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Conserved domains on  [gi|57242757|ref|NP_001009566|]
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calsyntenin-1 isoform 1 precursor [Homo sapiens]

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) ...
 566-919 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: 709.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   566 DLQVLEDSGRGVQIQAHPSQLVLTLEGEDLGELDKAMQHISYLNSRQFPTPGIRRLKITSTIKCFNEATCISVPPVDGYV 645
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   646 MVLQPEEPKISLSGVHHFARAASEFESSEGVFLFPELRIISTITREVEPEGDGAEDPTVQESLVSEEIVHDLDTCEVTVE 725
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   726 GEELNHEQESLEVDMARLQQKGIEVSSSELGMTFTGVDTMASYEEVLHLLRYRNWHARSLLDRKFKLICSELNGRYISNE 805
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   806 FKVEVNVIHTANPMEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSFLVFMIILGVFRIRAA 885
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320

                         330       340       350
                  ....*....|....*....|....*....|....
gi 57242757   886 HRRTMRDQDTGKENEMDWDDSALTITVNPMETYE 919
Cdd:pfam19699 321 HQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 168-258 4.85e-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: 60.02  E-value: 4.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757 168 SYKATVIEGKQYDS-ILRVEAVDADcSPQFSQIcSYEIITPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCG 243
Cdd:cd11304   1 SYEVSVPENAPPGTvVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                        90
                ....*....|....*
gi 57242757 244 KKRATEDVLVKISIK 258
Cdd:cd11304  79 GPPLSSTATVTITVL 93
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 41-159 1.34e-10

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: 58.86  E-value: 1.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757  41 TYHGIVTEND--NTVLLDppLIALDKDAPlrfaESFEVTvtkegeicgFKIHGQNvPFDAVVVDKSTGEgvIRSKEKLDC 118
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSG----ENGEVT---------YSIVSGN-EDGLFSIDPSTGE--ITTAKPLDR 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 57242757 119 ELQKDYSFTIQAYDCGKGPdgtnvkKSHKATVHIQVNDVNE 159
Cdd:cd11304  63 EEQSSYTLTVTATDGGGPP------LSSTATVTITVLDVND 97
Laminin_G_3 super family cl48183
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 365-477 1.40e-03

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


The actual alignment was detected with superfamily member pfam13385:

Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 40.06  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   365 FNGTQAVRIPDGVVSVSPkepFTISVWMRHGPFGRKKETILCSSDKTdmnrhHYSLYV-HGCRLIFLFRQDPSEEKKYRP 443
Cdd:pfam13385   1 DGGSDYVTLPDALLPTSD---FTVSAWVKPDSLPGWARAIISSSGGG-----GYSLGLdGDGRLRFAVNGGNGGWDTVTS 72

                          90       100       110
                  ....*....|....*....|....*....|....
gi 57242757   444 AefhwklNQVCDEEWHHYVLNVEFPSVTLYVDGT 477
Cdd:pfam13385  73 G------ASVPLGQWTHVAVTYDGGTLRLYVNGV 100
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 566-919 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: 709.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   566 DLQVLEDSGRGVQIQAHPSQLVLTLEGEDLGELDKAMQHISYLNSRQFPTPGIRRLKITSTIKCFNEATCISVPPVDGYV 645
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   646 MVLQPEEPKISLSGVHHFARAASEFESSEGVFLFPELRIISTITREVEPEGDGAEDPTVQESLVSEEIVHDLDTCEVTVE 725
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   726 GEELNHEQESLEVDMARLQQKGIEVSSSELGMTFTGVDTMASYEEVLHLLRYRNWHARSLLDRKFKLICSELNGRYISNE 805
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   806 FKVEVNVIHTANPMEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSFLVFMIILGVFRIRAA 885
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320

                         330       340       350
                  ....*....|....*....|....*....|....
gi 57242757   886 HRRTMRDQDTGKENEMDWDDSALTITVNPMETYE 919
Cdd:pfam19699 321 HQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 168-258 4.85e-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: 60.02  E-value: 4.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757 168 SYKATVIEGKQYDS-ILRVEAVDADcSPQFSQIcSYEIITPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCG 243
Cdd:cd11304   1 SYEVSVPENAPPGTvVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                        90
                ....*....|....*
gi 57242757 244 KKRATEDVLVKISIK 258
Cdd:cd11304  79 GPPLSSTATVTITVL 93
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 41-159 1.34e-10

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: 58.86  E-value: 1.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757  41 TYHGIVTEND--NTVLLDppLIALDKDAPlrfaESFEVTvtkegeicgFKIHGQNvPFDAVVVDKSTGEgvIRSKEKLDC 118
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSG----ENGEVT---------YSIVSGN-EDGLFSIDPSTGE--ITTAKPLDR 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 57242757 119 ELQKDYSFTIQAYDCGKGPdgtnvkKSHKATVHIQVNDVNE 159
Cdd:cd11304  63 EEQSSYTLTVTATDGGGPP------LSSTATVTITVLDVND 97
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 87-162 3.98e-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: 54.28  E-value: 3.98e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57242757     87 FKIHGQNvPFDAVVVDKSTGegVIRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNvkkshkATVHIQVNDVNEYAP 162
Cdd:smart00112  15 YSILSGN-DDGLFSIDPETG--EITTTKPLDREEQPEYTLTVEATDGGGPPLSST------ATVTITVLDVNDNAP 81
Cadherin pfam00028
Cadherin domain;
169-257 1.52e-07

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 49.99  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   169 YKATVIEGKQYDS-ILRVEAVDADCSPQfSQIcSYEIITPDVP--FTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGK 244
Cdd:pfam00028   1 YSASVPENAPVGTeVLTVTATDPDLGPN-GRI-FYSILGGGPGgnFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGG 78

                          90
                  ....*....|...
gi 57242757   245 KRATEDVLVKISI 257
Cdd:pfam00028  79 PPLSSTATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 187-258 2.21e-07

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: 49.27  E-value: 2.21e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57242757    187 AVDADcSPQFSQIcSYEIITPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIK 258
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILSGNDdgLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 365-477 1.40e-03

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 40.06  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   365 FNGTQAVRIPDGVVSVSPkepFTISVWMRHGPFGRKKETILCSSDKTdmnrhHYSLYV-HGCRLIFLFRQDPSEEKKYRP 443
Cdd:pfam13385   1 DGGSDYVTLPDALLPTSD---FTVSAWVKPDSLPGWARAIISSSGGG-----GYSLGLdGDGRLRFAVNGGNGGWDTVTS 72

                          90       100       110
                  ....*....|....*....|....*....|....
gi 57242757   444 AefhwklNQVCDEEWHHYVLNVEFPSVTLYVDGT 477
Cdd:pfam13385  73 G------ASVPLGQWTHVAVTYDGGTLRLYVNGV 100
Cadherin pfam00028
Cadherin domain;
101-154 4.57e-03

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 37.28  E-value: 4.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 57242757   101 VDKSTGEgvIRSKEKLDCELQKDYSFTIQAYDCGKGPdgtnvkKSHKATVHIQV 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) ...
 566-919 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: 709.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   566 DLQVLEDSGRGVQIQAHPSQLVLTLEGEDLGELDKAMQHISYLNSRQFPTPGIRRLKITSTIKCFNEATCISVPPVDGYV 645
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   646 MVLQPEEPKISLSGVHHFARAASEFESSEGVFLFPELRIISTITREVEPEGDGAEDPTVQESLVSEEIVHDLDTCEVTVE 725
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   726 GEELNHEQESLEVDMARLQQKGIEVSSSELGMTFTGVDTMASYEEVLHLLRYRNWHARSLLDRKFKLICSELNGRYISNE 805
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   806 FKVEVNVIHTANPMEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSFLVFMIILGVFRIRAA 885
Cdd:pfam19699 241 FKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIRSA 320

                         330       340       350
                  ....*....|....*....|....*....|....
gi 57242757   886 HRRTMRDQDTGKENEMDWDDSALTITVNPMETYE 919
Cdd:pfam19699 321 HQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 168-258 4.85e-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: 60.02  E-value: 4.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757 168 SYKATVIEGKQYDS-ILRVEAVDADcSPQFSQIcSYEIITPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCG 243
Cdd:cd11304   1 SYEVSVPENAPPGTvVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                        90
                ....*....|....*
gi 57242757 244 KKRATEDVLVKISIK 258
Cdd:cd11304  79 GPPLSSTATVTITVL 93
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 41-159 1.34e-10

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: 58.86  E-value: 1.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757  41 TYHGIVTEND--NTVLLDppLIALDKDAPlrfaESFEVTvtkegeicgFKIHGQNvPFDAVVVDKSTGEgvIRSKEKLDC 118
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSG----ENGEVT---------YSIVSGN-EDGLFSIDPSTGE--ITTAKPLDR 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 57242757 119 ELQKDYSFTIQAYDCGKGPdgtnvkKSHKATVHIQVNDVNE 159
Cdd:cd11304  63 EEQSSYTLTVTATDGGGPP------LSSTATVTITVLDVND 97
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 87-162 3.98e-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: 54.28  E-value: 3.98e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57242757     87 FKIHGQNvPFDAVVVDKSTGegVIRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNvkkshkATVHIQVNDVNEYAP 162
Cdd:smart00112  15 YSILSGN-DDGLFSIDPETG--EITTTKPLDREEQPEYTLTVEATDGGGPPLSST------ATVTITVLDVNDNAP 81
Cadherin pfam00028
Cadherin domain;
169-257 1.52e-07

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 49.99  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   169 YKATVIEGKQYDS-ILRVEAVDADCSPQfSQIcSYEIITPDVP--FTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGK 244
Cdd:pfam00028   1 YSASVPENAPVGTeVLTVTATDPDLGPN-GRI-FYSILGGGPGgnFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGG 78

                          90
                  ....*....|...
gi 57242757   245 KRATEDVLVKISI 257
Cdd:pfam00028  79 PPLSSTATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 187-258 2.21e-07

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: 49.27  E-value: 2.21e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57242757    187 AVDADcSPQFSQIcSYEIITPDV--PFTVDKD-GYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIK 258
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILSGNDdgLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 365-477 1.40e-03

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 40.06  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57242757   365 FNGTQAVRIPDGVVSVSPkepFTISVWMRHGPFGRKKETILCSSDKTdmnrhHYSLYV-HGCRLIFLFRQDPSEEKKYRP 443
Cdd:pfam13385   1 DGGSDYVTLPDALLPTSD---FTVSAWVKPDSLPGWARAIISSSGGG-----GYSLGLdGDGRLRFAVNGGNGGWDTVTS 72

                          90       100       110
                  ....*....|....*....|....*....|....
gi 57242757   444 AefhwklNQVCDEEWHHYVLNVEFPSVTLYVDGT 477
Cdd:pfam13385  73 G------ASVPLGQWTHVAVTYDGGTLRLYVNGV 100
Cadherin pfam00028
Cadherin domain;
101-154 4.57e-03

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 37.28  E-value: 4.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 57242757   101 VDKSTGEgvIRSKEKLDCELQKDYSFTIQAYDCGKGPdgtnvkKSHKATVHIQV 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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