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Conserved domains on  [gi|1694593143|ref|XP_029472675|]
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F-box-like/WD repeat-containing protein TBL1XR1 isoform X1 [Rhinatrema bivittatum]

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 ...
 166-472 1.16e-87

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: 272.29  E-value: 1.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 166 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSENsssgstQLVLRHCIREGGqdvpsnkdVTSLDWNSEGTLLATG 245
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG------ELLRTLKGHTGP--------VRDVAASADGTYLASG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 246 SYDGYARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNNTF 324
Cdd:cd00200    70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 325 -ASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDSCVHDLQAHNKEIYTIKWSP 403
Cdd:cd00200   150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1694593143 404 TGpgtnnpnanLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 472
Cdd:cd00200   230 DG---------YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.98e-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: 5.98e-07
                          10        20
                  ....*....|....*....|....*
gi 1694593143   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; ...
 446-511 4.52e-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: 39.57  E-value: 4.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1694593143 446 PVYSVAfSPDGRYLA---SGSFDKCVHIWNTQTGALVHSYRGTGGIFEVCWNAGGDKVGASASDGSKIY 511
Cdd:cd20778   283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNKVV 350
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 166-472 1.16e-87

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: 272.29  E-value: 1.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 166 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSENsssgstQLVLRHCIREGGqdvpsnkdVTSLDWNSEGTLLATG 245
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG------ELLRTLKGHTGP--------VRDVAASADGTYLASG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 246 SYDGYARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNNTF 324
Cdd:cd00200    70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 325 -ASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDSCVHDLQAHNKEIYTIKWSP 403
Cdd:cd00200   150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1694593143 404 TGpgtnnpnanLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 472
Cdd:cd00200   230 DG---------YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
164-475 9.59e-81

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 258.30  E-value: 9.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 164 AVVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSenssSGSTQLVLRHcireggqdvpSNKDVTSLDWNSEGTLLA 243
Cdd:COG2319   113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA----TGKLLRTLTG----------HSGAVTSVAFSPDGKLLA 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 244 TGSYDGYARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNN 322
Cdd:COG2319   179 SGSDDGTVRLWdLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDG 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 323 -TFASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDSCVHDLQAHNKEIYTIKW 401
Cdd:COG2319   259 rLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAF 338

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1694593143 402 SPTGPgtnnpnanlMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQT 475
Cdd:COG2319   339 SPDGK---------TLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 434-472 3.83e-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: 57.71  E-value: 3.83e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1694593143  434 GICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 472
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
434-472 2.22e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.81  E-value: 2.22e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1694593143 434 GICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 472
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 288-481 6.52e-10

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 61.45  E-value: 6.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 288 VDKTTIIWD-AHTGEAKQQFpfhsapaLDVDWQSNNTFASCSTDMCihvCKLGQDRPIktFQGHTNEVNAIKWDPTGNL- 365
Cdd:PTZ00421   23 VTPSTALWDcSNTIACNDRF-------IAVPWQQLGSTAVLKHTDY---GKLASNPPI--LLGQEGPIIDVAFNPFDPQk 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 366 LASCSDDMTLKIWSMKQ--------DSCVHdLQAHNKEIYTIKWsptgpgtnNPNANLMLASASFDSTVRLWDVDRGICI 437
Cdd:PTZ00421   91 LFTASEDGTIMGWGIPEegltqnisDPIVH-LQGHTKKVGIVSF--------HPSAMNVLASAGADMVVNVWDVERGKAV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1694593143 438 HTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHS 481
Cdd:PTZ00421  162 EVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSS 205
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.98e-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: 5.98e-07
                          10        20
                  ....*....|....*....|....*
gi 1694593143   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 6.34e-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: 6.34e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1694593143    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; ...
 446-511 4.52e-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: 39.57  E-value: 4.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1694593143 446 PVYSVAfSPDGRYLA---SGSFDKCVHIWNTQTGALVHSYRGTGGIFEVCWNAGGDKVGASASDGSKIY 511
Cdd:cd20778   283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNKVV 350
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 166-472 1.16e-87

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: 272.29  E-value: 1.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 166 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSENsssgstQLVLRHCIREGGqdvpsnkdVTSLDWNSEGTLLATG 245
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG------ELLRTLKGHTGP--------VRDVAASADGTYLASG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 246 SYDGYARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNNTF 324
Cdd:cd00200    70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 325 -ASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDSCVHDLQAHNKEIYTIKWSP 403
Cdd:cd00200   150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1694593143 404 TGpgtnnpnanLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 472
Cdd:cd00200   230 DG---------YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
164-475 9.59e-81

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 258.30  E-value: 9.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 164 AVVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSenssSGSTQLVLRHcireggqdvpSNKDVTSLDWNSEGTLLA 243
Cdd:COG2319   113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA----TGKLLRTLTG----------HSGAVTSVAFSPDGKLLA 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 244 TGSYDGYARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNN 322
Cdd:COG2319   179 SGSDDGTVRLWdLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDG 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 323 -TFASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDSCVHDLQAHNKEIYTIKW 401
Cdd:COG2319   259 rLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAF 338

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1694593143 402 SPTGPgtnnpnanlMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQT 475
Cdd:COG2319   339 SPDGK---------TLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
166-510 2.90e-80

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 257.15  E-value: 2.90e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 166 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSENsssgstqlvlrhciREGGQDVPSNKDVTSLDWNSEGTLLATG 245
Cdd:COG2319    73 TLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG--------------LLLRTLTGHTGAVRSVAFSPDGKTLASG 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 246 SYDGYARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSN-NT 323
Cdd:COG2319   139 SADGTVRLWdLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgKL 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 324 FASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDSCVHDLQAHNKEIYTIKWSP 403
Cdd:COG2319   219 LASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 404 TGPgtnnpnanlMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHSYR 483
Cdd:COG2319   299 DGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLT 369

                         330       340
                  ....*....|....*....|....*...
gi 1694593143 484 G-TGGIFEVCWNAGGDKVgASASDGSKI 510
Cdd:COG2319   370 GhTGAVTSVAFSPDGRTL-ASGSADGTV 396
WD40 COG2319
WD40 repeat [General function prediction only];
153-510 8.02e-63

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 211.31  E-value: 8.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 153 VDGDVEIPPNKAVVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSEnsssgstqlvlrhcIREGGQDVPSNKDVTS 232
Cdd:COG2319    18 LALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAA--------------GALLATLLGHTAAVLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 233 LDWNSEGTLLATGSYDGYARIW-TKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGeakqqfpfhsa 311
Cdd:COG2319    84 VAFSPDGRLLASASADGTVRLWdLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATG----------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 312 paldvdwqsnntfascstdmcihvcklgqdRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDSCVHDLQA 391
Cdd:COG2319   153 ------------------------------KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 392 HNKEIYTIKWSPTGPgtnnpnanlMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIW 471
Cdd:COG2319   203 HTGAVRSVAFSPDGK---------LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1694593143 472 NTQTGALVHSYRG-TGGIFEVCWNAGGDKVgASASDGSKI 510
Cdd:COG2319   274 DLATGELLRTLTGhSGGVNSVAFSPDGKLL-ASGSDDGTV 312
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 260-511 8.44e-62

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: 204.88  E-value: 8.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 260 LASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNNTF-ASCSTDMCIHVCKL 338
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYlASGSSDKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 339 GQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDSCVHDLQAHNKEIYTIKWSPTgpgtnnpnaNLMLA 418
Cdd:cd00200    81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPD---------GTFVA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 419 SASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHSYRG-TGGIFEVCWNAGG 497
Cdd:cd00200   152 SSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDG 231

                         250
                  ....*....|....
gi 1694593143 498 DKVgASASDGSKIY 511
Cdd:cd00200   232 YLL-ASGSEDGTIR 244
WD40 COG2319
WD40 repeat [General function prediction only];
239-510 1.80e-52

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 183.96  E-value: 1.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 239 GTLLATGSYDGYARIWT-KDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVD 317
Cdd:COG2319     6 GAALAAASADLALALLAaALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 318 WQSN-NTFASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDSCVHDLQAHNKEI 396
Cdd:COG2319    86 FSPDgRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 397 YTIKWSPTGpgtnnpnanLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTG 476
Cdd:COG2319   166 TSVAFSPDG---------KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG 236

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1694593143 477 ALVHSYRG-TGGIFEVCWNAGGDKVgASASDGSKI 510
Cdd:COG2319   237 KLLRTLTGhSGSVRSVAFSPDGRLL-ASGSADGTV 270
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 434-472 3.83e-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: 57.71  E-value: 3.83e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1694593143  434 GICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 472
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
434-472 2.22e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.81  E-value: 2.22e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1694593143 434 GICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWN 472
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 342-379 2.34e-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: 55.78  E-value: 2.34e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1694593143  342 RPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWS 379
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
 288-481 6.52e-10

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 61.45  E-value: 6.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 288 VDKTTIIWD-AHTGEAKQQFpfhsapaLDVDWQSNNTFASCSTDMCihvCKLGQDRPIktFQGHTNEVNAIKWDPTGNL- 365
Cdd:PTZ00421   23 VTPSTALWDcSNTIACNDRF-------IAVPWQQLGSTAVLKHTDY---GKLASNPPI--LLGQEGPIIDVAFNPFDPQk 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 366 LASCSDDMTLKIWSMKQ--------DSCVHdLQAHNKEIYTIKWsptgpgtnNPNANLMLASASFDSTVRLWDVDRGICI 437
Cdd:PTZ00421   91 LFTASEDGTIMGWGIPEegltqnisDPIVH-LQGHTKKVGIVSF--------HPSAMNVLASAGADMVVNVWDVERGKAV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1694593143 438 HTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHS 481
Cdd:PTZ00421  162 EVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSS 205
PTZ00420 PTZ00420
coronin; Provisional
 343-432 7.10e-10

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 61.50  E-value: 7.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 343 PIKTFQGHTNEVNAIKWDPT-GNLLASCSDDMTLKIWSMK-QDSCVHD-------LQAHNKEIYTIKWsptgpgtnNPNA 413
Cdd:PTZ00420   66 PVIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPhNDESVKEikdpqciLKGHKKKISIIDW--------NPMN 137

                          90
                  ....*....|....*....
gi 1694593143 414 NLMLASASFDSTVRLWDVD 432
Cdd:PTZ00420  138 YYIMCSSGFDSFVNIWDIE 156
PTZ00420 PTZ00420
coronin; Provisional
 160-310 8.83e-10

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 61.12  E-value: 8.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 160 PPnkAVVLRGHESEVFICAWNPV-SDLLASGSGDSTARIWNLSENSSSgSTQLVLRHCIREGGQdvpsnKDVTSLDWNSE 238
Cdd:PTZ00420   65 PP--VIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPHNDES-VKEIKDPQCILKGHK-----KKISIIDWNPM 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1694593143 239 GT-LLATGSYDGYARIWTKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHS 310
Cdd:PTZ00420  137 NYyIMCSSGFDSFVNIWDIENEKRAFQINMPKKLSSLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSFHIHD 209
WD40 pfam00400
WD domain, G-beta repeat;
342-379 1.42e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.50  E-value: 1.42e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1694593143 342 RPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWS 379
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
 274-482 1.24e-07

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


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 51.89  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 274 LKWNKKGNFIL---SAGVDKTTIIWdahTGEakqqfpfhsapaldvdwqsNNTFASCSTDMCIHVCKLGQDRPIKtfqgh 350
Cdd:pfam08662  11 LKWNKNGTYLLvltDTDVDKTGKSY---YGE-------------------TNLYLIGETGGPDCVVELDKEGPIH----- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 351 tnevnAIKWDPTGNLLASCSDDMTLKI--WSMKQDScVHDLQAHNKEiyTIKWSPTGPgtnnpnanlMLASASFDST--- 425
Cdd:pfam08662  64 -----DVAWSPNGKEFAVIYGYMPAKVsfFDLKGNV-IHSFGEQPRN--TIFWSPFGR---------LVLLAGFGNLagd 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1694593143 426 VRLWDVDRGICIHTlTKHQEPVYsVAFSPDGRYLASGS------FDKCVHIWnTQTGALVHSY 482
Cdd:pfam08662 127 IEFWDVVNKKKIAT-AEASNATL-CEWSPDGRYFLTATtaprlrVDNGFKIW-HYNGALVYKY 186
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 351-511 2.35e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 53.55  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 351 TNEVNAIKWDPTGNLLASCSDDMTLKIWS----MKQDSCVH----DLQAHNKeIYTIKWsptgpgtnNPNANLMLASASF 422
Cdd:PLN00181  483 SNLVCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHypvvELASRSK-LSGICW--------NSYIKSQVASSNF 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 423 DSTVRLWDVDRGICIHTLTKHQEPVYSVAF-SPDGRYLASGSFDKCVHIWNTQTGALVHSYRGTGGIFEVCWNAGGDKVG 501
Cdd:PLN00181  554 EGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFPSESGRSL 633

                         170
                  ....*....|
gi 1694593143 502 ASASDGSKIY 511
Cdd:PLN00181  634 AFGSADHKVY 643
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.98e-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: 5.98e-07
                          10        20
                  ....*....|....*....|....*
gi 1694593143   7 EVNFLVYRYLQESGFSHSAFTFGIE 31
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 166-199 1.73e-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: 44.61  E-value: 1.73e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1694593143  166 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWN 199
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 384-430 1.87e-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: 44.61  E-value: 1.87e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1694593143  384 SCVHDLQAHNKEIYTIKWSPTGPgtnnpnanlMLASASFDSTVRLWD 430
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGK---------YLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 273-508 3.05e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.09  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 273 ALKWNKKGNFILSAGVDKTTIIWDAHTgEAKQQFPFHSaPALDVD---------WQS--NNTFASCSTDMCIHVCKLGQD 341
Cdd:PLN00181  488 AIGFDRDGEFFATAGVNKKIKIFECES-IIKDGRDIHY-PVVELAsrsklsgicWNSyiKSQVASSNFEGVVQVWDVARS 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 342 RPIKTFQGHTNEVNAIKW---DPTgnLLASCSDDMTLKIWSMKQDSCVHDLQAhNKEIYTIKWsPTGPGTN--------- 409
Cdd:PLN00181  566 QLVTEMKEHEKRVWSIDYssaDPT--LLASGSDDGSVKLWSINQGVSIGTIKT-KANICCVQF-PSESGRSlafgsadhk 641

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 410 -------NPNANL-------------------MLASASFDSTVRLWDVDRGIC------IHTLTKHQEPVYSVAFSPDGR 457
Cdd:PLN00181  642 vyyydlrNPKLPLctmighsktvsyvrfvdssTLVSSSTDNTLKLWDLSMSISginetpLHSFMGHTNVKNFVGLSVSDG 721

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1694593143 458 YLASGSFDKCVHIWNTQTGALVHSYR--------------GTGGIFEVCWNAGGDKVGASASDGS 508
Cdd:PLN00181  722 YIATGSETNEVFVYHKAFPMPVLSYKfktidpvsglevddASQFISSVCWRGQSSTLVAANSTGN 786
PTZ00421 PTZ00421
coronin; Provisional
 165-324 4.82e-06

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 49.12  E-value: 4.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 165 VVLRGHESEVFICAWNP-VSDLLASGSGDSTARIWNLSENSSsgstqlvlrhciregGQDVPSNKD-VTSLDWNSEGTLL 242
Cdd:PTZ00421  119 VHLQGHTKKVGIVSFHPsAMNVLASAGADMVVNVWDVERGKA---------------VEVIKCHSDqITSLEWNLDGSLL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 243 ATGSYDGYARIW-TKDGNLASTLGQHKGPIFA-LKWNKKGNFILSAGVDKT----TIIWDAHTGEAkqqfPFHSapaLDV 316
Cdd:PTZ00421  184 CTTSKDKKLNIIdPRDGTIVSSVEAHASAKSQrCLWAKRKDLIITLGCSKSqqrqIMLWDTRKMAS----PYST---VDL 256


                  ....*...
gi 1694593143 317 DwQSNNTF 324
Cdd:PTZ00421  257 D-QSSALF 263
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 3-36 6.34e-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: 6.34e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1694593143    3 ISSDEVNFLVYRYLQESGFSHSAFTFGIESHISQ 36
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
WD40 pfam00400
WD domain, G-beta repeat;
384-430 1.09e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 1.09e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1694593143 384 SCVHDLQAHNKEIYTIKWSPTGPgtnnpnanlMLASASFDSTVRLWD 430
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGK---------LLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
166-199 1.29e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 1.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1694593143 166 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWN 199
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 257-296 1.30e-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: 42.30  E-value: 1.30e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1694593143  257 DGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWD 296
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 156-371 3.28e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 46.62  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 156 DVEIPpnkAVVLRGHESEVFICaWNP-VSDLLASGSGDSTARIWNLSENsssgstQLVLRhcIREggqdvpSNKDVTSLD 234
Cdd:PLN00181  521 DIHYP---VVELASRSKLSGIC-WNSyIKSQVASSNFEGVVQVWDVARS------QLVTE--MKE------HEKRVWSID 582

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 235 WNS-EGTLLATGSYDGYARIWTKDGNLASTLGQHKGPIFALKW-NKKGNFILSAGVDKTTIIWDAHTgeakQQFPF---- 308
Cdd:PLN00181  583 YSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFpSESGRSLAFGSADHKVYYYDLRN----PKLPLctmi 658

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 309 -HSAPALDVDWQSNNTFASCSTDMCIHVCKLG------QDRPIKTFQGHTNEVNAIKWDPTGNLLASCSD 371
Cdd:PLN00181  659 gHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSmsisgiNETPLHSFMGHTNVKNFVGLSVSDGYIATGSE 728
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 233-321 6.84e-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: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 233 LDWNSEGTLLATGSYDG--------YARIWTKDGnlastlGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQ 304
Cdd:pfam12894   1 MSWCPTMDLIALATEDGelllhrlnWQRVWTLSP------DKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVH 74

                          90
                  ....*....|....*..
gi 1694593143 305 QFPFHSAPALDVDWQSN 321
Cdd:pfam12894  75 HFSAGSDLITCLGWGEN 91
WD40 pfam00400
WD domain, G-beta repeat;
258-296 8.17e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.02  E-value: 8.17e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1694593143 258 GNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWD 296
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 227-254 1.53e-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: 1.53e-04
                           10        20
                   ....*....|....*....|....*...
gi 1694593143  227 NKDVTSLDWNSEGTLLATGSYDGYARIW 254
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
227-254 2.56e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 2.56e-04
                          10        20
                  ....*....|....*....|....*...
gi 1694593143 227 NKDVTSLDWNSEGTLLATGSYDGYARIW 254
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVW 38
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 357-453 3.02e-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: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 357 IKWDPTGNLLASCSDDMTL--------KIWSMKQDscvhdlqAHNKEIYTIKWSPTGPgtnnpnanlMLASASFDSTVRL 428
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELllhrlnwqRVWTLSPD-------KEDLEVTSLAWRPDGK---------LLAVGYSDGTVRL 64

                          90       100
                  ....*....|....*....|....*
gi 1694593143 429 WDVDRGICIHTLTKHQEPVYSVAFS 453
Cdd:pfam12894  65 LDAENGKIVHHFSAGSDLITCLGWG 89
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 353-460 3.71e-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: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143  353 EVNAIKWDPTGNLLASCSDDMTLKiwsmkqdscVHDL----------QAHNKEIYTIKWSPTG-------PGTNNPNAnl 415
Cdd:COG4946    390 RVFNPVWSPDGKKIAFTDNRGRLW---------VVDLasgkvrkvdtDGYGDGISDLAWSPDSkwlayskPGPNQLSQ-- 458

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1694593143  416 mlasasfdstVRLWDVDRGIcIHTLTKHQEPVYSVAFSPDGRYLA 460
Cdd:COG4946    459 ----------IFLYDVETGK-TVQLTDGRYDDGSPAFSPDGKYLY 492
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 328-402 2.40e-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: 37.26  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 328 STDMCIHVCKL-GQdrpiKTFQG----HTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDSCVHDLQAHNKEIYTIKWS 402
Cdd:pfam12894  14 TEDGELLLHRLnWQ----RVWTLspdkEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
PTZ00421 PTZ00421
coronin; Provisional
 258-392 3.04e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 40.26  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 258 GNLAST----LGQhKGPIFALKWNKKGNFIL-SAGVDKTTIIWDAHTGEAKQQFpfhSAPALDVDWQS------------ 320
Cdd:PTZ00421   62 GKLASNppilLGQ-EGPIIDVAFNPFDPQKLfTASEDGTIMGWGIPEEGLTQNI---SDPIVHLQGHTkkvgivsfhpsa 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1694593143 321 NNTFASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDSCVHDLQAH 392
Cdd:PTZ00421  138 MNVLASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAH 209
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 446-511 4.52e-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: 39.57  E-value: 4.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1694593143 446 PVYSVAfSPDGRYLA---SGSFDKCVHIWNTQTGALVHSYRGTGGIFEVCWNAGGDKVGASASDGSKIY 511
Cdd:cd20778   283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNKVV 350
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
410-500 6.19e-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: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 410 NPNANLMLASASFDSTVRLWDVDRGICIHTLTKHQEPvYSVAFSPDGRYL-----ASGSFDKCVHIWNTQTGALVHSYRG 484
Cdd:COG3391   118 DPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGP-HGIAVDPDGKRLyvansGSNTVSVIVSVIDTATGKVVATIPV 196

                          90
                  ....*....|....*.
gi 1694593143 485 TGGIFEVCWNAGGDKV 500
Cdd:COG3391   197 GGGPVGVAVSPDGRRL 212
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 427-494 6.56e-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: 6.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1694593143 427 RLWDVDrgicihtLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHSYR-GTGGIFEVCWN 494
Cdd:pfam12894  28 RVWTLS-------PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSaGSDLITCLGWG 89
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
401-511 6.77e-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: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 401 WSPTGPGTNNPNANLMLASASFDSTVRLWDVDRGICIHTLTKHQEPvYSVAFSPDGRYL-ASGSFDKCVHIWNTQTGALV 479
Cdd:COG3391    67 VADADGADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGGP-RGLAVDPDGGRLyVADSGNGRVSVIDTATGKVV 145

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1694593143 480 HSYRGTGGIFEVCWNAGGDKVGASASDGSKIY 511
Cdd:COG3391   146 ATIPVGAGPHGIAVDPDGKRLYVANSGSNTVS 177
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 411-471 7.13e-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: 7.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1694593143 411 PNANLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIW 471
Cdd:pfam20426  91 PSENFLISCGNWENSFQVISLNDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVW 151
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 178-277 7.16e-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: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694593143 178 AWNPVSDLLASGSGDSTARIWNLSensssgstqlvlRHCIREGGQDVPSNKdVTSLDWNSEGTLLATGSYDGYARIW-TK 256
Cdd:pfam12894   2 SWCPTMDLIALATEDGELLLHRLN------------WQRVWTLSPDKEDLE-VTSLAWRPDGKLLAVGYSDGTVRLLdAE 68

                          90       100
                  ....*....|....*....|.
gi 1694593143 257 DGNLASTLGQHKGPIFALKWN 277
Cdd:pfam12894  69 NGKIVHHFSAGSDLITCLGWG 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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