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Conserved domains on  [gi|40254527|ref|NP_071714|]
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calsyntenin-2 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 super family cl45102
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 548-896 8.56e-156

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: 463.09  E-value: 8.56e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   548 DINSLESLGRGIKYHFNPSQSILVMEGDDIGNINRALQKVSYINSRQFPTAGVRRLRLSSKVQCFGEDVCISIPDVDAYI 627
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   628 MVLQAIEPQITLQGTERFWRPAAQFESARGVTLFPDIKIVSTFAK-TEASGDMRATGTAPKSAVLEEMLHNLDFCDILVL 706
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITReVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   707 GGDLDPRQECLELNHSELHQRHLDATNSTAGYSIYGVGSMNRYEQVLHHLRYRNWHPTSLETRRFRIKCSELNGRYTSNE 786
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   787 FNLEVSVLHEVRVSdkEHVNHLIVQPPFLQSVHH--PE----TRSSIQRSSVVPSIATVVIIISVCMLVFVVAMGVYRVR 860
Cdd:pfam19699 241 FKVEVNVLHTANPV--EHPNHMAAQPQFVHPVHHafPDlsghNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIR 318

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 40254527   861 IAHQHFIQETEAAKEAEMDWDDSALTITVNPMEKHE 896
Cdd:pfam19699 319 SAHQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 167-258 8.14e-13

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: 65.03  E-value: 8.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527 167 YKAIVTEG-KIYDSILQVEAIDEDcSPQYSQIcNYEIVTTDV--PFAIDRN-GNIRNTEKLSYDKQHQYEILVTAYDCGQ 242
Cdd:cd11304   2 YEVSVPENaPPGTVVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGGG 79

                        90
                ....*....|....*.
gi 40254527 243 KPAAQDTLVQVDVKPV 258
Cdd:cd11304  80 PPLSSTATVTITVLDV 95
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 49-157 2.22e-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: 63.87  E-value: 2.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527  49 SYHGVITENN--DTVILDppLVALDKDAPVPfaGEIcAFKIHGQElPFEAVVLNKTSGEgrLRAKSPIDCELQKEYTFII 126
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSGEN--GEV-TYSIVSGN-EDGLFSIDPSTGE--ITTAKPLDREEQSSYTLTV 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 40254527 127 QAYDCGAGPREAawkkshKAVVHIQVKDVNE 157
Cdd:cd11304  73 TATDGGGPPLSS------TATVTITVLDVND 97
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 548-896 8.56e-156

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: 463.09  E-value: 8.56e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   548 DINSLESLGRGIKYHFNPSQSILVMEGDDIGNINRALQKVSYINSRQFPTAGVRRLRLSSKVQCFGEDVCISIPDVDAYI 627
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   628 MVLQAIEPQITLQGTERFWRPAAQFESARGVTLFPDIKIVSTFAK-TEASGDMRATGTAPKSAVLEEMLHNLDFCDILVL 706
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITReVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   707 GGDLDPRQECLELNHSELHQRHLDATNSTAGYSIYGVGSMNRYEQVLHHLRYRNWHPTSLETRRFRIKCSELNGRYTSNE 786
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   787 FNLEVSVLHEVRVSdkEHVNHLIVQPPFLQSVHH--PE----TRSSIQRSSVVPSIATVVIIISVCMLVFVVAMGVYRVR 860
Cdd:pfam19699 241 FKVEVNVLHTANPV--EHPNHMAAQPQFVHPVHHafPDlsghNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIR 318

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 40254527   861 IAHQHFIQETEAAKEAEMDWDDSALTITVNPMEKHE 896
Cdd:pfam19699 319 SAHQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 167-258 8.14e-13

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: 65.03  E-value: 8.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527 167 YKAIVTEG-KIYDSILQVEAIDEDcSPQYSQIcNYEIVTTDV--PFAIDRN-GNIRNTEKLSYDKQHQYEILVTAYDCGQ 242
Cdd:cd11304   2 YEVSVPENaPPGTVVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGGG 79

                        90
                ....*....|....*.
gi 40254527 243 KPAAQDTLVQVDVKPV 258
Cdd:cd11304  80 PPLSSTATVTITVLDV 95
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 49-157 2.22e-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: 63.87  E-value: 2.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527  49 SYHGVITENN--DTVILDppLVALDKDAPVPfaGEIcAFKIHGQElPFEAVVLNKTSGEgrLRAKSPIDCELQKEYTFII 126
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSGEN--GEV-TYSIVSGN-EDGLFSIDPSTGE--ITTAKPLDREEQSSYTLTV 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 40254527 127 QAYDCGAGPREAawkkshKAVVHIQVKDVNE 157
Cdd:cd11304  73 TATDGGGPPLSS------TATVTITVLDVND 97
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 68-160 6.95e-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: 56.20  E-value: 6.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527     68 VALDKDAPVPfaGEIcAFKIHGQElPFEAVVLNKTSGEgrLRAKSPIDCELQKEYTFIIQAYDCGAGPREAawkkshKAV 147
Cdd:smart00112   1 SATDADSGEN--GKV-TYSILSGN-DDGLFSIDPETGE--ITTTKPLDREEQPEYTLTVEATDGGGPPLSS------TAT 68

                           90
                   ....*....|...
gi 40254527    148 VHIQVKDVNEFAP 160
Cdd:smart00112  69 VTITVLDVNDNAP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 185-256 5.59e-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: 50.81  E-value: 5.59e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40254527    185 AIDEDcSPQYSQIcNYEIV--TTDVPFAIDRN-GNIRNTEKLSYDKQHQYEILVTAYDCGQKPAAQDTLVQVDVK 256
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILsgNDDGLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Cadherin pfam00028
Cadherin domain;
179-255 5.27e-07

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 48.45  E-value: 5.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   179 SILQVEAIDEDCSPQySQIcNYEIVTTDVP--FAIDR-NGNIRNTEKLSYDKQHQYEILVTAYDCGQKPAAQDTLVQVDV 255
Cdd:pfam00028  14 EVLTVTATDPDLGPN-GRI-FYSILGGGPGgnFRIDPdTGDISTTKPLDRESIGEYELTVEATDSGGPPLSSTATVTITV 91
Cadherin pfam00028
Cadherin domain;
50-152 1.46e-03

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 38.82  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527    50 YHGVITEN--NDTVILdpPLVALDKDAPvpfAGEICAFKI--HGQELPFEavvLNKTSGEgrLRAKSPIDCELQKEYTFI 125
Cdd:pfam00028   1 YSASVPENapVGTEVL--TVTATDPDLG---PNGRIFYSIlgGGPGGNFR---IDPDTGD--ISTTKPLDRESIGEYELT 70

                          90       100
                  ....*....|....*....|....*..
gi 40254527   126 IQAYDCGAGPREAawkkshKAVVHIQV 152
Cdd:pfam00028  71 VEATDSGGPPLSS------TATVTITV 91
 
Name Accession Description Interval E-value
CLSTN_C pfam19699
Calsyntenin C-terminal; This is the cytoplasmic C-terminal domain of clasyntenin (CLSTN) ...
 548-896 8.56e-156

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: 463.09  E-value: 8.56e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   548 DINSLESLGRGIKYHFNPSQSILVMEGDDIGNINRALQKVSYINSRQFPTAGVRRLRLSSKVQCFGEDVCISIPDVDAYI 627
Cdd:pfam19699   1 DLQDPENSGSGVKVHFNPSQSVLTLEGDDIESLNKAMQHVSYVNSRQFPTPGVRRLKLTTSVKCFNEESCISIPDVEGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   628 MVLQAIEPQITLQGTERFWRPAAQFESARGVTLFPDIKIVSTFAK-TEASGDMRATGTAPKSAVLEEMLHNLDFCDILVL 706
Cdd:pfam19699  81 MVLQPEEPKISLSGIDHFARPASEFESPEGVPLFPELRIVSTITReVESEGDGEDDPTVQESLVSEEIVHNLDGCEVTVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   707 GGDLDPRQECLELNHSELHQRHLDATNSTAGYSIYGVGSMNRYEQVLHHLRYRNWHPTSLETRRFRIKCSELNGRYTSNE 786
Cdd:pfam19699 161 GEELNPEQESLEVDMALLQQRGLEISSSTLGITITGVESMASYEEVLHLIRYRNWNTESLFERKFKLSCSELNGRYASNE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   787 FNLEVSVLHEVRVSdkEHVNHLIVQPPFLQSVHH--PE----TRSSIQRSSVVPSIATVVIIISVCMLVFVVAMGVYRVR 860
Cdd:pfam19699 241 FKVEVNVLHTANPV--EHPNHMAAQPQFVHPVHHafPDlsghNLANPHPSSVVPSAATVVIVVCVSFLVFMIILGVFRIR 318

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 40254527   861 IAHQHFIQETEAAKEAEMDWDDSALTITVNPMEKHE 896
Cdd:pfam19699 319 SAHQRGMRDQEGGKENEMDWDDSALTITVNPMETYE 354
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 167-258 8.14e-13

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: 65.03  E-value: 8.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527 167 YKAIVTEG-KIYDSILQVEAIDEDcSPQYSQIcNYEIVTTDV--PFAIDRN-GNIRNTEKLSYDKQHQYEILVTAYDCGQ 242
Cdd:cd11304   2 YEVSVPENaPPGTVVLTVSATDPD-SGENGEV-TYSIVSGNEdgLFSIDPStGEITTAKPLDREEQSSYTLTVTATDGGG 79

                        90
                ....*....|....*.
gi 40254527 243 KPAAQDTLVQVDVKPV 258
Cdd:cd11304  80 PPLSSTATVTITVLDV 95
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 49-157 2.22e-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: 63.87  E-value: 2.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527  49 SYHGVITENN--DTVILDppLVALDKDAPVPfaGEIcAFKIHGQElPFEAVVLNKTSGEgrLRAKSPIDCELQKEYTFII 126
Cdd:cd11304   1 SYEVSVPENAppGTVVLT--VSATDPDSGEN--GEV-TYSIVSGN-EDGLFSIDPSTGE--ITTAKPLDREEQSSYTLTV 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 40254527 127 QAYDCGAGPREAawkkshKAVVHIQVKDVNE 157
Cdd:cd11304  73 TATDGGGPPLSS------TATVTITVLDVND 97
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 68-160 6.95e-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: 56.20  E-value: 6.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527     68 VALDKDAPVPfaGEIcAFKIHGQElPFEAVVLNKTSGEgrLRAKSPIDCELQKEYTFIIQAYDCGAGPREAawkkshKAV 147
Cdd:smart00112   1 SATDADSGEN--GKV-TYSILSGN-DDGLFSIDPETGE--ITTTKPLDREEQPEYTLTVEATDGGGPPLSS------TAT 68

                           90
                   ....*....|...
gi 40254527    148 VHIQVKDVNEFAP 160
Cdd:smart00112  69 VTITVLDVNDNAP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 185-256 5.59e-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: 50.81  E-value: 5.59e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40254527    185 AIDEDcSPQYSQIcNYEIV--TTDVPFAIDRN-GNIRNTEKLSYDKQHQYEILVTAYDCGQKPAAQDTLVQVDVK 256
Cdd:smart00112   2 ATDAD-SGENGKV-TYSILsgNDDGLFSIDPEtGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVL 74
Cadherin pfam00028
Cadherin domain;
179-255 5.27e-07

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 48.45  E-value: 5.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527   179 SILQVEAIDEDCSPQySQIcNYEIVTTDVP--FAIDR-NGNIRNTEKLSYDKQHQYEILVTAYDCGQKPAAQDTLVQVDV 255
Cdd:pfam00028  14 EVLTVTATDPDLGPN-GRI-FYSILGGGPGgnFRIDPdTGDISTTKPLDRESIGEYELTVEATDSGGPPLSSTATVTITV 91
Cadherin pfam00028
Cadherin domain;
50-152 1.46e-03

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 38.82  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254527    50 YHGVITEN--NDTVILdpPLVALDKDAPvpfAGEICAFKI--HGQELPFEavvLNKTSGEgrLRAKSPIDCELQKEYTFI 125
Cdd:pfam00028   1 YSASVPENapVGTEVL--TVTATDPDLG---PNGRIFYSIlgGGPGGNFR---IDPDTGD--ISTTKPLDRESIGEYELT 70

                          90       100
                  ....*....|....*....|....*..
gi 40254527   126 IQAYDCGAGPREAawkkshKAVVHIQV 152
Cdd:pfam00028  71 VEATDSGGPPLSS------TATVTITV 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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