEicgdhgwvdmlidIARKLDKAEREplllCATYLKKLdspgyaAETYLKMGDLKSLVQLhvetqrWDEA 832
Cdd:COG2956   120 YEQEGDWEKAIE-------------VLERLLKLGPE----NAHAYCEL------AELYLEQGDYDEAIEA------LEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578807565  833 FALGEKHPEfkddIYMPYAQWLAENDRFEEAQKAFHKAGRQ-REAVQVLEQLTNNAVAESRFNDAAYYY 900
Cdd:COG2956   171 LKLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQdPDYLPALPRLAELYEKLGDPEEALELL 235
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
816-902 1.34e-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: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  816 LKSLVQLHVETQRWDEAFALGEK----HPEFKD-DIYMPYAQWLAENDRFEEAQKAFHKA-------------------- 870
Cdd:COG4700   127 LLGLAQALFELGRYAEALETLEKliakNPDFKSsDAHLLYARALEALGDLEAAEAELEALarrysgpearyryakflarq 206

                          90       100       110
                  ....*....|....*....|....*....|..
gi 578807565  871 GRQREAVQVLEQLTNNAVAESRFNDAAYYYWM 902
Cdd:COG4700   207 GRTAEAKELLEEILDEAKHMPKHYRRLNREWI 238
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 692-900 2.16e-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: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   692 AKLYKRSGHENLALEMYTDLcmfeYAKD-------------FLGSGDPKETKMLITKQADWARnikEPKAAVEM----YI 754
Cdd:TIGR02917  540 AGLYLRTGNEEEAVAWLEKA----AELNpqeiepalalaqyYLGKGQLKKALAILNEAADAAP---DSPEAWLMlgraQL 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565   755 SAGEHVKAIEIcgdhgwvdmlidiARKLdkAEREP------LLLCATYLKKLDSPGyaAETYLKmgdlKSLvqlhvetqr 828
Cdd:TIGR02917  613 AAGDLNKAVSS-------------FKKL--LALQPdsalalLLLADAYAVMKNYAK--AITSLK----RAL--------- 662

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578807565   829 wdeafalgEKHPEFKDDIYMpYAQWLAENDRFEEAQKAFHKAGRQR-EAVQVLEQLTNNAVAESRFNDAAYYY 900
Cdd:TIGR02917  663 --------ELKPDNTEAQIG-LAQLLLAAKRTESAKKIAKSLQKQHpKAALGFELEGDLYLRQKDYPAAIQAY 726
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 751-936 3.44e-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: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  751 EMYISAGEHVKAIEIC-------GDHGWVdmLIDIAR------KLDKAEreplllcATYLKKLDSPGYAAETYLKmgdlk 817
Cdd:COG2956    50 NLYRRRGEYDRAIRIHqkllerdPDRAEA--LLELAQdylkagLLDRAE-------ELLEKLLELDPDDAEALRL----- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807565  818 sLVQLHVETQRWDEAFALGEK----HPEfKDDIYMPYAQWLAENDRFEEAQKAFHKA-GRQREAVQVLEQLTNNAVAESR 892
Cdd:COG2956   116 -LAEIYEQEGDWEKAIEVLERllklGPE-NAHAYCELAELYLEQGDYDEAIEALEKAlKLDPDCARALLLLAELYLEQGD 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578807565  893 FNDAAYYYwmlsmqcLDIAQADPAQKDTMLgkfyhfqRLAELYH 936
Cdd:COG2956   194 YEEAIAAL-------ERALEQDPDYLPALP-------RLAELYE 223
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 578807565  285 CISYFTKGEYILLGGSDKQVSLF-TKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQLI 351
Cdd:cd00200    56 DVAASADGTYLASGSSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE 123
 
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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