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Conserved domains on  [gi|688611783|ref|XP_009295153|]
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calsyntenin-1 isoform X3 [Danio rerio]

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) ...
 544-903 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: 663.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  544 DVQLPEEVASAVKVEFNPNQSSLSLEGDDIESFEKVMQHISYLNSRQFPTPGIRHLRVSTTVKCFNEETCISVPDSEGYV 623
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  624 MVLQPEEPKISLSGIDHFARGAAEFESVEGVTLFPELRIVSTITREVEVEAEAEteaegeDDPTVQETVVSEEIMHNLDT 703
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGE------DDPTVQESLVSEEIVHNLDG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  704 CEVTVVGEDLNGDHESLEVDLAQIQQRALEMSSSNVGMVITGVNTMANYEQVLHLIRYRNWHTEALFDRKFKLVCSELNG 783
Cdd:pfam19699 155 CEVTVLGEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  784 RYISNEFKVEVNVIHTANPMDHANNAMVQPQFISQVQHASVDLSGHNLVNTHQASVVPSAATIVIVVCVSFLVFMIILGV 863
Cdd:pfam19699 235 RYASNEFKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGV 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 688611783  864 FRIRAAHQRTMRDQENGKENEMDWDDSALTITVNPMETYE 903
Cdd:pfam19699 315 FRIRSAHQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 165-255 3.18e-12

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: 63.49  E-value: 3.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783 165 SYKATVIEGKKYDS-IMKVEAVDADcSFQFSQIcSYEIVTPDV--PFTIDKD-GNIKNTEKLNYGKERMYKLTVTAYDCG 240
Cdd:cd11304    1 SYEVSVPENAPPGTvVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                         90
                 ....*....|....*
gi 688611783 241 KNRASEDVLVKINIK 255
Cdd:cd11304   79 GPPLSSTATVTITVL 93
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 38-156 1.39e-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: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  38 TYHGIVTEN---DDKVLLdppLIALDKD----APLRYaesfevtftkegeicgfRIHGQNvPFEAVVLDKSTGEgvIRAK 110
Cdd:cd11304    1 SYEVSVPENappGTVVLT---VSATDPDsgenGEVTY-----------------SIVSGN-EDGLFSIDPSTGE--ITTA 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 688611783 111 DKLDCELQKEHTFTIQAYDCGEGPdggnmkKSHKATVHIQVNDVNE 156
Cdd:cd11304   58 KPLDREEQSSYTLTVTATDGGGPP------LSSTATVTITVLDVND 97
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 544-903 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: 663.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  544 DVQLPEEVASAVKVEFNPNQSSLSLEGDDIESFEKVMQHISYLNSRQFPTPGIRHLRVSTTVKCFNEETCISVPDSEGYV 623
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  624 MVLQPEEPKISLSGIDHFARGAAEFESVEGVTLFPELRIVSTITREVEVEAEAEteaegeDDPTVQETVVSEEIMHNLDT 703
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGE------DDPTVQESLVSEEIVHNLDG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  704 CEVTVVGEDLNGDHESLEVDLAQIQQRALEMSSSNVGMVITGVNTMANYEQVLHLIRYRNWHTEALFDRKFKLVCSELNG 783
Cdd:pfam19699 155 CEVTVLGEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  784 RYISNEFKVEVNVIHTANPMDHANNAMVQPQFISQVQHASVDLSGHNLVNTHQASVVPSAATIVIVVCVSFLVFMIILGV 863
Cdd:pfam19699 235 RYASNEFKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGV 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 688611783  864 FRIRAAHQRTMRDQENGKENEMDWDDSALTITVNPMETYE 903
Cdd:pfam19699 315 FRIRSAHQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 165-255 3.18e-12

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: 63.49  E-value: 3.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783 165 SYKATVIEGKKYDS-IMKVEAVDADcSFQFSQIcSYEIVTPDV--PFTIDKD-GNIKNTEKLNYGKERMYKLTVTAYDCG 240
Cdd:cd11304    1 SYEVSVPENAPPGTvVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                         90
                 ....*....|....*
gi 688611783 241 KNRASEDVLVKINIK 255
Cdd:cd11304   79 GPPLSSTATVTITVL 93
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 38-156 1.39e-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: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  38 TYHGIVTEN---DDKVLLdppLIALDKD----APLRYaesfevtftkegeicgfRIHGQNvPFEAVVLDKSTGEgvIRAK 110
Cdd:cd11304    1 SYEVSVPENappGTVVLT---VSATDPDsgenGEVTY-----------------SIVSGN-EDGLFSIDPSTGE--ITTA 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 688611783 111 DKLDCELQKEHTFTIQAYDCGEGPdggnmkKSHKATVHIQVNDVNE 156
Cdd:cd11304   58 KPLDREEQSSYTLTVTATDGGGPP------LSSTATVTITVLDVND 97
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 84-159 5.77e-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: 53.89  E-value: 5.77e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688611783    84 FRIHGQNvPFEAVVLDKSTGegVIRAKDKLDCELQKEHTFTIQAYDCGEGPDGGNmkkshkATVHIQVNDVNEYSP 159
Cdd:smart00112  15 YSILSGN-DDGLFSIDPETG--EITTTKPLDREEQPEYTLTVEATDGGGPPLSST------ATVTITVLDVNDNAP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 184-255 2.19e-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: 2.19e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688611783   184 AVDADcSFQFSQIcSYEIVTPDV--PFTIDKD-GNIKNTEKLNYGKERMYKLTVTAYDCGKNRASEDVLVKINIK 255
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILSGNDdgLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Cadherin pfam00028
Cadherin domain;
178-254 4.46e-06

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 45.75  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  178 SIMKVEAVDADCSfQFSQIcSYEIVTPDVP--FTIDKD-GNIKNTEKLNYGKERMYKLTVTAYDCGKNRASEDVLVKINI 254
Cdd:pfam00028  14 EVLTVTATDPDLG-PNGRI-FYSILGGGPGgnFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGGPPLSSTATVTITV 91
Cadherin pfam00028
Cadherin domain;
39-151 2.54e-03

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 38.05  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783   39 YHGIVTENddkVLLDPPLI---ALDKDAPLRYAESFEVTFTKEGEIcgFRIHGQNvpfeavvldkstgeGVIRAKDKLDC 115
Cdd:pfam00028   1 YSASVPEN---APVGTEVLtvtATDPDLGPNGRIFYSILGGGPGGN--FRIDPDT--------------GDISTTKPLDR 61

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 688611783  116 ELQKEHTFTIQAYDCGEGPdggnmkKSHKATVHIQV 151
Cdd:pfam00028  62 ESIGEYELTVEATDSGGPP------LSSTATVTITV 91
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 544-903 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: 663.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  544 DVQLPEEVASAVKVEFNPNQSSLSLEGDDIESFEKVMQHISYLNSRQFPTPGIRHLRVSTTVKCFNEETCISVPDSEGYV 623
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  624 MVLQPEEPKISLSGIDHFARGAAEFESVEGVTLFPELRIVSTITREVEVEAEAEteaegeDDPTVQETVVSEEIMHNLDT 703
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITREVESEGDGE------DDPTVQESLVSEEIVHNLDG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  704 CEVTVVGEDLNGDHESLEVDLAQIQQRALEMSSSNVGMVITGVNTMANYEQVLHLIRYRNWHTEALFDRKFKLVCSELNG 783
Cdd:pfam19699 155 CEVTVLGEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  784 RYISNEFKVEVNVIHTANPMDHANNAMVQPQFISQVQHASVDLSGHNLVNTHQASVVPSAATIVIVVCVSFLVFMIILGV 863
Cdd:pfam19699 235 RYASNEFKVEVNVLHTANPVEHPNHMAAQPQFVHPVHHAFPDLSGHNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGV 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 688611783  864 FRIRAAHQRTMRDQENGKENEMDWDDSALTITVNPMETYE 903
Cdd:pfam19699 315 FRIRSAHQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 165-255 3.18e-12

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: 63.49  E-value: 3.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783 165 SYKATVIEGKKYDS-IMKVEAVDADcSFQFSQIcSYEIVTPDV--PFTIDKD-GNIKNTEKLNYGKERMYKLTVTAYDCG 240
Cdd:cd11304    1 SYEVSVPENAPPGTvVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGG 78

                         90
                 ....*....|....*
gi 688611783 241 KNRASEDVLVKINIK 255
Cdd:cd11304   79 GPPLSSTATVTITVL 93
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 38-156 1.39e-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: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  38 TYHGIVTEN---DDKVLLdppLIALDKD----APLRYaesfevtftkegeicgfRIHGQNvPFEAVVLDKSTGEgvIRAK 110
Cdd:cd11304    1 SYEVSVPENappGTVVLT---VSATDPDsgenGEVTY-----------------SIVSGN-EDGLFSIDPSTGE--ITTA 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 688611783 111 DKLDCELQKEHTFTIQAYDCGEGPdggnmkKSHKATVHIQVNDVNE 156
Cdd:cd11304   58 KPLDREEQSSYTLTVTATDGGGPP------LSSTATVTITVLDVND 97
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 84-159 5.77e-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: 53.89  E-value: 5.77e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688611783    84 FRIHGQNvPFEAVVLDKSTGegVIRAKDKLDCELQKEHTFTIQAYDCGEGPDGGNmkkshkATVHIQVNDVNEYSP 159
Cdd:smart00112  15 YSILSGN-DDGLFSIDPETG--EITTTKPLDREEQPEYTLTVEATDGGGPPLSST------ATVTITVLDVNDNAP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 184-255 2.19e-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: 2.19e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688611783   184 AVDADcSFQFSQIcSYEIVTPDV--PFTIDKD-GNIKNTEKLNYGKERMYKLTVTAYDCGKNRASEDVLVKINIK 255
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILSGNDdgLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Cadherin pfam00028
Cadherin domain;
178-254 4.46e-06

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 45.75  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783  178 SIMKVEAVDADCSfQFSQIcSYEIVTPDVP--FTIDKD-GNIKNTEKLNYGKERMYKLTVTAYDCGKNRASEDVLVKINI 254
Cdd:pfam00028  14 EVLTVTATDPDLG-PNGRI-FYSILGGGPGgnFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGGPPLSSTATVTITV 91
Cadherin pfam00028
Cadherin domain;
39-151 2.54e-03

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 38.05  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611783   39 YHGIVTENddkVLLDPPLI---ALDKDAPLRYAESFEVTFTKEGEIcgFRIHGQNvpfeavvldkstgeGVIRAKDKLDC 115
Cdd:pfam00028   1 YSASVPEN---APVGTEVLtvtATDPDLGPNGRIFYSILGGGPGGN--FRIDPDT--------------GDISTTKPLDR 61

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 688611783  116 ELQKEHTFTIQAYDCGEGPdggnmkKSHKATVHIQV 151
Cdd:pfam00028  62 ESIGEYELTVEATDSGGPP------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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