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Conserved domains on  [gi|12746426|ref|NP_075538|]
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calsyntenin-1 isoform 1 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 566-918 0e+00

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: 699.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   566 DLQVPEDANRGVQIQASSSQAVLTLEGDNVGELDKAMQHISYLNSRQFPTPGIRRLKITSTVKCFNEAACIEVPPVEGYV 645
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   646 MVLQPEEPKISLSGVHHFARAASEFESAEGISLFPELRIISTITREVEPEADGSEDPTVQESLVSEEIVHDLDTCEVTVE 725
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   726 GDELNAEQESLEVDVTRLQQKGIEASHSDLGVVFTGVETMASYEEVLHLLRYRNWHTRSLLDRKFKLICSELNGRYLSNE 805
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   806 FKVEVNVIHTANPVEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSFLVFMIILGVFRIRAA 885
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320

                         330       340       350
                  ....*....|....*....|....*....|...
gi 12746426   886 HQRTMRDQDTGKENEMDWDDSALTITVNPMETY 918
Cdd:pfam19699 321 HQRGMRDQEGGKENEMDWDDSALTITVNPMETY 353
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 168-258 1.13e-11

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: 61.95  E-value: 1.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426 168 SYKAAVVEG-KQHSSILRVEAVDADcSPQFSQIcSYEILTPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCG 243
Cdd:cd11304   1 SYEVSVPENaPPGTVVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                        90
                ....*....|....*
gi 12746426 244 KKRATEDVLVKISVK 258
Cdd:cd11304  79 GPPLSSTATVTITVL 93
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 41-159 2.62e-11

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: 60.79  E-value: 2.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426  41 TYHGIVTEND--NTVLLDppLIALDKDSPlrfaESFEVTvtkegeicgFKIHGQNvPFDAVVVDKSTGEgiIRSKEKLDC 118
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSG----ENGEVT---------YSIVSGN-EDGLFSIDPSTGE--ITTAKPLDR 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 12746426 119 ELQKDYTFTIQAYDCGKGPdgtgvkKSHKATVHIQVNDVNE 159
Cdd:cd11304  63 EEQSSYTLTVTATDGGGPP------LSSTATVTITVLDVND 97
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 566-918 0e+00

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: 699.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   566 DLQVPEDANRGVQIQASSSQAVLTLEGDNVGELDKAMQHISYLNSRQFPTPGIRRLKITSTVKCFNEAACIEVPPVEGYV 645
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   646 MVLQPEEPKISLSGVHHFARAASEFESAEGISLFPELRIISTITREVEPEADGSEDPTVQESLVSEEIVHDLDTCEVTVE 725
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   726 GDELNAEQESLEVDVTRLQQKGIEASHSDLGVVFTGVETMASYEEVLHLLRYRNWHTRSLLDRKFKLICSELNGRYLSNE 805
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   806 FKVEVNVIHTANPVEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSFLVFMIILGVFRIRAA 885
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320

                         330       340       350
                  ....*....|....*....|....*....|...
gi 12746426   886 HQRTMRDQDTGKENEMDWDDSALTITVNPMETY 918
Cdd:pfam19699 321 HQRGMRDQEGGKENEMDWDDSALTITVNPMETY 353
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 168-258 1.13e-11

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: 61.95  E-value: 1.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426 168 SYKAAVVEG-KQHSSILRVEAVDADcSPQFSQIcSYEILTPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCG 243
Cdd:cd11304   1 SYEVSVPENaPPGTVVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                        90
                ....*....|....*
gi 12746426 244 KKRATEDVLVKISVK 258
Cdd:cd11304  79 GPPLSSTATVTITVL 93
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 41-159 2.62e-11

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: 60.79  E-value: 2.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426  41 TYHGIVTEND--NTVLLDppLIALDKDSPlrfaESFEVTvtkegeicgFKIHGQNvPFDAVVVDKSTGEgiIRSKEKLDC 118
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSG----ENGEVT---------YSIVSGN-EDGLFSIDPSTGE--ITTAKPLDR 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 12746426 119 ELQKDYTFTIQAYDCGKGPdgtgvkKSHKATVHIQVNDVNE 159
Cdd:cd11304  63 EEQSSYTLTVTATDGGGPP------LSSTATVTITVLDVND 97
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 87-162 1.70e-09

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: 55.05  E-value: 1.70e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12746426     87 FKIHGQNvPFDAVVVDKSTGegIIRSKEKLDCELQKDYTFTIQAYDCGKGPdgtgvkKSHKATVHIQVNDVNEYAP 162
Cdd:smart00112  15 YSILSGN-DDGLFSIDPETG--EITTTKPLDREEQPEYTLTVEATDGGGPP------LSSTATVTITVLDVNDNAP 81
Cadherin pfam00028
Cadherin domain;
180-257 5.24e-08

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 51.53  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   180 SSILRVEAVDADCSPQfSQIcSYEILTPDVP--FTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKIS 256
Cdd:pfam00028  13 TEVLTVTATDPDLGPN-GRI-FYSILGGGPGgnFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGGPPLSSTATVTIT 90


                  .
gi 12746426   257 V 257
Cdd:pfam00028  91 V 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 187-258 9.99e-08

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: 50.04  E-value: 9.99e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12746426    187 AVDADcSPQFSQIcSYEILTPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISVK 258
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILSGNDdgLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Cadherin pfam00028
Cadherin domain;
101-154 4.17e-03

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 37.28  E-value: 4.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 12746426   101 VDKSTGEgiIRSKEKLDCELQKDYTFTIQAYDCGKGPdgtgvkKSHKATVHIQV 154
Cdd:pfam00028  46 IDPDTGD--ISTTKPLDRESIGEYELTVEATDSGGPP------LSSTATVTITV 91
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 566-918 0e+00

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: 699.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   566 DLQVPEDANRGVQIQASSSQAVLTLEGDNVGELDKAMQHISYLNSRQFPTPGIRRLKITSTVKCFNEAACIEVPPVEGYV 645
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   646 MVLQPEEPKISLSGVHHFARAASEFESAEGISLFPELRIISTITREVEPEADGSEDPTVQESLVSEEIVHDLDTCEVTVE 725
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   726 GDELNAEQESLEVDVTRLQQKGIEASHSDLGVVFTGVETMASYEEVLHLLRYRNWHTRSLLDRKFKLICSELNGRYLSNE 805
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   806 FKVEVNVIHTANPVEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSFLVFMIILGVFRIRAA 885
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320

                         330       340       350
                  ....*....|....*....|....*....|...
gi 12746426   886 HQRTMRDQDTGKENEMDWDDSALTITVNPMETY 918
Cdd:pfam19699 321 HQRGMRDQEGGKENEMDWDDSALTITVNPMETY 353
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 168-258 1.13e-11

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: 61.95  E-value: 1.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426 168 SYKAAVVEG-KQHSSILRVEAVDADcSPQFSQIcSYEILTPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCG 243
Cdd:cd11304   1 SYEVSVPENaPPGTVVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                        90
                ....*....|....*
gi 12746426 244 KKRATEDVLVKISVK 258
Cdd:cd11304  79 GPPLSSTATVTITVL 93
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 41-159 2.62e-11

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: 60.79  E-value: 2.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426  41 TYHGIVTEND--NTVLLDppLIALDKDSPlrfaESFEVTvtkegeicgFKIHGQNvPFDAVVVDKSTGEgiIRSKEKLDC 118
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSG----ENGEVT---------YSIVSGN-EDGLFSIDPSTGE--ITTAKPLDR 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 12746426 119 ELQKDYTFTIQAYDCGKGPdgtgvkKSHKATVHIQVNDVNE 159
Cdd:cd11304  63 EEQSSYTLTVTATDGGGPP------LSSTATVTITVLDVND 97
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 87-162 1.70e-09

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: 55.05  E-value: 1.70e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12746426     87 FKIHGQNvPFDAVVVDKSTGegIIRSKEKLDCELQKDYTFTIQAYDCGKGPdgtgvkKSHKATVHIQVNDVNEYAP 162
Cdd:smart00112  15 YSILSGN-DDGLFSIDPETG--EITTTKPLDREEQPEYTLTVEATDGGGPP------LSSTATVTITVLDVNDNAP 81
Cadherin pfam00028
Cadherin domain;
180-257 5.24e-08

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 51.53  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746426   180 SSILRVEAVDADCSPQfSQIcSYEILTPDVP--FTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKIS 256
Cdd:pfam00028  13 TEVLTVTATDPDLGPN-GRI-FYSILGGGPGgnFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGGPPLSSTATVTIT 90


                  .
gi 12746426   257 V 257
Cdd:pfam00028  91 V 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 187-258 9.99e-08

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: 50.04  E-value: 9.99e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12746426    187 AVDADcSPQFSQIcSYEILTPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISVK 258
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILSGNDdgLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Cadherin pfam00028
Cadherin domain;
101-154 4.17e-03

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 37.28  E-value: 4.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 12746426   101 VDKSTGEgiIRSKEKLDCELQKDYTFTIQAYDCGKGPdgtgvkKSHKATVHIQV 154
Cdd:pfam00028  46 IDPDTGD--ISTTKPLDRESIGEYELTVEATDSGGPP------LSSTATVTITV 91
 
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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