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Conserved domains on  [gi|157823413|ref|NP_001099529|]
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THO complex subunit 3 [Rattus norvegicus]

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];
49-305 1.44e-53

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 181.26  E-value: 1.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  49 REFPAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:COG2319  156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT--LTGHTGAVRSVAFSPDG-KLLASGSADGTVRLWD 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 129 VRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNGCI 206
Cdd:COG2319  233 LATGKLLRTLTGHSGSVRsVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFSPDGKLLASGSDDGTV 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 207 NILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 286
Cdd:COG2319  313 RLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSA 392

                        250
                 ....*....|....*....
gi 157823413 287 DHFIdiaevetgdKLWEVQ 305
Cdd:COG2319  393 DGTV---------RLWDLA 402
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
49-305 1.44e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 181.26  E-value: 1.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  49 REFPAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:COG2319  156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT--LTGHTGAVRSVAFSPDG-KLLASGSADGTVRLWD 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 129 VRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNGCI 206
Cdd:COG2319  233 LATGKLLRTLTGHSGSVRsVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFSPDGKLLASGSDDGTV 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 207 NILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 286
Cdd:COG2319  313 RLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSA 392

                        250
                 ....*....|....*....
gi 157823413 287 DHFIdiaevetgdKLWEVQ 305
Cdd:COG2319  393 DGTV---------RLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 49-290 7.49e-47

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: 160.58  E-value: 7.49e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  49 REFPAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNPdLFVTASGDKTIRIWD 128
Cdd:cd00200   45 RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT--LTGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWD 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 129 VRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNGCI 206
Cdd:cd00200  122 VETGKCLTTLRGHTDWVNsVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSSSDGTI 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 207 NILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 286
Cdd:cd00200  202 KLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSA 281


                 ....
gi 157823413 287 DHFI 290
Cdd:cd00200  282 DGTI 285
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 53-171 1.33e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.09  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  53 AHSAKVHSVAW-SCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNPDLFVTASGDKTIRIWDVRT 131
Cdd:PLN00181 530 ASRSKLSGICWnSYIKSQVASSNFEGVVQVWDVARSQLVTE--MKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQ 607

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 157823413 132 TKCIATVNTKGeniNICW----SPDGQTIAVGNKDDVVTFIDAK 171
Cdd:PLN00181 608 GVSIGTIKTKA---NICCvqfpSESGRSLAFGSADHKVYYYDLR 648
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 215-252 3.00e-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: 3.00e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 157823413   215 KPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWD 252
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
95-128 2.86e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 2.86e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 157823413   95 YRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDG-KLLASGSDDGTVKVWD 39
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 48-177 4.45e-03

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 38.48  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413   48 TREFPAhSAKVHSVAWSCDGRRL-ASGSFDKTASVFLLEKDRLVKEnnyRGHGDSVDQLCWHPSNPDLFVTASGDKTIRI 126
Cdd:TIGR03866  34 TRTFPV-GQRPRGITFSKDGKLLyVCASDSDTIQVIDPATGEVLHT---LPSGPDPEQFALHPNGKILYIANEDDALVTV 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157823413  127 WDVRTTKCIATVNTKGENINICWSPDGQTIAVGNK-DDVVTFIDAKTHRSKA 177
Cdd:TIGR03866 110 IDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSEtTNMAHWIDTATYEIVD 161
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
49-305 1.44e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 181.26  E-value: 1.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  49 REFPAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:COG2319  156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT--LTGHTGAVRSVAFSPDG-KLLASGSADGTVRLWD 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 129 VRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNGCI 206
Cdd:COG2319  233 LATGKLLRTLTGHSGSVRsVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFSPDGKLLASGSDDGTV 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 207 NILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 286
Cdd:COG2319  313 RLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSA 392

                        250
                 ....*....|....*....
gi 157823413 287 DHFIdiaevetgdKLWEVQ 305
Cdd:COG2319  393 DGTV---------RLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
48-349 2.92e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 180.49  E-value: 2.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  48 TREFPAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIW 127
Cdd:COG2319  113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRT--LTGHSGAVTSVAFSPDG-KLLASGSDDGTVRLW 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 128 DVRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAEEQFK-FEVNEISWNNDNNMFFLTNGNGC 205
Cdd:COG2319  190 DLATGKLLRTLTGHTGAVRsVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHsGSVRSVAFSPDGRLLASGSADGT 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 206 INILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASAS 285
Cdd:COG2319  270 VRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGS 349

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157823413 286 EDHFIDIAEVETGDKLWEVQ-CESPTFTVAWHPKRPLLAFACDDkdgkydssreaGTVKLFGLPN 349
Cdd:COG2319  350 DDGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSAD-----------GTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
32-344 2.05e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 167.78  E-value: 2.05e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  32 SRYVLGMQELFRGHSKTREFPAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSN 111
Cdd:COG2319   55 AGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRT--LTGHTGAVRSVAFSPDG 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 112 pDLFVTASGDKTIRIWDVRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEIS 189
Cdd:COG2319  133 -KTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTsVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVA 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 190 WNNDNNMFFLTNGNGCINILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPV 269
Cdd:COG2319  212 FSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGV 291

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823413 270 RTLSFSHDGKMLASASEDHFIDIAEVETGDKLWEVQCES-PTFTVAWHPKRPLLAFACDDkdgkydssreaGTVKL 344
Cdd:COG2319  292 NSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTgAVRSVAFSPDGKTLASGSDD-----------GTVRL 356
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 49-290 7.49e-47

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: 160.58  E-value: 7.49e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  49 REFPAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNPdLFVTASGDKTIRIWD 128
Cdd:cd00200   45 RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT--LTGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWD 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 129 VRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNGCI 206
Cdd:cd00200  122 VETGKCLTTLRGHTDWVNsVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSSSDGTI 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 207 NILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASE 286
Cdd:cd00200  202 KLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSA 281


                 ....
gi 157823413 287 DHFI 290
Cdd:cd00200  282 DGTI 285
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 47-252 5.23e-34

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: 126.68  E-value: 5.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  47 KTREFPAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGDKTIRI 126
Cdd:cd00200   85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT--LRGHTDWVNSVAFSPDG-TFVASSSQDGTIKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 127 WDVRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAE-EQFKFEVNEISWNNDNNMFFLTNGNG 204
Cdd:cd00200  162 WDLRTGKCVATLTGHTGEVNsVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSPDGYLLASGSEDG 241

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157823413 205 CINILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWD 252
Cdd:cd00200  242 TIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
66-345 6.01e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 107.30  E-value: 6.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  66 DGRRLASGSFDKTASVFLLEKDRLVKEnnyRGHGDSVDQLCWHPSNPDLFVTASGDKTIRIWDVRTTKCIATVNTKGENI 145
Cdd:COG2319    5 DGAALAAASADLALALLAAALGALLLL---LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 146 NIC-WSPDGQTIAVGNKDDVVTFIDAKTHRSKAEEQ-FKFEVNEISWNNDNNMFFLTNGNGCINILSYPELKPVQSINAH 223
Cdd:COG2319   82 LSVaFSPDGRLLASASADGTVRLWDLATGLLLRTLTgHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 224 PSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASEDHFIDIAEVETGDKLWE 303
Cdd:COG2319  162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 157823413 304 VQCESPT-FTVAWHPKRPLLAFACDDkdgkydssreaGTVKLF 345
Cdd:COG2319  242 LTGHSGSvRSVAFSPDGRLLASGSAD-----------GTVRLW 273
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 42-162 2.11e-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: 89.70  E-value: 2.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  42 FRGHSKTREFPAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNpDLFVTASGD 121
Cdd:cd00200  164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT--LRGHENGVNSVAFSPDG-YLLASGSED 240

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157823413 122 KTIRIWDVRTTKCIATVNTKGENIN-ICWSPDGQTIAVGNKD 162
Cdd:cd00200  241 GTIRVWDLRTGECVQTLSGHTNSVTsLAWSPDGKRLASGSAD 282
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 216-349 2.56e-15

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: 75.06  E-value: 2.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413 216 PVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASEDHFIDIAEV 295
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157823413 296 ETGDKLWEVQC-ESPTFTVAWHPKRPLLAfacddkdgkydSSREAGTVKLFGLPN 349
Cdd:cd00200   81 ETGECVRTLTGhTSYVSSVAFSPDGRILS-----------SSSRDKTIKVWDVET 124
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
1-207 4.69e-10

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 59.32  E-value: 4.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413   1 MAVPAAVLGPSALSQSGPGSMAPWCSVSSGPSRYVLGMQELFRGHSKTREFPAHSAKVHSVAWSCDGRRL-ASGSFDKTA 79
Cdd:COG3391   13 LAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  80 SVFLLEKDRLVKENNyrgHGDSVDQLCWHPSNPDLFVTASGDKTIRIWDVRTTKCIATVNTKGENINICWSPDGQTIAVG 159
Cdd:COG3391   93 SVIDLATGKVVATIP---VGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVA 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157823413 160 NKDD-----VVTFIDAKTHRSKAEEQFKFEVNEISWNNDNNMFFLTN-GNGCIN 207
Cdd:COG3391  170 NSGSntvsvIVSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLYVANrGSNTSN 223
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 53-171 1.33e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.09  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  53 AHSAKVHSVAW-SCDGRRLASGSFDKTASVFLLEKDRLVKEnnYRGHGDSVDQLCWHPSNPDLFVTASGDKTIRIWDVRT 131
Cdd:PLN00181 530 ASRSKLSGICWnSYIKSQVASSNFEGVVQVWDVARSQLVTE--MKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQ 607

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 157823413 132 TKCIATVNTKGeniNICW----SPDGQTIAVGNKDDVVTFIDAK 171
Cdd:PLN00181 608 GVSIGTIKTKA---NICCvqfpSESGRSLAFGSADHKVYYYDLR 648
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 215-252 3.00e-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: 3.00e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 157823413   215 KPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWD 252
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 95-128 3.65e-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: 3.65e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 157823413    95 YRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:smart00320   8 LKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 46-82 1.72e-05

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: 41.53  E-value: 1.72e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 157823413    46 SKTREFPAHSAKVHSVAWSCDGRRLASGSFDKTASVF 82
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
95-128 2.86e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 2.86e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 157823413   95 YRGHGDSVDQLCWHPSNpDLFVTASGDKTIRIWD 128
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDG-KLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
215-252 4.81e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.02  E-value: 4.81e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 157823413  215 KPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWD 252
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
46-82 6.65e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 6.65e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 157823413   46 SKTREFPAHSAKVHSVAWSCDGRRLASGSFDKTASVF 82
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00421 PTZ00421
coronin; Provisional
 96-171 7.43e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.50  E-value: 7.43e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823413  96 RGHGDSVDQLCWHPSNPDLFVTASGDKTIRIWDVRTTKCIATVNTKGENI-NICWSPDGQTIAVGNKDDVVTFIDAK 171
Cdd:PTZ00421 122 QGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGKAVEVIKCHSDQItSLEWNLDGSLLCTTSKDKKLNIIDPR 198
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 107-174 1.40e-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: 40.34  E-value: 1.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823413 107 WHPSNPDLFVTASGDKTIRIWDVRTTKCIATVNTKGENINICWSPDGQTIAV---GNKDDVVTFIDAKTHR 174
Cdd:cd20778  246 WAVAGDKAFVPAVGEHRVLVYDTNDWKFIKSIPLAGQPVFAVARPDGRYVWVnfsGPDNDTVQVIDTKTLK 316
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 137-238 2.57e-03

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 39.64  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413  137 TVNTKGENINICWSPDGQTIAVGNKDDVVTFIDAKTHRSK--AEEQFKFEVNEISWNNDNN----MFFLTNGNGCINILS 210
Cdd:COG4946   384 TLGDLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRkvDTDGYGDGISDLAWSPDSKwlaySKPGPNQLSQIFLYD 463

                          90       100
                  ....*....|....*....|....*...
gi 157823413  211 YPELKPVQsINAHPSNCICIKFDPMGKY 238
Cdd:COG4946   464 VETGKTVQ-LTDGRYDDGSPAFSPDGKY 490
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 48-177 4.45e-03

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 38.48  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823413   48 TREFPAhSAKVHSVAWSCDGRRL-ASGSFDKTASVFLLEKDRLVKEnnyRGHGDSVDQLCWHPSNPDLFVTASGDKTIRI 126
Cdd:TIGR03866  34 TRTFPV-GQRPRGITFSKDGKLLyVCASDSDTIQVIDPATGEVLHT---LPSGPDPEQFALHPNGKILYIANEDDALVTV 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157823413  127 WDVRTTKCIATVNTKGENINICWSPDGQTIAVGNK-DDVVTFIDAKTHRSKA 177
Cdd:TIGR03866 110 IDIETRKVLAQIDVGVEPEGMAVSPDGKIVVNTSEtTNMAHWIDTATYEIVD 161
propeller_TolB TIGR02800
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB ...
 107-162 4.91e-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: 4.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157823413  107 WHPSNPDL-FVTASGDK-TIRIWDVRTTKCIATVNTKGENINICWSPDGQTIAV-----GNKD 162
Cdd:TIGR02800 197 WSPDGQKLaYVSFESGKpEIYVQDLATGQREKVASFPGMNGAPAFSPDGSKLAVslskdGNPD 259
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 105-172 5.24e-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: 35.72  E-value: 5.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823413  105 LCWHPSNpDLFVTASGDKTI--------RIWDvrttkcIATVNTKGENINICWSPDGQTIAVGNKDDVVTFIDAKT 172
Cdd:pfam12894   1 MSWCPTM-DLIALATEDGELllhrlnwqRVWT------LSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAEN 69
 
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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