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Conserved domains on  [gi|57524675|ref|NP_001003758|]
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THO complex subunit 3 [Danio rerio]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 11455410)

WD40 repeat domain-containing protein similar to 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
PubMed:  10322433|8090199
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];
20-320 4.16e-58

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 192.43  E-value: 4.16e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  20 REFPAHSAKVHSVAWSCDGKRLASGSFDKTASVFVLEKDRLVKEnnYRGHGDSVDQLCWHPTNpDLFVTASGDKTIRIWD 99
Cdd:COG2319 114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRT--LTGHSGAVTSVAFSPDG-KLLASGSDDGTVRLWD 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 100 VRTTKCMATVSTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRPRAEEQFK-FEVNEISWNNDNDMFFLTNGNGCI 177
Cdd:COG2319 191 LATGKLLRTLTGHTGAVRsVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHsGSVRSVAFSPDGRLLASGSADGTV 270
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 178 NILSYPELKLIQSINAHPSNCICIKFDPTGKYFATGSADALVSLWNVEELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 257
Cdd:COG2319 271 RLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSD 350
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57524675 258 DHFIDIAEVETGEKLWEIQ-CESPTFTVAWHPKRPLLAYACDDkegkydsnreaGTVKLFGLPN 320
Cdd:COG2319 351 DGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSAD-----------GTVRLWDLAT 403
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
20-320 4.16e-58

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 192.43  E-value: 4.16e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  20 REFPAHSAKVHSVAWSCDGKRLASGSFDKTASVFVLEKDRLVKEnnYRGHGDSVDQLCWHPTNpDLFVTASGDKTIRIWD 99
Cdd:COG2319 114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRT--LTGHSGAVTSVAFSPDG-KLLASGSDDGTVRLWD 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 100 VRTTKCMATVSTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRPRAEEQFK-FEVNEISWNNDNDMFFLTNGNGCI 177
Cdd:COG2319 191 LATGKLLRTLTGHTGAVRsVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHsGSVRSVAFSPDGRLLASGSADGTV 270
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 178 NILSYPELKLIQSINAHPSNCICIKFDPTGKYFATGSADALVSLWNVEELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 257
Cdd:COG2319 271 RLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSD 350
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57524675 258 DHFIDIAEVETGEKLWEIQ-CESPTFTVAWHPKRPLLAYACDDkegkydsnreaGTVKLFGLPN 320
Cdd:COG2319 351 DGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSAD-----------GTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
15-261 4.99e-48

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: 162.89  E-value: 4.99e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  15 NNNKSREFPAHSAKVHSVAWSCDGKRLASGSFDKTASVFVLEKDRLVKEnnYRGHGDSVDQLCWHPTNPdLFVTASGDKT 94
Cdd:cd00200  40 TGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT--LTGHTSYVSSVAFSPDGR-ILSSSSRDKT 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  95 IRIWDVRTTKCMATVSTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRPRAE-EQFKFEVNEISWNNDNDMFFLTN 172
Cdd:cd00200 117 IKVWDVETGKCLTTLRGHTDWVNsVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSS 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 173 GNGCINILSYPELKLIQSINAHPSNCICIKFDPTGKYFATGSADALVSLWNVEELVCVRCFSRLDWPVRTLSFSHDGKML 252
Cdd:cd00200 197 SDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRL 276

                ....*....
gi 57524675 253 ASASEDHFI 261
Cdd:cd00200 277 ASGSADGTI 285
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
15-142 5.46e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 51.24  E-value: 5.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675   15 NNNKSREFP----AHSAKVHSVAWSCDGK-RLASGSFDKTASVFVLEKDRLVKEnnYRGHGDSVDQLCWHPTNPDLFVTA 89
Cdd:PLN00181 517 KDGRDIHYPvvelASRSKLSGICWNSYIKsQVASSNFEGVVQVWDVARSQLVTE--MKEHEKRVWSIDYSSADPTLLASG 594
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 57524675   90 SGDKTIRIWDVRTTKCMATVSTKGeniNICW----SPDGQTIAVGNKDDVVTFIDAK 142
Cdd:PLN00181 595 SDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpSESGRSLAFGSADHKVYYYDLR 648
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
66-99 2.49e-06

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: 43.46  E-value: 2.49e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 57524675     66 YRGHGDSVDQLCWHPTNpDLFVTASGDKTIRIWD 99
Cdd:smart00320   8 LKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
66-99 1.64e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.18  E-value: 1.64e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 57524675    66 YRGHGDSVDQLCWHPtNPDLFVTASGDKTIRIWD 99
Cdd:pfam00400   7 LEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
propeller_TolB TIGR02800
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB ...
78-133 4.33e-03

tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274305 [Multi-domain]  Cd Length: 417  Bit Score: 38.41  E-value: 4.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57524675    78 WHPTNPDL-FVTASGDK-TIRIWDVRTTKCMATVSTKGENINICWSPDGQTIAV-----GNKD 133
Cdd:TIGR02800 197 WSPDGQKLaYVSFESGKpEIYVQDLATGQREKVASFPGMNGAPAFSPDGSKLAVslskdGNPD 259
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
20-320 4.16e-58

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 192.43  E-value: 4.16e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  20 REFPAHSAKVHSVAWSCDGKRLASGSFDKTASVFVLEKDRLVKEnnYRGHGDSVDQLCWHPTNpDLFVTASGDKTIRIWD 99
Cdd:COG2319 114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRT--LTGHSGAVTSVAFSPDG-KLLASGSDDGTVRLWD 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 100 VRTTKCMATVSTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRPRAEEQFK-FEVNEISWNNDNDMFFLTNGNGCI 177
Cdd:COG2319 191 LATGKLLRTLTGHTGAVRsVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHsGSVRSVAFSPDGRLLASGSADGTV 270
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 178 NILSYPELKLIQSINAHPSNCICIKFDPTGKYFATGSADALVSLWNVEELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 257
Cdd:COG2319 271 RLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSD 350
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57524675 258 DHFIDIAEVETGEKLWEIQ-CESPTFTVAWHPKRPLLAYACDDkegkydsnreaGTVKLFGLPN 320
Cdd:COG2319 351 DGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSAD-----------GTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
20-315 2.96e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 179.72  E-value: 2.96e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  20 REFPAHSAKVHSVAWSCDGKRLASGSFDKTASVFVLEKDRLVKEnnYRGHGDSVDQLCWHPtNPDLFVTASGDKTIRIWD 99
Cdd:COG2319  72 ATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRT--LTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWD 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 100 VRTTKCMATVSTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRPRAE-EQFKFEVNEISWNNDNDMFFLTNGNGCI 177
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTsVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSADGTV 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 178 NILSYPELKLIQSINAHPSNCICIKFDPTGKYFATGSADALVSLWNVEELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 257
Cdd:COG2319 229 RLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSD 308
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 57524675 258 DHFIDIAEVETGEKLWEIQCES-PTFTVAWHPKRPLLAYACDDkegkydsnreaGTVKL 315
Cdd:COG2319 309 DGTVRLWDLATGKLLRTLTGHTgAVRSVAFSPDGKTLASGSDD-----------GTVRL 356
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
15-261 4.99e-48

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: 162.89  E-value: 4.99e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  15 NNNKSREFPAHSAKVHSVAWSCDGKRLASGSFDKTASVFVLEKDRLVKEnnYRGHGDSVDQLCWHPTNPdLFVTASGDKT 94
Cdd:cd00200  40 TGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT--LTGHTSYVSSVAFSPDGR-ILSSSSRDKT 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  95 IRIWDVRTTKCMATVSTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRPRAE-EQFKFEVNEISWNNDNDMFFLTN 172
Cdd:cd00200 117 IKVWDVETGKCLTTLRGHTDWVNsVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSS 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 173 GNGCINILSYPELKLIQSINAHPSNCICIKFDPTGKYFATGSADALVSLWNVEELVCVRCFSRLDWPVRTLSFSHDGKML 252
Cdd:cd00200 197 SDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRL 276

                ....*....
gi 57524675 253 ASASEDHFI 261
Cdd:cd00200 277 ASGSADGTI 285
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
14-223 4.30e-35

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: 128.99  E-value: 4.30e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  14 RNNNKSREFPAHSAKVHSVAWSCDGKRLASGSFDKTASVFVLEKDRLVKEnnYRGHGDSVDQLCWHPTNpDLFVTASGDK 93
Cdd:cd00200  81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT--LRGHTDWVNSVAFSPDG-TFVASSSQDG 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  94 TIRIWDVRTTKCMATVSTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKT----HRPRAEEQFkfeVNEISWNNDNDMF 168
Cdd:cd00200 158 TIKLWDLRTGKCVATLTGHTGEVNsVAFSPDGEKLLSSSSDGTIKLWDLSTgkclGTLRGHENG---VNSVAFSPDGYLL 234
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 57524675 169 FLTNGNGCINILSYPELKLIQSINAHPSNCICIKFDPTGKYFATGSADALVSLWN 223
Cdd:cd00200 235 ASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
37-316 3.71e-22

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 95.75  E-value: 3.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  37 DGKRLASGSFDKTASVFVLEKDRLVKEnnyRGHGDSVDQLCWHPTNPDLFVTASGDKTIRIWDVRTTKCMATVSTKGENI 116
Cdd:COG2319   5 DGAALAAASADLALALLAAALGALLLL---LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 117 NIC-WSPDGQTIAVGNKDDVVTFIDAKTHRPRAeeqfkfevneiswnndndmffltngngcinilsypelkliqSINAHP 195
Cdd:COG2319  82 LSVaFSPDGRLLASASADGTVRLWDLATGLLLR-----------------------------------------TLTGHT 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 196 SNCICIKFDPTGKYFATGSADALVSLWNVEELVCVRCFSRLDWPVRTLSFSHDGKMLASASEDHFIDIAEVETGEKLWEI 275
Cdd:COG2319 121 GAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTL 200
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 57524675 276 QCESPTFT-VAWHPKRPLLAYACDDkegkydsnreaGTVKLF 316
Cdd:COG2319 201 TGHTGAVRsVAFSPDGKLLASGSAD-----------GTVRLW 231
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
187-300 1.66e-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: 78.15  E-value: 1.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675 187 LIQSINAHPSNCICIKFDPTGKYFATGSADALVSLWNVEELVCVRCFSRLDWPVRTLSFSHDGKMLASASEDHFIDIAEV 266
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 57524675 267 ETGEKLWEIQC-ESPTFTVAWHPKRPLLAYACDDK 300
Cdd:cd00200  81 ETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDK 115
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
37-178 1.19e-09

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 57.78  E-value: 1.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  37 DGKRL-ASGSFDKTASVFVLEKDRLVKENNyrgHGDSVDQLCWHPTNPDLFVTASGDKTIRIWDVRTTKCMATVSTKGEN 115
Cdd:COG3391  78 DGRRLyVANSGSGRVSVIDLATGKVVATIP---VGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGP 154
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57524675 116 INICWSPDGQTIAVGNKDD-----VVTFIDAKTHRPRAEEQFKFEVNEISWNNDNDMFFLTN-GNGCIN 178
Cdd:COG3391 155 HGIAVDPDGKRLYVANSGSntvsvIVSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLYVANrGSNTSN 223
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
15-142 5.46e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 51.24  E-value: 5.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675   15 NNNKSREFP----AHSAKVHSVAWSCDGK-RLASGSFDKTASVFVLEKDRLVKEnnYRGHGDSVDQLCWHPTNPDLFVTA 89
Cdd:PLN00181 517 KDGRDIHYPvvelASRSKLSGICWNSYIKsQVASSNFEGVVQVWDVARSQLVTE--MKEHEKRVWSIDYSSADPTLLASG 594
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 57524675   90 SGDKTIRIWDVRTTKCMATVSTKGeniNICW----SPDGQTIAVGNKDDVVTFIDAK 142
Cdd:PLN00181 595 SDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpSESGRSLAFGSADHKVYYYDLR 648
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
66-99 2.49e-06

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: 43.46  E-value: 2.49e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 57524675     66 YRGHGDSVDQLCWHPTNpDLFVTASGDKTIRIWD 99
Cdd:smart00320   8 LKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
186-223 3.48e-06

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: 43.07  E-value: 3.48e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 57524675    186 KLIQSINAHPSNCICIKFDPTGKYFATGSADALVSLWN 223
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
15-53 7.63e-06

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: 42.30  E-value: 7.63e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 57524675     15 NNNKSREFPAHSAKVHSVAWSCDGKRLASGSFDKTASVF 53
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
66-99 1.64e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.18  E-value: 1.64e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 57524675    66 YRGHGDSVDQLCWHPtNPDLFVTASGDKTIRIWD 99
Cdd:pfam00400   7 LEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
20-53 4.73e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.02  E-value: 4.73e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 57524675    20 REFPAHSAKVHSVAWSCDGKRLASGSFDKTASVF 53
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 pfam00400
WD domain, G-beta repeat;
186-223 5.87e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 5.87e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 57524675   186 KLIQSINAHPSNCICIKFDPTGKYFATGSADALVSLWN 223
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
67-142 9.05e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.11  E-value: 9.05e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57524675   67 RGHGDSVDQLCWHPTNPDLFVTASGDKTIRIWDVRTTKCMATVSTKGENI-NICWSPDGQTIAVGNKDDVVTFIDAK 142
Cdd:PTZ00421 122 QGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGKAVEVIKCHSDQItSLEWNLDGSLLCTTSKDKKLNIIDPR 198
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
120-209 1.08e-03

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 40.79  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  120 WSPDGQTIAVGNKDDVVTFIDAKTHRPR--AEEQFKFEVNEISWNNDND----MFFLTNGNGCINILSYPELKLIQsINA 193
Cdd:COG4946  396 WSPDGKKIAFTDNRGRLWVVDLASGKVRkvDTDGYGDGISDLAWSPDSKwlaySKPGPNQLSQIFLYDVETGKTVQ-LTD 474
                         90
                 ....*....|....*.
gi 57524675  194 HPSNCICIKFDPTGKY 209
Cdd:COG4946  475 GRYDDGSPAFSPDGKY 490
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
85-196 1.47e-03

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 39.96  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  85 LFVTASGDKTIRIWDVRTTKCMATVSTKGENINICWSPDGQTIAV---GNKDDVVTFIDAKTHRPRAEEQFKFEVNEISW 161
Cdd:cd20778 253 AFVPAVGEHRVLVYDTNDWKFIKSIPLAGQPVFAVARPDGRYVWVnfsGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEF 332
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 57524675 162 NNDNDMFFLT-NGNGCINILSYPELKLIQSINAH-PS 196
Cdd:cd20778 333 TPRGEAVYISvNDDNKVVVYDTRTFREIKEVPAKkPS 369
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
230-286 1.77e-03

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 36.87  E-value: 1.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57524675   230 VRCFsRLDW-------------PVRTLSFSHDGKMLASASEDHFIDIAEVETGEKLWEIQCESPTFT-VAW 286
Cdd:pfam12894  19 LLLH-RLNWqrvwtlspdkedlEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITcLGW 88
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
76-143 2.89e-03

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 36.49  E-value: 2.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57524675    76 LCWHPTNpDLFVTASGDKTI--------RIWDVRTTKcmatvsTKGENINICWSPDGQTIAVGNKDDVVTFIDAKT 143
Cdd:pfam12894   1 MSWCPTM-DLIALATEDGELllhrlnwqRVWTLSPDK------EDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAEN 69
PTZ00421 PTZ00421
coronin; Provisional
79-263 3.26e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 39.11  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675   79 HPTNPD---LFVTASGdktiRIWDvrttkCMATVSTKGENINICWSPDGQTiAVGNKDDvvtFIDAKTHRPRAEEQfKFE 155
Cdd:PTZ00421  12 VPARPDrhfLNVTPST----ALWD-----CSNTIACNDRFIAVPWQQLGST-AVLKHTD---YGKLASNPPILLGQ-EGP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  156 VNEISWNN-DNDMFFLTNGNGCINILSYPELKLIQSIN-------AHPSNCICIKFDPTGK-YFATGSADALVSLWNVEE 226
Cdd:PTZ00421  78 IIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhlqGHTKKVGIVSFHPSAMnVLASAGADMVVNVWDVER 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 57524675  227 LVCVRCFSRLDWPVRTLSFSHDGKMLASASEDHFIDI 263
Cdd:PTZ00421 158 GKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNI 194
propeller_TolB TIGR02800
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB ...
78-133 4.33e-03

tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274305 [Multi-domain]  Cd Length: 417  Bit Score: 38.41  E-value: 4.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57524675    78 WHPTNPDL-FVTASGDK-TIRIWDVRTTKCMATVSTKGENINICWSPDGQTIAV-----GNKD 133
Cdd:TIGR02800 197 WSPDGQKLaYVSFESGKpEIYVQDLATGQREKVASFPGMNGAPAFSPDGSKLAVslskdGNPD 259
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
105-212 5.10e-03

Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors.


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 37.64  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675   105 CMATVSTKGENINICWSPDGQTIAVgnkddVVTFIDAKT--HRPRAEEQFKFE---VNEISWNnDNDMFFLTNG----NG 175
Cdd:pfam08662  52 CVVELDKEGPIHDVAWSPNGKEFAV-----IYGYMPAKVsfFDLKGNVIHSFGeqpRNTIFWS-PFGRLVLLAGfgnlAG 125
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 57524675   176 CINILSYPELKLIQSINAhpSNCICIKFDPTGKYFAT 212
Cdd:pfam08662 126 DIEFWDVVNKKKIATAEA--SNATLCEWSPDGRYFLT 160
PTZ00420 PTZ00420
coronin; Provisional
12-104 5.60e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 38.39  E-value: 5.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675   12 VFRNNNKSREFPAHSAKVHSVAW------SCDGKRLASGSFDKTASVF-VLEKDRLVKENN-----YRGHGDSVDQLCWH 79
Cdd:PTZ00420  55 AIRLENQMRKPPVIKLKGHTSSIldlqfnPCFSEILASGSEDLTIRVWeIPHNDESVKEIKdpqciLKGHKKKISIIDWN 134
                         90       100
                 ....*....|....*....|....*
gi 57524675   80 PTNPDLFVTASGDKTIRIWDVRTTK 104
Cdd:PTZ00420 135 PMNYYIMCSSGFDSFVNIWDIENEK 159
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
88-211 6.23e-03

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 36.96  E-value: 6.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57524675  88 TASGDKTIRIWDVRTTKCMATVSTKGENINICWSPDGQTIAV----GNKDDVVTfIDAKTHRPRAEEQFKFEVNEISWNN 163
Cdd:COG0823   6 SRDGNSDIYVVDLDGGEPRRLTNSPGIDTSPAWSPDGRRIAFtsdrGGGPQIYV-VDADGGEPRRLTFGGGYNASPSWSP 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 57524675 164 DND-MFFLTNGNGCINILSYP----ELKLIQSINAHPSncicikFDPTGKYFA 211
Cdd:COG0823  85 DGKrLAFVSRSDGRFDIYVLDldggAPRRLTDGPGSPS------WSPDGRRIV 131
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
229-261 6.51e-03

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: 33.83  E-value: 6.51e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 57524675    229 CVRCFSRLDWPVRTLSFSHDGKMLASASEDHFI 261
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTI 36
 
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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