NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4758178|ref|NP_004402|]
View 

cytoplasmic dynein 1 intermediate chain 1 isoform a [Homo sapiens]

Protein Classification

cytoplasmic dynein 1 intermediate chain( domain architecture ID 12110212)

cytoplasmic dynein 1 intermediate chain is a non-catalytic accessory component of the cytoplasmic dynein 1 complex and may 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 COG2319
WD40 repeat [General function prediction only];
318-607 8.74e-17

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 8.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  318 DGVALVWNMKFKKTTPEYVFHcQSSVMSVcfaRFHPN--LVVGGTYSGQIVLWDnrshRRTPVQRTPLSAaaHTHPVYCV 395
Cdd:COG2319 141 DGTVRLWDLATGKLLRTLTGH-SGAVTSV---AFSPDgkLLASGSDDGTVRLWD----LATGKLLRTLTG--HTGAVRSV 210
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  396 NVvgTQNAHNLITVSTDGKMCSWSLDmlsTPQESMELvynKSKPVAVTGMAF-PTGDVnnFVVGSEEGTVY------TAC 468
Cdd:COG2319 211 AF--SPDGKLLASGSADGTVRLWDLA---TGKLLRTL---TGHSGSVRSVAFsPDGRL--LASGSADGTVRlwdlatGEL 280
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  469 RHgskagigeVFEGHQGPVTGInchmavgpiDFS---HLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHP 545
Cdd:COG2319 281 LR--------TLTGHSGGVNSV---------AFSpdgKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGK 343
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758178  546 ALFACVDGmGRLDLWNLNNDTEVPTASvaiEGASALNRVRWAQAGKEVAVGDSEGRIWVYDV 607
Cdd:COG2319 344 TLASGSDD-GTVRLWDLATGELLRTLT---GHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
143-173 9.25e-12

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: 59.48  E-value: 9.25e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4758178    143 RRLHKLGVSKVTQVDFLPREVVSYSKETQTP 173
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
318-607 8.74e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 8.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  318 DGVALVWNMKFKKTTPEYVFHcQSSVMSVcfaRFHPN--LVVGGTYSGQIVLWDnrshRRTPVQRTPLSAaaHTHPVYCV 395
Cdd:COG2319 141 DGTVRLWDLATGKLLRTLTGH-SGAVTSV---AFSPDgkLLASGSDDGTVRLWD----LATGKLLRTLTG--HTGAVRSV 210
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  396 NVvgTQNAHNLITVSTDGKMCSWSLDmlsTPQESMELvynKSKPVAVTGMAF-PTGDVnnFVVGSEEGTVY------TAC 468
Cdd:COG2319 211 AF--SPDGKLLASGSADGTVRLWDLA---TGKLLRTL---TGHSGSVRSVAFsPDGRL--LASGSADGTVRlwdlatGEL 280
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  469 RHgskagigeVFEGHQGPVTGInchmavgpiDFS---HLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHP 545
Cdd:COG2319 281 LR--------TLTGHSGGVNSV---------AFSpdgKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGK 343
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758178  546 ALFACVDGmGRLDLWNLNNDTEVPTASvaiEGASALNRVRWAQAGKEVAVGDSEGRIWVYDV 607
Cdd:COG2319 344 TLASGSDD-GTVRLWDLATGELLRTLT---GHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
283-606 7.15e-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: 78.53  E-value: 7.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  283 HWSKHR-VVTCMDWSLQYPELMVASYnnnedaphepDGVALVWNMKFKKTTPEYVFHcQSSVMSVCFARFHPNLVVGGtY 361
Cdd:cd00200   4 TLKGHTgGVTCVAFSPDGKLLATGSG----------DGTIKVWDLETGELLRTLKGH-TGPVRDVAASADGTYLASGS-S 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  362 SGQIVLWDnrshRRTPVQRTPLsaAAHTHPVYCVNVvgTQNAHNLITVSTDGKMCSWSLDmlstpqesmelvynKSKPVA 441
Cdd:cd00200  72 DKTIRLWD----LETGECVRTL--TGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVE--------------TGKCLT 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  442 VtgMAFPTGDVNNFVVGSEEGTVYTACRHG-------SKAGIGEVFEGHQGPVTGINCHmavgPIDFShlFVTSSFDWTV 514
Cdd:cd00200 130 T--LRGHTDWVNSVAFSPDGTFVASSSQDGtiklwdlRTGKCVATLTGHTGEVNSVAFS----PDGEK--LLSSSSDGTI 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  515 KLWTTKHNKPLYSFEDNADYVYDVMWSPvHPALFACVDGMGRLDLWNLNNDTEVPTasvaIEG-ASALNRVRWAQAGKEV 593
Cdd:cd00200 202 KLWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQT----LSGhTNSVTSLAWSPDGKRL 276
                       330
                ....*....|...
gi 4758178  594 AVGDSEGRIWVYD 606
Cdd:cd00200 277 ASGSADGTIRIWD 289
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
143-173 9.25e-12

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: 59.48  E-value: 9.25e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4758178    143 RRLHKLGVSKVTQVDFLPREVVSYSKETQTP 173
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
507-613 1.70e-03

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 41.61  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178   507 TSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNNDTEVPTasvaIEGASALNRVRW 586
Cdd:PLN00181 550 SSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGT----IKTKANICCVQF 625
                         90       100
                 ....*....|....*....|....*...
gi 4758178   587 -AQAGKEVAVGDSEGRIWVYDVGELAVP 613
Cdd:PLN00181 626 pSESGRSLAFGSADHKVYYYDLRNPKLP 653
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
479-517 2.26e-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: 2.26e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4758178     479 VFEGHQGPVTGINCHmavgpiDFSHLFVTSSFDWTVKLW 517
Cdd:smart00320   7 TLKGHTGPVTSVAFS------PDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
479-517 7.18e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.63  E-value: 7.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 4758178    479 VFEGHQGPVTGINCHmavgpiDFSHLFVTSSFDWTVKLW 517
Cdd:pfam00400   6 TLEGHTGSVTSLAFS------PDGKLLASGSDDGTVKVW 38
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
318-607 8.74e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 8.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  318 DGVALVWNMKFKKTTPEYVFHcQSSVMSVcfaRFHPN--LVVGGTYSGQIVLWDnrshRRTPVQRTPLSAaaHTHPVYCV 395
Cdd:COG2319 141 DGTVRLWDLATGKLLRTLTGH-SGAVTSV---AFSPDgkLLASGSDDGTVRLWD----LATGKLLRTLTG--HTGAVRSV 210
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  396 NVvgTQNAHNLITVSTDGKMCSWSLDmlsTPQESMELvynKSKPVAVTGMAF-PTGDVnnFVVGSEEGTVY------TAC 468
Cdd:COG2319 211 AF--SPDGKLLASGSADGTVRLWDLA---TGKLLRTL---TGHSGSVRSVAFsPDGRL--LASGSADGTVRlwdlatGEL 280
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  469 RHgskagigeVFEGHQGPVTGInchmavgpiDFS---HLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHP 545
Cdd:COG2319 281 LR--------TLTGHSGGVNSV---------AFSpdgKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGK 343
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758178  546 ALFACVDGmGRLDLWNLNNDTEVPTASvaiEGASALNRVRWAQAGKEVAVGDSEGRIWVYDV 607
Cdd:COG2319 344 TLASGSDD-GTVRLWDLATGELLRTLT---GHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
283-606 7.15e-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: 78.53  E-value: 7.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  283 HWSKHR-VVTCMDWSLQYPELMVASYnnnedaphepDGVALVWNMKFKKTTPEYVFHcQSSVMSVCFARFHPNLVVGGtY 361
Cdd:cd00200   4 TLKGHTgGVTCVAFSPDGKLLATGSG----------DGTIKVWDLETGELLRTLKGH-TGPVRDVAASADGTYLASGS-S 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  362 SGQIVLWDnrshRRTPVQRTPLsaAAHTHPVYCVNVvgTQNAHNLITVSTDGKMCSWSLDmlstpqesmelvynKSKPVA 441
Cdd:cd00200  72 DKTIRLWD----LETGECVRTL--TGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVE--------------TGKCLT 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  442 VtgMAFPTGDVNNFVVGSEEGTVYTACRHG-------SKAGIGEVFEGHQGPVTGINCHmavgPIDFShlFVTSSFDWTV 514
Cdd:cd00200 130 T--LRGHTDWVNSVAFSPDGTFVASSSQDGtiklwdlRTGKCVATLTGHTGEVNSVAFS----PDGEK--LLSSSSDGTI 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  515 KLWTTKHNKPLYSFEDNADYVYDVMWSPvHPALFACVDGMGRLDLWNLNNDTEVPTasvaIEG-ASALNRVRWAQAGKEV 593
Cdd:cd00200 202 KLWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQT----LSGhTNSVTSLAWSPDGKRL 276
                       330
                ....*....|...
gi 4758178  594 AVGDSEGRIWVYD 606
Cdd:cd00200 277 ASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
318-614 1.90e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.80  E-value: 1.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  318 DGVALVWNMKFKKTTPEYVFHcQSSVMSVCFARFHPNLVVGGtYSGQIVLWDNRSHRRTPVQRtplsaaAHTHPVYCVNV 397
Cdd:COG2319  57 DLTLLLLDAAAGALLATLLGH-TAAVLSVAFSPDGRLLASAS-ADGTVRLWDLATGLLLRTLT------GHTGAVRSVAF 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  398 vgTQNAHNLITVSTDGKMCSWSLDmlsTPQESMELvynKSKPVAVTGMAF-PTGDVnnFVVGSEEGTVYTACRHGSKAGi 476
Cdd:COG2319 129 --SPDGKTLASGSADGTVRLWDLA---TGKLLRTL---TGHSGAVTSVAFsPDGKL--LASGSDDGTVRLWDLATGKLL- 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  477 gEVFEGHQGPVTGInchmAVGPiDfSHLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALfACVDGMGR 556
Cdd:COG2319 198 -RTLTGHTGAVRSV----AFSP-D-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLL-ASGSADGT 269
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4758178  557 LDLWNLNNDTEVPTASvaiEGASALNRVRWAQAGKEVAVGDSEGRIWVYDVGELAVPH 614
Cdd:COG2319 270 VRLWDLATGELLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR 324
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
341-607 6.48e-13

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: 69.67  E-value: 6.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  341 SSVMSVCFARFHPNLVVGGtYSGQIVLWD--NRSHRRTPVQrtplsaaaHTHPVYCVNVVGtqNAHNLITVSTDGKMCSW 418
Cdd:cd00200  10 GGVTCVAFSPDGKLLATGS-GDGTIKVWDleTGELLRTLKG--------HTGPVRDVAASA--DGTYLASGSSDKTIRLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  419 SLdmlSTPQESMELVYNKSkpvAVTGMAF-PTGDVnnFVVGSEEGTVytACRHGSKAGIGEVFEGHQGPVtginchMAVG 497
Cdd:cd00200  79 DL---ETGECVRTLTGHTS---YVSSVAFsPDGRI--LSSSSRDKTI--KVWDVETGKCLTTLRGHTDWV------NSVA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  498 PIDFSHLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGmGRLDLWNLNNDTEVPTasvaIEG 577
Cdd:cd00200 143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSD-GTIKLWDLSTGKCLGT----LRG 217
                       250       260       270
                ....*....|....*....|....*....|.
gi 4758178  578 -ASALNRVRWAQAGKEVAVGDSEGRIWVYDV 607
Cdd:cd00200 218 hENGVNSVAFSPDGYLLASGSEDGTIRVWDL 248
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
143-173 9.25e-12

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: 59.48  E-value: 9.25e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4758178    143 RRLHKLGVSKVTQVDFLPREVVSYSKETQTP 173
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
436-607 1.14e-09

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: 60.04  E-value: 1.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  436 KSKPVAVTGMAFpTGDVNNFVVGSEEGTVYTACRHGSKAGIgeVFEGHQGPVTGINChmavgpIDFSHLFVTSSFDWTVK 515
Cdd:cd00200   6 KGHTGGVTCVAF-SPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAA------SADGTYLASGSSDKTIR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178  516 LWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFAC-VDgmGRLDLWNLNNDTEVPTasvaIEGASA-LNRVRWAQAGKEV 593
Cdd:cd00200  77 LWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSsRD--KTIKVWDVETGKCLTT----LRGHTDwVNSVAFSPDGTFV 150
                       170
                ....*....|....
gi 4758178  594 AVGDSEGRIWVYDV 607
Cdd:cd00200 151 ASSSQDGTIKLWDL 164
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
507-613 1.70e-03

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 41.61  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758178   507 TSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNNDTEVPTasvaIEGASALNRVRW 586
Cdd:PLN00181 550 SSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGT----IKTKANICCVQF 625
                         90       100
                 ....*....|....*....|....*...
gi 4758178   587 -AQAGKEVAVGDSEGRIWVYDVGELAVP 613
Cdd:PLN00181 626 pSESGRSLAFGSADHKVYYYDLRNPKLP 653
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
479-517 2.26e-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: 2.26e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4758178     479 VFEGHQGPVTGINCHmavgpiDFSHLFVTSSFDWTVKLW 517
Cdd:smart00320   7 TLKGHTGPVTSVAFS------PDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
479-517 7.18e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.63  E-value: 7.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 4758178    479 VFEGHQGPVTGINCHmavgpiDFSHLFVTSSFDWTVKLW 517
Cdd:pfam00400   6 TLEGHTGSVTSLAFS------PDGKLLASGSDDGTVKVW 38
 
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