juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 1 (Notch1) and similar proteins; Neurogenic locus notch homolog protein 1 (Notch1), also called translocation-associated notch protein TAN-1, functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. It affects the implementation of differentiation, proliferation and apoptotic programs. It is also involved in angiogenesis, and also negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch1, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859115 1712 AVTSEGGP-PKTGEMYPMFLVLLALAVLALAAVGVVVSRKRKREHGQLWFPEGFKVNEP-KKKRREPVGEDSVGLKPLKN 1789
Cdd:cd21702    1 AVKSETVEpPPPSQLYPMYVVLAALVLLAFVGVGVLVSRKRRREHGQLWFPEGFKVSEPsKKKRREPVGEDSVGLKPLKN 80

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. The role of the NOD and NODP domains remains to be elucidated.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 18859115   1663 VKGSIVYLEIDNRQCFQQSDECFQSATDVAAFLGALASSGNLNVPYIIEAVTSEGGPP 1720
Cdd:pfam07684    1 VIGSVVYLEIDNRKCSQSSDECFSTAQSAADFLAALAAKGGLDLPYPIKEVRSEPPPP 58

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.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 18859115  177 DVNECAvSPSPCRNGGTCINEVGSYLCRCPPEYTGPHCQ 215
Cdd:cd00054    1 DIDECA-SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 18859115  411 DIDECSLGaNPCEHGGRCLNTKGSFQCKCLQGYEGPRCE 449
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 18859115   1523 EGQCNPlydQYCRDHYADGHCDQGCNNAECEWDGLDC 1559
Cdd:pfam00066    1 WPNCPY---PYCWDKFGNGVCDEECNNAECLWDGGDC 34

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.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 18859115 1019 DVNECDSR-PCQNGGSCQDGYGTYKCTCPHGYTGLNCQ 1055
Cdd:cd00054    1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 18859115  943 DIDECVSA-PCRNGGNCTDCVNSYTCSCPAGFSGINCE 979
Cdd:cd00054    1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 18859115  867 DINECV-RNPCTNGGVCENLRGGFQCRCNPGFTGALCE 903
Cdd:cd00054    1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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.

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 18859115 1182 INECLSQ-PCQNGGTCIDLVNTYKCSCPRGTQGVHCE 1217
Cdd:cd00054    2 IDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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.

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 18859115  905 DIDDCE-PNPCSNGGVCQDRVNGFVCVCLAGFRGERC 940
Cdd:cd00054    1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37

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.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 18859115  751 NINECLS-NPCVNGGTCKDMTSGYLCTCRAGFSGPNCQ 787
Cdd:cd00054    1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 18859115  789 NINECAS-NPCLNQGSCIDDVAGFKCNCMLPYTGEVCE 825
Cdd:cd00054    1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 18859115 1265 DVNECLS-DPCDPSGSynCVQLINDFRCECRTGYTGKRCE 1303
Cdd:cd00054    1 DIDECASgNPCQNGGT--CVNTVGSYRCSCPPGYTGRNCE 38

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.

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 18859115  716 NECSS-NPC-IHGSCLDQINSYRCVCEAGWMGRNC 748
Cdd:cd00054    3 DECASgNPCqNGGTCVNTVGSYRCSCPPGYTGRNC 37

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.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 18859115  491 DDCASQ-PCLN-GKCIDKINSFHCECPKGFSGSLCQ 524
Cdd:cd00054    3 DECASGnPCQNgGTCVNTVGSYRCSCPPGYTGRNCE 38

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.

                         10        20        30
                 ....*....|....*....|....*....|..
gi 18859115 1313 PCKNGGTCavaSNTKHGYICKCQPGYSGSSCE 1344
Cdd:cd00054   10 PCQNGGTC---VNTVGSYRCSCPPGYTGRNCE 38

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 1 (Notch1) and similar proteins; Neurogenic locus notch homolog protein 1 (Notch1), also called translocation-associated notch protein TAN-1, functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. It affects the implementation of differentiation, proliferation and apoptotic programs. It is also involved in angiogenesis, and also negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch1, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859115 1712 AVTSEGGP-PKTGEMYPMFLVLLALAVLALAAVGVVVSRKRKREHGQLWFPEGFKVNEP-KKKRREPVGEDSVGLKPLKN 1789
Cdd:cd21702    1 AVKSETVEpPPPSQLYPMYVVLAALVLLAFVGVGVLVSRKRRREHGQLWFPEGFKVSEPsKKKRREPVGEDSVGLKPLKN 80

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. The role of the NOD and NODP domains remains to be elucidated.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 18859115   1663 VKGSIVYLEIDNRQCFQQSDECFQSATDVAAFLGALASSGNLNVPYIIEAVTSEGGPP 1720
Cdd:pfam07684    1 VIGSVVYLEIDNRKCSQSSDECFSTAQSAADFLAALAAKGGLDLPYPIKEVRSEPPPP 58

ankyrin repeat protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859115  1910 NQTDRTGETALHLAARYARSDAAKRLLESCADANVQDNMGRTPLHAAVA-ADAQGVFQILIRNRATDlDARMHDGTTPLI 1988
Cdd:PHA02875   29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEeGDVKAVEELLDLGKFAD-DVFYKDGMTPLH 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859115  1989 LATRLAVEGMVEELINCHADPNAVDDSGKSALHWAAAVNNVDAAVVLLKNGANKDLQNNKEETPLFLAAREGSYETAKVL 2068
Cdd:PHA02875  108 LATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187

                         170       180       190
                  ....*....|....*....|....*....|....
gi 18859115  2069 LDHLANRD-IADHLDQLPRDIAHERMHHDIVRLL 2101
Cdd:PHA02875  188 LDSGANIDyFGKNGCVAALCYAIENNKIDIVRLF 221

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.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 18859115  177 DVNECAvSPSPCRNGGTCINEVGSYLCRCPPEYTGPHCQ 215
Cdd:cd00054    1 DIDECA-SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 18859115   1485 WQNCSAAlQCWRYFNDGKCDEQCATAGCLYDGFDCQ 1520
Cdd:pfam00066    1 WPNCPYP-YCWDKFGNGVCDEECNNAECLWDGGDCS 35

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.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 18859115  294 DVDECElSPNACQNGGTCHNTIGGFHCVCVNGWTGDDC 331
Cdd:cd00054    1 DIDECA-SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859115   2185 LESPHgylsdvssPPMmtSPFQQSPPISLNQLQGLADSHMGGALQGLGKPFDSAPRLSHLPVANNVGG--AQAGACD--- 2259
Cdd:pfam03154  242 LPSPH--------PPL--QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPltPQSSQSQvpp 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859115   2260 ---------WLQRVQQQQQQQQQQQQ----------AGMLMPTML--SATNMPQVmgyPTMQS----SHLGAPSHMIAHQ 2314
Cdd:pfam03154  312 gpspaapgqSQQRIHTPPSQSQLQSQqppreqplppAPLSMPHIKppPTTPIPQL---PNPQShkhpPHLSGPSPFQMNS 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859115   2315 NMAPMQHqnishhfLGDLSGLDL-QSSSGHAPIQTILPQDSQRMAPP-----ISSTQFLTPP-SQHSYSNPMDNTPNHQQ 2387
Cdd:pfam03154  389 NLPPPPA-------LKPLSSLSThHPPSAHPPPLQLMPQSQQLPPPPaqppvLTQSQSLPPPaASHPPTSGLHQVPSQSP 461

                          250       260
                   ....*....|....*....|.
gi 18859115   2388 VPDHPF-------LTPSAGSP 2401
Cdd:pfam03154  462 FPQHPFvpggpppITPPSGPP 482

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.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 18859115 1019 DVNECDSR-PCQNGGSCQDGYGTYKCTCPHGYTGLNCQ 1055
Cdd:cd00054    1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 18859115  451 DVNECKS-NPCQNDATCLDQIGGFHCICMPGYEGVFCQ 487
Cdd:cd00054    1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 18859115 1144 VDECQ-PNPCQNGATCTDYLGGYSCECVPGYHGMNC 1178
Cdd:cd00054    2 IDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 18859115    1519 CQRLEGQCNplyDQYCRDHYADGHCDQGCNNAECEWDGLDC 1559
Cdd:smart00004    1 PQDPWSRCE---DAQCWDKFGDGVCDEECNNAECLWDGGDC 38

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 18859115     411 DIDECSLGaNPCEHGGRCLNTKGSFQCKCLQGYE-GPRCE 449
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 18859115   1446 RCEIAQCEGRGGNAICDTQCNNHACGWDGGDCS 1478
Cdd:pfam00066    3 NCPYPYCWDKFGNGVCDEECNNAECLWDGGDCS 35

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 18859115     294 DVDECElSPNACQNGGTCHNTIGGFHCVCVNGWT-GDDC 331
Cdd:smart00179    1 DIDECA-SGNPCQNGGTCVNTVGSYRCECPPGYTdGRNC 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 18859115     943 DIDECVSA-PCRNGGNCTDCVNSYTCSCPAGFS-GINCE 979
Cdd:smart00179    1 DIDECASGnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....
gi 18859115     676 NIDDCAL-NPCHNGGTCIDGVNSFTCLCPDGFRD 708
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTD 34

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 18859115     867 DINECV-RNPCTNGGVCENLRGGFQCRCNPGFT-GALCE 903
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 18859115    1019 DVNECDSR-PCQNGGSCQDGYGTYKCTCPHGYT-GLNCQ 1055
Cdd:smart00179    1 DIDECASGnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

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.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 18859115  751 NINECLS-NPCVNGGTCKDMTSGYLCTCRAGFSGPNCQ 787
Cdd:cd00054    1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 18859115     905 DIDDCE-PNPCSNGGVCQDRVNGFVCVCLAGFR-GERC 940
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNC 38

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 18859115    294 DVDECELSPNACQNGGTCHNTIGGFHCVCVNG 325
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 18859115 1219 DIDDCSPsvdpltgEPRCFNGGRCVDRVGGYGCVCPAGFVGERCE 1263
Cdd:cd00054    1 DIDECAS-------GNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 18859115     601 NINECLS-QPCRNGGTCQDRENAYICTCPKG-TTGVNCE 637
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGyTDGRNCE 39

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 18859115 1265 DVNECLS-DPCDPSGSynCVQLINDFRCECRTGYTGKRCE 1303
Cdd:cd00054    1 DIDECASgNPCQNGGT--CVNTVGSYRCSCPPGYTGRNCE 38

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.

                           10        20        30
                   ....*....|....*....|....*....|.
gi 18859115   1023 CDSRPCQNGGSCQDGYGTYKCTCPHGYTGLN 1053
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31

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.

                         10        20        30
                 ....*....|....*....|....*....|..
gi 18859115  986 TESSCFNGGTCVDGISSFSCVCLPGFTGNYCQ 1017
Cdd:cd00054    7 SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38