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Conserved domains on  [gi|1102835216|ref|NP_001334102|]
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cytoplasmic dynein 1 intermediate chain 2 isoform 6 [Mus musculus]

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

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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 ...
 380-605 3.84e-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: 79.30  E-value: 3.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 380 HTHPVYCVNVVGTQNahNLISISTDGKICSWSLDMLSHPQDSMelVHKQSKAVAVTSmsfpvGDVNNFVVGSEEGSVY-- 457
Cdd:cd00200     8 HTGGVTCVAFSPDGK--LLATGSGDGTIKVWDLETGELLRTLK--GHTGPVRDVAAS-----ADGTYLASGSSDKTIRlw 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 458 ----TACRHgskagiseMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWS 533
Cdd:cd00200    79 dletGECVR--------TLTGHTSYVSSVAFSPD------GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1102835216 534 PTHPALF-ACVDGMGRLdlWNLNNDTEVPTASISvegNPALNRVRWTHSGREIAVGDSEGQIVIYDV--GEQIAV 605
Cdd:cd00200   145 PDGTFVAsSSQDGTIKL--WDLRTGKCVATLTGH---TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstGKCLGT 214
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
 133-163 1.02e-13

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: 1.02e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1102835216 133 RGPIKLGMAKITQVDFPPREIVTYTKETQTP 163
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
WD40 super family cl43672
WD40 repeat [General function prediction only];
310-413 5.72e-03

WD40 repeat [General function prediction only];


The actual alignment was detected with superfamily member COG2319:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.51  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 310 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFakfHPN--LVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCV 387
Cdd:COG2319   309 DGTVRLWDLATGKLLRTLTGH-TGAVRSVAF---SPDgkTLASGSDDGTVRLWDLATGELLRTLT------GHTGAVTSV 378

                          90       100
                  ....*....|....*....|....*.
gi 1102835216 388 NVvgTQNAHNLISISTDGKICSWSLD 413
Cdd:COG2319   379 AF--SPDGRTLASGSADGTVRLWDLA 402
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 380-605 3.84e-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: 79.30  E-value: 3.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 380 HTHPVYCVNVVGTQNahNLISISTDGKICSWSLDMLSHPQDSMelVHKQSKAVAVTSmsfpvGDVNNFVVGSEEGSVY-- 457
Cdd:cd00200     8 HTGGVTCVAFSPDGK--LLATGSGDGTIKVWDLETGELLRTLK--GHTGPVRDVAAS-----ADGTYLASGSSDKTIRlw 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 458 ----TACRHgskagiseMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWS 533
Cdd:cd00200    79 dletGECVR--------TLTGHTSYVSSVAFSPD------GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1102835216 534 PTHPALF-ACVDGMGRLdlWNLNNDTEVPTASISvegNPALNRVRWTHSGREIAVGDSEGQIVIYDV--GEQIAV 605
Cdd:cd00200   145 PDGTFVAsSSQDGTIKL--WDLRTGKCVATLTGH---TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
310-619 1.47e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.18  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 310 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFAkFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCVNV 389
Cdd:COG2319    57 DLTLLLLDAAAGALLATLLGH-TAAVLSVAFS-PDGRLLASASADGTVRLWDLATGLLLRTLT------GHTGAVRSVAF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 390 vgTQNAHNLISISTDGKICSWSLDmlshpqDSMELVHKQSKAVAVTSMSF-PVGDVnnFVVGSEEGSVYTACRHGSKAGI 468
Cdd:COG2319   129 --SPDGKTLASGSADGTVRLWDLA------TGKLLRTLTGHSGAVTSVAFsPDGKL--LASGSDDGTVRLWDLATGKLLR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 469 SemFEGHQGPITgihchaavgAVDFS---HLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALfACVDG 545
Cdd:COG2319   199 T--LTGHTGAVR---------SVAFSpdgKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLL-ASGSA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 546 MGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDSEGQIVIYDV--GEQIAVPRNDE-------WARFGR 616
Cdd:COG2319   267 DGTVRLWDLATGELLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLatGKLLRTLTGHTgavrsvaFSPDGK 343


                  ...
gi 1102835216 617 TLA 619
Cdd:COG2319   344 TLA 346
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
 133-163 1.02e-13

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: 1.02e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1102835216 133 RGPIKLGMAKITQVDFPPREIVTYTKETQTP 163
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 472-509 3.41e-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: 35.75  E-value: 3.41e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1102835216  472 FEGHQGPITGIHCHaavgavDFSHLFVTSSFDWTVKLW 509
Cdd:smart00320   8 LKGHTGPVTSVAFS------PDGKYLASGSDDGTIKLW 39
WD40 COG2319
WD40 repeat [General function prediction only];
310-413 5.72e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.51  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 310 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFakfHPN--LVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCV 387
Cdd:COG2319   309 DGTVRLWDLATGKLLRTLTGH-TGAVRSVAF---SPDgkTLASGSDDGTVRLWDLATGELLRTLT------GHTGAVTSV 378

                          90       100
                  ....*....|....*....|....*.
gi 1102835216 388 NVvgTQNAHNLISISTDGKICSWSLD 413
Cdd:COG2319   379 AF--SPDGRTLASGSADGTVRLWDLA 402
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 380-605 3.84e-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: 79.30  E-value: 3.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 380 HTHPVYCVNVVGTQNahNLISISTDGKICSWSLDMLSHPQDSMelVHKQSKAVAVTSmsfpvGDVNNFVVGSEEGSVY-- 457
Cdd:cd00200     8 HTGGVTCVAFSPDGK--LLATGSGDGTIKVWDLETGELLRTLK--GHTGPVRDVAAS-----ADGTYLASGSSDKTIRlw 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 458 ----TACRHgskagiseMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWS 533
Cdd:cd00200    79 dletGECVR--------TLTGHTSYVSSVAFSPD------GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1102835216 534 PTHPALF-ACVDGMGRLdlWNLNNDTEVPTASISvegNPALNRVRWTHSGREIAVGDSEGQIVIYDV--GEQIAV 605
Cdd:cd00200   145 PDGTFVAsSSQDGTIKL--WDLRTGKCVATLTGH---TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstGKCLGT 214
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 279-598 4.42e-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: 79.30  E-value: 4.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 279 HR-VVSCLDWSSQYPELLVASYnnneeaphepDGVALVWNMKYKKTTPEYVFHcQSAVMSATFAKFHPNLVVGGtYSGQI 357
Cdd:cd00200     8 HTgGVTCVAFSPDGKLLATGSG----------DGTIKVWDLETGELLRTLKGH-TGPVRDVAASADGTYLASGS-SDKTI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 358 VLWDNRSNKRTpvqRTplsAAAHTHPVYCVNVvgTQNAHNLISISTDGKICSWSLDmlshpqdsmelvhkqsKAVAVTSM 437
Cdd:cd00200    76 RLWDLETGECV---RT---LTGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVE----------------TGKCLTTL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 438 SFPVGDVNNFVVGSEEGSVYTACRHG-------SKAGISEMFEGHQGPITGIHCHAAvgavdfSHLFVTSSFDWTVKLWT 510
Cdd:cd00200   132 RGHTDWVNSVAFSPDGTFVASSSQDGtiklwdlRTGKCVATLTGHTGEVNSVAFSPD------GEKLLSSSSDGTIKLWD 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 511 TKNNKPLYSFEDNSDYVYDVMWSPtHPALFACVDGMGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDS 590
Cdd:cd00200   206 LSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLS---GHTNSVTSLAWSPDGKRLASGSA 281


                  ....*...
gi 1102835216 591 EGQIVIYD 598
Cdd:cd00200   282 DGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
310-619 1.47e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.18  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 310 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFAkFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCVNV 389
Cdd:COG2319    57 DLTLLLLDAAAGALLATLLGH-TAAVLSVAFS-PDGRLLASASADGTVRLWDLATGLLLRTLT------GHTGAVRSVAF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 390 vgTQNAHNLISISTDGKICSWSLDmlshpqDSMELVHKQSKAVAVTSMSF-PVGDVnnFVVGSEEGSVYTACRHGSKAGI 468
Cdd:COG2319   129 --SPDGKTLASGSADGTVRLWDLA------TGKLLRTLTGHSGAVTSVAFsPDGKL--LASGSDDGTVRLWDLATGKLLR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 469 SemFEGHQGPITgihchaavgAVDFS---HLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALfACVDG 545
Cdd:COG2319   199 T--LTGHTGAVR---------SVAFSpdgKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLL-ASGSA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 546 MGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDSEGQIVIYDV--GEQIAVPRNDE-------WARFGR 616
Cdd:COG2319   267 DGTVRLWDLATGELLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLatGKLLRTLTGHTgavrsvaFSPDGK 343


                  ...
gi 1102835216 617 TLA 619
Cdd:COG2319   344 TLA 346
WD40 COG2319
WD40 repeat [General function prediction only];
310-599 2.06e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.80  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 310 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFakfHPN--LVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCV 387
Cdd:COG2319   141 DGTVRLWDLATGKLLRTLTGH-SGAVTSVAF---SPDgkLLASGSDDGTVRLWDLATGKLLRTLT------GHTGAVRSV 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 388 NVvgTQNAHNLISISTDGKICSWSLDmlshpqdSMELVHK-QSKAVAVTSMSF-PVGDVnnFVVGSEEGSVY------TA 459
Cdd:COG2319   211 AF--SPDGKLLASGSADGTVRLWDLA-------TGKLLRTlTGHSGSVRSVAFsPDGRL--LASGSADGTVRlwdlatGE 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 460 CRHgskagiseMFEGHQGPITgihchaavgAVDFS---HLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTH 536
Cdd:COG2319   280 LLR--------TLTGHSGGVN---------SVAFSpdgKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDG 342

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1102835216 537 PALFACVDGmGRLDLWNLNNDTEVPTASisvEGNPALNRVRWTHSGREIAVGDSEGQIVIYDV 599
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 ...
 133-163 1.02e-13

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: 1.02e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1102835216 133 RGPIKLGMAKITQVDFPPREIVTYTKETQTP 163
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 472-509 3.41e-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: 35.75  E-value: 3.41e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1102835216  472 FEGHQGPITGIHCHaavgavDFSHLFVTSSFDWTVKLW 509
Cdd:smart00320   8 LKGHTGPVTSVAFS------PDGKYLASGSDDGTIKLW 39
WD40 COG2319
WD40 repeat [General function prediction only];
310-413 5.72e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.51  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102835216 310 DGVALVWNMKYKKTTPEYVFHcQSAVMSATFakfHPN--LVVGGTYSGQIVLWDNRSNKRTPVQRtplsaaAHTHPVYCV 387
Cdd:COG2319   309 DGTVRLWDLATGKLLRTLTGH-TGAVRSVAF---SPDgkTLASGSDDGTVRLWDLATGELLRTLT------GHTGAVTSV 378

                          90       100
                  ....*....|....*....|....*.
gi 1102835216 388 NVvgTQNAHNLISISTDGKICSWSLD 413
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.
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