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Conserved domains on  [gi|19913371|ref|NP_078941|]
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F-box-like/WD repeat-containing protein TBL1XR1 isoform 1 [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 ...
 164-470 1.68e-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: 268.05  E-value: 1.68e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 164 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSENstsgstQLVLRHCIREGGqdvpsnkdVTSLDWNSEGTLLATG 243
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG------ELLRTLKGHTGP--------VRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 244 SYDGFARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNNTF 322
Cdd:cd00200  70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 323 -ASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAHNKEIYTIKWSP 401
Cdd:cd00200 150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19913371 402 TGpgtnnpnanLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 470
Cdd:cd00200 230 DG---------YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.63e-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: 5.63e-07
                          10        20
                  ....*....|....*....|....*
gi 19913371     7 EVNFLVYRYLQESGFSHSAFTFGIE 31
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; ...
 444-514 4.61e-03

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: 39.19  E-value: 4.61e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19913371 444 PVYSVAfSPDGRYLA---SGSFDKCVHIWNTQTGALVHSYRGTGGIFEVCWNAAGDKVGASASDGS-VCVLDLRK 514
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 ...
 164-470 1.68e-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: 268.05  E-value: 1.68e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 164 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSENstsgstQLVLRHCIREGGqdvpsnkdVTSLDWNSEGTLLATG 243
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG------ELLRTLKGHTGP--------VRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 244 SYDGFARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNNTF 322
Cdd:cd00200  70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 323 -ASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAHNKEIYTIKWSP 401
Cdd:cd00200 150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19913371 402 TGpgtnnpnanLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 470
Cdd:cd00200 230 DG---------YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
164-513 1.33e-80

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 256.76  E-value: 1.33e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 164 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSensTSGSTQLVLRHcireggqdvpsNKDVTSLDWNSEGTLLATG 243
Cdd:COG2319  73 TLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA---TGLLLRTLTGH-----------TGAVRSVAFSPDGKTLASG 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 244 SYDGFARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSN-NT 321
Cdd:COG2319 139 SADGTVRLWdLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgKL 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 322 FASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAHNKEIYTIKWSP 401
Cdd:COG2319 219 LASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP 298

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 402 TGPgtnnpnanlMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHSYR 481
Cdd:COG2319 299 DGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLT 369

                       330       340       350
                ....*....|....*....|....*....|...
gi 19913371 482 G-TGGIFEVCWNAAGDKVGASASDGSVCVLDLR 513
Cdd:COG2319 370 GhTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 432-470 6.93e-11

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: 56.94  E-value: 6.93e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 19913371    432 GICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 470
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
 286-479 1.62e-10

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 63.37  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  286 VDKTTIIWD-AHTGEAKQQFpfhsapaLDVDWQSNNTFASCSTDMCihvCKLGQDRPIktFQGHTNEVNAIKWDPTGNL- 363
Cdd:PTZ00421  23 VTPSTALWDcSNTIACNDRF-------IAVPWQQLGSTAVLKHTDY---GKLASNPPI--LLGQEGPIIDVAFNPFDPQk 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  364 LASCSDDMTLKIWSMKQ--------DNCVHdLQAHNKEIYTIKWsptgpgtnNPNANLMLASASFDSTVRLWDVDRGICI 435
Cdd:PTZ00421  91 LFTASEDGTIMGWGIPEegltqnisDPIVH-LQGHTKKVGIVSF--------HPSAMNVLASAGADMVVNVWDVERGKAV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19913371  436 HTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHS 479
Cdd:PTZ00421 162 EVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSS 205
WD40 pfam00400
WD domain, G-beta repeat;
432-470 3.82e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 3.82e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 19913371   432 GICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 470
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.63e-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: 5.63e-07
                          10        20
                  ....*....|....*....|....*
gi 19913371     7 EVNFLVYRYLQESGFSHSAFTFGIE 31
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 3-36 5.97e-06

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: 42.81  E-value: 5.97e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 19913371      3 ISSDEVNFLVYRYLQESGFSHSAFTFGIESHISQ 36
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 444-514 4.61e-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: 39.19  E-value: 4.61e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19913371 444 PVYSVAfSPDGRYLA---SGSFDKCVHIWNTQTGALVHSYRGTGGIFEVCWNAAGDKVGASASDGS-VCVLDLRK 514
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 ...
 164-470 1.68e-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: 268.05  E-value: 1.68e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 164 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSENstsgstQLVLRHCIREGGqdvpsnkdVTSLDWNSEGTLLATG 243
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG------ELLRTLKGHTGP--------VRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 244 SYDGFARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNNTF 322
Cdd:cd00200  70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 323 -ASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAHNKEIYTIKWSP 401
Cdd:cd00200 150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19913371 402 TGpgtnnpnanLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 470
Cdd:cd00200 230 DG---------YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
164-513 1.33e-80

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 256.76  E-value: 1.33e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 164 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSensTSGSTQLVLRHcireggqdvpsNKDVTSLDWNSEGTLLATG 243
Cdd:COG2319  73 TLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA---TGLLLRTLTGH-----------TGAVRSVAFSPDGKTLASG 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 244 SYDGFARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSN-NT 321
Cdd:COG2319 139 SADGTVRLWdLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgKL 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 322 FASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAHNKEIYTIKWSP 401
Cdd:COG2319 219 LASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP 298

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 402 TGPgtnnpnanlMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHSYR 481
Cdd:COG2319 299 DGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLT 369

                       330       340       350
                ....*....|....*....|....*....|...
gi 19913371 482 G-TGGIFEVCWNAAGDKVGASASDGSVCVLDLR 513
Cdd:COG2319 370 GhTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
162-473 4.81e-79

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 252.91  E-value: 4.81e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 162 AVVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLsensTSGSTQLVLRHcireggqdvpSNKDVTSLDWNSEGTLLA 241
Cdd:COG2319 113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDL----ATGKLLRTLTG----------HSGAVTSVAFSPDGKLLA 178

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 242 TGSYDGFARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNN 320
Cdd:COG2319 179 SGSDDGTVRLWdLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDG 258

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 321 -TFASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAHNKEIYTIKW 399
Cdd:COG2319 259 rLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAF 338

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19913371 400 SPTGPgtnnpnanlMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQT 473
Cdd:COG2319 339 SPDGK---------TLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 258-514 2.18e-63

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: 208.34  E-value: 2.18e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 258 LASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNNTF-ASCSTDMCIHVCKL 336
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYlASGSSDKTIRLWDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 337 GQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAHNKEIYTIKWSPTgpgtnnpnaNLMLA 416
Cdd:cd00200  81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPD---------GTFVA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 417 SASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHSYRG-TGGIFEVCWNAAG 495
Cdd:cd00200 152 SSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDG 231

                       250
                ....*....|....*....
gi 19913371 496 DKVGASASDGSVCVLDLRK 514
Cdd:cd00200 232 YLLASGSEDGTIRVWDLRT 250
WD40 COG2319
WD40 repeat [General function prediction only];
151-513 8.97e-63

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 210.54  E-value: 8.97e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 151 VDGDVEIPPNKAVVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSEnstsgstqlvlrhcIREGGQDVPSNKDVTS 230
Cdd:COG2319  18 LALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAA--------------GALLATLLGHTAAVLS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 231 LDWNSEGTLLATGSYDGFARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGeakqqfpfhsa 309
Cdd:COG2319  84 VAFSPDGRLLASASADGTVRLWdLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATG----------- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 310 paldvdwqsnntfascstdmcihvcklgqdRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQA 389
Cdd:COG2319 153 ------------------------------KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 390 HNKEIYTIKWSPTGPgtnnpnanlMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIW 469
Cdd:COG2319 203 HTGAVRSVAFSPDGK---------LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 19913371 470 NTQTGALVHSYRG-TGGIFEVCWNAAGDKVGASASDGSVCVLDLR 513
Cdd:COG2319 274 DLATGELLRTLTGhSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
WD40 COG2319
WD40 repeat [General function prediction only];
238-513 1.37e-52

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 183.19  E-value: 1.37e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 238 TLLATGSYDGFARIWTKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQ 317
Cdd:COG2319   8 ALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFS 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 318 SN-NTFASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAHNKEIYT 396
Cdd:COG2319  88 PDgRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTS 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 397 IKWSPTGpgtnnpnanLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGAL 476
Cdd:COG2319 168 VAFSPDG---------KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKL 238

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 19913371 477 VHSYRG-TGGIFEVCWNAAGDKVgASAS-DGSVCVLDLR 513
Cdd:COG2319 239 LRTLTGhSGSVRSVAFSPDGRLL-ASGSaDGTVRLWDLA 276
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 432-470 6.93e-11

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: 56.94  E-value: 6.93e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 19913371    432 GICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 470
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
 286-479 1.62e-10

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 63.37  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  286 VDKTTIIWD-AHTGEAKQQFpfhsapaLDVDWQSNNTFASCSTDMCihvCKLGQDRPIktFQGHTNEVNAIKWDPTGNL- 363
Cdd:PTZ00421  23 VTPSTALWDcSNTIACNDRF-------IAVPWQQLGSTAVLKHTDY---GKLASNPPI--LLGQEGPIIDVAFNPFDPQk 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  364 LASCSDDMTLKIWSMKQ--------DNCVHdLQAHNKEIYTIKWsptgpgtnNPNANLMLASASFDSTVRLWDVDRGICI 435
Cdd:PTZ00421  91 LFTASEDGTIMGWGIPEegltqnisDPIVH-LQGHTKKVGIVSF--------HPSAMNVLASAGADMVVNVWDVERGKAV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19913371  436 HTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHS 479
Cdd:PTZ00421 162 EVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSS 205
PTZ00420 PTZ00420
coronin; Provisional
 158-308 2.33e-10

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 63.05  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  158 PPnkAVVLRGHESEVFICAWNPV-SDLLASGSGDSTARIWNLSENSTSgSTQLVLRHCIREGGQdvpsnKDVTSLDWNSE 236
Cdd:PTZ00420  65 PP--VIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPHNDES-VKEIKDPQCILKGHK-----KKISIIDWNPM 136

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19913371  237 GT-LLATGSYDGFARIWTKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHS 308
Cdd:PTZ00420 137 NYyIMCSSGFDSFVNIWDIENEKRAFQINMPKKLSSLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSFHIHD 209
WD40 pfam00400
WD domain, G-beta repeat;
432-470 3.82e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 3.82e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 19913371   432 GICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 470
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 340-377 3.99e-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: 55.01  E-value: 3.99e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 19913371    340 RPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWS 377
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
 341-430 4.93e-10

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 61.89  E-value: 4.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  341 PIKTFQGHTNEVNAIKWDPT-GNLLASCSDDMTLKIWSMKQDN----------CVhdLQAHNKEIYTIKWsptgpgtnNP 409
Cdd:PTZ00420  66 PVIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPHNDesvkeikdpqCI--LKGHKKKISIIDW--------NP 135

                         90       100
                 ....*....|....*....|.
gi 19913371  410 NANLMLASASFDSTVRLWDVD 430
Cdd:PTZ00420 136 MNYYIMCSSGFDSFVNIWDIE 156
WD40 pfam00400
WD domain, G-beta repeat;
340-377 2.40e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 52.73  E-value: 2.40e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 19913371   340 RPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWS 377
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 349-513 3.06e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 56.25  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  349 TNEVNAIKWDPTGNLLASCSDDMTLKIW---SMKQDNcvHDLQ------AHNKEIYTIKWsptgpgtnNPNANLMLASAS 419
Cdd:PLN00181 483 SNLVCAIGFDRDGEFFATAGVNKKIKIFeceSIIKDG--RDIHypvvelASRSKLSGICW--------NSYIKSQVASSN 552

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  420 FDSTVRLWDVDRGICIHTLTKHQEPVYSVAF-SPDGRYLASGSFDKCVHIWNTQTGALVHSYRGTGGIFEVCW-NAAGDK 497
Cdd:PLN00181 553 FEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFpSESGRS 632

                        170
                 ....*....|....*.
gi 19913371  498 VGASASDGSVCVLDLR 513
Cdd:PLN00181 633 LAFGSADHKVYYYDLR 648
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
 272-480 5.63e-08

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


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 53.05  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371   272 LKWNKKGNFIL---SAGVDKTTIIWdahTGEakqqfpfhsapaldvdwqsNNTFASCSTDMCIHVCKLGQDRPIKtfqgh 348
Cdd:pfam08662  11 LKWNKNGTYLLvltDTDVDKTGKSY---YGE-------------------TNLYLIGETGGPDCVVELDKEGPIH----- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371   349 tnevnAIKWDPTGNLLASCSDDMTLKIwSM--KQDNCVHDLQAHNKEiyTIKWSPTGPgtnnpnanlMLASASFDST--- 423
Cdd:pfam08662  64 -----DVAWSPNGKEFAVIYGYMPAKV-SFfdLKGNVIHSFGEQPRN--TIFWSPFGR---------LVLLAGFGNLagd 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19913371   424 VRLWDVDRGICIHTlTKHQEPVYsVAFSPDGRYLASGS------FDKCVHIWnTQTGALVHSY 480
Cdd:pfam08662 127 IEFWDVVNKKKIAT-AEASNATL-CEWSPDGRYFLTATtaprlrVDNGFKIW-HYNGALVYKY 186
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 271-512 1.78e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 53.94  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  271 ALKWNKKGNFILSAGVDKTTIIWDAHTgEAKQQFPFHSaPALDVD---------WQS--NNTFASCSTDMCIHVCKLGQD 339
Cdd:PLN00181 488 AIGFDRDGEFFATAGVNKKIKIFECES-IIKDGRDIHY-PVVELAsrsklsgicWNSyiKSQVASSNFEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  340 RPIKTFQGHTNEVNAIKW---DPTgnLLASCSDDMTLKIWSMKQDNCVHDLQAhNKEIYTIKWsPTGPGTN--------- 407
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYssaDPT--LLASGSDDGSVKLWSINQGVSIGTIKT-KANICCVQF-PSESGRSlafgsadhk 641

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  408 -------NPNANL-------------------MLASASFDSTVRLWDVDRGIC------IHTLTKHQEPVYSVAFSPDGR 455
Cdd:PLN00181 642 vyyydlrNPKLPLctmighsktvsyvrfvdssTLVSSSTDNTLKLWDLSMSISginetpLHSFMGHTNVKNFVGLSVSDG 721

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19913371  456 YLASGSFDKCVHIWNTQTGALVHSYR--------------GTGGIFEVCWNAAGDKVGASASDGSVCVLDL 512
Cdd:PLN00181 722 YIATGSETNEVFVYHKAFPMPVLSYKfktidpvsglevddASQFISSVCWRGQSSTLVAANSTGNIKILEM 792
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.63e-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: 5.63e-07
                          10        20
                  ....*....|....*....|....*
gi 19913371     7 EVNFLVYRYLQESGFSHSAFTFGIE 31
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
PTZ00421 PTZ00421
coronin; Provisional
 163-322 2.11e-06

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 50.28  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  163 VVLRGHESEVFICAWNP-VSDLLASGSGDSTARIWNLsENSTSGSTqlvlrhcireggqdVPSNKD-VTSLDWNSEGTLL 240
Cdd:PTZ00421 119 VHLQGHTKKVGIVSFHPsAMNVLASAGADMVVNVWDV-ERGKAVEV--------------IKCHSDqITSLEWNLDGSLL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  241 ATGSYDGFARIW-TKDGNLASTLGQHKGPIFA-LKWNKKGNFILSAGVDKT----TIIWDAHTGEAkqqfPFHSapaLDV 314
Cdd:PTZ00421 184 CTTSKDKKLNIIdPRDGTIVSSVEAHASAKSQrCLWAKRKDLIITLGCSKSqqrqIMLWDTRKMAS----PYST---VDL 256


                 ....*...
gi 19913371  315 DwQSNNTF 322
Cdd:PTZ00421 257 D-QSSALF 263
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 164-197 2.56e-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: 2.56e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 19913371    164 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWN 197
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 382-428 2.93e-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: 2.93e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 19913371    382 NCVHDLQAHNKEIYTIKWSPTGPgtnnpnanlMLASASFDSTVRLWD 428
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGK---------YLASGSDDGTIKLWD 40
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 3-36 5.97e-06

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: 42.81  E-value: 5.97e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 19913371      3 ISSDEVNFLVYRYLQESGFSHSAFTFGIESHISQ 36
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
WD40 pfam00400
WD domain, G-beta repeat;
382-428 1.88e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.56  E-value: 1.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 19913371   382 NCVHDLQAHNKEIYTIKWSPTGPgtnnpnanlMLASASFDSTVRLWD 428
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGK---------LLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
164-197 1.94e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.56  E-value: 1.94e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 19913371   164 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWN 197
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 255-294 1.95e-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: 1.95e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 19913371    255 DGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWD 294
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 231-319 5.58e-05

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: 41.88  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371   231 LDWNSEGTLLATGSYDG--------FARIWTKDGnlastlGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQ 302
Cdd:pfam12894   1 MSWCPTMDLIALATEDGelllhrlnWQRVWTLSP------DKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVH 74

                          90
                  ....*....|....*..
gi 19913371   303 QFPFHSAPALDVDWQSN 319
Cdd:pfam12894  75 HFSAGSDLITCLGWGEN 91
WD40 pfam00400
WD domain, G-beta repeat;
256-294 1.20e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 19913371   256 GNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWD 294
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 225-252 2.64e-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: 38.45  E-value: 2.64e-04
                           10        20
                   ....*....|....*....|....*...
gi 19913371    225 NKDVTSLDWNSEGTLLATGSYDGFARIW 252
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLW 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 355-451 2.77e-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: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371   355 IKWDPTGNLLASCSDDMTL--------KIWSMKQDNcvhdlqaHNKEIYTIKWSPTGPgtnnpnanlMLASASFDSTVRL 426
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELllhrlnwqRVWTLSPDK-------EDLEVTSLAWRPDGK---------LLAVGYSDGTVRL 64

                          90       100
                  ....*....|....*....|....*
gi 19913371   427 WDVDRGICIHTLTKHQEPVYSVAFS 451
Cdd:pfam12894  65 LDAENGKIVHHFSAGSDLITCLGWG 89
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 351-458 3.39e-04

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 43.49  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  351 EVNAIKWDPTGNLLASCSDDMTLKiwsmkqdncVHDL----------QAHNKEIYTIKWSPTG-------PGTNNPNAnl 413
Cdd:COG4946  390 RVFNPVWSPDGKKIAFTDNRGRLW---------VVDLasgkvrkvdtDGYGDGISDLAWSPDSkwlayskPGPNQLSQ-- 458

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 19913371  414 mlasasfdstVRLWDVDRGIcIHTLTKHQEPVYSVAFSPDGRYLA 458
Cdd:COG4946  459 ----------IFLYDVETGK-TVQLTDGRYDDGSPAFSPDGKYLY 492
WD40 pfam00400
WD domain, G-beta repeat;
225-252 4.42e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 4.42e-04
                          10        20
                  ....*....|....*....|....*...
gi 19913371   225 NKDVTSLDWNSEGTLLATGSYDGFARIW 252
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVW 38
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
408-512 5.26e-04

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 41.60  E-value: 5.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 408 NPNANLMLASASFDSTVRLWDVDRGICIHTLTKHQEPvYSVAFSPDGRYL-----ASGSFDKCVHIWNTQTGALVHSYRG 482
Cdd:COG3391 118 DPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGP-HGIAVDPDGKRLyvansGSNTVSVIVSVIDTATGKVVATIPV 196

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 19913371 483 TGGIFEVCWNAAGDKV--------GASASDGSVCVLDL 512
Cdd:COG3391 197 GGGPVGVAVSPDGRRLyvanrgsnTSNGGSNTVSVIDL 234
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 326-400 1.40e-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: 38.03  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371   326 STDMCIHVCKL-GQdrpiKTFQG----HTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAHNKEIYTIKWS 400
Cdd:pfam12894  14 TEDGELLLHRLnWQ----RVWTLspdkEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
PTZ00421 PTZ00421
coronin; Provisional
 256-390 3.05e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 40.26  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371  256 GNLAST----LGQhKGPIFALKWNKKGNFIL-SAGVDKTTIIWDAHTGEAKQQFpfhSAPALDVDWQS------------ 318
Cdd:PTZ00421  62 GKLASNppilLGQ-EGPIIDVAFNPFDPQKLfTASEDGTIMGWGIPEEGLTQNI---SDPIVHLQGHTkkvgivsfhpsa 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19913371  319 NNTFASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAH 390
Cdd:PTZ00421 138 MNVLASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAH 209
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 444-514 4.61e-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: 39.19  E-value: 4.61e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19913371 444 PVYSVAfSPDGRYLA---SGSFDKCVHIWNTQTGALVHSYRGTGGIFEVCWNAAGDKVGASASDGS-VCVLDLRK 514
Cdd:cd20778 283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNkVVVYDTRT 356
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
399-510 5.27e-03

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 38.52  E-value: 5.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913371 399 WSPTGPGTNNPNANLMLASASFDSTVRLWDVDRGICIHTLTKHQEPvYSVAFSPDGRYL-ASGSFDKCVHIWNTQTGALV 477
Cdd:COG3391  67 VADADGADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGGP-RGLAVDPDGGRLyVADSGNGRVSVIDTATGKVV 145

                        90       100       110
                ....*....|....*....|....*....|....
gi 19913371 478 HSYRGTGGIFEVCWNAAGDKV-GASASDGSVCVL 510
Cdd:COG3391 146 ATIPVGAGPHGIAVDPDGKRLyVANSGSNTVSVI 179
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 409-469 6.98e-03

Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.


Pssm-ID: 466575 [Multi-domain]  Cd Length: 350  Bit Score: 38.90  E-value: 6.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19913371   409 PNANLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIW 469
Cdd:pfam20426  91 PSENFLISCGNWENSFQVISLNDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVW 151
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 425-492 8.14e-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: 8.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19913371   425 RLWDVDrgicihtLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHSYR-GTGGIFEVCWN 492
Cdd:pfam12894  28 RVWTLS-------PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSaGSDLITCLGWG 89
 
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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