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Conserved domains on  [gi|1767231539|ref|NP_001362170|]
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Doublecortin domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 713-823 3.29e-22

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


:

Pssm-ID: 238061  Cd Length: 116  Bit Score: 93.17  E-value: 3.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  713 GRWEFRLHTLNSDLGGTTSHLKIIGYGdENWLADDIPNDSLLR--DPSQVPRIQVDFG-NIGRLQKVRFEIQPAGDQPNY 789
Cdd:cd00113      1 CRYTVTIKTGDKKGAGTDSNISLALYG-ENGNSSDIPILDGPGsfERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGW 79

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1767231539  790 YLEYVEAQDLDTRERCVLMVNNWLLKEATPGYRK 823
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWVLGGKWYTSVR 113
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 564-684 8.93e-12

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


The actual alignment was detected with superfamily member cd01756:

Pssm-ID: 412108  Cd Length: 120  Bit Score: 63.34  E-value: 8.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  564 YTFEVMLGNRFGLDFDTPLFFVLHGENGSSEKIytqaddwlflpsscydpesWILSSTRSLK---------------LGV 628
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKR-------------------KLKKSNNKNKfergqtdkftveavdLGK 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1767231539  629 LTSIDVGHEQEGYGAGTFIDKIVITEDEKGakecRRFYFQVEKWFDSGQVDGLIVR 684
Cdd:cd01756     64 LKKIRIGHDNSGLGAGWFLDKVEIREPGTG----DEYTFPCNRWLDKDEDDGQIVR 115
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
 26-94 1.15e-08

Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin (DCX) is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its DCX protein domains can occur in double tandem or as single DCX repeats. Proteins with DCX tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK). Single DCX repeat proteins are normally localized to actin-rich subcellular structures, or the nucleus such as DCDC2. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.


:

Pssm-ID: 340456  Cd Length: 73  Bit Score: 53.00  E-value: 1.15e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767231539   26 KEVLFVLNGrGKFHRE---LINPMKMPTLDQLLEECSTRLEI---AIHRLYTPQGKLITTVEEIlsYDGLKIIAC 94
Cdd:cd01617      1 KRITVFRNG-DKNFKGvkvLVKPRRFRTFDQLLDELTEKLGLptgGVRKLYTPSGKLVKSLSDL--EDGESYVVC 72
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 514-550 4.37e-05

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 41.76  E-value: 4.37e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1767231539  514 TAERERLGEAATKIQAAYKGYTVRKkhvQFLKEKERK 550
Cdd:cd23767      2 EEELQRMNRAATLIQALWRGYKVRK---ELKKKKKKG 35
PTZ00112 super family cl36513
origin recognition complex 1 protein; Provisional
 95-410 2.99e-03

origin recognition complex 1 protein; Provisional


The actual alignment was detected with superfamily member PTZ00112:

Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 41.90  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539   95 PRNERpylNENSTKEKLPQILPKRYAPREAYSISEKKSSTGGSDPATSG-NSSGNSIEK--RQPLPSINNRYVSRRPQEN 171
Cdd:PTZ00112    93 DLNER---SKTPIKNNDNVTTPIKANKKEKHNLDSSSSSSISSSLTNISfFSSPTSIYSclSNSLSSKHSPKVIKENQST 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  172 GVSNSTTTTSPYVPKSYASKLKQT-VPPTTKLNNKTTSKEVNKKPKKDTAMSSAESNKTKDSGKGTSLNNSQQSERHEKM 250
Cdd:PTZ00112   170 HVNISSDNSPRNKEISNKQLKKQTnVTHTTCYDKMRRSPRNTSTIKNNTNDKNKEKNKEKDKNIKKDRDGDKQTKRNSEK 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  251 TEKK-----AQMIREELRTNLKQQNH---------------QNSSSDQYSEEDLIREAESDFEHDATGIQSGTSDEEEEE 310
Cdd:PTZ00112   250 SKVQnshfdVRILRSYTKENKKDEKNvvsgirssvllkrksQCLRKDSYVYSNHQKKAKTGDPKNIIHRNNGSSNSNNDD 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  311 AATsnatsaaesakkrSAHSSHRTPAQKTPSTSESDRlpSLSKSKMNQKQRRKTMSRQDTPYQAtPSRQTT--------- 381
Cdd:PTZ00112   330 TSS-------------SNHLGSNRISNRNPSSPYKKQ--TTTKHTNNTKNNKYNKTKTTQKFNH-PLRHHAtinkrssml 393

                          330       340
                   ....*....|....*....|....*....
gi 1767231539  382 AATEASRLSTSGSSEPHSRYSSRPTTSST 410
Cdd:PTZ00112   394 PMSEQKGRGASEKSEYIKEFTMEEVAKLT 422
 
Name Accession Description Interval E-value
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 713-823 3.29e-22

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 93.17  E-value: 3.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  713 GRWEFRLHTLNSDLGGTTSHLKIIGYGdENWLADDIPNDSLLR--DPSQVPRIQVDFG-NIGRLQKVRFEIQPAGDQPNY 789
Cdd:cd00113      1 CRYTVTIKTGDKKGAGTDSNISLALYG-ENGNSSDIPILDGPGsfERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGW 79

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1767231539  790 YLEYVEAQDLDTRERCVLMVNNWLLKEATPGYRK 823
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWVLGGKWYTSVR 113
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
713-816 3.30e-18

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 81.15  E-value: 3.30e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539   713 GRWEFRLHTLNSDLGGTTS--HLKIIGYGDENWLADDIPNDSLL--RDPSQVPRIQVDFgNIGRLQKVRFEIQPagDQPN 788
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTAsvSLSLVGAEGDGKESKLDYLFKGIfaRGSTYEFTFDVDE-DFGELGAVKIKNEH--RHPE 77

                            90       100
                    ....*....|....*....|....*...
gi 1767231539   789 YYLEYVEAQDLDTRERCVLMVNNWLLKE 816
Cdd:smart00308   78 WFLKSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 564-684 8.93e-12

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 63.34  E-value: 8.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  564 YTFEVMLGNRFGLDFDTPLFFVLHGENGSSEKIytqaddwlflpsscydpesWILSSTRSLK---------------LGV 628
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKR-------------------KLKKSNNKNKfergqtdkftveavdLGK 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1767231539  629 LTSIDVGHEQEGYGAGTFIDKIVITEDEKGakecRRFYFQVEKWFDSGQVDGLIVR 684
Cdd:cd01756     64 LKKIRIGHDNSGLGAGWFLDKVEIREPGTG----DEYTFPCNRWLDKDEDDGQIVR 115
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
 26-94 1.15e-08

Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin (DCX) is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its DCX protein domains can occur in double tandem or as single DCX repeats. Proteins with DCX tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK). Single DCX repeat proteins are normally localized to actin-rich subcellular structures, or the nucleus such as DCDC2. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.


Pssm-ID: 340456  Cd Length: 73  Bit Score: 53.00  E-value: 1.15e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767231539   26 KEVLFVLNGrGKFHRE---LINPMKMPTLDQLLEECSTRLEI---AIHRLYTPQGKLITTVEEIlsYDGLKIIAC 94
Cdd:cd01617      1 KRITVFRNG-DKNFKGvkvLVKPRRFRTFDQLLDELTEKLGLptgGVRKLYTPSGKLVKSLSDL--EDGESYVVC 72
DCX pfam03607
Doublecortin;
42-94 4.89e-06

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 45.13  E-value: 4.89e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1767231539   42 LINPMKMPTLDQLLEECSTRLEI----AIHRLYTPQGKLITTVEEIlsYDGLKIIAC 94
Cdd:pfam03607    1 VVNKRRFRSFDALLDELTEKVVKlpfgAVRKLYTLDGKRVTSLDEL--EDGGVYVAA 55
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 514-550 4.37e-05

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 41.76  E-value: 4.37e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1767231539  514 TAERERLGEAATKIQAAYKGYTVRKkhvQFLKEKERK 550
Cdd:cd23767      2 EEELQRMNRAATLIQALWRGYKVRK---ELKKKKKKG 35
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 22-98 1.78e-04

Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.


Pssm-ID: 214711  Cd Length: 89  Bit Score: 41.47  E-value: 1.78e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539    22 TVSAKEVLFVLNGRGKFH--RELINPMKMPTLDQLLEECS----TRLEIAIHRLYTPQGKLITTVEEIlsYDGLKIIACP 95
Cdd:smart00537    2 LVKPKRIRFYRNGDRFFKgvRLVVNRKRFKSFEALLQDLTevvkLDLPHGVRKLYTLDGKKVTSLDEL--EDGGSYVASG 79


                    ...
gi 1767231539    96 RNE 98
Cdd:smart00537   80 TEA 82
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 715-813 9.36e-04

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 40.11  E-value: 9.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  715 WEFRLHTLNSDLGGTTSHLKIIGYG---DENWLADDIPNDSLLRDPSQVPRIQVDFgNIGRLQKVRFEIQPAGDQPNYYL 791
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGkvgESAQLEITLDNPDFERGAEDSFEIDTDW-DVGAILKINLHWDNNGLSDEWFL 79

                           90       100
                   ....*....|....*....|...
gi 1767231539  792 EYVEAQDLDTRERCVLM-VNNWL 813
Cdd:pfam01477   80 KSITVEVPGETGGKYTFpCNSWV 102
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 95-410 2.99e-03

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 41.90  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539   95 PRNERpylNENSTKEKLPQILPKRYAPREAYSISEKKSSTGGSDPATSG-NSSGNSIEK--RQPLPSINNRYVSRRPQEN 171
Cdd:PTZ00112    93 DLNER---SKTPIKNNDNVTTPIKANKKEKHNLDSSSSSSISSSLTNISfFSSPTSIYSclSNSLSSKHSPKVIKENQST 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  172 GVSNSTTTTSPYVPKSYASKLKQT-VPPTTKLNNKTTSKEVNKKPKKDTAMSSAESNKTKDSGKGTSLNNSQQSERHEKM 250
Cdd:PTZ00112   170 HVNISSDNSPRNKEISNKQLKKQTnVTHTTCYDKMRRSPRNTSTIKNNTNDKNKEKNKEKDKNIKKDRDGDKQTKRNSEK 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  251 TEKK-----AQMIREELRTNLKQQNH---------------QNSSSDQYSEEDLIREAESDFEHDATGIQSGTSDEEEEE 310
Cdd:PTZ00112   250 SKVQnshfdVRILRSYTKENKKDEKNvvsgirssvllkrksQCLRKDSYVYSNHQKKAKTGDPKNIIHRNNGSSNSNNDD 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  311 AATsnatsaaesakkrSAHSSHRTPAQKTPSTSESDRlpSLSKSKMNQKQRRKTMSRQDTPYQAtPSRQTT--------- 381
Cdd:PTZ00112   330 TSS-------------SNHLGSNRISNRNPSSPYKKQ--TTTKHTNNTKNNKYNKTKTTQKFNH-PLRHHAtinkrssml 393

                          330       340
                   ....*....|....*....|....*....
gi 1767231539  382 AATEASRLSTSGSSEPHSRYSSRPTTSST 410
Cdd:PTZ00112   394 PMSEQKGRGASEKSEYIKEFTMEEVAKLT 422
 
Name Accession Description Interval E-value
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 713-823 3.29e-22

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 93.17  E-value: 3.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  713 GRWEFRLHTLNSDLGGTTSHLKIIGYGdENWLADDIPNDSLLR--DPSQVPRIQVDFG-NIGRLQKVRFEIQPAGDQPNY 789
Cdd:cd00113      1 CRYTVTIKTGDKKGAGTDSNISLALYG-ENGNSSDIPILDGPGsfERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGW 79

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1767231539  790 YLEYVEAQDLDTRERCVLMVNNWLLKEATPGYRK 823
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWVLGGKWYTSVR 113
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
713-816 3.30e-18

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 81.15  E-value: 3.30e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539   713 GRWEFRLHTLNSDLGGTTS--HLKIIGYGDENWLADDIPNDSLL--RDPSQVPRIQVDFgNIGRLQKVRFEIQPagDQPN 788
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTAsvSLSLVGAEGDGKESKLDYLFKGIfaRGSTYEFTFDVDE-DFGELGAVKIKNEH--RHPE 77

                            90       100
                    ....*....|....*....|....*...
gi 1767231539   789 YYLEYVEAQDLDTRERCVLMVNNWLLKE 816
Cdd:smart00308   78 WFLKSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 564-684 8.93e-12

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 63.34  E-value: 8.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  564 YTFEVMLGNRFGLDFDTPLFFVLHGENGSSEKIytqaddwlflpsscydpesWILSSTRSLK---------------LGV 628
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKR-------------------KLKKSNNKNKfergqtdkftveavdLGK 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1767231539  629 LTSIDVGHEQEGYGAGTFIDKIVITEDEKGakecRRFYFQVEKWFDSGQVDGLIVR 684
Cdd:cd01756     64 LKKIRIGHDNSGLGAGWFLDKVEIREPGTG----DEYTFPCNRWLDKDEDDGQIVR 115
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
 26-94 1.15e-08

Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin (DCX) is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its DCX protein domains can occur in double tandem or as single DCX repeats. Proteins with DCX tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK). Single DCX repeat proteins are normally localized to actin-rich subcellular structures, or the nucleus such as DCDC2. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.


Pssm-ID: 340456  Cd Length: 73  Bit Score: 53.00  E-value: 1.15e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767231539   26 KEVLFVLNGrGKFHRE---LINPMKMPTLDQLLEECSTRLEI---AIHRLYTPQGKLITTVEEIlsYDGLKIIAC 94
Cdd:cd01617      1 KRITVFRNG-DKNFKGvkvLVKPRRFRTFDQLLDELTEKLGLptgGVRKLYTPSGKLVKSLSDL--EDGESYVVC 72
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 727-813 2.72e-06

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 47.66  E-value: 2.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  727 GGTTSHLKIIGYGDENwladdipnDSLLRDPSQvPRIQV-------DF-----GNIGRLQKVRFEIQPAGDQPNYYLEYV 794
Cdd:cd01752     15 AGTTAKVTITLYGAEG--------ESEPHHLRD-PEKPIfergsvdSFllttpFPLGELQSIRLWHDNSGLSPSWYLSRV 85

                           90
                   ....*....|....*....
gi 1767231539  795 EAQDLDTRERCVLMVNNWL 813
Cdd:cd01752     86 IVRDLQTGKKWFFLCNDWL 104
DCX pfam03607
Doublecortin;
42-94 4.89e-06

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 45.13  E-value: 4.89e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1767231539   42 LINPMKMPTLDQLLEECSTRLEI----AIHRLYTPQGKLITTVEEIlsYDGLKIIAC 94
Cdd:pfam03607    1 VVNKRRFRSFDALLDELTEKVVKlpfgAVRKLYTLDGKRVTSLDEL--EDGGVYVAA 55
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 563-688 6.89e-06

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 46.50  E-value: 6.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  563 HYTFEVMLGNRFGLDFDTPLFFVLHGENGSSE-KIYTQADDWLFLPSSCydpESWILSSTRSLklGVLTSIDVGHEQEGY 641
Cdd:cd01752      2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEpHHLRDPEKPIFERGSV---DSFLLTTPFPL--GELQSIRLWHDNSGL 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1767231539  642 GAGTFIDKIVITEDEKGakecRRFYFQVEKWFDSGQVDGLIVRNIKV 688
Cdd:cd01752     77 SPSWYLSRVIVRDLQTG----KKWFFLCNDWLSVEEGDGTVERTFPV 119
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 514-550 4.37e-05

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 41.76  E-value: 4.37e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1767231539  514 TAERERLGEAATKIQAAYKGYTVRKkhvQFLKEKERK 550
Cdd:cd23767      2 EEELQRMNRAATLIQALWRGYKVRK---ELKKKKKKG 35
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 39-84 1.17e-04

Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein family is part of doublecortin (DCX) superfamily with double tandem DCX repeats that are associated with retinitis pigmentosa. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. RP-like proteins are colocalized to the photoreceptor and share a function in outer segment disc morphogenesis.


Pssm-ID: 340590  Cd Length: 69  Bit Score: 41.46  E-value: 1.17e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1767231539   39 HRELINPMKMPTLDQLLEECSTRLEIAIHRLYTPQGKLITTVEEIL 84
Cdd:cd17070     15 HTILLNRRTTQSFEQVLQDLSELLKGPVRKLYTTDGKKVESLSALF 60
DCX2_DCDC2_like cd16113
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 14-83 1.32e-04

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340530  Cd Length: 74  Bit Score: 41.41  E-value: 1.32e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767231539   14 SRLIHAFRtvsakevlfvlNGRGKFH--RELINPMKMPTLDQLLEECSTRLEI---AIHRLYTPQGKLITTVEEI 83
Cdd:cd16113      1 PKTIHVFP-----------NGDLLHPpsKVLLTKRRLPNWDTVLEEVTEKVKLqtgAVRKLYTLDGKRISDPDEL 64
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 22-98 1.78e-04

Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.


Pssm-ID: 214711  Cd Length: 89  Bit Score: 41.47  E-value: 1.78e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539    22 TVSAKEVLFVLNGRGKFH--RELINPMKMPTLDQLLEECS----TRLEIAIHRLYTPQGKLITTVEEIlsYDGLKIIACP 95
Cdd:smart00537    2 LVKPKRIRFYRNGDRFFKgvRLVVNRKRFKSFEALLQDLTevvkLDLPHGVRKLYTLDGKKVTSLDEL--EDGGSYVASG 79


                    ...
gi 1767231539    96 RNE 98
Cdd:smart00537   80 TEA 82
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 715-813 9.36e-04

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 40.11  E-value: 9.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  715 WEFRLHTLNSDLGGTTSHLKIIGYG---DENWLADDIPNDSLLRDPSQVPRIQVDFgNIGRLQKVRFEIQPAGDQPNYYL 791
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGkvgESAQLEITLDNPDFERGAEDSFEIDTDW-DVGAILKINLHWDNNGLSDEWFL 79

                           90       100
                   ....*....|....*....|...
gi 1767231539  792 EYVEAQDLDTRERCVLM-VNNWL 813
Cdd:pfam01477   80 KSITVEVPGETGGKYTFpCNSWV 102
DCX_DCDC5_like cd17072
Doublecortin-like domain found in doublecortin domain-containing protein 5 (DCDC5) and similar ...
 26-83 2.70e-03

Doublecortin-like domain found in doublecortin domain-containing protein 5 (DCDC5) and similar proteins; DCDC5 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC5 is expressed during mitosis and involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8 as well as with the Rab8 nucleotide exchange factor Rabin8. This family also includes DCDC1, which is a hydrophilic intracellular protein that contains only one DCX repeat. Therefore, DCDC1 might only bind to microtubules without microtubule polymerization properties. DCDC1 is mainly expressed in adult testis.


Pssm-ID: 340592  Cd Length: 71  Bit Score: 37.64  E-value: 2.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539   26 KEVLFVLNGRGKFHRELINPMKMPTLDQLLEECSTRLEI--AIHRLYTPQGKLITTVEEI 83
Cdd:cd17072      1 VRLRVLKNGERDLERAVYVVGPDLELQLFLDRCTERLNLpfAARRLFDENGKEIFTLRDL 60
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 95-410 2.99e-03

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 41.90  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539   95 PRNERpylNENSTKEKLPQILPKRYAPREAYSISEKKSSTGGSDPATSG-NSSGNSIEK--RQPLPSINNRYVSRRPQEN 171
Cdd:PTZ00112    93 DLNER---SKTPIKNNDNVTTPIKANKKEKHNLDSSSSSSISSSLTNISfFSSPTSIYSclSNSLSSKHSPKVIKENQST 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  172 GVSNSTTTTSPYVPKSYASKLKQT-VPPTTKLNNKTTSKEVNKKPKKDTAMSSAESNKTKDSGKGTSLNNSQQSERHEKM 250
Cdd:PTZ00112   170 HVNISSDNSPRNKEISNKQLKKQTnVTHTTCYDKMRRSPRNTSTIKNNTNDKNKEKNKEKDKNIKKDRDGDKQTKRNSEK 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  251 TEKK-----AQMIREELRTNLKQQNH---------------QNSSSDQYSEEDLIREAESDFEHDATGIQSGTSDEEEEE 310
Cdd:PTZ00112   250 SKVQnshfdVRILRSYTKENKKDEKNvvsgirssvllkrksQCLRKDSYVYSNHQKKAKTGDPKNIIHRNNGSSNSNNDD 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  311 AATsnatsaaesakkrSAHSSHRTPAQKTPSTSESDRlpSLSKSKMNQKQRRKTMSRQDTPYQAtPSRQTT--------- 381
Cdd:PTZ00112   330 TSS-------------SNHLGSNRISNRNPSSPYKKQ--TTTKHTNNTKNNKYNKTKTTQKFNH-PLRHHAtinkrssml 393

                          330       340
                   ....*....|....*....|....*....
gi 1767231539  382 AATEASRLSTSGSSEPHSRYSSRPTTSST 410
Cdd:PTZ00112   394 PMSEQKGRGASEKSEYIKEFTMEEVAKLT 422
PRK08581 PRK08581
amidase domain-containing protein;
202-402 3.23e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 41.70  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  202 LNNKTTSKEVNKKPKKDTAMSSAESNKTKDSGKGTSLNNSQQSERHEKM-TEKKAQM----IREELRTNLKQQNHQN--- 273
Cdd:PRK08581    30 PQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFsTIDSSTSdsnnIIDFIYKNLPQTNINQllt 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231539  274 --SSSDQYSEEDLIrEAESDFEHDATGIQSGTSDEEEEEAATSNATSAAESAKKRSAHSSHRTPAQKTPSTSESdrLPSL 351
Cdd:PRK08581   110 knKYDDNYSLTTLI-QNLFNLNSDISDYEQPRNSEKSTNDSNKNSDSSIKNDTDTQSSKQDKADNQKAPSSNNT--KPST 186

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1767231539  352 SKSKMNQKQRRKTMSRQDTPYQATPSRQTTAATEASRLSTSGSSEPHSRYS 402
Cdd:PRK08581   187 SNKQPNSPKPTQPNQSNSQPASDDTANQKSSSKDNQSMSDSALDSILDQYS 237
DCX4_DCDC5 cd17159
Doublecortin-like domain 4 found in doublecortin domain-containing protein 5 (DCDC5); DCDC5 is ...
 50-83 7.33e-03

Doublecortin-like domain 4 found in doublecortin domain-containing protein 5 (DCDC5); DCDC5 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC5 is expressed during mitosis and involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8, as well as with the Rab8 nucleotide exchange factor Rabin8.


Pssm-ID: 340679  Cd Length: 73  Bit Score: 36.50  E-value: 7.33e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1767231539   50 TLDQLLEECSTRLEI--AIHRLYTPQGKLITTVEEI 83
Cdd:cd17159     22 SIEELLDSCTERLGLrkPAKYLYTPDGEQIQSWDDI 57
 
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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