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Conserved domains on  [gi|71980534|ref|NP_001021110|]
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Secreted calsyntenin-1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLSTN_C super family cl45102
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 538-764 3.68e-25

Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) proteins 1, 2 and 3 (also known as Alcadein-alpha, gamma and beta). These are postsynaptic Ca2-binding proteins, evolutionarily conserved type I membrane proteins. CLSTN forms a complex with APP and X11-like that stabilizes both APP and CLSTN proteins metabolically. CLSTN strongly associates with kinesin-1 light chains (KLC1) that induce kinesin-1 association with vesicles and functions as a novel cargo in axonal anterograde transport. This domain includes the WD motifs required for KLC1 interaction (although one WD motif is sufficient), and the NP motif.


The actual alignment was detected with superfamily member pfam19699:

Pssm-ID: 466150  Cd Length: 354  Bit Score: 108.32  E-value: 3.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534   538 VDELLESQSATFSPDQTSLTLKAETSKQIGQMLKRVAYVNTQEKPAPGHRVFLVETEVTCKQDDKKMKLPSSKGYVFVQQ 617
Cdd:pfam19699   5 PENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYVMVLQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534   618 AAEPTLSIS-------ASSQLKSNQhmvkvGQAMVPDLTITIS---QNNADGELED---VTQS-------HKIDYCKM-- 675
Cdd:pfam19699  85 PEEPKISLSgidhfarPASEFESPE-----GVPLFPELRIVSTitrEVESEGDGEDdptVQESlvseeivHNLDGCEVtv 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534   676 ---HLQPARdmdvEYFSSPASLIAALNIEFEHDKDGILLRGEESAQGYKEVLSKVHYFNTRPESYAKRVYTVQCAMLKGR 752
Cdd:pfam19699 160 lgeELNPEQ----ESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGR 235

                         250
                  ....*....|..
gi 71980534   753 VLSNQLFVTMTI 764
Cdd:pfam19699 236 YASNEFKVEVNV 247
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 163-236 4.34e-14

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 68.88  E-value: 4.34e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980534 163 LKASDKDCGhPNGEIcEYEITNGLKELPFAINNH-GVLRTTQPLNFTQSKSYILTVVAIDCAmRKSKSSLVTVHV 236
Cdd:cd11304  19 VSATDPDSG-ENGEV-TYSIVSGNEDGLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG-GPPLSSTATVTI 90
CA_like super family cl46864
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 70-140 7.87e-05

Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers. This family also includes the cadherin-like repeats of extracellular alpha-dystroglycan.


The actual alignment was detected with superfamily member smart00112:

Pssm-ID: 481204 [Multi-domain]  Cd Length: 81  Bit Score: 41.95  E-value: 7.87e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980534     70 SQNNEPVPFDIqvvDKYTGaavlRVKDAATLDC-KKPEYNLQVQAVkcDNDNVKSEG-VSLKIRVKDTNNHAP 140
Cdd:smart00112  18 LSGNDDGLFSI---DPETG----EITTTKPLDReEQPEYTLTVEAT--DGGGPPLSStATVTITVLDVNDNAP 81
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 398-512 4.59e-03

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


The actual alignment was detected with superfamily member smart00282:

Pssm-ID: 473984 [Multi-domain]  Cd Length: 132  Bit Score: 38.47  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534    398 HFSVYIRHCKLEVVLRREAGAtsdfraAEWRWSMPEVCDNEWHSYSLLFNGiDDVNVIVDGKSfKADERNPEILDDWPLH 477
Cdd:smart00282  26 YLALELRDGRLVLRYDLGSGP------ARLTSDPTPLNDGQWHRVAVERNG-RSVTLSVDGGN-RVSGESPGGLTILNLD 97

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 71980534    478 ktkatkTKLVVGAC---WHGRQQKLAQFFRGQLSSLYL 512
Cdd:smart00282  98 ------GPLYLGGLpedLKLPPLPVTPGFRGCIRNLKV 129
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 538-764 3.68e-25

Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) proteins 1, 2 and 3 (also known as Alcadein-alpha, gamma and beta). These are postsynaptic Ca2-binding proteins, evolutionarily conserved type I membrane proteins. CLSTN forms a complex with APP and X11-like that stabilizes both APP and CLSTN proteins metabolically. CLSTN strongly associates with kinesin-1 light chains (KLC1) that induce kinesin-1 association with vesicles and functions as a novel cargo in axonal anterograde transport. This domain includes the WD motifs required for KLC1 interaction (although one WD motif is sufficient), and the NP motif.


Pssm-ID: 466150  Cd Length: 354  Bit Score: 108.32  E-value: 3.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534   538 VDELLESQSATFSPDQTSLTLKAETSKQIGQMLKRVAYVNTQEKPAPGHRVFLVETEVTCKQDDKKMKLPSSKGYVFVQQ 617
Cdd:pfam19699   5 PENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYVMVLQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534   618 AAEPTLSIS-------ASSQLKSNQhmvkvGQAMVPDLTITIS---QNNADGELED---VTQS-------HKIDYCKM-- 675
Cdd:pfam19699  85 PEEPKISLSgidhfarPASEFESPE-----GVPLFPELRIVSTitrEVESEGDGEDdptVQESlvseeivHNLDGCEVtv 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534   676 ---HLQPARdmdvEYFSSPASLIAALNIEFEHDKDGILLRGEESAQGYKEVLSKVHYFNTRPESYAKRVYTVQCAMLKGR 752
Cdd:pfam19699 160 lgeELNPEQ----ESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGR 235

                         250
                  ....*....|..
gi 71980534   753 VLSNQLFVTMTI 764
Cdd:pfam19699 236 YASNEFKVEVNV 247
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 163-236 4.34e-14

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 68.88  E-value: 4.34e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980534 163 LKASDKDCGhPNGEIcEYEITNGLKELPFAINNH-GVLRTTQPLNFTQSKSYILTVVAIDCAmRKSKSSLVTVHV 236
Cdd:cd11304  19 VSATDPDSG-ENGEV-TYSIVSGNEDGLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG-GPPLSSTATVTI 90
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 164-236 3.57e-10

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 56.97  E-value: 3.57e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980534    164 KASDKDCGhPNGEIcEYEITNGLKELPFAINNH-GVLRTTQPLNFTQSKSYILTVVAIDCAMrKSKSSLVTVHV 236
Cdd:smart00112   1 SATDADSG-ENGKV-TYSILSGNDDGLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGG-PPLSSTATVTI 71
Cadherin pfam00028
Cadherin domain;
163-236 1.42e-08

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 53.07  E-value: 1.42e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980534   163 LKASDKDCGhPNGEIcEYEITNGLKELPFAINNH-GVLRTTQPLNFTQSKSYILTVVAIDCAMR-KSKSSLVTVHV 236
Cdd:pfam00028  18 VTATDPDLG-PNGRI-FYSILGGGPGGNFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGGPpLSSTATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 70-140 7.87e-05

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 41.95  E-value: 7.87e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980534     70 SQNNEPVPFDIqvvDKYTGaavlRVKDAATLDC-KKPEYNLQVQAVkcDNDNVKSEG-VSLKIRVKDTNNHAP 140
Cdd:smart00112  18 LSGNDDGLFSI---DPETG----EITTTKPLDReEQPEYTLTVEAT--DGGGPPLSStATVTITVLDVNDNAP 81
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 36-138 2.56e-04

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 41.14  E-value: 2.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534  36 ELVAVVREDENIISTV-------PDfailSETGPVCNYLLTSQNNEPvPFDIqvvDKYTGaaVLRVKdaATLDC-KKPEY 107
Cdd:cd11304   1 SYEVSVPENAPPGTVVltvsatdPD----SGENGEVTYSIVSGNEDG-LFSI---DPSTG--EITTA--KPLDReEQSSY 68

                        90       100       110
                ....*....|....*....|....*....|.
gi 71980534 108 NLQVQAVKCDNDNVKSEgVSLKIRVKDTNNH 138
Cdd:cd11304  69 TLTVTATDGGGPPLSST-ATVTITVLDVNDN 98
LamG smart00282
Laminin G domain;
398-512 4.59e-03

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 38.47  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534    398 HFSVYIRHCKLEVVLRREAGAtsdfraAEWRWSMPEVCDNEWHSYSLLFNGiDDVNVIVDGKSfKADERNPEILDDWPLH 477
Cdd:smart00282  26 YLALELRDGRLVLRYDLGSGP------ARLTSDPTPLNDGQWHRVAVERNG-RSVTLSVDGGN-RVSGESPGGLTILNLD 97

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 71980534    478 ktkatkTKLVVGAC---WHGRQQKLAQFFRGQLSSLYL 512
Cdd:smart00282  98 ------GPLYLGGLpedLKLPPLPVTPGFRGCIRNLKV 129
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 538-764 3.68e-25

Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) proteins 1, 2 and 3 (also known as Alcadein-alpha, gamma and beta). These are postsynaptic Ca2-binding proteins, evolutionarily conserved type I membrane proteins. CLSTN forms a complex with APP and X11-like that stabilizes both APP and CLSTN proteins metabolically. CLSTN strongly associates with kinesin-1 light chains (KLC1) that induce kinesin-1 association with vesicles and functions as a novel cargo in axonal anterograde transport. This domain includes the WD motifs required for KLC1 interaction (although one WD motif is sufficient), and the NP motif.


Pssm-ID: 466150  Cd Length: 354  Bit Score: 108.32  E-value: 3.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534   538 VDELLESQSATFSPDQTSLTLKAETSKQIGQMLKRVAYVNTQEKPAPGHRVFLVETEVTCKQDDKKMKLPSSKGYVFVQQ 617
Cdd:pfam19699   5 PENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYVMVLQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534   618 AAEPTLSIS-------ASSQLKSNQhmvkvGQAMVPDLTITIS---QNNADGELED---VTQS-------HKIDYCKM-- 675
Cdd:pfam19699  85 PEEPKISLSgidhfarPASEFESPE-----GVPLFPELRIVSTitrEVESEGDGEDdptVQESlvseeivHNLDGCEVtv 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534   676 ---HLQPARdmdvEYFSSPASLIAALNIEFEHDKDGILLRGEESAQGYKEVLSKVHYFNTRPESYAKRVYTVQCAMLKGR 752
Cdd:pfam19699 160 lgeELNPEQ----ESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGR 235

                         250
                  ....*....|..
gi 71980534   753 VLSNQLFVTMTI 764
Cdd:pfam19699 236 YASNEFKVEVNV 247
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 163-236 4.34e-14

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 68.88  E-value: 4.34e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980534 163 LKASDKDCGhPNGEIcEYEITNGLKELPFAINNH-GVLRTTQPLNFTQSKSYILTVVAIDCAmRKSKSSLVTVHV 236
Cdd:cd11304  19 VSATDPDSG-ENGEV-TYSIVSGNEDGLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG-GPPLSSTATVTI 90
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 164-236 3.57e-10

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 56.97  E-value: 3.57e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980534    164 KASDKDCGhPNGEIcEYEITNGLKELPFAINNH-GVLRTTQPLNFTQSKSYILTVVAIDCAMrKSKSSLVTVHV 236
Cdd:smart00112   1 SATDADSG-ENGKV-TYSILSGNDDGLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGG-PPLSSTATVTI 71
Cadherin pfam00028
Cadherin domain;
163-236 1.42e-08

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 53.07  E-value: 1.42e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980534   163 LKASDKDCGhPNGEIcEYEITNGLKELPFAINNH-GVLRTTQPLNFTQSKSYILTVVAIDCAMR-KSKSSLVTVHV 236
Cdd:pfam00028  18 VTATDPDLG-PNGRI-FYSILGGGPGGNFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGGPpLSSTATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 70-140 7.87e-05

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 41.95  E-value: 7.87e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980534     70 SQNNEPVPFDIqvvDKYTGaavlRVKDAATLDC-KKPEYNLQVQAVkcDNDNVKSEG-VSLKIRVKDTNNHAP 140
Cdd:smart00112  18 LSGNDDGLFSI---DPETG----EITTTKPLDReEQPEYTLTVEAT--DGGGPPLSStATVTITVLDVNDNAP 81
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 36-138 2.56e-04

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 41.14  E-value: 2.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534  36 ELVAVVREDENIISTV-------PDfailSETGPVCNYLLTSQNNEPvPFDIqvvDKYTGaaVLRVKdaATLDC-KKPEY 107
Cdd:cd11304   1 SYEVSVPENAPPGTVVltvsatdPD----SGENGEVTYSIVSGNEDG-LFSI---DPSTG--EITTA--KPLDReEQSSY 68

                        90       100       110
                ....*....|....*....|....*....|.
gi 71980534 108 NLQVQAVKCDNDNVKSEgVSLKIRVKDTNNH 138
Cdd:cd11304  69 TLTVTATDGGGPPLSST-ATVTITVLDVNDN 98
LamG smart00282
Laminin G domain;
398-512 4.59e-03

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 38.47  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980534    398 HFSVYIRHCKLEVVLRREAGAtsdfraAEWRWSMPEVCDNEWHSYSLLFNGiDDVNVIVDGKSfKADERNPEILDDWPLH 477
Cdd:smart00282  26 YLALELRDGRLVLRYDLGSGP------ARLTSDPTPLNDGQWHRVAVERNG-RSVTLSVDGGN-RVSGESPGGLTILNLD 97

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 71980534    478 ktkatkTKLVVGAC---WHGRQQKLAQFFRGQLSSLYL 512
Cdd:smart00282  98 ------GPLYLGGLpedLKLPPLPVTPGFRGCIRNLKV 129
 
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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