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Conserved domains on  [gi|242005460|ref|XP_002423583|]
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Katanin p80 WD40-containing subunit B1, putative [Pediculus humanus corporis]

Protein Classification

WD repeat KATNB1 family protein( domain architecture ID 10078096)

WD repeat KATNB1 family protein similar to Mus musculus katanin p80 WD40 repeat-containing subunit B1 (KATNB1) that participates in a complex which severs microtubules in an ATP-dependent manner

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Katanin_con80 pfam13925
con80 domain of Katanin; The con80 domain of katanin is the C-terminal region of the protein ...
612-770 3.19e-67

con80 domain of Katanin; The con80 domain of katanin is the C-terminal region of the protein that binds to the N-terminal domain of katanin-p60, the catalytic ATPase. The complex associates with a specific subregion of the mitotic spindle leading to increased microtubule disassembly and targeting of p60 to the spindle poles. The assembly and function of the mitotic spindle requires the activity of a number of microtubule-binding proteins. Katanin, a heterodimeric microtubule-severing ATPase, is found localized at mitotic spindle poles. A proposed model is that katanin is targeted to spindle poles through a combination of direct microtubule binding by the p60 subunit and through interactions between the WD40 domain and an unknown protein.


:

Pssm-ID: 464044  Cd Length: 160  Bit Score: 219.41  E-value: 3.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  612 RDHNSMMAVLMNRHKSLKTVFSVWHRKDTKAAIEYAVALENPSVMVDLLSVLVLRPSIWTLDICGNVLPSISNLLQSKYE 691
Cdd:pfam13925   1 KDHDTMLSVLQSRLLKLQVVRTLWRRNDIKGAIEAAVRMQDPSVLVDVLSVLQLKPELITLDLCVDLLPLLKELLKSKYE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242005460  692 LHMTTGCAALSLILRNFSHIIKTNVRAPIHTVGVDISREERYNKCLKCYKSLISIRSFLLKKQTVQGKMGQSFRELLTL 770
Cdd:pfam13925  81 RYIIVGLDFLRLILKNFGPVIKSALSAPPSSVGVDLSREERLEKCNECFKELQKIRQILKKLARRSGKLGELARELNLL 159
WD40 COG2319
WD40 repeat [General function prediction only];
11-250 1.36e-64

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 220.94  E-value: 1.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  11 LQEFIAHEAKVNCLAlgqIS--GRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIW 88
Cdd:COG2319  155 LRTLTGHSGAVTSVA---FSpdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLW 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  89 DLEANKKTRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGV 168
Cdd:COG2319  232 DLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGT 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 169 VKLWDVRVGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTGKGSNSINCLHFTPEGECLYAGV 248
Cdd:COG2319  312 VRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGS 391

                 ..
gi 242005460 249 ED 250
Cdd:COG2319  392 AD 393
 
Name Accession Description Interval E-value
Katanin_con80 pfam13925
con80 domain of Katanin; The con80 domain of katanin is the C-terminal region of the protein ...
612-770 3.19e-67

con80 domain of Katanin; The con80 domain of katanin is the C-terminal region of the protein that binds to the N-terminal domain of katanin-p60, the catalytic ATPase. The complex associates with a specific subregion of the mitotic spindle leading to increased microtubule disassembly and targeting of p60 to the spindle poles. The assembly and function of the mitotic spindle requires the activity of a number of microtubule-binding proteins. Katanin, a heterodimeric microtubule-severing ATPase, is found localized at mitotic spindle poles. A proposed model is that katanin is targeted to spindle poles through a combination of direct microtubule binding by the p60 subunit and through interactions between the WD40 domain and an unknown protein.


Pssm-ID: 464044  Cd Length: 160  Bit Score: 219.41  E-value: 3.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  612 RDHNSMMAVLMNRHKSLKTVFSVWHRKDTKAAIEYAVALENPSVMVDLLSVLVLRPSIWTLDICGNVLPSISNLLQSKYE 691
Cdd:pfam13925   1 KDHDTMLSVLQSRLLKLQVVRTLWRRNDIKGAIEAAVRMQDPSVLVDVLSVLQLKPELITLDLCVDLLPLLKELLKSKYE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242005460  692 LHMTTGCAALSLILRNFSHIIKTNVRAPIHTVGVDISREERYNKCLKCYKSLISIRSFLLKKQTVQGKMGQSFRELLTL 770
Cdd:pfam13925  81 RYIIVGLDFLRLILKNFGPVIKSALSAPPSSVGVDLSREERLEKCNECFKELQKIRQILKKLARRSGKLGELARELNLL 159
WD40 COG2319
WD40 repeat [General function prediction only];
11-250 1.36e-64

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 220.94  E-value: 1.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  11 LQEFIAHEAKVNCLAlgqIS--GRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIW 88
Cdd:COG2319  155 LRTLTGHSGAVTSVA---FSpdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLW 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  89 DLEANKKTRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGV 168
Cdd:COG2319  232 DLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGT 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 169 VKLWDVRVGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTGKGSNSINCLHFTPEGECLYAGV 248
Cdd:COG2319  312 VRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGS 391

                 ..
gi 242005460 249 ED 250
Cdd:COG2319  392 AD 393
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
11-250 9.72e-64

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: 214.89  E-value: 9.72e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  11 LQEFIAHEAKVNCLALGQiSGRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIWDL 90
Cdd:cd00200   44 LRTLKGHTGPVRDVAASA-DGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  91 EANKKTRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGVVK 170
Cdd:cd00200  123 ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIK 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 171 LWDVRVGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTGKGSNSINCLHFTPEGECLYAGVED 250
Cdd:cd00200  203 LWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSAD 282
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
137-173 6.24e-10

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 55.01  E-value: 6.24e-10
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 242005460   137 CISNYRGHILTVNSVRFSPDGLWLASGGDDGVVKLWD 173
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
137-173 1.37e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.89  E-value: 1.37e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 242005460  137 CISNYRGHILTVNSVRFSPDGLWLASGGDDGVVKLWD 173
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
160-258 3.11e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 57.40  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 160 LASGGDDGVVKLWDVRVGRLLQEFRDHLGSVLSVEFHPHE-FLLASGSSDGTVNFWDLEKFQLVSTTGKGSNsINCLHFT 238
Cdd:PLN00181 548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADpTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFP 626
                         90       100
                 ....*....|....*....|.
gi 242005460 239 PE-GECLYAGVEDYlKVFGWE 258
Cdd:PLN00181 627 SEsGRSLAFGSADH-KVYYYD 646
 
Name Accession Description Interval E-value
Katanin_con80 pfam13925
con80 domain of Katanin; The con80 domain of katanin is the C-terminal region of the protein ...
612-770 3.19e-67

con80 domain of Katanin; The con80 domain of katanin is the C-terminal region of the protein that binds to the N-terminal domain of katanin-p60, the catalytic ATPase. The complex associates with a specific subregion of the mitotic spindle leading to increased microtubule disassembly and targeting of p60 to the spindle poles. The assembly and function of the mitotic spindle requires the activity of a number of microtubule-binding proteins. Katanin, a heterodimeric microtubule-severing ATPase, is found localized at mitotic spindle poles. A proposed model is that katanin is targeted to spindle poles through a combination of direct microtubule binding by the p60 subunit and through interactions between the WD40 domain and an unknown protein.


Pssm-ID: 464044  Cd Length: 160  Bit Score: 219.41  E-value: 3.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  612 RDHNSMMAVLMNRHKSLKTVFSVWHRKDTKAAIEYAVALENPSVMVDLLSVLVLRPSIWTLDICGNVLPSISNLLQSKYE 691
Cdd:pfam13925   1 KDHDTMLSVLQSRLLKLQVVRTLWRRNDIKGAIEAAVRMQDPSVLVDVLSVLQLKPELITLDLCVDLLPLLKELLKSKYE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242005460  692 LHMTTGCAALSLILRNFSHIIKTNVRAPIHTVGVDISREERYNKCLKCYKSLISIRSFLLKKQTVQGKMGQSFRELLTL 770
Cdd:pfam13925  81 RYIIVGLDFLRLILKNFGPVIKSALSAPPSSVGVDLSREERLEKCNECFKELQKIRQILKKLARRSGKLGELARELNLL 159
WD40 COG2319
WD40 repeat [General function prediction only];
11-250 1.36e-64

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 220.94  E-value: 1.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  11 LQEFIAHEAKVNCLAlgqIS--GRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIW 88
Cdd:COG2319  155 LRTLTGHSGAVTSVA---FSpdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLW 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  89 DLEANKKTRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGV 168
Cdd:COG2319  232 DLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGT 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 169 VKLWDVRVGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTGKGSNSINCLHFTPEGECLYAGV 248
Cdd:COG2319  312 VRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGS 391

                 ..
gi 242005460 249 ED 250
Cdd:COG2319  392 AD 393
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
11-250 9.72e-64

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: 214.89  E-value: 9.72e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  11 LQEFIAHEAKVNCLALGQiSGRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIWDL 90
Cdd:cd00200   44 LRTLKGHTGPVRDVAASA-DGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  91 EANKKTRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGVVK 170
Cdd:cd00200  123 ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIK 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 171 LWDVRVGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTGKGSNSINCLHFTPEGECLYAGVED 250
Cdd:cd00200  203 LWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSAD 282
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
17-250 1.83e-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: 211.42  E-value: 1.83e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  17 HEAKVNCLALGQiSGRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIWDLEANKKT 96
Cdd:cd00200    8 HTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  97 RTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGVVKLWDVRV 176
Cdd:cd00200   87 RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRT 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242005460 177 GRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVST-TGKgSNSINCLHFTPEGECLYAGVED 250
Cdd:cd00200  167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTlRGH-ENGVNSVAFSPDGYLLASGSED 240
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
10-215 1.64e-59

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: 203.34  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  10 KLQEFIAHEAKVNCLALGQiSGRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIWD 89
Cdd:cd00200   85 CVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  90 LEANKKTRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGVV 169
Cdd:cd00200  164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTI 243
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 242005460 170 KLWDVRVGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWD 215
Cdd:cd00200  244 RVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
11-217 4.37e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 205.92  E-value: 4.37e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  11 LQEFIAHEAKVNCLAlgqIS--GRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIW 88
Cdd:COG2319  197 LRTLTGHTGAVRSVA---FSpdGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  89 DLEANKKTRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGV 168
Cdd:COG2319  274 DLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGT 353
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 242005460 169 VKLWDVRVGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDLE 217
Cdd:COG2319  354 VRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
11-250 6.04e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 205.53  E-value: 6.04e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  11 LQEFIAHEAKVNCLALgQISGRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIWDL 90
Cdd:COG2319   71 LATLLGHTAAVLSVAF-SPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  91 EANKKTRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGVVK 170
Cdd:COG2319  150 ATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVR 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 171 LWDVRVGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTGKGSNSINCLHFTPEGECLYAGVED 250
Cdd:COG2319  230 LWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDD 309
WD40 COG2319
WD40 repeat [General function prediction only];
30-270 3.28e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 189.74  E-value: 3.28e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  30 SGRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIWDLEANKKTRTFVGHKDAIKCM 109
Cdd:COG2319   47 DGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 110 DFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGVVKLWDVRVGRLLQEFRDHLGS 189
Cdd:COG2319  127 AFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGA 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 190 VLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTGKGSNSINCLHFTPEGECLYAGVED-YLKVF---GWEPARTFDS 265
Cdd:COG2319  207 VRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADgTVRLWdlaTGELLRTLTG 286

                 ....*
gi 242005460 266 vPTGW 270
Cdd:COG2319  287 -HSGG 290
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
57-295 4.95e-52

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: 182.92  E-value: 4.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  57 LNAHTNPVECVKFGHTEEFVCSGSQAGELYIWDLEANKKTRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWDLRRRG 136
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 137 CISNYRGHILTVNSVRFSPDGLWLASGGDDGVVKLWDVRVGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDL 216
Cdd:cd00200   85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 217 EKFQLVsTTGKG-SNSINCLHFTPEGECLYAGVEDY-LKVfgWEPaRTFDSVPTGWGQvqdmvktTNQLIGASFHKSKVM 294
Cdd:cd00200  165 RTGKCV-ATLTGhTGEVNSVAFSPDGEKLLSSSSDGtIKL--WDL-STGKCLGTLRGH-------ENGVNSVAFSPDGYL 233

                 .
gi 242005460 295 L 295
Cdd:cd00200  234 L 234
WD40 COG2319
WD40 repeat [General function prediction only];
30-250 1.20e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 160.08  E-value: 1.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  30 SGRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIWDLEANKKTRTFVGHKDAIKCM 109
Cdd:COG2319    5 DGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 110 DFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGVVKLWDVRVGRLLQEFRDHLGS 189
Cdd:COG2319   85 AFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242005460 190 VLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTGKGSNSINCLHFTPEGECLYAGVED 250
Cdd:COG2319  165 VTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSAD 225
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
96-263 7.53e-41

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: 151.72  E-value: 7.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  96 TRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGVVKLWDVR 175
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 176 VGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTGKGSNSINCLHFTPEGECLYAGVED-YLKV 254
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDgTIKL 161
                        170
                 ....*....|..
gi 242005460 255 F---GWEPARTF 263
Cdd:cd00200  162 WdlrTGKCVATL 173
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
137-250 2.04e-22

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: 98.18  E-value: 2.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 137 CISNYRGHILTVNSVRFSPDGLWLASGGDDGVVKLWDVRVGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDL 216
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 242005460 217 EKFQLVSTTGKGSNSINCLHFTPEGECLYAGVED 250
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRD 114
WD40 COG2319
WD40 repeat [General function prediction only];
110-260 9.51e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.96  E-value: 9.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 110 DFHPYGDFLTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSPDGLWLASGGDDGVVKLWDVRVGRLLQEFRDHLGS 189
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242005460 190 VLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTGKGSNSINCLHFTPEGECLYAGVEDY-LKVfgWEPA 260
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGtVRL--WDLA 150
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
137-173 6.24e-10

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 55.01  E-value: 6.24e-10
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 242005460   137 CISNYRGHILTVNSVRFSPDGLWLASGGDDGVVKLWD 173
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
137-173 1.37e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.89  E-value: 1.37e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 242005460  137 CISNYRGHILTVNSVRFSPDGLWLASGGDDGVVKLWD 173
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
93-131 1.64e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.50  E-value: 1.64e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 242005460   93 NKKTRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWD 131
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
177-215 8.42e-09

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: 51.54  E-value: 8.42e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 242005460   177 GRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWD 215
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
94-131 1.30e-08

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: 51.16  E-value: 1.30e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 242005460    94 KKTRTFVGHKDAIKCMDFHPYGDFLTSGSLDTSIKLWD 131
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
160-258 3.11e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 57.40  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 160 LASGGDDGVVKLWDVRVGRLLQEFRDHLGSVLSVEFHPHE-FLLASGSSDGTVNFWDLEKFQLVSTTGKGSNsINCLHFT 238
Cdd:PLN00181 548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADpTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFP 626
                         90       100
                 ....*....|....*....|.
gi 242005460 239 PE-GECLYAGVEDYlKVFGWE 258
Cdd:PLN00181 627 SEsGRSLAFGSADH-KVYYYD 646
WD40 pfam00400
WD domain, G-beta repeat;
177-215 2.02e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.73  E-value: 2.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 242005460  177 GRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWD 215
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
118-255 1.53e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 51.63  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 118 LTSGSLDTSIKLWDLRRRGCISNYRGHILTVNSVRFSP-DGLWLASGGDDGVVKLWDVRVGRLLQEFRDHlGSVLSVEFh 196
Cdd:PLN00181 548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTK-ANICCVQF- 625
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242005460 197 PHEF--LLASGSSDGTVNFWDLE--KFQLVSTTGKgSNSINCLHFTPEGECLYAGVEDYLKVF 255
Cdd:PLN00181 626 PSESgrSLAFGSADHKVYYYDLRnpKLPLCTMIGH-SKTVSYVRFVDSSTLVSSSTDNTLKLW 687
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
7-165 2.74e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.86  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460   7 RSFKLQEFIAHEAKVNCLALGQISGRVLVTGGDDKKVNLWAIGTTNYVLSLNAHTNpVECVKF-GHTEEFVCSGSQAGEL 85
Cdd:PLN00181 564 RSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFpSESGRSLAFGSADHKV 642
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  86 YIWDLEANK-KTRTFVGHKDAIKCMDFHPyGDFLTSGSLDTSIKLWDLR------RRGCISNYRGHILTVNSVRFSPDGL 158
Cdd:PLN00181 643 YYYDLRNPKlPLCTMIGHSKTVSYVRFVD-SSTLVSSSTDNTLKLWDLSmsisgiNETPLHSFMGHTNVKNFVGLSVSDG 721

                 ....*..
gi 242005460 159 WLASGGD 165
Cdd:PLN00181 722 YIATGSE 728
PTZ00421 PTZ00421
coronin; Provisional
100-235 3.51e-06

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 50.28  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 100 VGHKDAIKCMDFHPYGDF-LTSGSLDTSIKLWDLRRRGCISN-------YRGHILTVNSVRFSPDGL-WLASGGDDGVVK 170
Cdd:PTZ00421  72 LGQEGPIIDVAFNPFDPQkLFTASEDGTIMGWGIPEEGLTQNisdpivhLQGHTKKVGIVSFHPSAMnVLASAGADMVVN 151
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242005460 171 LWDVRVGRLLQEFRDHLGSVLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTG--KGSNSINCL 235
Cdd:PTZ00421 152 VWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEahASAKSQRCL 218
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
76-216 9.07e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 46.23  E-value: 9.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460  76 VCSGSQAGELYIWDLEANKKTRTFVGHKDAIKCMDFHPYG-DFLTSGSLDTSIKLWDLRRRGCISNYRGHIlTVNSVRFS 154
Cdd:PLN00181 548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADpTLLASGSDDGSVKLWSINQGVSIGTIKTKA-NICCVQFP 626
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242005460 155 PD-GLWLASGGDDGVVKLWDVRVGRL-LQEFRDHLGSVLSVEFHPHEFLLASgSSDGTVNFWDL 216
Cdd:PLN00181 627 SEsGRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFVDSSTLVSS-STDNTLKLWDL 689
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
50-89 1.61e-04

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.60  E-value: 1.61e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 242005460    50 TTNYVLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIWD 89
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
11-46 1.48e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 242005460   11 LQEFIAHEAKVNCLALGQiSGRVLVTGGDDKKVNLW 46
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVW 38
WD40 pfam00400
WD domain, G-beta repeat;
54-89 1.95e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 1.95e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 242005460   54 VLSLNAHTNPVECVKFGHTEEFVCSGSQAGELYIWD 89
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
188-238 1.95e-03

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


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 38.03  E-value: 1.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 242005460  188 GSVLSVEFHPHEFLLASGSSDGTVNFWDLEKFQLVSTTGKGSNSINCLHFT 238
Cdd:pfam12894  39 LEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
11-46 2.41e-03

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: 36.14  E-value: 2.41e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 242005460    11 LQEFIAHEAKVNCLALGQiSGRVLVTGGDDKKVNLW 46
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLW 39
PTZ00420 PTZ00420
coronin; Provisional
101-174 2.67e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 41.09  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242005460 101 GHKDAIKCMDFHP-YGDFLTSGSLDTSIKLWDLRRRG----------CISNyrGHILTVNSVRFSPDGLW-LASGGDDGV 168
Cdd:PTZ00420  72 GHTSSILDLQFNPcFSEILASGSEDLTIRVWEIPHNDesvkeikdpqCILK--GHKKKISIIDWNPMNYYiMCSSGFDSF 149

                 ....*.
gi 242005460 169 VKLWDV 174
Cdd:PTZ00420 150 VNIWDI 155
 
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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