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Conserved domains on  [gi|5032159|ref|NP_005638|]
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F-box-like/WD repeat-containing protein TBL1X isoform a [Homo sapiens]

Protein Classification

WD40 domain-containing protein( domain architecture ID 10553538)

WD40 domain-containing protein similar to Homo sapiens F-box-like/WD repeat-containing protein TBL1X/TBL1Y/TBL1XR1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 227-533 1.04e-86

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: 270.75  E-value: 1.04e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  227 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENsnggstqlvlRHCIREGGHDVPsnkdVTSLDWNTNGTLLATG 306
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG----------ELLRTLKGHTGP----VRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  307 SYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQNNTTF 385
Cdd:cd00200  70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  386 -ASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWSP 464
Cdd:cd00200 150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5032159  465 tgpatsnpnSNIMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 533
Cdd:cd00200 230 ---------DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 58-82 6.30e-07

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


:

Pssm-ID: 462501  Cd Length: 25  Bit Score: 45.77  E-value: 6.30e-07
                          10        20
                  ....*....|....*....|....*
gi 5032159     58 EVNFLVYRYLQESGFSHSAFTFGIE 82
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
8prop_heme_binding_protein super family cl49617
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 507-577 7.50e-04

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> 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 nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


The actual alignment was detected with superfamily member cd20778:

Pssm-ID: 483957 [Multi-domain]  Cd Length: 381  Bit Score: 42.27  E-value: 7.50e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5032159  507 PVYSVAfSPDGKYLA---SGSFDKCVHIWNTQSGNLVHSYRGTGGIFEVCWNARGDKVGASASDGS-VCVLDLRK 577
Cdd:cd20778 283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNkVVVYDTRT 356
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 227-533 1.04e-86

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: 270.75  E-value: 1.04e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  227 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENsnggstqlvlRHCIREGGHDVPsnkdVTSLDWNTNGTLLATG 306
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG----------ELLRTLKGHTGP----VRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  307 SYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQNNTTF 385
Cdd:cd00200  70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  386 -ASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWSP 464
Cdd:cd00200 150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5032159  465 tgpatsnpnSNIMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 533
Cdd:cd00200 230 ---------DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
225-576 4.35e-79

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 254.84  E-value: 4.35e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  225 ATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDvpsnKDVTSLDWNTNGTLLA 304
Cdd:COG2319  71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA----TGLLLRTLT------GHT----GAVRSVAFSPDGKTLA 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  305 TGSYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNN 382
Cdd:COG2319 137 SGSADGTVRLWdLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFsPDG 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  383 TTFASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKW 462
Cdd:COG2319 217 KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAF 296

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  463 SPTGPatsnpnsniMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHS 542
Cdd:COG2319 297 SPDGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367

                       330       340       350
                ....*....|....*....|....*....|....*
gi 5032159  543 YRG-TGGIFEVCWNARGDKVGASASDGSVCVLDLR 576
Cdd:COG2319 368 LTGhTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
PTZ00420 PTZ00420
coronin; Provisional
 404-493 1.26e-11

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 67.28  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   404 PVKTFQGHTNEVNAIKWDPS-GMLLASCSDDMTLKIWSMKQE----------VCIhdLQAHNKEIYTIKWsptgpatsNP 472
Cdd:PTZ00420  66 PVIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPHNdesvkeikdpQCI--LKGHKKKISIIDW--------NP 135

                         90       100
                 ....*....|....*....|.
gi 5032159   473 NSNIMLASASFDSTVRLWDIE 493
Cdd:PTZ00420 136 MNYYIMCSSGFDSFVNIWDIE 156
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 495-533 1.34e-10

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: 56.55  E-value: 1.34e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 5032159     495 GVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 533
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
495-533 4.50e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 4.50e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 5032159    495 GVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 533
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 58-82 6.30e-07

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 45.77  E-value: 6.30e-07
                          10        20
                  ....*....|....*....|....*
gi 5032159     58 EVNFLVYRYLQESGFSHSAFTFGIE 82
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 58-87 1.59e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 42.04  E-value: 1.59e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 5032159      58 EVNFLVYRYLQESGFSHSAFTFGIESHISQ 87
Cdd:smart00667   5 ELNRLILEYLLRNGYEETAETLQKESGLSL 34
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 507-577 7.50e-04

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: 42.27  E-value: 7.50e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5032159  507 PVYSVAfSPDGKYLA---SGSFDKCVHIWNTQSGNLVHSYRGTGGIFEVCWNARGDKVGASASDGS-VCVLDLRK 577
Cdd:cd20778 283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNkVVVYDTRT 356
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 227-533 1.04e-86

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: 270.75  E-value: 1.04e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  227 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENsnggstqlvlRHCIREGGHDVPsnkdVTSLDWNTNGTLLATG 306
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG----------ELLRTLKGHTGP----VRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  307 SYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQNNTTF 385
Cdd:cd00200  70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  386 -ASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWSP 464
Cdd:cd00200 150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5032159  465 tgpatsnpnSNIMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 533
Cdd:cd00200 230 ---------DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
225-576 4.35e-79

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 254.84  E-value: 4.35e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  225 ATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDvpsnKDVTSLDWNTNGTLLA 304
Cdd:COG2319  71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA----TGLLLRTLT------GHT----GAVRSVAFSPDGKTLA 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  305 TGSYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNN 382
Cdd:COG2319 137 SGSADGTVRLWdLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFsPDG 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  383 TTFASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKW 462
Cdd:COG2319 217 KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAF 296

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  463 SPTGPatsnpnsniMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHS 542
Cdd:COG2319 297 SPDGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367

                       330       340       350
                ....*....|....*....|....*....|....*
gi 5032159  543 YRG-TGGIFEVCWNARGDKVGASASDGSVCVLDLR 576
Cdd:COG2319 368 LTGhTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
225-536 7.32e-79

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 254.45  E-value: 7.32e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  225 ATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDvpsnKDVTSLDWNTNGTLLA 304
Cdd:COG2319 113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA----TGKLLRTLT------GHS----GAVTSVAFSPDGKLLA 178

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  305 TGSYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNN 382
Cdd:COG2319 179 SGSDDGTVRLWdLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFsPDG 258

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  383 TTFASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKW 462
Cdd:COG2319 259 RLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAF 338

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5032159  463 SPTGPatsnpnsniMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQS 536
Cdd:COG2319 339 SPDGK---------TLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 321-577 8.63e-61

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: 202.95  E-value: 8.63e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  321 LASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNNTTFASCSTDMCIHVCRL 399
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAsADGTYLASGSSDKTIRLWDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  400 GCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWSPTgpatsnpnsNIMLA 479
Cdd:cd00200  81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPD---------GTFVA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  480 SASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHSYRG-TGGIFEVCWNARG 558
Cdd:cd00200 152 SSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDG 231

                       250
                ....*....|....*....
gi 5032159  559 DKVGASASDGSVCVLDLRK 577
Cdd:cd00200 232 YLLASGSEDGTIRVWDLRT 250
WD40 COG2319
WD40 repeat [General function prediction only];
225-576 9.22e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 206.69  E-value: 9.22e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  225 ATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDVPsnkdVTSLDWNTNGTLLA 304
Cdd:COG2319  29 LLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAA----AGALLATLL------GHTAA----VLSVAFSPDGRLLA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  305 TGSYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGeakqqfpfhsapaldvdwqnnt 383
Cdd:COG2319  95 SASADGTVRLWdLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATG---------------------- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  384 tfascstdmcihvcrlgcdRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWS 463
Cdd:COG2319 153 -------------------KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFS 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  464 PTGPatsnpnsniMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHSY 543
Cdd:COG2319 214 PDGK---------LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTL 284

                       330       340       350
                ....*....|....*....|....*....|....
gi 5032159  544 RG-TGGIFEVCWNARGDKVGASASDGSVCVLDLR 576
Cdd:COG2319 285 TGhSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
WD40 COG2319
WD40 repeat [General function prediction only];
300-576 2.36e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.57  E-value: 2.36e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  300 GTLLATGSYDGFARIWT-EDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVD 378
Cdd:COG2319   6 GAALAAASADLALALLAaALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  379 WQ-NNTTFASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEI 457
Cdd:COG2319  86 FSpDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAV 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  458 YTIKWSPTGPatsnpnsniMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSG 537
Cdd:COG2319 166 TSVAFSPDGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG 236

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 5032159  538 NLVHSYRG-TGGIFEVCWNARGDKVgASAS-DGSVCVLDLR 576
Cdd:COG2319 237 KLLRTLTGhSGSVRSVAFSPDGRLL-ASGSaDGTVRLWDLA 276
PTZ00420 PTZ00420
coronin; Provisional
 404-493 1.26e-11

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 67.28  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   404 PVKTFQGHTNEVNAIKWDPS-GMLLASCSDDMTLKIWSMKQE----------VCIhdLQAHNKEIYTIKWsptgpatsNP 472
Cdd:PTZ00420  66 PVIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPHNdesvkeikdpQCI--LKGHKKKISIIDW--------NP 135

                         90       100
                 ....*....|....*....|.
gi 5032159   473 NSNIMLASASFDSTVRLWDIE 493
Cdd:PTZ00420 136 MNYYIMCSSGFDSFVNIWDIE 156
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 495-533 1.34e-10

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: 56.55  E-value: 1.34e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 5032159     495 GVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 533
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
 228-371 1.89e-10

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 63.43  E-value: 1.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   228 LRGHESEVFICAWNPV-SDLLASGSGDSTARIWNLNENSNgGSTQLVLRHCIREGghdvpSNKDVTSLDWN-TNGTLLAT 305
Cdd:PTZ00420  70 LKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPHNDE-SVKEIKDPQCILKG-----HKKKISIIDWNpMNYYIMCS 143

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5032159   306 GSYDGFARIW-TEDGNLASTLGQHKgPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHS 371
Cdd:PTZ00420 144 SGFDSFVNIWdIENEKRAFQINMPK-KLSSLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSFHIHD 209
WD40 pfam00400
WD domain, G-beta repeat;
495-533 4.50e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 4.50e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 5032159    495 GVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 533
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 403-440 8.05e-10

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: 54.24  E-value: 8.05e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 5032159     403 RPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWS 440
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
403-440 5.35e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 51.96  E-value: 5.35e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 5032159    403 RPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWS 440
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 410-542 6.56e-09

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 58.37  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   410 GHTNEVNAIKWDP-SGMLLASCSDDMTLKIWSMKQEVC-------IHDLQAHNKEIytikwsptGPATSNPNSNIMLASA 481
Cdd:PTZ00421  73 GQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGLtqnisdpIVHLQGHTKKV--------GIVSFHPSAMNVLASA 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5032159   482 SFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHS 542
Cdd:PTZ00421 145 GADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSS 205
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 58-82 6.30e-07

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 45.77  E-value: 6.30e-07
                          10        20
                  ....*....|....*....|....*
gi 5032159     58 EVNFLVYRYLQESGFSHSAFTFGIE 82
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 412-576 8.02e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 52.01  E-value: 8.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   412 TNEVNAIKWDPSGMLLASCSDDMTLKIWS----MKQEVCIH----DLQAHNKeIYTIKWsptgpatsnpNSNI--MLASA 481
Cdd:PLN00181 483 SNLVCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHypvvELASRSK-LSGICW----------NSYIksQVASS 551

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   482 SFDSTVRLWDIERGVCTHTLTKHQEPVYSVAF-SPDGKYLASGSFDKCVHIWNTQSGNLVHSYRGTGGIFEVCW-NARGD 559
Cdd:PLN00181 552 NFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFpSESGR 631

                        170
                 ....*....|....*..
gi 5032159   560 KVGASASDGSVCVLDLR 576
Cdd:PLN00181 632 SLAFGSADHKVYYYDLR 648
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 334-575 9.53e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 52.01  E-value: 9.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   334 ALKWNRKGNYILSAGVDKTTIIWDAHTgEAKQQFPFHSaPALDVD---------WQN--NTTFASCSTDMCIHVCRLGCD 402
Cdd:PLN00181 488 AIGFDRDGEFFATAGVNKKIKIFECES-IIKDGRDIHY-PVVELAsrsklsgicWNSyiKSQVASSNFEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   403 RPVKTFQGHTNEVNAIKW---DPSgmLLASCSDDMTLKIWSMKQEVCIHDLQAhNKEIYTIKW-SPTGPATS-------- 470
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYssaDPT--LLASGSDDGSVKLWSINQGVSIGTIKT-KANICCVQFpSESGRSLAfgsadhkv 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   471 ------NPN-------------------SNIMLASASFDSTVRLWDIERGVC------THTLTKHQEPVYSVAFSPDGKY 519
Cdd:PLN00181 643 yyydlrNPKlplctmighsktvsyvrfvDSSTLVSSSTDNTLKLWDLSMSISginetpLHSFMGHTNVKNFVGLSVSDGY 722

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   520 LASGSFDKCVHIWNTQSGNLVHSYR--------------GTGGIFEVCWNARGDKVGASASDGSVCVLDL 575
Cdd:PLN00181 723 IATGSETNEVFVYHKAFPMPVLSYKfktidpvsglevddASQFISSVCWRGQSSTLVAANSTGNIKILEM 792
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 227-260 2.68e-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: 44.23  E-value: 2.68e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 5032159     227 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWN 260
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
 335-543 2.88e-06

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


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 48.04  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159    335 LKWNRKGNYIL---SAGVDKTTIIWdahTGEakqqfpfhsapaldvdwqnnTTFASCSTDMcIHVCRLGCDRpvktfqgh 411
Cdd:pfam08662  11 LKWNKNGTYLLvltDTDVDKTGKSY---YGE--------------------TNLYLIGETG-GPDCVVELDK-------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159    412 TNEVNAIKWDPSGMLLASCSDDMTLKI--WSMKQEVcIHDLQAHNKEiyTIKWSPTGPatsnpnsniMLASASFDST--- 486
Cdd:pfam08662  59 EGPIHDVAWSPNGKEFAVIYGYMPAKVsfFDLKGNV-IHSFGEQPRN--TIFWSPFGR---------LVLLAGFGNLagd 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5032159    487 VRLWDIERGVCTHTlTKHQEPVYsVAFSPDGKYLASGS------FDKCVHIWnTQSGNLVHSY 543
Cdd:pfam08662 127 IEFWDVVNKKKIAT-AEASNATL-CEWSPDGRYFLTATtaprlrVDNGFKIW-HYNGALVYKY 186
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 446-491 3.97e-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: 43.84  E-value: 3.97e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 5032159     446 CIHDLQAHNKEIYTIKWSPTGPatsnpnsniMLASASFDSTVRLWD 491
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGK---------YLASGSDDGTIKLWD 40
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 58-87 1.59e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 42.04  E-value: 1.59e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 5032159      58 EVNFLVYRYLQESGFSHSAFTFGIESHISQ 87
Cdd:smart00667   5 ELNRLILEYLLRNGYEETAETLQKESGLSL 34
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 318-357 1.65e-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: 41.91  E-value: 1.65e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 5032159     318 DGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWD 357
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
226-260 1.81e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.95  E-value: 1.81e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 5032159    226 TVLRGHESEVFICAWNPVSDLLASGSGDSTARIWN 260
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
446-491 2.18e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.56  E-value: 2.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 5032159    446 CIHDLQAHNKEIYTIKWSPTGPatsnpnsniMLASASFDSTVRLWD 491
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGK---------LLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 222-385 3.63e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 46.42  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   222 SSKATVLRGHESEVFICAWNP-VSDLLASGSGDSTARIWNLNEnsnGGSTQLVLRHciregghdvpsNKDVTSLDWNTNG 300
Cdd:PTZ00421 115 SDPIVHLQGHTKKVGIVSFHPsAMNVLASAGADMVVNVWDVER---GKAVEVIKCH-----------SDQITSLEWNLDG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   301 TLLATGSYDGFARIWT-EDGNLASTLGQHKGPIFA-LKWNRKGNYILSAGVDKT----TIIWDAHTGEAkqqfPFHSapa 374
Cdd:PTZ00421 181 SLLCTTSKDKKLNIIDpRDGTIVSSVEAHASAKSQrCLWAKRKDLIITLGCSKSqqrqIMLWDTRKMAS----PYST--- 253

                        170
                 ....*....|.
gi 5032159   375 LDVDwQNNTTF 385
Cdd:PTZ00421 254 VDLD-QSSALF 263
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
452-575 9.93e-05

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 44.30  E-value: 9.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159  452 AHNKEIYTIK--WSPTGPATSnPNSNIMLASASFDSTVRLWDIERGVCTHTLTKHQEPvYSVAFSPDGKYL-----ASGS 524
Cdd:COG3391  98 ATGKVVATIPvgGGPRGLAVD-PDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGP-HGIAVDPDGKRLyvansGSNT 175

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5032159  525 FDKCVHIWNTQSGNLVHSYRGTGGIFEVCWNARGDKV--------GASASDGSVCVLDL 575
Cdd:COG3391 176 VSVIVSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLyvanrgsnTSNGGSNTVSVIDL 234
WD40 pfam00400
WD domain, G-beta repeat;
319-357 1.51e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 1.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 5032159    319 GNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWD 357
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 288-315 1.61e-04

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: 39.22  E-value: 1.61e-04
                           10        20
                   ....*....|....*....|....*...
gi 5032159     288 NKDVTSLDWNTNGTLLATGSYDGFARIW 315
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLW 39
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 414-521 1.67e-04

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 44.64  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   414 EVNAIKWDPSGMLLASCSDDMTLKIWSMK----QEVcihDLQAHNKEIYTIKWSPTGP--ATSNPNSNIMlasasfdSTV 487
Cdd:COG4946  390 RVFNPVWSPDGKKIAFTDNRGRLWVVDLAsgkvRKV---DTDGYGDGISDLAWSPDSKwlAYSKPGPNQL-------SQI 459

                         90       100       110
                 ....*....|....*....|....*....|....
gi 5032159   488 RLWDIERGVcTHTLTKHQEPVYSVAFSPDGKYLA 521
Cdd:COG4946  460 FLYDVETGK-TVQLTDGRYDDGSPAFSPDGKYLY 492
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 239-338 2.79e-04

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: 39.95  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159    239 AWNPVSDLLASGSGD--------STARIWNLNENSNGGStqlvlrhciregghdvpsnkdVTSLDWNTNGTLLATGSYDG 310
Cdd:pfam12894   2 SWCPTMDLIALATEDgelllhrlNWQRVWTLSPDKEDLE---------------------VTSLAWRPDGKLLAVGYSDG 60

                          90       100
                  ....*....|....*....|....*....
gi 5032159    311 FARIW-TEDGNLASTLGQHKGPIFALKWN 338
Cdd:pfam12894  61 TVRLLdAENGKIVHHFSAGSDLITCLGWG 89
WD40 pfam00400
WD domain, G-beta repeat;
288-315 3.16e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 3.16e-04
                          10        20
                  ....*....|....*....|....*...
gi 5032159    288 NKDVTSLDWNTNGTLLATGSYDGFARIW 315
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVW 38
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 507-577 7.50e-04

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: 42.27  E-value: 7.50e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5032159  507 PVYSVAfSPDGKYLA---SGSFDKCVHIWNTQSGNLVHSYRGTGGIFEVCWNARGDKVGASASDGS-VCVLDLRK 577
Cdd:cd20778 283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNkVVVYDTRT 356
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 389-463 9.65e-04

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: 38.41  E-value: 9.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5032159    389 STDMCIHVCRLGCDRPVKTFQ-GHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWS 463
Cdd:pfam12894  14 TEDGELLLHRLNWQRVWTLSPdKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
PTZ00420 PTZ00420
coronin; Provisional
 227-357 1.04e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 41.86  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159   227 VLRGHESEVFICAWNPVSDLLASGSG-DSTARIWNL-NENSnggSTQLVLrhciregghdvpsNKDVTSLDWNTNGTLLa 304
Cdd:PTZ00420 120 ILKGHKKKISIIDWNPMNYYIMCSSGfDSFVNIWDIeNEKR---AFQINM-------------PKKLSSLKWNIKGNLL- 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5032159   305 TGSYDG--FARIWTEDGNLASTLGQHKGP-----IFALKWNRKGNYILSAGVDKTTI----IWD 357
Cdd:PTZ00420 183 SGTCVGkhMHIIDPRKQEIASSFHIHDGGkntknIWIDGLGGDDNYILSTGFSKNNMremkLWD 246
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 488-555 2.24e-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: 37.64  E-value: 2.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5032159    488 RLWDIergvcthTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHSYR-GTGGIFEVCWN 555
Cdd:pfam12894  28 RVWTL-------SPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSaGSDLITCLGWG 89
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 294-382 7.96e-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: 36.10  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032159    294 LDWNTNGTLLATGSYDG--------FARIWTEDGnlastlGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQ 365
Cdd:pfam12894   1 MSWCPTMDLIALATEDGelllhrlnWQRVWTLSP------DKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVH 74

                          90
                  ....*....|....*..
gi 5032159    366 QFPFHSAPALDVDWQNN 382
Cdd:pfam12894  75 HFSAGSDLITCLGWGEN 91
 
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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