NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|311893380|ref|NP_001185804|]
View 

cytoplasmic dynein 1 intermediate chain 2 isoform 4 [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 ...
 256-578 1.48e-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: 80.46  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 256 WSKHR-VVSCLDWSSQYPELLVASYnnneeaphepDGVALVWNMKYKKTTPEYVFHcQSAVMSATFAKFHPNLVVGGtYS 334
Cdd:cd00200    5 LKGHTgGVTCVAFSPDGKLLATGSG----------DGTIKVWDLETGELLRTLKGH-TGPVRDVAASADGTYLASGS-SD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 335 GQIVLWDNRSNKRTpvqRTplsAAAHTHPVYCVNVvgTQNAHNLISISTDGKICSWSLDmlshpqdsmelvhkqsKAVAV 414
Cdd:cd00200   73 KTIRLWDLETGECV---RT---LTGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVE----------------TGKCL 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 415 TSMSFPVGDVNNFVVGSEEGSVYTACRHG-------SKAGISEMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVK 487
Cdd:cd00200  129 TTLRGHTDWVNSVAFSPDGTFVASSSQDGtiklwdlRTGKCVATLTGHTGEVNSVAFSPD------GEKLLSSSSDGTIK 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 488 LWTTKNNKPLYSFEDNSDYVYDVMWSPtHPALFACVDGMGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAV 567
Cdd:cd00200  203 LWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLS---GHTNSVTSLAWSPDGKRLAS 278

                        330
                 ....*....|.
gi 311893380 568 GDSEGQIVIYD 578
Cdd:cd00200  279 GSADGTIRIWD 289
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
 113-143 9.86e-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: 9.86e-14
                          10        20        30
                  ....*....|....*....|....*....|.
gi 311893380  113 RGPIKLGMAKITQVDFPPREIVTYTKETQTP 143
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 ...
 256-578 1.48e-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: 80.46  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 256 WSKHR-VVSCLDWSSQYPELLVASYnnneeaphepDGVALVWNMKYKKTTPEYVFHcQSAVMSATFAKFHPNLVVGGtYS 334
Cdd:cd00200    5 LKGHTgGVTCVAFSPDGKLLATGSG----------DGTIKVWDLETGELLRTLKGH-TGPVRDVAASADGTYLASGS-SD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 335 GQIVLWDNRSNKRTpvqRTplsAAAHTHPVYCVNVvgTQNAHNLISISTDGKICSWSLDmlshpqdsmelvhkqsKAVAV 414
Cdd:cd00200   73 KTIRLWDLETGECV---RT---LTGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVE----------------TGKCL 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 415 TSMSFPVGDVNNFVVGSEEGSVYTACRHG-------SKAGISEMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVK 487
Cdd:cd00200  129 TTLRGHTDWVNSVAFSPDGTFVASSSQDGtiklwdlRTGKCVATLTGHTGEVNSVAFSPD------GEKLLSSSSDGTIK 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 488 LWTTKNNKPLYSFEDNSDYVYDVMWSPtHPALFACVDGMGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAV 567
Cdd:cd00200  203 LWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLS---GHTNSVTSLAWSPDGKRLAS 278

                        330
                 ....*....|.
gi 311893380 568 GDSEGQIVIYD 578
Cdd:cd00200  279 GSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
290-599 4.80e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 80.34  E-value: 4.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 290 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFAkFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCVNV 369
Cdd:COG2319   57 DLTLLLLDAAAGALLATLLGH-TAAVLSVAFS-PDGRLLASASADGTVRLWDLATGLLLRTLT------GHTGAVRSVAF 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 370 vgTQNAHNLISISTDGKICSWSLDmlshpqDSMELVHKQSKAVAVTSMSF-PVGDVnnFVVGSEEGSVYTACRHGSKAGI 448
Cdd:COG2319  129 --SPDGKTLASGSADGTVRLWDLA------TGKLLRTLTGHSGAVTSVAFsPDGKL--LASGSDDGTVRLWDLATGKLLR 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 449 SemFEGHQGPITgihchaavgAVDFS---HLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALfACVDG 525
Cdd:COG2319  199 T--LTGHTGAVR---------SVAFSpdgKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLL-ASGSA 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 526 MGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDSEGQIVIYDV--GEQIAVPRNDE-------WARFGR 596
Cdd:COG2319  267 DGTVRLWDLATGELLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLatGKLLRTLTGHTgavrsvaFSPDGK 343


                 ...
gi 311893380 597 TLA 599
Cdd:COG2319  344 TLA 346
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
 113-143 9.86e-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: 9.86e-14
                          10        20        30
                  ....*....|....*....|....*....|.
gi 311893380  113 RGPIKLGMAKITQVDFPPREIVTYTKETQTP 143
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 452-489 2.46e-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: 2.46e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 311893380   452 FEGHQGPITGIHCHaavgavDFSHLFVTSSFDWTVKLW 489
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 ...
 256-578 1.48e-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: 80.46  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 256 WSKHR-VVSCLDWSSQYPELLVASYnnneeaphepDGVALVWNMKYKKTTPEYVFHcQSAVMSATFAKFHPNLVVGGtYS 334
Cdd:cd00200    5 LKGHTgGVTCVAFSPDGKLLATGSG----------DGTIKVWDLETGELLRTLKGH-TGPVRDVAASADGTYLASGS-SD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 335 GQIVLWDNRSNKRTpvqRTplsAAAHTHPVYCVNVvgTQNAHNLISISTDGKICSWSLDmlshpqdsmelvhkqsKAVAV 414
Cdd:cd00200   73 KTIRLWDLETGECV---RT---LTGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVE----------------TGKCL 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 415 TSMSFPVGDVNNFVVGSEEGSVYTACRHG-------SKAGISEMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVK 487
Cdd:cd00200  129 TTLRGHTDWVNSVAFSPDGTFVASSSQDGtiklwdlRTGKCVATLTGHTGEVNSVAFSPD------GEKLLSSSSDGTIK 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 488 LWTTKNNKPLYSFEDNSDYVYDVMWSPtHPALFACVDGMGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAV 567
Cdd:cd00200  203 LWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLS---GHTNSVTSLAWSPDGKRLAS 278

                        330
                 ....*....|.
gi 311893380 568 GDSEGQIVIYD 578
Cdd:cd00200  279 GSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 360-585 1.66e-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: 80.46  E-value: 1.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 360 HTHPVYCVNVVGTQNahNLISISTDGKICSWSLDMLSHPQDSMelVHKQSKAVAVTSmsfpvGDVNNFVVGSEEGSVY-- 437
Cdd:cd00200    8 HTGGVTCVAFSPDGK--LLATGSGDGTIKVWDLETGELLRTLK--GHTGPVRDVAAS-----ADGTYLASGSSDKTIRlw 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 438 ----TACRHgskagiseMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWS 513
Cdd:cd00200   79 dletGECVR--------TLTGHTSYVSSVAFSPD------GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311893380 514 PTHPALF-ACVDGMGRLdlWNLNNDTEVPTASISvegNPALNRVRWTHSGREIAVGDSEGQIVIYDV--GEQIAV 585
Cdd:cd00200  145 PDGTFVAsSSQDGTIKL--WDLRTGKCVATLTGH---TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
290-599 4.80e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 80.34  E-value: 4.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 290 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFAkFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCVNV 369
Cdd:COG2319   57 DLTLLLLDAAAGALLATLLGH-TAAVLSVAFS-PDGRLLASASADGTVRLWDLATGLLLRTLT------GHTGAVRSVAF 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 370 vgTQNAHNLISISTDGKICSWSLDmlshpqDSMELVHKQSKAVAVTSMSF-PVGDVnnFVVGSEEGSVYTACRHGSKAGI 448
Cdd:COG2319  129 --SPDGKTLASGSADGTVRLWDLA------TGKLLRTLTGHSGAVTSVAFsPDGKL--LASGSDDGTVRLWDLATGKLLR 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 449 SemFEGHQGPITgihchaavgAVDFS---HLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALfACVDG 525
Cdd:COG2319  199 T--LTGHTGAVR---------SVAFSpdgKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLL-ASGSA 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 526 MGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDSEGQIVIYDV--GEQIAVPRNDE-------WARFGR 596
Cdd:COG2319  267 DGTVRLWDLATGELLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLatGKLLRTLTGHTgavrsvaFSPDGK 343


                 ...
gi 311893380 597 TLA 599
Cdd:COG2319  344 TLA 346
WD40 COG2319
WD40 repeat [General function prediction only];
290-579 6.51e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.96  E-value: 6.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 290 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFakfHPN--LVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCV 367
Cdd:COG2319  141 DGTVRLWDLATGKLLRTLTGH-SGAVTSVAF---SPDgkLLASGSDDGTVRLWDLATGKLLRTLT------GHTGAVRSV 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 368 NVvgTQNAHNLISISTDGKICSWSLDmlshpqdSMELVHK-QSKAVAVTSMSF-PVGDVnnFVVGSEEGSVY------TA 439
Cdd:COG2319  211 AF--SPDGKLLASGSADGTVRLWDLA-------TGKLLRTlTGHSGSVRSVAFsPDGRL--LASGSADGTVRlwdlatGE 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 440 CRHgskagiseMFEGHQGPITgihchaavgAVDFS---HLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTH 516
Cdd:COG2319  280 LLR--------TLTGHSGGVN---------SVAFSpdgKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDG 342

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311893380 517 PALFACVDGmGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDSEGQIVIYDV 579
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 ...
 113-143 9.86e-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: 9.86e-14
                          10        20        30
                  ....*....|....*....|....*....|.
gi 311893380  113 RGPIKLGMAKITQVDFPPREIVTYTKETQTP 143
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 452-489 2.46e-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: 2.46e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 311893380   452 FEGHQGPITGIHCHaavgavDFSHLFVTSSFDWTVKLW 489
Cdd:smart00320   8 LKGHTGPVTSVAFS------PDGKYLASGSDDGTIKLW 39
WD40 COG2319
WD40 repeat [General function prediction only];
290-393 3.50e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.28  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893380 290 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFakfHPN--LVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCV 367
Cdd:COG2319  309 DGTVRLWDLATGKLLRTLTGH-TGAVRSVAF---SPDgkTLASGSDDGTVRLWDLATGELLRTLT------GHTGAVTSV 378

                         90       100
                 ....*....|....*....|....*.
gi 311893380 368 NVvgTQNAHNLISISTDGKICSWSLD 393
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