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Conserved domains on  [gi|22831379|gb|AAF45366|]
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Sperm-specific dynein intermediate chain 1, isoform A [Drosophila melanogaster]

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

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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 ...
 196-445 6.25e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 69.29  E-value: 6.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 196 ITSMDWSTHFPELVVGSYhnneespnepDGVVMVWN--TKFKKSTPEDVFHCQSAVMSTCFAKFnpnlILGGTYSGQIVL 273
Cdd:cd00200  12 VTCVAFSPDGKLLATGSG----------DGTIKVWDleTGELLRTLKGHTGPVRDVAASADGTY----LASGSSDKTIRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 274 WDnrVQKRTPIQRtplsAAAHTHPVYCLQMvgTQNAHNVISISSDGKLCSWSLDMlSQPQDTLELQQRQskaiaitsmaf 353
Cdd:cd00200  78 WD--LETGECVRT----LTGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVET-GKCLTTLRGHTDW----------- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 354 paneINSLVMGSEDGYVYSASRHG------LRSG-VNEVYERHLGPITGISthynqLSPDfGHLFLTSSIDWTIKLWSLK 426
Cdd:cd00200 138 ----VNSVAFSPDGTFVASSSQDGtiklwdLRTGkCVATLTGHTGEVNSVA-----FSPD-GEKLLSSSSDGTIKLWDLS 207

                       250       260
                ....*....|....*....|....*
gi 22831379 427 DTKPLYSFE------QYIAWSPVRR 445
Cdd:cd00200 208 TGKCLGTLRghengvNSVAFSPDGY 232
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
 21-51 1.05e-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: 62.18  E-value: 1.05e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 22831379    21 KQPLNLSVYNVQATNIPPKETLVYTKQTQTT 51
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 ...
 196-445 6.25e-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: 69.29  E-value: 6.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 196 ITSMDWSTHFPELVVGSYhnneespnepDGVVMVWN--TKFKKSTPEDVFHCQSAVMSTCFAKFnpnlILGGTYSGQIVL 273
Cdd:cd00200  12 VTCVAFSPDGKLLATGSG----------DGTIKVWDleTGELLRTLKGHTGPVRDVAASADGTY----LASGSSDKTIRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 274 WDnrVQKRTPIQRtplsAAAHTHPVYCLQMvgTQNAHNVISISSDGKLCSWSLDMlSQPQDTLELQQRQskaiaitsmaf 353
Cdd:cd00200  78 WD--LETGECVRT----LTGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVET-GKCLTTLRGHTDW----------- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 354 paneINSLVMGSEDGYVYSASRHG------LRSG-VNEVYERHLGPITGISthynqLSPDfGHLFLTSSIDWTIKLWSLK 426
Cdd:cd00200 138 ----VNSVAFSPDGTFVASSSQDGtiklwdLRTGkCVATLTGHTGEVNSVA-----FSPD-GEKLLSSSSDGTIKLWDLS 207

                       250       260
                ....*....|....*....|....*
gi 22831379 427 DTKPLYSFE------QYIAWSPVRR 445
Cdd:cd00200 208 TGKCLGTLRghengvNSVAFSPDGY 232
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
 21-51 1.05e-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: 62.18  E-value: 1.05e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 22831379    21 KQPLNLSVYNVQATNIPPKETLVYTKQTQTT 51
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
WD40 COG2319
WD40 repeat [General function prediction only];
196-427 8.01e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.78  E-value: 8.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 196 ITSMDWSthfPE---LVVGSYhnneespnepDGVVMVWNTKfkksTPEDVF---HCQSAVMStcfAKFNPN--LILGGTY 267
Cdd:COG2319 207 VRSVAFS---PDgklLASGSA----------DGTVRLWDLA----TGKLLRtltGHSGSVRS---VAFSPDgrLLASGSA 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 268 SGQIVLWDnrVQKRTPIQRTPlsaaAHTHPVYCLQMvgTQNAHNVISISSDGKLCSWSLDmlsqpqDTLELQQRQSKAIA 347
Cdd:COG2319 267 DGTVRLWD--LATGELLRTLT----GHSGGVNSVAF--SPDGKLLASGSDDGTVRLWDLA------TGKLLRTLTGHTGA 332

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 348 ITSMAFPANEiNSLVMGSEDG--YVYSASRHGLRsgvnEVYERHLGPITGISthynqLSPDfGHLFLTSSIDWTIKLWSL 425
Cdd:COG2319 333 VRSVAFSPDG-KTLASGSDDGtvRLWDLATGELL----RTLTGHTGAVTSVA-----FSPD-GRTLASGSADGTVRLWDL 401


                ..
gi 22831379 426 KD 427
Cdd:COG2319 402 AT 403
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 385-424 8.50e-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: 34.21  E-value: 8.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 22831379    385 VYERHLGPITGISthynqLSPDfGHLFLTSSIDWTIKLWS 424
Cdd:smart00320   7 TLKGHTGPVTSVA-----FSPD-GKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 196-445 6.25e-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: 69.29  E-value: 6.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 196 ITSMDWSTHFPELVVGSYhnneespnepDGVVMVWN--TKFKKSTPEDVFHCQSAVMSTCFAKFnpnlILGGTYSGQIVL 273
Cdd:cd00200  12 VTCVAFSPDGKLLATGSG----------DGTIKVWDleTGELLRTLKGHTGPVRDVAASADGTY----LASGSSDKTIRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 274 WDnrVQKRTPIQRtplsAAAHTHPVYCLQMvgTQNAHNVISISSDGKLCSWSLDMlSQPQDTLELQQRQskaiaitsmaf 353
Cdd:cd00200  78 WD--LETGECVRT----LTGHTSYVSSVAF--SPDGRILSSSSRDKTIKVWDVET-GKCLTTLRGHTDW----------- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 354 paneINSLVMGSEDGYVYSASRHG------LRSG-VNEVYERHLGPITGISthynqLSPDfGHLFLTSSIDWTIKLWSLK 426
Cdd:cd00200 138 ----VNSVAFSPDGTFVASSSQDGtiklwdLRTGkCVATLTGHTGEVNSVA-----FSPD-GEKLLSSSSDGTIKLWDLS 207

                       250       260
                ....*....|....*....|....*
gi 22831379 427 DTKPLYSFE------QYIAWSPVRR 445
Cdd:cd00200 208 TGKCLGTLRghengvNSVAFSPDGY 232
Dynein_IC2 pfam11540
Cytoplasmic dynein 1 intermediate chain 2; Intermediate chain IC 2 forms part of the complex ...
 21-51 1.05e-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: 62.18  E-value: 1.05e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 22831379    21 KQPLNLSVYNVQATNIPPKETLVYTKQTQTT 51
Cdd:pfam11540   1 RKPPRLSVSKVQETDIPPKETVTYSKETQTP 31
WD40 COG2319
WD40 repeat [General function prediction only];
196-427 8.01e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.78  E-value: 8.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 196 ITSMDWSthfPE---LVVGSYhnneespnepDGVVMVWNTKfkksTPEDVF---HCQSAVMStcfAKFNPN--LILGGTY 267
Cdd:COG2319 207 VRSVAFS---PDgklLASGSA----------DGTVRLWDLA----TGKLLRtltGHSGSVRS---VAFSPDgrLLASGSA 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 268 SGQIVLWDnrVQKRTPIQRTPlsaaAHTHPVYCLQMvgTQNAHNVISISSDGKLCSWSLDmlsqpqDTLELQQRQSKAIA 347
Cdd:COG2319 267 DGTVRLWD--LATGELLRTLT----GHSGGVNSVAF--SPDGKLLASGSDDGTVRLWDLA------TGKLLRTLTGHTGA 332

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 348 ITSMAFPANEiNSLVMGSEDG--YVYSASRHGLRsgvnEVYERHLGPITGISthynqLSPDfGHLFLTSSIDWTIKLWSL 425
Cdd:COG2319 333 VRSVAFSPDG-KTLASGSDDGtvRLWDLATGELL----RTLTGHTGAVTSVA-----FSPD-GRTLASGSADGTVRLWDL 401


                ..
gi 22831379 426 KD 427
Cdd:COG2319 402 AT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 195-442 3.31e-10

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: 61.20  E-value: 3.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 195 CITSMDWSTHFPELVVGSYhnneespnepDGVVMVWNTKFKKSTpeDVFHC-QSAVMStcfAKFNPN--LILGGTYSGQI 271
Cdd:cd00200  53 PVRDVAASADGTYLASGSS----------DKTIRLWDLETGECV--RTLTGhTSYVSS---VAFSPDgrILSSSSRDKTI 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 272 VLWDnrVQKRTPIQrtplSAAAHTHPVYCLQMVGTQNAhnVISISSDGKLCSWSLDMLSqPQDTLELQQRQskaiaITSM 351
Cdd:cd00200 118 KVWD--VETGKCLT----TLRGHTDWVNSVAFSPDGTF--VASSSQDGTIKLWDLRTGK-CVATLTGHTGE-----VNSV 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 352 AFPANEiNSLVMGSEDGyvySASRHGLRSGVN-EVYERHLGPITGISThynqlSPDfGHLFLTSSIDWTIKLWSLKDTKP 430
Cdd:cd00200 184 AFSPDG-EKLLSSSSDG---TIKLWDLSTGKClGTLRGHENGVNSVAF-----SPD-GYLLASGSEDGTIRVWDLRTGEC 253

                       250
                ....*....|....*...
gi 22831379 431 LYSFEQY------IAWSP 442
Cdd:cd00200 254 VQTLSGHtnsvtsLAWSP 271
WD40 COG2319
WD40 repeat [General function prediction only];
208-446 4.68e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.47  E-value: 4.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 208 LVVGSYhnneespnepDGVVMVWNTKFKKSTPEDVFHcQSAVmsTCFAkFNPN--LILGGTYSGQIVLWDnrVQKRTPIQ 285
Cdd:COG2319 135 LASGSA----------DGTVRLWDLATGKLLRTLTGH-SGAV--TSVA-FSPDgkLLASGSDDGTVRLWD--LATGKLLR 198

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 286 RTPlsaaAHTHPVYCLQMvgTQNAHNVISISSDGKLCSWSLDmlsqpqDTLELQQRQSKAIAITSMAF-PANEInsLVMG 364
Cdd:COG2319 199 TLT----GHTGAVRSVAF--SPDGKLLASGSADGTVRLWDLA------TGKLLRTLTGHSGSVRSVAFsPDGRL--LASG 264

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 365 SEDGYVY---SASRHGLRsgvneVYERHLGPITGISthynqLSPDfGHLFLTSSIDWTIKLWSLKDTKPLYSFEQY---- 437
Cdd:COG2319 265 SADGTVRlwdLATGELLR-----TLTGHSGGVNSVA-----FSPD-GKLLASGSDDGTVRLWDLATGKLLRTLTGHtgav 333

                       250
                ....*....|.
gi 22831379 438 --IAWSPVRRQ 446
Cdd:COG2319 334 rsVAFSPDGKT 344
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 196-424 7.97e-10

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: 7.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 196 ITSMDWSTHfPELVVGSYHnneespnepDGVVMVWNtkFKKSTPEDVFHCQSA-VMSTCFAKFNpNLILGGTYSGQIVLW 274
Cdd:cd00200  96 VSSVAFSPD-GRILSSSSR---------DKTIKVWD--VETGKCLTTLRGHTDwVNSVAFSPDG-TFVASSSQDGTIKLW 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 275 DNRVQKrtPIQRtplsAAAHTHPVYCLQMVGTQNahNVISISSDGKLCSWSLDMLSQpqdtleLQQRQSKAIAITSMAF- 353
Cdd:cd00200 163 DLRTGK--CVAT----LTGHTGEVNSVAFSPDGE--KLLSSSSDGTIKLWDLSTGKC------LGTLRGHENGVNSVAFs 228

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22831379 354 PANEInsLVMGSEDG--YVYSasrhgLRSGV-NEVYERHLGPITGISthynqLSPDfGHLFLTSSIDWTIKLWS 424
Cdd:cd00200 229 PDGYL--LASGSEDGtiRVWD-----LRTGEcVQTLSGHTNSVTSLA-----WSPD-GKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
224-442 9.86e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 60.31  E-value: 9.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 224 DGVVMVWNTKFKKSTPEDVFHcQSAVMStcfAKFNPN--LILGGTYSGQIVLWDnrVQKRTPIQRTPlsaaAHTHPVYCl 301
Cdd:COG2319 183 DGTVRLWDLATGKLLRTLTGH-TGAVRS---VAFSPDgkLLASGSADGTVRLWD--LATGKLLRTLT----GHSGSVRS- 251

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 302 qmvgtqnahnvISISSDGK-LCSWSLD---MLSQPQDTLELQQRQSKAIAITSMAFPANEiNSLVMGSEDG--YVYSASR 375
Cdd:COG2319 252 -----------VAFSPDGRlLASGSADgtvRLWDLATGELLRTLTGHSGGVNSVAFSPDG-KLLASGSDDGtvRLWDLAT 319

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22831379 376 HGLRSGvnevYERHLGPITGISthynqLSPDfGHLFLTSSIDWTIKLWSLKDTKPLYSFEQY------IAWSP 442
Cdd:COG2319 320 GKLLRT----LTGHTGAVRSVA-----FSPD-GKTLASGSDDGTVRLWDLATGELLRTLTGHtgavtsVAFSP 382
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 294-435 5.87e-06

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: 48.10  E-value: 5.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 294 HTHPVYCLQMVGTQNahNVISISSDGKLCSWSLDMLSQpqdtleLQQRQSKAIAITSMAFPANEiNSLVMGSEDGYVYSA 373
Cdd:cd00200   8 HTGGVTCVAFSPDGK--LLATGSGDGTIKVWDLETGEL------LRTLKGHTGPVRDVAASADG-TYLASGSSDKTIRLW 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22831379 374 SRHGLRsgVNEVYERHLGPITGISthynqLSPDfGHLFLTSSIDWTIKLWSLKDTKPLYSFE 435
Cdd:cd00200  79 DLETGE--CVRTLTGHTSYVSSVA-----FSPD-GRILSSSSRDKTIKVWDVETGKCLTTLR 132
WD40 COG2319
WD40 repeat [General function prediction only];
323-442 1.65e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 47.21  E-value: 1.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831379 323 SWSLDMLSQPQDTLELQQRQSKAIAITSMAFPANEiNSLVMGSEDGYV--YSASRHGLRSgvneVYERHLGPITGISthy 400
Cdd:COG2319  56 GDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDG-RLLASASADGTVrlWDLATGLLLR----TLTGHTGAVRSVA--- 127

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 22831379 401 nqLSPDfGHLFLTSSIDWTIKLWSLKDTKPLYSFEQY------IAWSP 442
Cdd:COG2319 128 --FSPD-GKTLASGSADGTVRLWDLATGKLLRTLTGHsgavtsVAFSP 172
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 385-424 8.50e-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: 34.21  E-value: 8.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 22831379    385 VYERHLGPITGISthynqLSPDfGHLFLTSSIDWTIKLWS 424
Cdd:smart00320   7 TLKGHTGPVTSVA-----FSPD-GKYLASGSDDGTIKLWD 40
 
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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