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Conserved domains on  [gi|13161072|gb|AAK13473|]
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transducin beta-like 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 ...
 174-480 8.42e-85

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: 264.20  E-value: 8.42e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 174 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENsnggstqlvlRHCIREGGHDVPsnkdVTSLDWNSDGTLLAMG 253
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG----------ELLRTLKGHTGP----VRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 254 SYDGFARIW-TENGNLASTLGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNNMT 331
Cdd:cd00200  70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFsPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 332 FASCSTDMCIHVCRLGCDHPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQDACVHDLQAHSKEIYTIKWSP 411
Cdd:cd00200 150 VASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13161072 412 tgpatsnpnSSIMLASASFDSTVRLWDVEQGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWN 480
Cdd:cd00200 230 ---------DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.71e-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: 5.71e-07
                          10        20
                  ....*....|....*....|....*
gi 13161072     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; ...
 454-521 5.89e-04

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


The actual alignment was detected with superfamily member cd20778:

Pssm-ID: 483957 [Multi-domain]  Cd Length: 381  Bit Score: 42.27  E-value: 5.89e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13161072 454 PVYSVAfSPDGKYLA---SGSFDKYVHIWNTQSGSLVHSYQGTGGIFEVCWNARGDKVGASASDGS-VCVLD 521
Cdd:cd20778 283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNkVVVYD 353
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 174-480 8.42e-85

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: 264.20  E-value: 8.42e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 174 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENsnggstqlvlRHCIREGGHDVPsnkdVTSLDWNSDGTLLAMG 253
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG----------ELLRTLKGHTGP----VRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 254 SYDGFARIW-TENGNLASTLGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNNMT 331
Cdd:cd00200  70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFsPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 332 FASCSTDMCIHVCRLGCDHPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQDACVHDLQAHSKEIYTIKWSP 411
Cdd:cd00200 150 VASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13161072 412 tgpatsnpnSSIMLASASFDSTVRLWDVEQGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWN 480
Cdd:cd00200 230 ---------DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
172-522 1.46e-78

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 251.75  E-value: 1.46e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 172 ATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDvpsnKDVTSLDWNSDGTLLA 251
Cdd:COG2319  71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA----TGLLLRTLT------GHT----GAVRSVAFSPDGKTLA 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 252 MGSYDGFARIW-TENGNLASTLGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNN 329
Cdd:COG2319 137 SGSADGTVRLWdLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFsPDG 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 330 MTFASCSTDMCIHVCRLGCDHPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQDACVHDLQAHSKEIYTIKW 409
Cdd:COG2319 217 KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAF 296

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 410 SPTGPatsnpnssiMLASASFDSTVRLWDVEQGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWNTQSGSLVHS 489
Cdd:COG2319 297 SPDGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367

                       330       340       350
                ....*....|....*....|....*....|....
gi 13161072 490 YQG-TGGIFEVCWNARGDKVGASASDGSVCVLDL 522
Cdd:COG2319 368 LTGhTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
PTZ00420 PTZ00420
coronin; Provisional
 351-440 6.81e-11

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 64.59  E-value: 6.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  351 PVKTFQGHTNEVNAIKWDPS-GMLLASCSDDMTLKIWSMK-QDACVHD-------LQAHSKEIYTIKWsptgpatsNPNS 421
Cdd:PTZ00420  66 PVIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPhNDESVKEikdpqciLKGHKKKISIIDW--------NPMN 137

                         90
                 ....*....|....*....
gi 13161072  422 SIMLASASFDSTVRLWDVE 440
Cdd:PTZ00420 138 YYIMCSSGFDSFVNIWDIE 156
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 441-480 3.20e-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: 55.40  E-value: 3.20e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 13161072    441 QGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWN 480
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
442-480 1.53e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.12  E-value: 1.53e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 13161072   442 GVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWN 480
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.71e-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: 5.71e-07
                          10        20
                  ....*....|....*....|....*
gi 13161072     7 EVNFLVYRYLQESGFSHSAFTFGIE 31
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 7-36 1.44e-05

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


Pssm-ID: 128913  Cd Length: 34  Bit Score: 42.04  E-value: 1.44e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 13161072      7 EVNFLVYRYLQESGFSHSAFTFGIESHISQ 36
Cdd:smart00667   5 ELNRLILEYLLRNGYEETAETLQKESGLSL 34
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 454-521 5.89e-04

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


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 42.27  E-value: 5.89e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13161072 454 PVYSVAfSPDGKYLA---SGSFDKYVHIWNTQSGSLVHSYQGTGGIFEVCWNARGDKVGASASDGS-VCVLD 521
Cdd:cd20778 283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNkVVVYD 353
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 174-480 8.42e-85

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: 264.20  E-value: 8.42e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 174 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENsnggstqlvlRHCIREGGHDVPsnkdVTSLDWNSDGTLLAMG 253
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG----------ELLRTLKGHTGP----VRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 254 SYDGFARIW-TENGNLASTLGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNNMT 331
Cdd:cd00200  70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFsPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 332 FASCSTDMCIHVCRLGCDHPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQDACVHDLQAHSKEIYTIKWSP 411
Cdd:cd00200 150 VASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13161072 412 tgpatsnpnSSIMLASASFDSTVRLWDVEQGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWN 480
Cdd:cd00200 230 ---------DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
172-522 1.46e-78

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 251.75  E-value: 1.46e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 172 ATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDvpsnKDVTSLDWNSDGTLLA 251
Cdd:COG2319  71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA----TGLLLRTLT------GHT----GAVRSVAFSPDGKTLA 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 252 MGSYDGFARIW-TENGNLASTLGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNN 329
Cdd:COG2319 137 SGSADGTVRLWdLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFsPDG 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 330 MTFASCSTDMCIHVCRLGCDHPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQDACVHDLQAHSKEIYTIKW 409
Cdd:COG2319 217 KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAF 296

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 410 SPTGPatsnpnssiMLASASFDSTVRLWDVEQGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWNTQSGSLVHS 489
Cdd:COG2319 297 SPDGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367

                       330       340       350
                ....*....|....*....|....*....|....
gi 13161072 490 YQG-TGGIFEVCWNARGDKVGASASDGSVCVLDL 522
Cdd:COG2319 368 LTGhTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
172-483 2.99e-78

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 250.98  E-value: 2.99e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 172 ATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDvpsnKDVTSLDWNSDGTLLA 251
Cdd:COG2319 113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA----TGKLLRTLT------GHS----GAVTSVAFSPDGKLLA 178

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 252 MGSYDGFARIW-TENGNLASTLGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNN 329
Cdd:COG2319 179 SGSDDGTVRLWdLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFsPDG 258

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 330 MTFASCSTDMCIHVCRLGCDHPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQDACVHDLQAHSKEIYTIKW 409
Cdd:COG2319 259 RLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAF 338

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13161072 410 SPTGPatsnpnssiMLASASFDSTVRLWDVEQGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWNTQS 483
Cdd:COG2319 339 SPDGK---------TLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
169-522 5.88e-63

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 210.92  E-value: 5.88e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 169 PNKATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDVPsnkdVTSLDWNSDGT 248
Cdd:COG2319  26 GALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAA----AGALLATLL------GHTAA----VLSVAFSPDGR 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 249 LLAMGSYDGFARIW-TENGNLASTLGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWDAHTGEakqqfpfhsapaldvdwq 327
Cdd:COG2319  92 LLASASADGTVRLWdLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK------------------ 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 328 nnmtfascstdmcihvcrlgcdhPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQDACVHDLQAHSKEIYTI 407
Cdd:COG2319 154 -----------------------LLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 408 KWSPTGPatsnpnssiMLASASFDSTVRLWDVEQGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWNTQSGSLV 487
Cdd:COG2319 211 AFSPDGK---------LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELL 281

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 13161072 488 HSYQG-TGGIFEVCWNARGDKVgASAS-DGSVCVLDL 522
Cdd:COG2319 282 RTLTGhSGGVNSVAFSPDGKLL-ASGSdDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 268-522 2.72e-58

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: 195.25  E-value: 2.72e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 268 LASTLGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNNMTFASCSTDMCIHVCRL 346
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAsADGTYLASGSSDKTIRLWDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 347 GCDHPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQDACVHDLQAHSKEIYTIKWSPTGPatsnpnssiMLA 426
Cdd:cd00200  81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGT---------FVA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 427 SASFDSTVRLWDVEQGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWNTQSGSLVHSYQG-TGGIFEVCWNARG 505
Cdd:cd00200 152 SSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDG 231

                       250
                ....*....|....*..
gi 13161072 506 DKVGASASDGSVCVLDL 522
Cdd:cd00200 232 YLLASGSEDGTIRVWDL 248
WD40 COG2319
WD40 repeat [General function prediction only];
245-522 6.43e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.95  E-value: 6.43e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 245 SDGTLLAMGSYDGFARIWTEN-GNLASTLGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWDAHTGEAKQQFPFHSAPALD 323
Cdd:COG2319   4 ADGAALAAASADLALALLAAAlGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 324 VDWQ-NNMTFASCSTDMCIHVCRLGCDHPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQDACVHDLQAHSK 402
Cdd:COG2319  84 VAFSpDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 403 EIYTIKWSPTGPatsnpnssiMLASASFDSTVRLWDVEQGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWNTQ 482
Cdd:COG2319 164 AVTSVAFSPDGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 13161072 483 SGSLVHSYQG-TGGIFEVCWNARGDKVgASAS-DGSVCVLDL 522
Cdd:COG2319 235 TGKLLRTLTGhSGSVRSVAFSPDGRLL-ASGSaDGTVRLWDL 275
PTZ00420 PTZ00420
coronin; Provisional
 351-440 6.81e-11

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 64.59  E-value: 6.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  351 PVKTFQGHTNEVNAIKWDPS-GMLLASCSDDMTLKIWSMK-QDACVHD-------LQAHSKEIYTIKWsptgpatsNPNS 421
Cdd:PTZ00420  66 PVIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPhNDESVKEikdpqciLKGHKKKISIIDW--------NPMN 137

                         90
                 ....*....|....*....
gi 13161072  422 SIMLASASFDSTVRLWDVE 440
Cdd:PTZ00420 138 YYIMCSSGFDSFVNIWDIE 156
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 441-480 3.20e-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: 55.40  E-value: 3.20e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 13161072    441 QGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWN 480
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
 175-318 4.81e-10

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 61.89  E-value: 4.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  175 LRGHESEVFICAWNPV-SDLLASGSGDSTARIWNLNENSNgGSTQLVLRHCIREGghdvpSNKDVTSLDWNS-DGTLLAM 252
Cdd:PTZ00420  70 LKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPHNDE-SVKEIKDPQCILKG-----HKKKISIIDWNPmNYYIMCS 143

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13161072  253 GSYDGFARIW-TENGNLASTLGQHKgPIFALKWNKKGNYVLSAGVDKTTIIWDAHTGEAKQQFPFHS 318
Cdd:PTZ00420 144 SGFDSFVNIWdIENEKRAFQINMPK-KLSSLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSFHIHD 209
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 350-387 9.04e-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: 53.86  E-value: 9.04e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 13161072    350 HPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWS 387
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
442-480 1.53e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.12  E-value: 1.53e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 13161072   442 GVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWN 480
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
351-387 5.66e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 51.58  E-value: 5.66e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 13161072   351 PVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWS 387
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 374-486 2.58e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 56.63  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  374 LASCSDDMTLKIWSMKQDACVHDLQAHSKEIYTIKWSPTGPAtsnpnssiMLASASFDSTVRLWDVEQGVCTHTLmKHQE 453
Cdd:PLN00181 548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPT--------LLASGSDDGSVKLWSINQGVSIGTI-KTKA 618

                         90       100       110
                 ....*....|....*....|....*....|....
gi 13161072  454 PVYSVAFSPD-GKYLASGSFDKYVHIWNTQSGSL 486
Cdd:PLN00181 619 NICCVQFPSEsGRSLAFGSADHKVYYYDLRNPKL 652
PTZ00421 PTZ00421
coronin; Provisional
 357-489 3.13e-08

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 56.05  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  357 GHTNEVNAIKWDP-SGMLLASCSDDMTLKIWSMKQ--------DACVHdLQAHSKEIytikwsptGPATSNPNSSIMLAS 427
Cdd:PTZ00421  73 GQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEegltqnisDPIVH-LQGHTKKV--------GIVSFHPSAMNVLAS 143

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13161072  428 ASFDSTVRLWDVEQGVCTHTLMKHQEPVYSVAFSPDGKYLASGSFDKYVHIWNTQSGSLVHS 489
Cdd:PTZ00421 144 AGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSS 205
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.71e-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: 5.71e-07
                          10        20
                  ....*....|....*....|....*
gi 13161072     7 EVNFLVYRYLQESGFSHSAFTFGIE 31
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 359-484 1.34e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 51.24  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  359 TNEVNAIKWDPSGMLLASCSDDMTLKIWS----MKQDACVH----DLQAHSKeIYTIKWsptgpatsnpNSSI--MLASA 428
Cdd:PLN00181 483 SNLVCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHypvvELASRSK-LSGICW----------NSYIksQVASS 551

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13161072  429 SFDSTVRLWDVEQGVCTHTLMKHQEPVYSVAF-SPDGKYLASGSFDKYVHIWNTQSG 484
Cdd:PLN00181 552 NFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQG 608
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 281-522 1.69e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.86  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  281 ALKWNKKGNYVLSAGVDKTTIIWDAHTgEAKQQFPFHSaPALDVDWQNNMT-----------FASCSTDMCIHVCRLGCD 349
Cdd:PLN00181 488 AIGFDRDGEFFATAGVNKKIKIFECES-IIKDGRDIHY-PVVELASRSKLSgicwnsyiksqVASSNFEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  350 HPVKTFQGHTNEVNAIKW---DPSgmLLASCSDDMTLKIWSMKQDACVHDLQAHSKeIYTIKW-SPTGPATS-------- 417
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYssaDPT--LLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFpSESGRSLAfgsadhkv 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  418 ------NPN-------------------SSIMLASASFDSTVRLWDVEQGVC------THTLMKHQEPVYSVAFSPDGKY 466
Cdd:PLN00181 643 yyydlrNPKlplctmighsktvsyvrfvDSSTLVSSSTDNTLKLWDLSMSISginetpLHSFMGHTNVKNFVGLSVSDGY 722

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  467 LASGSFDKYVHIWNTQSGSLVHSYQ--------------GTGGIFEVCWNARGDKVGASASDGSVCVLDL 522
Cdd:PLN00181 723 IATGSETNEVFVYHKAFPMPVLSYKfktidpvsglevddASQFISSVCWRGQSSTLVAANSTGNIKILEM 792
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 174-207 2.40e-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: 2.40e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13161072    174 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWN 207
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 393-438 3.35e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.84  E-value: 3.35e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 13161072    393 CVHDLQAHSKEIYTIKWSPTGPatsnpnssiMLASASFDSTVRLWD 438
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGK---------YLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
393-438 1.30e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 1.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 13161072   393 CVHDLQAHSKEIYTIKWSPTGPatsnpnssiMLASASFDSTVRLWD 438
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGK---------LLASGSDDGTVKVWD 39
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 7-36 1.44e-05

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


Pssm-ID: 128913  Cd Length: 34  Bit Score: 42.04  E-value: 1.44e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 13161072      7 EVNFLVYRYLQESGFSHSAFTFGIESHISQ 36
Cdd:smart00667   5 ELNRLILEYLLRNGYEETAETLQKESGLSL 34
WD40 pfam00400
WD domain, G-beta repeat;
173-207 1.59e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.95  E-value: 1.59e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 13161072   173 TVLRGHESEVFICAWNPVSDLLASGSGDSTARIWN 207
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 265-304 1.83e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.91  E-value: 1.83e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 13161072    265 NGNLASTLGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWD 304
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 186-285 2.62e-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: 42.65  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072   186 AWNPVSDLLASGSGD--------STARIWNLNENSNGGStqlvlrhciregghdvpsnkdVTSLDWNSDGTLLAMGSYDG 257
Cdd:pfam12894   2 SWCPTMDLIALATEDgelllhrlNWQRVWTLSPDKEDLE---------------------VTSLAWRPDGKLLAVGYSDG 60

                          90       100
                  ....*....|....*....|....*....
gi 13161072   258 FARIW-TENGNLASTLGQHKGPIFALKWN 285
Cdd:pfam12894  61 TVRLLdAENGKIVHHFSAGSDLITCLGWG 89
PTZ00421 PTZ00421
coronin; Provisional
 175-310 8.91e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.88  E-value: 8.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  175 LRGHESEVFICAWNP-VSDLLASGSGDSTARIWNLNEnsnGGSTQLVLRHciregghdvpsNKDVTSLDWNSDGTLLAMG 253
Cdd:PTZ00421 121 LQGHTKKVGIVSFHPsAMNVLASAGADMVVNVWDVER---GKAVEVIKCH-----------SDQITSLEWNLDGSLLCTT 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13161072  254 SYDGFARIWT-ENGNLASTLGQHKGPIFA-LKWNKKGNYVLSAGVDKT----TIIWDAHTGEA 310
Cdd:PTZ00421 187 SKDKKLNIIDpRDGTIVSSVEAHASAKSQrCLWAKRKDLIITLGCSKSqqrqIMLWDTRKMAS 249
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
 282-490 8.92e-05

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


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 43.42  E-value: 8.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072   282 LKWNKKGNYVL---SAGVDKTTIIWdahTGEakqqfpfhsapaldvdwqNNMTFasCSTDMcIHVCRLGCDHpvktfqgh 358
Cdd:pfam08662  11 LKWNKNGTYLLvltDTDVDKTGKSY---YGE------------------TNLYL--IGETG-GPDCVVELDK-------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072   359 TNEVNAIKWDPSGMLLASCSDDMTLKI--WSMKQDAcVHDLQAHSKEiyTIKWSPTGPatsnpnssiMLASASFDST--- 433
Cdd:pfam08662  59 EGPIHDVAWSPNGKEFAVIYGYMPAKVsfFDLKGNV-IHSFGEQPRN--TIFWSPFGR---------LVLLAGFGNLagd 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13161072   434 VRLWDVeQGVCTHTLMKHQEPVYsVAFSPDGKYLASGS------FDKYVHIWnTQSGSLVHSY 490
Cdd:pfam08662 127 IEFWDV-VNKKKIATAEASNATL-CEWSPDGRYFLTATtaprlrVDNGFKIW-HYNGALVYKY 186
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
410-522 1.31e-04

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 43.53  E-value: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072 410 SPTGPATSnPNSSIMLASASFDSTVRLWDVEQGVCTHTLMKHQEPvYSVAFSPDGKYL-----ASGSFDKYVHIWNTQSG 484
Cdd:COG3391 111 GPRGLAVD-PDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGP-HGIAVDPDGKRLyvansGSNTVSVIVSVIDTATG 188

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13161072 485 SLVHSYQGTGGIFEVCWNARGDKV--------GASASDGSVCVLDL 522
Cdd:COG3391 189 KVVATIPVGGGPVGVAVSPDGRRLyvanrgsnTSNGGSNTVSVIDL 234
WD40 pfam00400
WD domain, G-beta repeat;
266-304 1.41e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 1.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 13161072   266 GNLASTLGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWD 304
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 435-502 5.53e-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: 39.18  E-value: 5.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13161072   435 RLWDVEQGvcthtlmKHQEPVYSVAFSPDGKYLASGSFDKYVHIWNTQSGSLVHSYQ-GTGGIFEVCWN 502
Cdd:pfam12894  28 RVWTLSPD-------KEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSaGSDLITCLGWG 89
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 454-521 5.89e-04

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


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 42.27  E-value: 5.89e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13161072 454 PVYSVAfSPDGKYLA---SGSFDKYVHIWNTQSGSLVHSYQGTGGIFEVCWNARGDKVGASASDGS-VCVLD 521
Cdd:cd20778 283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNkVVVYD 353
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 235-262 8.90e-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: 36.91  E-value: 8.90e-04
                           10        20
                   ....*....|....*....|....*...
gi 13161072    235 NKDVTSLDWNSDGTLLAMGSYDGFARIW 262
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLW 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 241-329 1.06e-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: 38.41  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072   241 LDWNSDGTLLAMGSYDG--------FARIWTENGnlastlGQHKGPIFALKWNKKGNYVLSAGVDKTTIIWDAHTGEAKQ 312
Cdd:pfam12894   1 MSWCPTMDLIALATEDGelllhrlnWQRVWTLSP------DKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVH 74

                          90
                  ....*....|....*..
gi 13161072   313 QFPFHSAPALDVDWQNN 329
Cdd:pfam12894  75 HFSAGSDLITCLGWGEN 91
WD40 pfam00400
WD domain, G-beta repeat;
235-262 1.07e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.07e-03
                          10        20
                  ....*....|....*....|....*...
gi 13161072   235 NKDVTSLDWNSDGTLLAMGSYDGFARIW 262
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00420 PTZ00420
coronin; Provisional
 166-251 1.88e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 41.09  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13161072  166 EIPPNKATV---------LRGHESEVFICAWNPVSDLLASGSG-DSTARIWNL-NENSnggSTQLVLrhciregghdvps 234
Cdd:PTZ00420 103 EIPHNDESVkeikdpqciLKGHKKKISIIDWNPMNYYIMCSSGfDSFVNIWDIeNEKR---AFQINM------------- 166

                         90
                 ....*....|....*..
gi 13161072  235 NKDVTSLDWNSDGTLLA 251
Cdd:PTZ00420 167 PKKLSSLKWNIKGNLLS 183
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 336-410 3.34e-03

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


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 36.87  E-value: 3.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13161072   336 STDMCIHVCRLGCDHPVKTFQ-GHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQDACVHDLQAHSKEIYTIKWS 410
Cdd:pfam12894  14 TEDGELLLHRLNWQRVWTLSPdKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 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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