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Conserved domains on  [gi|193207741|ref|NP_506256|]
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Cadherin EGF LAG seven-pass G-type receptor fmi-1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
274-371 1.26e-37

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: 137.06  E-value: 1.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  274 SYFGEIREDAPIGTTVLSVFARDLDSGENGEIEYSLGEGNGKNLLAINAKSGVIQTAAPLDRETLSLIRLDVIASDKGTP 353
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                          90
                  ....*....|....*...
gi 193207741  354 KRESTAMVEITVVDVNDN 371
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
686-780 2.86e-32

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: 122.04  E-value: 2.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  686 PFSVKIPEHSPIGYPVITLKAEDHDRGDNARIVYSI---DSSQFFRIDPSSGDISVSSDLDREDRATFSVIVTASDHASP 762
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIvsgNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                          90
                  ....*....|....*...
gi 193207741  763 PLNTSTQIEVILDDINDN 780
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
486-577 4.69e-32

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: 121.27  E-value: 4.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  486 ITLEENVAIGEEVGRVYAIDEDSGPNGIIKYSMEGSED---FIIDEDSGLIKTTKLLDRETTARYSLKVTARDMGTPSLN 562
Cdd:cd11304     4 VSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEdglFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPPLS 83
                          90
                  ....*....|....*
gi 193207741  563 TSTTIAVVLKDINDN 577
Cdd:cd11304    84 STATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
788-888 3.72e-31

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: 118.57  E-value: 3.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  788 SYAATISEDIPVGTSFLQVSAIDADIGPNGIVDYFLnesSSSPSIQLFRLDRTSGTLRVSSKLDREQFAVIVLPIFARDR 867
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSI---VSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77
                          90       100
                  ....*....|....*....|.
gi 193207741  868 GTPSLSAASEITLTLSDVNDN 888
Cdd:cd11304    78 GGPPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
379-475 3.33e-28

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: 110.48  E-value: 3.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  379 SYNVTILENITIPAVIATVKATDEDFGTNGKVHYSMASSSGIGGLTIDYSTGEVTLRERIDA-KNSPITAVIRAKDGAQP 457
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDReEQSSYTLTVTATDGGGP 80
                          90
                  ....*....|....*...
gi 193207741  458 ALSSTVPLTINVIDINDH 475
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
896-996 2.75e-26

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: 104.70  E-value: 2.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  896 SYDLYIAENSPVGSTVGTIVARDADEGDNADISFRIFGGADAKLFDIEEDaeqNGVVRilTRAEFDYEAKAnKFFFELQA 975
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPS---TGEIT--TAKPLDREEQS-SYTLTVTA 74
                          90       100
                  ....*....|....*....|....
gi 193207741  976 SSG---QLSSTVPVRIHVSDVNDN 996
Cdd:cd11304    75 TDGggpPLSSTATVTITVLDVNDN 98
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1333-1504 3.41e-23

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


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 97.87  E-value: 3.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 1333 SVSFDGEGLLNV-NLDLPRTQWTMKFRVSTIAHNGVLVFTGDK-RSDFVEVSVVDRVLKVQFSLGGEKIDAkmenDVENR 1410
Cdd:cd00110     1 GVSFSGSSYVRLpTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVL----SSKTP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 1411 INDGEWHTVALEYSNKQITMSLDDCetnpslLLNTSPNCAIRAKLNLEKKcedptvpcyryldisngLFLGGRPGTSKQ- 1489
Cdd:cd00110    77 LNDGQWHSVSVERNGRSVTLSVDGE------RVVESGSPGGSALLNLDGP-----------------LYLGGLPEDLKSp 133
                         170
                  ....*....|....*...
gi 193207741 1490 ---IEKAFSGCISDLSVD 1504
Cdd:cd00110   134 glpVSPGFVGCIRDLKVN 151
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
170-266 1.68e-22

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: 93.92  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  170 YVKELPEDTPIETIIASVKASHA---SSQPLYYSMVAPQDSrsqNLFTLDTMSGEIRLAKSMDREVLDKHILKVTAYERV 246
Cdd:cd11304     2 YEVSVPENAPPGTVVLTVSATDPdsgENGEVTYSIVSGNED---GLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGG 78
                          90       100
                  ....*....|....*....|
gi 193207741  247 DPTISASTTVVVHVLDVQDN 266
Cdd:cd11304    79 GPPLSSTATVTITVLDVNDN 98
HormR smart00008
Domain present in hormone receptors;
1917-1974 1.00e-12

Domain present in hormone receptors;


:

Pssm-ID: 214468  Cd Length: 70  Bit Score: 65.23  E-value: 1.00e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193207741   1917 CPSEIEYSIQWPASQKGSIVRQSCPVGESGL-----ATRKCLETGRWS--DVNAWNCTRPEYSIM 1974
Cdd:smart00008    5 CPATWDGIICWPQTPAGQLVEVPCPKYFSGFsyktgASRNCTENGGWSppFPNYSNCTSNDYEEL 69
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
2170-2218 2.07e-11

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


:

Pssm-ID: 197639  Cd Length: 49  Bit Score: 60.86  E-value: 2.07e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 193207741   2170 KYPECVRFDEKSGTWTARGAALIGLNLTHAACEYNRIGVFTMFVNDQSS 2218
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1252-1287 3.89e-09

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 54.18  E-value: 3.89e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 193207741 1252 IDECYRGR-CSNNSTCVAFENTYQCECKPGWIGRHCE 1287
Cdd:cd00054     2 IDECASGNpCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1582-1716 1.08e-08

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


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 56.27  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 1582 FEEESFV-LYQPSQVSVPFEVSFEFRTSRADMQVFALEFTQRSVHYNLEVDDGTLK--YNIGDSEVELPAPE-VTSKHWM 1657
Cdd:cd00110     4 FSGSSYVrLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVlrYDLGSGSLVLSSKTpLNDGQWH 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193207741 1658 NVVIKFEADSVATSINGIYSAEAKASISDMNL---ESLYFGIAPGTGHPSR------FEGCIRNVLVD 1716
Cdd:cd00110    84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLnldGPLYLGGLPEDLKSPGlpvspgFVGCIRDLKVN 151
7tm_GPCRs super family cl28897
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
2237-2455 1.29e-07

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


The actual alignment was detected with superfamily member cd15040:

Pssm-ID: 475119 [Multi-domain]  Cd Length: 253  Bit Score: 55.27  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2237 VALFLCFLSILLTLSRRSLKTHSVRIgfILFFAINILNLFFVhkTAINQAY----CPVRNAMLSFTSSAPFAWLFLYGLY 2312
Cdd:cd15040    17 LGLLLTIITYILFRKLRKRKPTKILL--NLCLALLLANLLFL--FGINSTDnpvlCTAVAALLHYFLLASFMWMLVEALL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2313 IYRML---ADGSSSPSLTTSLLVGIVFPCLISFTTFFV--------TDQCSLSPHLWLFWCIILPIGLFLL--LSFYAAA 2379
Cdd:cd15040    93 LYLRLvkvFGTYPRHFILKYALIGWGLPLIIVIITLAVdpdsygnsSGYCWLSNGNGLYYAFLGPVLLIILvnLVIFVLV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2380 TSVLVSLHKKydVFVAKYNVKRAVFQHFILTIFTLGMT-LTGLFAnqlplpmeimEISQSII--YLIAA------LVIFL 2450
Cdd:cd15040   173 LRKLLRLSAK--RNKKKRKKTKAQLRAAVSLFFLLGLTwIFGILA----------IFGARVVfqYLFAIfnslqgFFIFI 240

                  ....*.
gi 193207741 2451 W-CVCD 2455
Cdd:cd15040   241 FhCLRN 246
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1865-1911 9.46e-06

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 44.65  E-value: 9.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 193207741 1865 CEC-GFGADSTEC-SADGHCKCNGDAVGRRCDRCSRFDHQLDSKTLKCR 1911
Cdd:cd00055     2 CDCnGHGSLSGQCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1774-1808 2.06e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 2.06e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 193207741 1774 CSVANVCS-SGTCVssNTTAGYECICPAGKTGKNCQ 1808
Cdd:cd00054     5 CASGNPCQnGGTCV--NTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
274-371 1.26e-37

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: 137.06  E-value: 1.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  274 SYFGEIREDAPIGTTVLSVFARDLDSGENGEIEYSLGEGNGKNLLAINAKSGVIQTAAPLDRETLSLIRLDVIASDKGTP 353
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                          90
                  ....*....|....*...
gi 193207741  354 KRESTAMVEITVVDVNDN 371
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
686-780 2.86e-32

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: 122.04  E-value: 2.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  686 PFSVKIPEHSPIGYPVITLKAEDHDRGDNARIVYSI---DSSQFFRIDPSSGDISVSSDLDREDRATFSVIVTASDHASP 762
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIvsgNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                          90
                  ....*....|....*...
gi 193207741  763 PLNTSTQIEVILDDINDN 780
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
486-577 4.69e-32

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: 121.27  E-value: 4.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  486 ITLEENVAIGEEVGRVYAIDEDSGPNGIIKYSMEGSED---FIIDEDSGLIKTTKLLDRETTARYSLKVTARDMGTPSLN 562
Cdd:cd11304     4 VSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEdglFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPPLS 83
                          90
                  ....*....|....*
gi 193207741  563 TSTTIAVVLKDINDN 577
Cdd:cd11304    84 STATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
788-888 3.72e-31

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: 118.57  E-value: 3.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  788 SYAATISEDIPVGTSFLQVSAIDADIGPNGIVDYFLnesSSSPSIQLFRLDRTSGTLRVSSKLDREQFAVIVLPIFARDR 867
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSI---VSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77
                          90       100
                  ....*....|....*....|.
gi 193207741  868 GTPSLSAASEITLTLSDVNDN 888
Cdd:cd11304    78 GGPPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
379-475 3.33e-28

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: 110.48  E-value: 3.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  379 SYNVTILENITIPAVIATVKATDEDFGTNGKVHYSMASSSGIGGLTIDYSTGEVTLRERIDA-KNSPITAVIRAKDGAQP 457
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDReEQSSYTLTVTATDGGGP 80
                          90
                  ....*....|....*...
gi 193207741  458 ALSSTVPLTINVIDINDH 475
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
294-373 1.70e-27

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: 107.82  E-value: 1.70e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    294 ARDLDSGENGEIEYSLGEGNGKNLLAINAKSGVIQTAAPLDRETLSLIRLDVIASDKGTPKRESTAMVEITVVDVNDNAP 373
Cdd:smart00112    2 ATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNAP 81
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
896-996 2.75e-26

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: 104.70  E-value: 2.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  896 SYDLYIAENSPVGSTVGTIVARDADEGDNADISFRIFGGADAKLFDIEEDaeqNGVVRilTRAEFDYEAKAnKFFFELQA 975
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPS---TGEIT--TAKPLDREEQS-SYTLTVTA 74
                          90       100
                  ....*....|....*....|....
gi 193207741  976 SSG---QLSSTVPVRIHVSDVNDN 996
Cdd:cd11304    75 TDGggpPLSSTATVTITVLDVNDN 98
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
503-579 2.90e-26

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: 104.35  E-value: 2.90e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    503 AIDEDSGPNGIIKYSMEGSED---FIIDEDSGLIKTTKLLDRETTARYSLKVTARDMGTPSLNTSTTIAVVLKDINDNAP 579
Cdd:smart00112    2 ATDADSGENGKVTYSILSGNDdglFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNAP 81
Cadherin pfam00028
Cadherin domain;
275-365 1.41e-24

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 99.68  E-value: 1.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   275 YFGEIREDAPIGTTVLSVFARDLDSGENGEIEYSLGEGNGKNLLAINAKSGVIQTAAPLDRETLSLIRLDVIASDKGTPK 354
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80
                           90
                   ....*....|.
gi 193207741   355 RESTAMVEITV 365
Cdd:pfam00028   81 LSSTATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
705-782 6.05e-24

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: 97.42  E-value: 6.05e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    705 KAEDHDRGDNARIVYSIDSS---QFFRIDPSSGDISVSSDLDREDRATFSVIVTASDHASPPLNTSTQIEVILDDINDNS 781
Cdd:smart00112    1 SATDADSGENGKVTYSILSGnddGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80

                    .
gi 193207741    782 P 782
Cdd:smart00112   81 P 81
Cadherin pfam00028
Cadherin domain;
687-774 2.17e-23

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 96.22  E-value: 2.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   687 FSVKIPEHSPIGYPVITLKAEDHDRGDNARIVYSI---DSSQFFRIDPSSGDISVSSDLDREDRATFSVIVTASDHASPP 763
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSIlggGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80
                           90
                   ....*....|.
gi 193207741   764 LNTSTQIEVIL 774
Cdd:pfam00028   81 LSSTATVTITV 91
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1333-1504 3.41e-23

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 97.87  E-value: 3.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 1333 SVSFDGEGLLNV-NLDLPRTQWTMKFRVSTIAHNGVLVFTGDK-RSDFVEVSVVDRVLKVQFSLGGEKIDAkmenDVENR 1410
Cdd:cd00110     1 GVSFSGSSYVRLpTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVL----SSKTP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 1411 INDGEWHTVALEYSNKQITMSLDDCetnpslLLNTSPNCAIRAKLNLEKKcedptvpcyryldisngLFLGGRPGTSKQ- 1489
Cdd:cd00110    77 LNDGQWHSVSVERNGRSVTLSVDGE------RVVESGSPGGSALLNLDGP-----------------LYLGGLPEDLKSp 133
                         170
                  ....*....|....*...
gi 193207741 1490 ---IEKAFSGCISDLSVD 1504
Cdd:cd00110   134 glpVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1354-1506 6.20e-23

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 96.64  E-value: 6.20e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   1354 TMKFRVSTIAHNGVLVFTGDK-RSDFVEVSVVDRVLKVQFSLGGEKIDAKMENdveNRINDGEWHTVALEYSNKQITMSL 1432
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDP---TPLNDGQWHRVAVERNGRSVTLSV 77
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193207741   1433 DDCEtnpsLLLNTSPncairaklnlekkcedptvPCYRYLDISNGLFLGGRPGTSKQ----IEKAFSGCISDLSVDKE 1506
Cdd:smart00282   78 DGGN----RVSGESP-------------------GGLTILNLDGPLYLGGLPEDLKLpplpVTPGFRGCIRNLKVNGK 132
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
170-266 1.68e-22

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: 93.92  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  170 YVKELPEDTPIETIIASVKASHA---SSQPLYYSMVAPQDSrsqNLFTLDTMSGEIRLAKSMDREVLDKHILKVTAYERV 246
Cdd:cd11304     2 YEVSVPENAPPGTVVLTVSATDPdsgENGEVTYSIVSGNED---GLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGG 78
                          90       100
                  ....*....|....*....|
gi 193207741  247 DPTISASTTVVVHVLDVQDN 266
Cdd:cd11304    79 GPPLSSTATVTITVLDVNDN 98
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
807-890 2.62e-21

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: 90.10  E-value: 2.62e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    807 SAIDADIGPNGIVDYFLnesSSSPSIQLFRLDRTSGTLRVSSKLDREQFAVIVLPIFARDRGTPSLSAASEITLTLSDVN 886
Cdd:smart00112    1 SATDADSGENGKVTYSI---LSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVN 77

                    ....
gi 193207741    887 DNAP 890
Cdd:smart00112   78 DNAP 81
Cadherin pfam00028
Cadherin domain;
486-571 3.24e-21

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 90.05  E-value: 3.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   486 ITLEENVAIGEEVGRVYAIDEDSGPNGIIKYSM-EGSED--FIIDEDSGLIKTTKLLDRETTARYSLKVTARDMGTPSLN 562
Cdd:pfam00028    3 ASVPENAPVGTEVLTVTATDPDLGPNGRIFYSIlGGGPGgnFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPPLS 82

                   ....*....
gi 193207741   563 TSTTIAVVL 571
Cdd:pfam00028   83 STATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
398-477 4.00e-20

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: 86.63  E-value: 4.00e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    398 KATDEDFGTNGKVHYSMASSSGIGGLTIDYSTGEVTLRERIDAKNSPI-TAVIRAKDGAQPALSSTVPLTINVIDINDHA 476
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEyTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80

                    .
gi 193207741    477 P 477
Cdd:smart00112   81 P 81
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1365-1506 1.19e-19

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 87.09  E-value: 1.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  1365 NGVLVFTGDKRSDFVEVSVVDRVLKVQFSLGGEKIDAKMENdveNRINDGEWHTVALEYSNKQITMSLDDCETNPSLLLN 1444
Cdd:pfam02210    7 NGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSG---KNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPPG 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193207741  1445 TSPNcairaklnlekkcedptvpcyryLDISNGLFLGG----RPGTSKQIEKAFSGCISDLSVDKE 1506
Cdd:pfam02210   84 ESLL-----------------------LNLNGPLYLGGlpplLLLPALPVRAGFVGCIRDVRVNGE 126
Cadherin pfam00028
Cadherin domain;
789-882 4.86e-19

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 83.89  E-value: 4.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   789 YAATISEDIPVGTSFLQVSAIDADIGPNGIVDYFLnesSSSPSIQLFRLDRTSGTLRVSSKLDREQFAVIVLPIFARDRG 868
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSI---LGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSG 77
                           90
                   ....*....|....
gi 193207741   869 TPSLSAASEITLTL 882
Cdd:pfam00028   78 GPPLSSTATVTITV 91
Cadherin pfam00028
Cadherin domain;
380-470 1.81e-18

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 82.35  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   380 YNVTILENITIPAVIATVKATDEDFGTNGKVHYSMASSSGIGGLTIDYSTGEVTLRERIDAKNSPI-TAVIRAKDGAQPA 458
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEyELTVEATDSGGPP 80
                           90
                   ....*....|..
gi 193207741   459 LSSTVPLTINVI 470
Cdd:pfam00028   81 LSSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
915-998 1.40e-16

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: 76.62  E-value: 1.40e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    915 VARDADEGDNADISFRIFGGADAKLFDIEEDaeqNGVvrILTRAEFDYEAKANkFFFELQASSG---QLSSTVPVRIHVS 991
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPE---TGE--ITTTKPLDREEQPE-YTLTVEATDGggpPLSSTATVTITVL 74

                    ....*..
gi 193207741    992 DVNDNKP 998
Cdd:smart00112   75 DVNDNAP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
197-268 3.31e-13

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: 66.99  E-value: 3.31e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193207741    197 LYYSMVapqDSRSQNLFTLDTMSGEIRLAKSMDREVLDKHILKVTAYERVDPTISASTTVVVHVLDVQDNSP 268
Cdd:smart00112   13 VTYSIL---SGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNAP 81
Cadherin pfam00028
Cadherin domain;
897-990 4.96e-13

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 66.94  E-value: 4.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   897 YDLYIAENSPVGSTVGTIVARDADEGDNADISFRIFGGADAKLFDIEEDaeqNGVVRilTRAEFDYEAKaNKFFFELQAS 976
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPD---TGDIS--TTKPLDRESI-GEYELTVEAT 74
                           90
                   ....*....|....*..
gi 193207741   977 SGQ---LSSTVPVRIHV 990
Cdd:pfam00028   75 DSGgppLSSTATVTITV 91
HormR smart00008
Domain present in hormone receptors;
1917-1974 1.00e-12

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 65.23  E-value: 1.00e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193207741   1917 CPSEIEYSIQWPASQKGSIVRQSCPVGESGL-----ATRKCLETGRWS--DVNAWNCTRPEYSIM 1974
Cdd:smart00008    5 CPATWDGIICWPQTPAGQLVEVPCPKYFSGFsyktgASRNCTENGGWSppFPNYSNCTSNDYEEL 69
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
2170-2218 2.07e-11

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 60.86  E-value: 2.07e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 193207741   2170 KYPECVRFDEKSGTWTARGAALIGLNLTHAACEYNRIGVFTMFVNDQSS 2218
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
Cadherin pfam00028
Cadherin domain;
170-261 8.95e-11

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 60.39  E-value: 8.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   170 YVKELPEDTPIETIIASVKASHASSQP---LYYSMVapQDSRSQNlFTLDTMSGEIRLAKSMDREVLDKHILKVTAYERV 246
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPngrIFYSIL--GGGPGGN-FRIDPDTGDISTTKPLDRESIGEYELTVEATDSG 77
                           90
                   ....*....|....*
gi 193207741   247 DPTISASTTVVVHVL 261
Cdd:pfam00028   78 GPPLSSTATVTITVL 92
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1252-1287 3.89e-09

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 54.18  E-value: 3.89e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 193207741 1252 IDECYRGR-CSNNSTCVAFENTYQCECKPGWIGRHCE 1287
Cdd:cd00054     2 IDECASGNpCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1582-1716 1.08e-08

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 56.27  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 1582 FEEESFV-LYQPSQVSVPFEVSFEFRTSRADMQVFALEFTQRSVHYNLEVDDGTLK--YNIGDSEVELPAPE-VTSKHWM 1657
Cdd:cd00110     4 FSGSSYVrLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVlrYDLGSGSLVLSSKTpLNDGQWH 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193207741 1658 NVVIKFEADSVATSINGIYSAEAKASISDMNL---ESLYFGIAPGTGHPSR------FEGCIRNVLVD 1716
Cdd:cd00110    84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLnldGPLYLGGLPEDLKSPGlpvspgFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1600-1718 1.81e-08

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 55.04  E-value: 1.81e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   1600 EVSFEFRTSRADMQVFALEFTQRSVHYNLEVDDGTLK--YNIGDSEVELPAPEVTSK--HWMNVVIKFEADSVATSINGI 1675
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVlrYDLGSGPARLTSDPTPLNdgQWHRVAVERNGRSVTLSVDGG 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 193207741   1676 YSAEAKASIS--DMNLES-LYFGIAPGTGHPSR------FEGCIRNVLVDGR 1718
Cdd:smart00282   81 NRVSGESPGGltILNLDGpLYLGGLPEDLKLPPlpvtpgFRGCIRNLKVNGK 132
EGF_CA smart00179
Calcium-binding EGF-like domain;
1252-1287 9.05e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 50.32  E-value: 9.05e-08
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 193207741   1252 IDECY-RGRCSNNSTCVAFENTYQCECKPGWI-GRHCE 1287
Cdd:smart00179    2 IDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
7tmB2_Adhesion cd15040
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ...
2237-2455 1.29e-07

adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G protein-coupled receptors; The B2 subfamily of class B GPCRs consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320168 [Multi-domain]  Cd Length: 253  Bit Score: 55.27  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2237 VALFLCFLSILLTLSRRSLKTHSVRIgfILFFAINILNLFFVhkTAINQAY----CPVRNAMLSFTSSAPFAWLFLYGLY 2312
Cdd:cd15040    17 LGLLLTIITYILFRKLRKRKPTKILL--NLCLALLLANLLFL--FGINSTDnpvlCTAVAALLHYFLLASFMWMLVEALL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2313 IYRML---ADGSSSPSLTTSLLVGIVFPCLISFTTFFV--------TDQCSLSPHLWLFWCIILPIGLFLL--LSFYAAA 2379
Cdd:cd15040    93 LYLRLvkvFGTYPRHFILKYALIGWGLPLIIVIITLAVdpdsygnsSGYCWLSNGNGLYYAFLGPVLLIILvnLVIFVLV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2380 TSVLVSLHKKydVFVAKYNVKRAVFQHFILTIFTLGMT-LTGLFAnqlplpmeimEISQSII--YLIAA------LVIFL 2450
Cdd:cd15040   173 LRKLLRLSAK--RNKKKRKKTKAQLRAAVSLFFLLGLTwIFGILA----------IFGARVVfqYLFAIfnslqgFFIFI 240

                  ....*.
gi 193207741 2451 W-CVCD 2455
Cdd:cd15040   241 FhCLRN 246
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
1917-1969 1.99e-06

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 47.36  E-value: 1.99e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193207741  1917 CPSEIEYSIQWPASQKGSIVRQSCP-----VGESGLATRKCLETGRWSDV---NAWNCTRP 1969
Cdd:pfam02793    4 CPRTWDGILCWPRTPAGETVEVPCPdyfsgFDPRGNASRNCTEDGTWSEHppsNYSNCTSN 64
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1255-1285 6.13e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 44.68  E-value: 6.13e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 193207741  1255 CYRGRCSNNSTCVAFENTYQCECKPGWIGRH 1285
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1865-1911 9.46e-06

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 44.65  E-value: 9.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 193207741 1865 CEC-GFGADSTEC-SADGHCKCNGDAVGRRCDRCSRFDHQLDSKTLKCR 1911
Cdd:cd00055     2 CDCnGHGSLSGQCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1774-1808 2.06e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 2.06e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 193207741 1774 CSVANVCS-SGTCVssNTTAGYECICPAGKTGKNCQ 1808
Cdd:cd00054     5 CASGNPCQnGGTCV--NTVGSYRCSCPPGYTGRNCE 38
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
2237-2423 3.89e-05

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 47.66  E-value: 3.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  2237 VALFLCFLsILLTLsrRSLktHSVRIG-----FILFFAINILnlFFVHKTAI---------NQAYCPVRNAMLSFTSSAP 2302
Cdd:pfam00002   17 VALLLAIA-IFLLF--RKL--HCTRNYihlnlFASFILRALL--FLVGDAVLfnkqdldhcSWVGCKVVAVFLHYFFLAN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  2303 FAWLFLYGLYIYRMLADGSSSPSLTTSLLVGI------VFPCLISFTT---FFVTDQCSLSPHLWLFWCIILPIGLFLLL 2373
Cdd:pfam00002   90 FFWMLVEGLYLYTLLVEVFFSERKYFWWYLLIgwgvpaLVVGIWAGVDpkgYGEDDGCWLSNENGLWWIIRGPILLIILV 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 193207741  2374 SFYAAATSVLVSLHKK---YDVFVAKYNVKRAVFQHFILtIFTLGMT-LTGLFA 2423
Cdd:pfam00002  170 NFIIFINIVRILVQKLretNMGKSDLKQYRRLAKSTLLL-LPLLGITwVFGLFA 222
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1605-1718 1.70e-04

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 43.56  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  1605 FRTSRADMQVFALEfTQRSVHYNLEVDDGTLK--YNIGDSEVELPAPE--VTSKHWMNVVIKFEADSVATSINGIYSAEA 1680
Cdd:pfam02210    1 FRTRQPNGLLLYAG-GGGSDFLALELVNGRLVlrYDLGSGPESLLSSGknLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 193207741  1681 KAS--ISDMNLES-LYFGiapGTGHPSR---------FEGCIRNVLVDGR 1718
Cdd:pfam02210   80 LPPgeSLLLNLNGpLYLG---GLPPLLLlpalpvragFVGCIRDVRVNGE 126
EGF smart00181
Epidermal growth factor-like domain;
1774-1808 6.08e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 39.42  E-value: 6.08e-04
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 193207741   1774 CSVANVCSSGTCVssNTTAGYECICPAGKTG-KNCQ 1808
Cdd:smart00181    2 CASGGPCSNGTCI--NTPGSYTCSCPPGYTGdKRCE 35
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1865-1896 5.22e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 36.91  E-value: 5.22e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 193207741   1865 CEC-GFGADSTECSAD-GHCKCNGDAVGRRCDRC 1896
Cdd:smart00180    1 CDCdPGGSASGTCDPDtGQCECKPNVTGRRCDRC 34
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1865-1896 9.12e-03

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 36.56  E-value: 9.12e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 193207741  1865 CEC-GFGADSTEC-SADGHCKCNGDAVGRRCDRC 1896
Cdd:pfam00053    1 CDCnPHGSLSDTCdPETGQCLCKPGVTGRHCDRC 34
 
Name Accession Description Interval E-value
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
274-371 1.26e-37

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: 137.06  E-value: 1.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  274 SYFGEIREDAPIGTTVLSVFARDLDSGENGEIEYSLGEGNGKNLLAINAKSGVIQTAAPLDRETLSLIRLDVIASDKGTP 353
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                          90
                  ....*....|....*...
gi 193207741  354 KRESTAMVEITVVDVNDN 371
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
686-780 2.86e-32

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: 122.04  E-value: 2.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  686 PFSVKIPEHSPIGYPVITLKAEDHDRGDNARIVYSI---DSSQFFRIDPSSGDISVSSDLDREDRATFSVIVTASDHASP 762
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIvsgNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                          90
                  ....*....|....*...
gi 193207741  763 PLNTSTQIEVILDDINDN 780
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
486-577 4.69e-32

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: 121.27  E-value: 4.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  486 ITLEENVAIGEEVGRVYAIDEDSGPNGIIKYSMEGSED---FIIDEDSGLIKTTKLLDRETTARYSLKVTARDMGTPSLN 562
Cdd:cd11304     4 VSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEdglFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPPLS 83
                          90
                  ....*....|....*
gi 193207741  563 TSTTIAVVLKDINDN 577
Cdd:cd11304    84 STATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
788-888 3.72e-31

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: 118.57  E-value: 3.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  788 SYAATISEDIPVGTSFLQVSAIDADIGPNGIVDYFLnesSSSPSIQLFRLDRTSGTLRVSSKLDREQFAVIVLPIFARDR 867
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSI---VSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77
                          90       100
                  ....*....|....*....|.
gi 193207741  868 GTPSLSAASEITLTLSDVNDN 888
Cdd:cd11304    78 GGPPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
379-475 3.33e-28

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: 110.48  E-value: 3.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  379 SYNVTILENITIPAVIATVKATDEDFGTNGKVHYSMASSSGIGGLTIDYSTGEVTLRERIDA-KNSPITAVIRAKDGAQP 457
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDReEQSSYTLTVTATDGGGP 80
                          90
                  ....*....|....*...
gi 193207741  458 ALSSTVPLTINVIDINDH 475
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
294-373 1.70e-27

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: 107.82  E-value: 1.70e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    294 ARDLDSGENGEIEYSLGEGNGKNLLAINAKSGVIQTAAPLDRETLSLIRLDVIASDKGTPKRESTAMVEITVVDVNDNAP 373
Cdd:smart00112    2 ATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNAP 81
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
896-996 2.75e-26

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: 104.70  E-value: 2.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  896 SYDLYIAENSPVGSTVGTIVARDADEGDNADISFRIFGGADAKLFDIEEDaeqNGVVRilTRAEFDYEAKAnKFFFELQA 975
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPS---TGEIT--TAKPLDREEQS-SYTLTVTA 74
                          90       100
                  ....*....|....*....|....
gi 193207741  976 SSG---QLSSTVPVRIHVSDVNDN 996
Cdd:cd11304    75 TDGggpPLSSTATVTITVLDVNDN 98
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
503-579 2.90e-26

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: 104.35  E-value: 2.90e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    503 AIDEDSGPNGIIKYSMEGSED---FIIDEDSGLIKTTKLLDRETTARYSLKVTARDMGTPSLNTSTTIAVVLKDINDNAP 579
Cdd:smart00112    2 ATDADSGENGKVTYSILSGNDdglFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNAP 81
Cadherin pfam00028
Cadherin domain;
275-365 1.41e-24

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 99.68  E-value: 1.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   275 YFGEIREDAPIGTTVLSVFARDLDSGENGEIEYSLGEGNGKNLLAINAKSGVIQTAAPLDRETLSLIRLDVIASDKGTPK 354
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80
                           90
                   ....*....|.
gi 193207741   355 RESTAMVEITV 365
Cdd:pfam00028   81 LSSTATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
705-782 6.05e-24

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: 97.42  E-value: 6.05e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    705 KAEDHDRGDNARIVYSIDSS---QFFRIDPSSGDISVSSDLDREDRATFSVIVTASDHASPPLNTSTQIEVILDDINDNS 781
Cdd:smart00112    1 SATDADSGENGKVTYSILSGnddGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80

                    .
gi 193207741    782 P 782
Cdd:smart00112   81 P 81
Cadherin pfam00028
Cadherin domain;
687-774 2.17e-23

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 96.22  E-value: 2.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   687 FSVKIPEHSPIGYPVITLKAEDHDRGDNARIVYSI---DSSQFFRIDPSSGDISVSSDLDREDRATFSVIVTASDHASPP 763
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSIlggGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80
                           90
                   ....*....|.
gi 193207741   764 LNTSTQIEVIL 774
Cdd:pfam00028   81 LSSTATVTITV 91
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1333-1504 3.41e-23

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 97.87  E-value: 3.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 1333 SVSFDGEGLLNV-NLDLPRTQWTMKFRVSTIAHNGVLVFTGDK-RSDFVEVSVVDRVLKVQFSLGGEKIDAkmenDVENR 1410
Cdd:cd00110     1 GVSFSGSSYVRLpTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVL----SSKTP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 1411 INDGEWHTVALEYSNKQITMSLDDCetnpslLLNTSPNCAIRAKLNLEKKcedptvpcyryldisngLFLGGRPGTSKQ- 1489
Cdd:cd00110    77 LNDGQWHSVSVERNGRSVTLSVDGE------RVVESGSPGGSALLNLDGP-----------------LYLGGLPEDLKSp 133
                         170
                  ....*....|....*...
gi 193207741 1490 ---IEKAFSGCISDLSVD 1504
Cdd:cd00110   134 glpVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1354-1506 6.20e-23

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 96.64  E-value: 6.20e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   1354 TMKFRVSTIAHNGVLVFTGDK-RSDFVEVSVVDRVLKVQFSLGGEKIDAKMENdveNRINDGEWHTVALEYSNKQITMSL 1432
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDP---TPLNDGQWHRVAVERNGRSVTLSV 77
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193207741   1433 DDCEtnpsLLLNTSPncairaklnlekkcedptvPCYRYLDISNGLFLGGRPGTSKQ----IEKAFSGCISDLSVDKE 1506
Cdd:smart00282   78 DGGN----RVSGESP-------------------GGLTILNLDGPLYLGGLPEDLKLpplpVTPGFRGCIRNLKVNGK 132
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
170-266 1.68e-22

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: 93.92  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  170 YVKELPEDTPIETIIASVKASHA---SSQPLYYSMVAPQDSrsqNLFTLDTMSGEIRLAKSMDREVLDKHILKVTAYERV 246
Cdd:cd11304     2 YEVSVPENAPPGTVVLTVSATDPdsgENGEVTYSIVSGNED---GLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGG 78
                          90       100
                  ....*....|....*....|
gi 193207741  247 DPTISASTTVVVHVLDVQDN 266
Cdd:cd11304    79 GPPLSSTATVTITVLDVNDN 98
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
807-890 2.62e-21

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: 90.10  E-value: 2.62e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    807 SAIDADIGPNGIVDYFLnesSSSPSIQLFRLDRTSGTLRVSSKLDREQFAVIVLPIFARDRGTPSLSAASEITLTLSDVN 886
Cdd:smart00112    1 SATDADSGENGKVTYSI---LSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVN 77

                    ....
gi 193207741    887 DNAP 890
Cdd:smart00112   78 DNAP 81
Cadherin pfam00028
Cadherin domain;
486-571 3.24e-21

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 90.05  E-value: 3.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   486 ITLEENVAIGEEVGRVYAIDEDSGPNGIIKYSM-EGSED--FIIDEDSGLIKTTKLLDRETTARYSLKVTARDMGTPSLN 562
Cdd:pfam00028    3 ASVPENAPVGTEVLTVTATDPDLGPNGRIFYSIlGGGPGgnFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPPLS 82

                   ....*....
gi 193207741   563 TSTTIAVVL 571
Cdd:pfam00028   83 STATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
398-477 4.00e-20

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: 86.63  E-value: 4.00e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    398 KATDEDFGTNGKVHYSMASSSGIGGLTIDYSTGEVTLRERIDAKNSPI-TAVIRAKDGAQPALSSTVPLTINVIDINDHA 476
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEyTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80

                    .
gi 193207741    477 P 477
Cdd:smart00112   81 P 81
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1365-1506 1.19e-19

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 87.09  E-value: 1.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  1365 NGVLVFTGDKRSDFVEVSVVDRVLKVQFSLGGEKIDAKMENdveNRINDGEWHTVALEYSNKQITMSLDDCETNPSLLLN 1444
Cdd:pfam02210    7 NGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSG---KNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPPG 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193207741  1445 TSPNcairaklnlekkcedptvpcyryLDISNGLFLGG----RPGTSKQIEKAFSGCISDLSVDKE 1506
Cdd:pfam02210   84 ESLL-----------------------LNLNGPLYLGGlpplLLLPALPVRAGFVGCIRDVRVNGE 126
Cadherin pfam00028
Cadherin domain;
789-882 4.86e-19

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 83.89  E-value: 4.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   789 YAATISEDIPVGTSFLQVSAIDADIGPNGIVDYFLnesSSSPSIQLFRLDRTSGTLRVSSKLDREQFAVIVLPIFARDRG 868
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSI---LGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSG 77
                           90
                   ....*....|....
gi 193207741   869 TPSLSAASEITLTL 882
Cdd:pfam00028   78 GPPLSSTATVTITV 91
Cadherin pfam00028
Cadherin domain;
380-470 1.81e-18

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 82.35  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   380 YNVTILENITIPAVIATVKATDEDFGTNGKVHYSMASSSGIGGLTIDYSTGEVTLRERIDAKNSPI-TAVIRAKDGAQPA 458
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEyELTVEATDSGGPP 80
                           90
                   ....*....|..
gi 193207741   459 LSSTVPLTINVI 470
Cdd:pfam00028   81 LSSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
915-998 1.40e-16

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: 76.62  E-value: 1.40e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741    915 VARDADEGDNADISFRIFGGADAKLFDIEEDaeqNGVvrILTRAEFDYEAKANkFFFELQASSG---QLSSTVPVRIHVS 991
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPE---TGE--ITTTKPLDREEQPE-YTLTVEATDGggpPLSSTATVTITVL 74

                    ....*..
gi 193207741    992 DVNDNKP 998
Cdd:smart00112   75 DVNDNAP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
197-268 3.31e-13

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: 66.99  E-value: 3.31e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193207741    197 LYYSMVapqDSRSQNLFTLDTMSGEIRLAKSMDREVLDKHILKVTAYERVDPTISASTTVVVHVLDVQDNSP 268
Cdd:smart00112   13 VTYSIL---SGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNAP 81
Cadherin pfam00028
Cadherin domain;
897-990 4.96e-13

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 66.94  E-value: 4.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   897 YDLYIAENSPVGSTVGTIVARDADEGDNADISFRIFGGADAKLFDIEEDaeqNGVVRilTRAEFDYEAKaNKFFFELQAS 976
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPD---TGDIS--TTKPLDRESI-GEYELTVEAT 74
                           90
                   ....*....|....*..
gi 193207741   977 SGQ---LSSTVPVRIHV 990
Cdd:pfam00028   75 DSGgppLSSTATVTITV 91
HormR smart00008
Domain present in hormone receptors;
1917-1974 1.00e-12

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 65.23  E-value: 1.00e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193207741   1917 CPSEIEYSIQWPASQKGSIVRQSCPVGESGL-----ATRKCLETGRWS--DVNAWNCTRPEYSIM 1974
Cdd:smart00008    5 CPATWDGIICWPQTPAGQLVEVPCPKYFSGFsyktgASRNCTENGGWSppFPNYSNCTSNDYEEL 69
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
2170-2218 2.07e-11

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 60.86  E-value: 2.07e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 193207741   2170 KYPECVRFDEKSGTWTARGAALIGLNLTHAACEYNRIGVFTMFVNDQSS 2218
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
Cadherin pfam00028
Cadherin domain;
170-261 8.95e-11

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 60.39  E-value: 8.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   170 YVKELPEDTPIETIIASVKASHASSQP---LYYSMVapQDSRSQNlFTLDTMSGEIRLAKSMDREVLDKHILKVTAYERV 246
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPngrIFYSIL--GGGPGGN-FRIDPDTGDISTTKPLDRESIGEYELTVEATDSG 77
                           90
                   ....*....|....*
gi 193207741   247 DPTISASTTVVVHVL 261
Cdd:pfam00028   78 GPPLSSTATVTITVL 92
Laminin_G_1 pfam00054
Laminin G domain;
1359-1509 1.07e-10

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 61.56  E-value: 1.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  1359 VSTIAHNGVLVFTGDKR-SDFVEVSVVDRVLKVQFSLGGEKIdAKMENDvenRINDGEWHTVALEYSNKQITMSLDDCEt 1437
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTeRDFLALELRDGRLEVSYDLGSGAA-VVRSGD---KLNDGKWHSVELERNGRSGTLSVDGEA- 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193207741  1438 NPSLLLNTSPNcairAKLNLEKKcedptvpcyryldisngLFLGGRPGTSKQ-----IEKAFSGCISDLSVDKEDVD 1509
Cdd:pfam00054   76 RPTGESPLGAT----TDLDVDGP-----------------LYVGGLPSLGVKkrrlaISPSFDGCIRDVIVNGKPLD 131
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1252-1287 3.89e-09

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 54.18  E-value: 3.89e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 193207741 1252 IDECYRGR-CSNNSTCVAFENTYQCECKPGWIGRHCE 1287
Cdd:cd00054     2 IDECASGNpCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1582-1716 1.08e-08

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 56.27  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 1582 FEEESFV-LYQPSQVSVPFEVSFEFRTSRADMQVFALEFTQRSVHYNLEVDDGTLK--YNIGDSEVELPAPE-VTSKHWM 1657
Cdd:cd00110     4 FSGSSYVrLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVlrYDLGSGSLVLSSKTpLNDGQWH 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193207741 1658 NVVIKFEADSVATSINGIYSAEAKASISDMNL---ESLYFGIAPGTGHPSR------FEGCIRNVLVD 1716
Cdd:cd00110    84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLnldGPLYLGGLPEDLKSPGlpvspgFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1600-1718 1.81e-08

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 55.04  E-value: 1.81e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741   1600 EVSFEFRTSRADMQVFALEFTQRSVHYNLEVDDGTLK--YNIGDSEVELPAPEVTSK--HWMNVVIKFEADSVATSINGI 1675
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVlrYDLGSGPARLTSDPTPLNdgQWHRVAVERNGRSVTLSVDGG 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 193207741   1676 YSAEAKASIS--DMNLES-LYFGIAPGTGHPSR------FEGCIRNVLVDGR 1718
Cdd:smart00282   81 NRVSGESPGGltILNLDGpLYLGGLPEDLKLPPlpvtpgFRGCIRNLKVNGK 132
EGF_CA smart00179
Calcium-binding EGF-like domain;
1252-1287 9.05e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 50.32  E-value: 9.05e-08
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 193207741   1252 IDECY-RGRCSNNSTCVAFENTYQCECKPGWI-GRHCE 1287
Cdd:smart00179    2 IDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
7tmB2_Adhesion cd15040
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ...
2237-2455 1.29e-07

adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G protein-coupled receptors; The B2 subfamily of class B GPCRs consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320168 [Multi-domain]  Cd Length: 253  Bit Score: 55.27  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2237 VALFLCFLSILLTLSRRSLKTHSVRIgfILFFAINILNLFFVhkTAINQAY----CPVRNAMLSFTSSAPFAWLFLYGLY 2312
Cdd:cd15040    17 LGLLLTIITYILFRKLRKRKPTKILL--NLCLALLLANLLFL--FGINSTDnpvlCTAVAALLHYFLLASFMWMLVEALL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2313 IYRML---ADGSSSPSLTTSLLVGIVFPCLISFTTFFV--------TDQCSLSPHLWLFWCIILPIGLFLL--LSFYAAA 2379
Cdd:cd15040    93 LYLRLvkvFGTYPRHFILKYALIGWGLPLIIVIITLAVdpdsygnsSGYCWLSNGNGLYYAFLGPVLLIILvnLVIFVLV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2380 TSVLVSLHKKydVFVAKYNVKRAVFQHFILTIFTLGMT-LTGLFAnqlplpmeimEISQSII--YLIAA------LVIFL 2450
Cdd:cd15040   173 LRKLLRLSAK--RNKKKRKKTKAQLRAAVSLFFLLGLTwIFGILA----------IFGARVVfqYLFAIfnslqgFFIFI 240

                  ....*.
gi 193207741 2451 W-CVCD 2455
Cdd:cd15040   241 FhCLRN 246
7tm_classB cd13952
class B family of seven-transmembrane G protein-coupled receptors; The class B of ...
2236-2454 1.93e-07

class B family of seven-transmembrane G protein-coupled receptors; The class B of seven-transmembrane GPCRs is classified into three major subfamilies: subfamily B1 (secretin-like receptor family), B2 (adhesion family), and B3 (Methuselah-like family). The class B receptors have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi or prokaryotes. The B1 subfamily comprises receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the subfamily B1 receptors preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The subfamily B2 consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Furthermore, the subfamily B3 includes Methuselah (Mth) protein, which was originally identified in Drosophila as a GPCR affecting stress resistance and aging, and its closely related proteins.


Pssm-ID: 410627 [Multi-domain]  Cd Length: 260  Bit Score: 54.91  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2236 GVALFLCFLSILLTLSRRSLKTHSVRIGFILFFAINILNLFFV----HKTAINQAYCPVRNAMLSFTSSAPFAWLFLYGL 2311
Cdd:cd13952    13 SLSLVGLLLTIITYLLFPKLRNLRGKILINLCLSLLLAQLLFLigqlLTSSDRPVLCKALAILLHYFLLASFFWMLVEAF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2312 YIYRMLADGSSSPSLTTSLL---VGIVFPCLISFTTFFV------------TDQCSLSPHLWLFWCIILPIGLFLL--LS 2374
Cdd:cd13952    93 DLYRTFVKVFGSSERRRFLKyslYGWGLPLLIVIITAIVdfslygpspgygGEYCWLSNGNALLWAFYGPVLLILLvnLV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2375 FYAAATSVLVSlHKKYDVFVAKYNVKRAVFQHFILTIFTLGMT-LTGLFANQLPLPMEIMEISqSIIYLIAALVIFLWCV 2453
Cdd:cd13952   173 FFILTVRILLR-KLRETPKQSERKSDRKQLRAYLKLFPLMGLTwIFGILAPFVGGSLVFWYLF-DILNSLQGFFIFLIFC 250

                  .
gi 193207741 2454 C 2454
Cdd:cd13952   251 L 251
7tmB2_CELSR1 cd15991
Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of ...
2230-2423 1.11e-06

Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320657 [Multi-domain]  Cd Length: 254  Bit Score: 52.54  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2230 TSPAIAGVALFLCFLSILLTLSRRSlKTHSVRIGFI--LFFAInilnlfFVHKTAINQA----YCPVRNAMLSFTSSAPF 2303
Cdd:cd15991    10 TTVSLSLVALLITFILLVLIRTLRS-NLHSIHKNLVaaLFFSE------LIFLIGINQTenpfVCTVVAILLHYFYMSTF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2304 AWLFLYGLYIYRMLAD--GSSSPSLTTSLLVGIVFPCLISFTTFFVTDQ-------CSLSPHLWLFWCIILPIGLFLLLS 2374
Cdd:cd15991    83 AWMFVEGLHIYRMLTEvrNINTGHMRFYYVVGWGIPAIITGLAVGLDPQgygnpdfCWLSVQDTLIWSFAGPIGIVVIIN 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 193207741 2375 FYAAATSVLVSLHKKYDVFvAKYNVKRAVFQHFILTIFTLGMTLTGLFA 2423
Cdd:cd15991   163 TVIFVLAAKASCGRRQRYF-EKSGVISMLRTAFLLLLLISATWLLGLMA 210
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
1917-1969 1.99e-06

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 47.36  E-value: 1.99e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193207741  1917 CPSEIEYSIQWPASQKGSIVRQSCP-----VGESGLATRKCLETGRWSDV---NAWNCTRP 1969
Cdd:pfam02793    4 CPRTWDGILCWPRTPAGETVEVPCPdyfsgFDPRGNASRNCTEDGTWSEHppsNYSNCTSN 64
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1255-1285 6.13e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 44.68  E-value: 6.13e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 193207741  1255 CYRGRCSNNSTCVAFENTYQCECKPGWIGRH 1285
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
1254-1287 9.00e-06

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 44.39  E-value: 9.00e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 193207741 1254 EC-YRGRCSNNSTCVAFENTYQCECKPGWIG-RHCE 1287
Cdd:cd00053     1 ECaASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1865-1911 9.46e-06

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 44.65  E-value: 9.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 193207741 1865 CEC-GFGADSTEC-SADGHCKCNGDAVGRRCDRCSRFDHQLDSKTLKCR 1911
Cdd:cd00055     2 CDCnGHGSLSGQCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1774-1808 2.06e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 2.06e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 193207741 1774 CSVANVCS-SGTCVssNTTAGYECICPAGKTGKNCQ 1808
Cdd:cd00054     5 CASGNPCQnGGTCV--NTVGSYRCSCPPGYTGRNCE 38
7tmB2_CELSR_Adhesion_IV cd15441
cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 ...
2233-2450 3.48e-05

cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuron migration and axon guidance in the CNS.


Pssm-ID: 320557 [Multi-domain]  Cd Length: 254  Bit Score: 48.02  E-value: 3.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2233 AIAGVALFLCFLsILLTLSRRSLKTHSVRIGFIL-FFAINILNLFFVHKTAiNQAYCPVRNAMLSFTSSAPFAWLFLYGL 2311
Cdd:cd15441    13 GISLVLLVIAFL-VLSCLRGLQSNSNSIHKNLVAcLLLAELLFLLGINQTE-NLFPCKLIAILLHYFYLSAFSWLLVESL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2312 YIYRMLADGSSSPSLTTS--LLVGIVFPCLISFTTFFV-TDQ------CSLSPHLWLFWCIILPIGLFLLLSFYAAATSV 2382
Cdd:cd15441    91 HLYRMLTEPRDINHGHMRfyYLLGYGIPAIIVGLSVGLrPDGygnpdfCWLSVNETLIWSFAGPIAFVIVITLIIFILAL 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193207741 2383 LVSLHKKYDVFvAKYNVKRAVFQHFILTIFTLGMTLTGLFAnqLPLPMEIMEISQSIIYLIAALVIFL 2450
Cdd:cd15441   171 RASCTLKRHVL-EKASVRTDLRSSFLLLPLLGATWVFGLLA--VNEDSELLHYLFAGLNFLQGLFIFL 235
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
2237-2423 3.89e-05

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 47.66  E-value: 3.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  2237 VALFLCFLsILLTLsrRSLktHSVRIG-----FILFFAINILnlFFVHKTAI---------NQAYCPVRNAMLSFTSSAP 2302
Cdd:pfam00002   17 VALLLAIA-IFLLF--RKL--HCTRNYihlnlFASFILRALL--FLVGDAVLfnkqdldhcSWVGCKVVAVFLHYFFLAN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  2303 FAWLFLYGLYIYRMLADGSSSPSLTTSLLVGI------VFPCLISFTT---FFVTDQCSLSPHLWLFWCIILPIGLFLLL 2373
Cdd:pfam00002   90 FFWMLVEGLYLYTLLVEVFFSERKYFWWYLLIgwgvpaLVVGIWAGVDpkgYGEDDGCWLSNENGLWWIIRGPILLIILV 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 193207741  2374 SFYAAATSVLVSLHKK---YDVFVAKYNVKRAVFQHFILtIFTLGMT-LTGLFA 2423
Cdd:pfam00002  170 NFIIFINIVRILVQKLretNMGKSDLKQYRRLAKSTLLL-LPLLGITwVFGLFA 222
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
792-888 5.70e-05

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


Pssm-ID: 206635  Cd Length: 98  Bit Score: 44.26  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  792 TISEDIPVGTSFLQ-VSAIDADIGPNGIVDYFLNESSSSPSIQLFRLDRTSGTLRVSSKLDREQFAVIVLPIFARDRGTP 870
Cdd:cd00031     1 IPDGSAVEGRSRGSfRVSIPTDLIASSGEIIKISAAGKEALPSWLHWEPHSGILEGLEKLDREDKGVHYISVSAASLGAN 80
                          90
                  ....*....|....*...
gi 193207741  871 SLSAASEITLTLSDVNDN 888
Cdd:cd00031    81 VPQTSSVFSIEVYDENDN 98
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
1260-1281 9.40e-05

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 41.17  E-value: 9.40e-05
                           10        20
                   ....*....|....*....|..
gi 193207741  1260 CSNNSTCVAFENTYQCECKPGW 1281
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPPGY 22
7tmB2_CELSR2 cd15992
Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of ...
2236-2319 1.25e-04

Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320658  Cd Length: 255  Bit Score: 46.35  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2236 GVALFLCFLSILLTLSRRSLKTHSVRIGFILFFAINILNLFFVhkTAINQA----YCPVRNAMLSFTSSAPFAWLFLYGL 2311
Cdd:cd15992    13 GVTLGFLLLTFLFLLCLRALRSNKTSIRKNGATALFLSELVFI--LGINQAdnpfACTVIAILLHFFYLCTFSWLFLEGL 90

                  ....*...
gi 193207741 2312 YIYRMLAD 2319
Cdd:cd15992    91 HIYRMLSE 98
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
294-371 1.58e-04

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


Pssm-ID: 206635  Cd Length: 98  Bit Score: 43.10  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  294 ARDLDSgENGEIEYSLGEGNGK--NLLAINAKSGVIQTAAPLDRETLSLIRLDVIASDKGTPKRESTAMVEITVVDVNDN 371
Cdd:cd00031    20 PTDLIA-SSGEIIKISAAGKEAlpSWLHWEPHSGILEGLEKLDREDKGVHYISVSAASLGANVPQTSSVFSIEVYDENDN 98
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1605-1718 1.70e-04

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 43.56  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  1605 FRTSRADMQVFALEfTQRSVHYNLEVDDGTLK--YNIGDSEVELPAPE--VTSKHWMNVVIKFEADSVATSINGIYSAEA 1680
Cdd:pfam02210    1 FRTRQPNGLLLYAG-GGGSDFLALELVNGRLVlrYDLGSGPESLLSSGknLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 193207741  1681 KAS--ISDMNLES-LYFGiapGTGHPSR---------FEGCIRNVLVDGR 1718
Cdd:pfam02210   80 LPPgeSLLLNLNGpLYLG---GLPPLLLlpalpvragFVGCIRDVRVNGE 126
7tmB2_CELSR3 cd15993
Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of ...
2230-2449 4.43e-04

Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuronal migration and axon guidance in the CNS. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320659 [Multi-domain]  Cd Length: 254  Bit Score: 44.45  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2230 TSPAIAGVALFLCFlSILLTLsrRSLKT-----HSvRIGFILFFAiNILNLFFVHKTAiNQAYCPVRNAMLSFTSSAPFA 2304
Cdd:cd15993    10 SSVSASLAALVLTF-SVLTCL--RGLKSntrgiHS-NIAAALFLS-ELLFLLGINRTE-NQFLCTVVAILLHYFFLSTFA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2305 WLFLYGLYIYRMLADGSSSPSLTTS--LLVGIVFPCLISFTT-------FFVTDQCSLSPHLWLFWCIILPIGLFLLLS- 2374
Cdd:cd15993    84 WLFVQGLHIYRMQTEARNVNFGAMRfyYAIGWGVPAIITGLAvgldpegYGNPDFCWISIHDKLVWSFAGPIVVVIVMNg 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193207741 2375 --FYAAATSVLVSLHKKydvfVAKYNVKRAVFQHFILTIFTLGMTLTGLFA-NQLPLPMEIMEISQSIIYLIAALVIF 2449
Cdd:cd15993   164 vmFLLVARMSCSPGQKE----TKKTSVLMTLRSSFLLLLLISATWLFGLLAvNNSVLAFHYLHAILCCLQGLAVLLLF 237
Cadherin_4 pfam17803
Bacterial cadherin-like domain; This entry contains numerous bacterial cadherin-like domains ...
359-433 4.94e-04

Bacterial cadherin-like domain; This entry contains numerous bacterial cadherin-like domains found in extracelullar proteins.


Pssm-ID: 465514 [Multi-domain]  Cd Length: 71  Bit Score: 40.63  E-value: 4.94e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193207741   359 AMVEITVVDVNDnAPVFASDSYNVTILENITIPA-VIATvkATDEDfgtNGKVHYSMASSSGIGG-LTIDySTGEVT 433
Cdd:pfam17803    1 ATVTITVTGVND-APVAVDDTATVDEDTPVTITGnVLAN--DTDVD---GDTLTVTSVTGAPAYGtLTLN-ADGSFT 70
7tmB2_Latrophilin-1 cd16007
Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled ...
2265-2388 5.34e-04

Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320673 [Multi-domain]  Cd Length: 258  Bit Score: 44.53  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2265 ILFFAINILNLFFVHKTAiNQAYCPVRNAMLSFTSSAPFAWLFLYGLYIYRMLAD--GSSSPSLTTSLLVGIVFPCL--- 2339
Cdd:cd16007    45 INLFLAELLFLIGIDKTQ-YQIACPIFAGLLHFFFLAAFSWLCLEGVQLYLMLVEvfESEYSRKKYYYLCGYCFPALvvg 123
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 193207741 2340 ----ISFTTFFVTDQCSLSPHLWLFWCIILPIGLFLLLSFyaaaTSVLVSLHK 2388
Cdd:cd16007   124 isaaIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNL----VFLMVTLHK 172
EGF smart00181
Epidermal growth factor-like domain;
1774-1808 6.08e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 39.42  E-value: 6.08e-04
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 193207741   1774 CSVANVCSSGTCVssNTTAGYECICPAGKTG-KNCQ 1808
Cdd:smart00181    2 CASGGPCSNGTCI--NTPGSYTCSCPPGYTGdKRCE 35
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1261-1299 6.86e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.60  E-value: 6.86e-04
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 193207741   1261 SNNSTCVAFenTYQCECKPGWIGRHCEisvhalTCVPGY 1299
Cdd:smart00180    8 SASGTCDPD--TGQCECKPNVTGRRCD------RCAPGY 38
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
486-577 7.11e-04

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


Pssm-ID: 206635  Cd Length: 98  Bit Score: 41.18  E-value: 7.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741  486 ITLEENVAIGEEVGRVyAIDEDSGPNGIIKYSMEGSED----FIIDEDSGLIKTTKLLDRETTARYSLKVTARDMGTPSL 561
Cdd:cd00031     4 GSAVEGRSRGSFRVSI-PTDLIASSGEIIKISAAGKEAlpswLHWEPHSGILEGLEKLDREDKGVHYISVSAASLGANVP 82
                          90
                  ....*....|....*.
gi 193207741  562 NTSTTIAVVLKDINDN 577
Cdd:cd00031    83 QTSSVFSIEVYDENDN 98
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
710-780 7.69e-04

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


Pssm-ID: 206635  Cd Length: 98  Bit Score: 41.18  E-value: 7.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193207741  710 DRGDNARIVYSIDSS------QFFRIDPSSGDISVSSDLDREDRATFSVIVTASDHASPPLNTSTQIEVILDDINDN 780
Cdd:cd00031    22 DLIASSGEIIKISAAgkealpSWLHWEPHSGILEGLEKLDREDKGVHYISVSAASLGANVPQTSSVFSIEVYDENDN 98
EGF_CA smart00179
Calcium-binding EGF-like domain;
1774-1808 8.57e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 8.57e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 193207741   1774 CSVANVCSSG-TCVssNTTAGYECICPAG-KTGKNCQ 1808
Cdd:smart00179    5 CASGNPCQNGgTCV--NTVGSYRCECPPGyTDGRNCE 39
EGF smart00181
Epidermal growth factor-like domain;
1254-1287 1.23e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 38.65  E-value: 1.23e-03
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 193207741   1254 EC-YRGRCSNNsTCVAFENTYQCECKPGWIG-RHCE 1287
Cdd:smart00181    1 ECaSGGPCSNG-TCINTPGSYTCSCPPGYTGdKRCE 35
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
1774-1808 1.85e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 37.84  E-value: 1.85e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 193207741 1774 CSVANVCSS-GTCVssNTTAGYECICPAGKTG-KNCQ 1808
Cdd:cd00053     2 CAASNPCSNgGTCV--NTPGSYRCVCPPGYTGdRSCE 36
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1261-1299 2.13e-03

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 38.10  E-value: 2.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 193207741 1261 SNNSTCvaFENTYQCECKPGWIGRHCEisvhalTCVPGY 1299
Cdd:cd00055     9 SLSGQC--DPGTGQCECKPNTTGRRCD------RCAPGY 39
7tmB2_GPR133-like_Adhesion_V cd15933
orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of ...
2233-2316 2.28e-03

orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group V adhesion GPCRs include orphan receptors GPR133, GPR144, and closely related proteins. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the G(s) protein, leading to activation of adenylate cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320599 [Multi-domain]  Cd Length: 252  Bit Score: 42.31  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2233 AIAGVALFLCFL--SILLTLSRRSLKTHSVRIGFILFFAINILNLFFV--HKTAINQAYCPVRNAMLSFTSSAPFAWLFL 2308
Cdd:cd15933     8 SYIGCGISIACLalTLIIFLVLRVLSSDRFQIHKNLCVALLLAQILLLagEWAEGNKVACKVVAILLHFFFMAAFSWMLV 87

                  ....*...
gi 193207741 2309 YGLYIYRM 2316
Cdd:cd15933    88 EGLHLYLM 95
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
1260-1286 2.67e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 37.33  E-value: 2.67e-03
                           10        20
                   ....*....|....*....|....*..
gi 193207741  1260 CSNNSTCVAFenTYQCECKPGWIGRHC 1286
Cdd:pfam07974    2 CSGRGTCVNQ--CGKCVCDSGYQGATC 26
7tmB1_hormone_R cd15041
The subfamily B1 of hormone receptors (secretin-like), member of the class B family ...
2236-2376 3.63e-03

The subfamily B1 of hormone receptors (secretin-like), member of the class B family seven-transmembrane G protein-coupled receptors; The B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of this subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. Moreover, the B1 subfamily receptors play key roles in hormone homeostasis and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression). Furthermore, the subfamilies B2 and B3 consist of receptors that are capable of interacting with epidermal growth factors (EGF) and the Drosophila melanogaster Methuselah gene product (Mth), respectively. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 341321 [Multi-domain]  Cd Length: 273  Bit Score: 41.83  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2236 GVALFLCFLSILLTLSRRSLKTHSVRI------GFILFFAINIL--NLFFVHK-------TAINQ--AYCPVRNAMLSFT 2298
Cdd:cd15041    13 SLSLVALLPAIVIFLYFRSLRCTRIRLhinlflSFILRAVFWIIwdLLVVYDRltssgveTVLMQnpVGCKLLSVLKRYF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207741 2299 SSAPFAWLFLYGLYIYRMLADGSSSPSLTTSL--LVGIVFPCLISFTTFFV-----TDQCSLS-PHLWLFWCIILPIGLF 2370
Cdd:cd15041    93 KSANYFWMLCEGLYLHRLIVVAFFSEPSSLKLyyAIGWGLPLVIVVIWAIVrallsNESCWISyNNGHYEWILYGPNLLA 172

                  ....*.
gi 193207741 2371 LLLSFY 2376
Cdd:cd15041   173 LLVNLF 178
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1865-1896 5.22e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 36.91  E-value: 5.22e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 193207741   1865 CEC-GFGADSTECSAD-GHCKCNGDAVGRRCDRC 1896
Cdd:smart00180    1 CDCdPGGSASGTCDPDtGQCECKPNVTGRRCDRC 34
Big_9 pfam17963
Bacterial Ig domain; This entry represents a wide variety of bacterial Ig domains.
358-433 6.60e-03

Bacterial Ig domain; This entry represents a wide variety of bacterial Ig domains.


Pssm-ID: 465590 [Multi-domain]  Cd Length: 90  Bit Score: 38.09  E-value: 6.60e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193207741   358 TAMVEITVVDVNDnAPVFASDSYNVTilENitipAVIATVKATDEDFGTNGKVHYSMASSSGIGGLTIDySTGEVT 433
Cdd:pfam17963    1 TATVTVTVTPVND-APVAVDDSVTVT--ED----TVLANDSDPDGDPLTITSLTVTIVTAPANGTVTVN-ADGTLT 68
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1865-1896 9.12e-03

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 36.56  E-value: 9.12e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 193207741  1865 CEC-GFGADSTEC-SADGHCKCNGDAVGRRCDRC 1896
Cdd:pfam00053    1 CDCnPHGSLSDTCdPETGQCLCKPGVTGRHCDRC 34
 
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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