NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|311893382|ref|NP_001185805|]
View 

cytoplasmic dynein 1 intermediate chain 2 isoform 5 [Mus musculus]

Protein Classification

cytoplasmic dynein 1 intermediate chain( domain architecture ID 13773840)

cytoplasmic dynein 1 intermediate chain acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 253-572 1.19e-16

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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 80.84  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 253 HR-VVSCLDWSSQYPELLVASYnnneeaphepDGVALVWNMKYKKTTPEYVFHcQSAVMSATFAKFHPNLVVGGtYSGQI 331
Cdd:cd00200    8 HTgGVTCVAFSPDGKLLATGSG----------DGTIKVWDLETGELLRTLKGH-TGPVRDVAASADGTYLASGS-SDKTI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 332 VLWDNRSNKRTpvqRTplsAAAHTHPVYCVNVvgTQNAHNLISISTDGKICSWSLDmlshpqdsmelvhkqsKAVAVTSM 411
Cdd:cd00200   76 RLWDLETGECV---RT---LTGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVE----------------TGKCLTTL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 412 SFPVGDVNNFVVGSEEGSVYTACRHG-------SKAGISEMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVKLWT 484
Cdd:cd00200  132 RGHTDWVNSVAFSPDGTFVASSSQDGtiklwdlRTGKCVATLTGHTGEVNSVAFSPD------GEKLLSSSSDGTIKLWD 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 485 TKNNKPLYSFEDNSDYVYDVMWSPtHPALFACVDGMGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDS 564
Cdd:cd00200  206 LSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLS---GHTNSVTSLAWSPDGKRLASGSA 281


                 ....*...
gi 311893382 565 EGQIVIYD 572
Cdd:cd00200  282 DGTIRIWD 289
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
 107-137 9.77e-14

Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex cytoplasmic dynein 1 along with a heavy chain (HC), two light intermediate chains (LICs) and three light chains (LCs). The complex is responsible for hydrolysing ATP to generate force toward the minus end of microtubules. IC binds to the HC via the N terminal binding domain on the HC and ICs contain binding sites for the LCs. The ICs are responsible for binding to kinetochores and the Golgi apparatus through an interaction with the p150Glued subunit of dynactin which is another complex.


:

Pssm-ID: 463291  Cd Length: 31  Bit Score: 65.26  E-value: 9.77e-14
                          10        20        30
                  ....*....|....*....|....*....|.
gi 311893382  107 RGPIKLGMAKITQVDFPPREIVTYTKETQTP 137
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 253-572 1.19e-16

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: 80.84  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 253 HR-VVSCLDWSSQYPELLVASYnnneeaphepDGVALVWNMKYKKTTPEYVFHcQSAVMSATFAKFHPNLVVGGtYSGQI 331
Cdd:cd00200    8 HTgGVTCVAFSPDGKLLATGSG----------DGTIKVWDLETGELLRTLKGH-TGPVRDVAASADGTYLASGS-SDKTI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 332 VLWDNRSNKRTpvqRTplsAAAHTHPVYCVNVvgTQNAHNLISISTDGKICSWSLDmlshpqdsmelvhkqsKAVAVTSM 411
Cdd:cd00200   76 RLWDLETGECV---RT---LTGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVE----------------TGKCLTTL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 412 SFPVGDVNNFVVGSEEGSVYTACRHG-------SKAGISEMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVKLWT 484
Cdd:cd00200  132 RGHTDWVNSVAFSPDGTFVASSSQDGtiklwdlRTGKCVATLTGHTGEVNSVAFSPD------GEKLLSSSSDGTIKLWD 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 485 TKNNKPLYSFEDNSDYVYDVMWSPtHPALFACVDGMGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDS 564
Cdd:cd00200  206 LSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLS---GHTNSVTSLAWSPDGKRLASGSA 281


                 ....*...
gi 311893382 565 EGQIVIYD 572
Cdd:cd00200  282 DGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
284-593 4.42e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 80.73  E-value: 4.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 284 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFAkFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCVNV 363
Cdd:COG2319   57 DLTLLLLDAAAGALLATLLGH-TAAVLSVAFS-PDGRLLASASADGTVRLWDLATGLLLRTLT------GHTGAVRSVAF 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 364 vgTQNAHNLISISTDGKICSWSLDmlshpqDSMELVHKQSKAVAVTSMSF-PVGDVnnFVVGSEEGSVYTACRHGSKAGI 442
Cdd:COG2319  129 --SPDGKTLASGSADGTVRLWDLA------TGKLLRTLTGHSGAVTSVAFsPDGKL--LASGSDDGTVRLWDLATGKLLR 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 443 SemFEGHQGPITgihchaavgAVDFS---HLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALfACVDG 519
Cdd:COG2319  199 T--LTGHTGAVR---------SVAFSpdgKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLL-ASGSA 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 520 MGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDSEGQIVIYDV--GEQIAVPRNDE-------WARFGR 590
Cdd:COG2319  267 DGTVRLWDLATGELLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLatGKLLRTLTGHTgavrsvaFSPDGK 343


                 ...
gi 311893382 591 TLA 593
Cdd:COG2319  344 TLA 346
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
 107-137 9.77e-14

Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex cytoplasmic dynein 1 along with a heavy chain (HC), two light intermediate chains (LICs) and three light chains (LCs). The complex is responsible for hydrolysing ATP to generate force toward the minus end of microtubules. IC binds to the HC via the N terminal binding domain on the HC and ICs contain binding sites for the LCs. The ICs are responsible for binding to kinetochores and the Golgi apparatus through an interaction with the p150Glued subunit of dynactin which is another complex.


Pssm-ID: 463291  Cd Length: 31  Bit Score: 65.26  E-value: 9.77e-14
                          10        20        30
                  ....*....|....*....|....*....|.
gi 311893382  107 RGPIKLGMAKITQVDFPPREIVTYTKETQTP 137
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 446-483 2.12e-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: 2.12e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 311893382   446 FEGHQGPITGIHCHaavgavDFSHLFVTSSFDWTVKLW 483
Cdd:smart00320   8 LKGHTGPVTSVAFS------PDGKYLASGSDDGTIKLW 39
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 253-572 1.19e-16

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: 80.84  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 253 HR-VVSCLDWSSQYPELLVASYnnneeaphepDGVALVWNMKYKKTTPEYVFHcQSAVMSATFAKFHPNLVVGGtYSGQI 331
Cdd:cd00200    8 HTgGVTCVAFSPDGKLLATGSG----------DGTIKVWDLETGELLRTLKGH-TGPVRDVAASADGTYLASGS-SDKTI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 332 VLWDNRSNKRTpvqRTplsAAAHTHPVYCVNVvgTQNAHNLISISTDGKICSWSLDmlshpqdsmelvhkqsKAVAVTSM 411
Cdd:cd00200   76 RLWDLETGECV---RT---LTGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVE----------------TGKCLTTL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 412 SFPVGDVNNFVVGSEEGSVYTACRHG-------SKAGISEMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVKLWT 484
Cdd:cd00200  132 RGHTDWVNSVAFSPDGTFVASSSQDGtiklwdlRTGKCVATLTGHTGEVNSVAFSPD------GEKLLSSSSDGTIKLWD 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 485 TKNNKPLYSFEDNSDYVYDVMWSPtHPALFACVDGMGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDS 564
Cdd:cd00200  206 LSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLS---GHTNSVTSLAWSPDGKRLASGSA 281


                 ....*...
gi 311893382 565 EGQIVIYD 572
Cdd:cd00200  282 DGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 354-579 1.25e-16

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: 80.84  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 354 HTHPVYCVNVVGTQNahNLISISTDGKICSWSLDMLSHPQDSMelVHKQSKAVAVTSmsfpvGDVNNFVVGSEEGSVY-- 431
Cdd:cd00200    8 HTGGVTCVAFSPDGK--LLATGSGDGTIKVWDLETGELLRTLK--GHTGPVRDVAAS-----ADGTYLASGSSDKTIRlw 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 432 ----TACRHgskagiseMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWS 507
Cdd:cd00200   79 dletGECVR--------TLTGHTSYVSSVAFSPD------GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311893382 508 PTHPALF-ACVDGMGRLdlWNLNNDTEVPTASISvegNPALNRVRWTHSGREIAVGDSEGQIVIYDV--GEQIAV 579
Cdd:cd00200  145 PDGTFVAsSSQDGTIKL--WDLRTGKCVATLTGH---TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
284-593 4.42e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 80.73  E-value: 4.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 284 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFAkFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCVNV 363
Cdd:COG2319   57 DLTLLLLDAAAGALLATLLGH-TAAVLSVAFS-PDGRLLASASADGTVRLWDLATGLLLRTLT------GHTGAVRSVAF 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 364 vgTQNAHNLISISTDGKICSWSLDmlshpqDSMELVHKQSKAVAVTSMSF-PVGDVnnFVVGSEEGSVYTACRHGSKAGI 442
Cdd:COG2319  129 --SPDGKTLASGSADGTVRLWDLA------TGKLLRTLTGHSGAVTSVAFsPDGKL--LASGSDDGTVRLWDLATGKLLR 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 443 SemFEGHQGPITgihchaavgAVDFS---HLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALfACVDG 519
Cdd:COG2319  199 T--LTGHTGAVR---------SVAFSpdgKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLL-ASGSA 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 520 MGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDSEGQIVIYDV--GEQIAVPRNDE-------WARFGR 590
Cdd:COG2319  267 DGTVRLWDLATGELLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLatGKLLRTLTGHTgavrsvaFSPDGK 343


                 ...
gi 311893382 591 TLA 593
Cdd:COG2319  344 TLA 346
WD40 COG2319
WD40 repeat [General function prediction only];
284-573 6.12e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 80.34  E-value: 6.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 284 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFakfHPN--LVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCV 361
Cdd:COG2319  141 DGTVRLWDLATGKLLRTLTGH-SGAVTSVAF---SPDgkLLASGSDDGTVRLWDLATGKLLRTLT------GHTGAVRSV 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 362 NVvgTQNAHNLISISTDGKICSWSLDmlshpqdSMELVHK-QSKAVAVTSMSF-PVGDVnnFVVGSEEGSVY------TA 433
Cdd:COG2319  211 AF--SPDGKLLASGSADGTVRLWDLA-------TGKLLRTlTGHSGSVRSVAFsPDGRL--LASGSADGTVRlwdlatGE 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 434 CRHgskagiseMFEGHQGPITgihchaavgAVDFS---HLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTH 510
Cdd:COG2319  280 LLR--------TLTGHSGGVN---------SVAFSpdgKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDG 342

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311893382 511 PALFACVDGmGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDSEGQIVIYDV 573
Cdd:COG2319  343 KTLASGSDD-GTVRLWDLATGELLRTLT---GHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
 107-137 9.77e-14

Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex cytoplasmic dynein 1 along with a heavy chain (HC), two light intermediate chains (LICs) and three light chains (LCs). The complex is responsible for hydrolysing ATP to generate force toward the minus end of microtubules. IC binds to the HC via the N terminal binding domain on the HC and ICs contain binding sites for the LCs. The ICs are responsible for binding to kinetochores and the Golgi apparatus through an interaction with the p150Glued subunit of dynactin which is another complex.


Pssm-ID: 463291  Cd Length: 31  Bit Score: 65.26  E-value: 9.77e-14
                          10        20        30
                  ....*....|....*....|....*....|.
gi 311893382  107 RGPIKLGMAKITQVDFPPREIVTYTKETQTP 137
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 446-483 2.12e-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: 2.12e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 311893382   446 FEGHQGPITGIHCHaavgavDFSHLFVTSSFDWTVKLW 483
Cdd:smart00320   8 LKGHTGPVTSVAFS------PDGKYLASGSDDGTIKLW 39
WD40 COG2319
WD40 repeat [General function prediction only];
284-387 3.33e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.28  E-value: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893382 284 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFakfHPN--LVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCV 361
Cdd:COG2319  309 DGTVRLWDLATGKLLRTLTGH-TGAVRSVAF---SPDgkTLASGSDDGTVRLWDLATGELLRTLT------GHTGAVTSV 378

                         90       100
                 ....*....|....*....|....*.
gi 311893382 362 NVvgTQNAHNLISISTDGKICSWSLD 387
Cdd:COG2319  379 AF--SPDGRTLASGSADGTVRLWDLA 402
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH