juxtamembrane and transmembrane (JMTM) domain found in Drosophila melanogaster neurogenic locus Notch protein (dNotch) and similar proteins; Drosophila melanogaster neurogenic locus Notch protein (dNotch) is an essential signaling protein which has a major role in many developmental processes. It functions as a receptor for membrane-bound ligands Delta and Serrate to regulate cell-fate determination. It regulates oogenesis, the differentiation of the ectoderm and the development of the central and peripheral nervous system, eye, wing disk, muscles and segmental appendages such as antennae and legs, through lateral inhibition or induction. It also regulates neuroblast self-renewal, identity and proliferation through the regulation of bHLH-O proteins; in larval brains, it is involved in the maintenance of type II neuroblast self-renewal and identity by suppressing erm expression together with pnt. It might also regulate dpn expression through the activation of the transcriptional regulator Su(H). This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of dNotch, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036756858 1717 DFPIYSVRGIKNPGDEDNgEPPANVKYVITGIILVILVLAFFGMVLSTQRKRAHGVTWFPEGF---RAPAAVMSRRRRDP 1793
Cdd:cd21706      1 DFPIYQVRGEDPPDPPPE-PPPSNLTYVVIGVVVVLLIGLLLGVLVTTQRKRARGITWFPEGFfttSSSQRRRRSRRRGP 79

                           90
                   ....*....|.
gi 1036756858 1794 HGQEMRNLNKQ 1804
Cdd:cd21706     80 DGQEMRNLKKQ 90

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 1036756858  450 DIDECGQGSPCEHNGICVNTPGSYRCNCSQGFTGPRCE 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 1036756858  908 DIDECALSSPCRNGASCLNVPGSYRCLCTKGYEGRDC 944
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 1036756858  218 DVEECQS-NPCKYGGTCVNTHGSYQCMCPTGYTGKDC 253
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 1036756858  527 DIDECQS-NPCLNDGTCHDKINGFKCSCALGFTGARCQ 563
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 1036756858  754 DVDECAS-NPCVNGGRCEDGINEFICHCPPGYAGKRCE 790
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 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
                   ....*....|....*....|....*....
gi 1036756858 1563 AYCQKHYGDGFCDYGCNNAECSWDGLDCE 1591
Cdd:pfam00066    7 PYCWDKFGNGVCDEECNNAECLWDGGDCS 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 1036756858  565 NIDDCQSQ-PCRNRGICHDSIAGYSCECPPGYTGTSCE 601
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 1036756858  332 DVDECAqrEHPVCQNGATCTNTHGSYSCICVNGWEGPDC 370
Cdd:cd00054      1 DIDECA--SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 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 1036756858  985 DINEC-ISQPCQNGATCSQYVNSYTCTCPLGFSGINCQ 1021
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 1036756858 1298 DINECLS-NPCSNAGTldCVQLVNNYHCNCRPGHMGRHCE 1336
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 1036756858  716 NVDEC-ISSPCANNGVCIDQVNGYKCECPRGFYDAHC 751
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 1036756858  294 NFDDCV-GHLCQNGATCIDGISDYSCSCPPNFTGRYCQ 330
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 1036756858  603 NINDCDS-NPCHR-GKCIDDVNSFKCLCDPGYTGYICQ 638
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 1036756858 1028 TESSCLNGGSCIDGINAYNCSCLAGFSGANCQ 1059
Cdd:cd00054      7 SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 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 1036756858  260 CSPSPCQNGGICRSNGLTYDCKCPKGFDGKN 290
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 1036756858 1339 VDFCAQ-SPCQNGGNCNIRQSGHHCICNNGFYGKNCE 1374
Cdd:cd00054      2 IDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

juxtamembrane and transmembrane (JMTM) domain found in Drosophila melanogaster neurogenic locus Notch protein (dNotch) and similar proteins; Drosophila melanogaster neurogenic locus Notch protein (dNotch) is an essential signaling protein which has a major role in many developmental processes. It functions as a receptor for membrane-bound ligands Delta and Serrate to regulate cell-fate determination. It regulates oogenesis, the differentiation of the ectoderm and the development of the central and peripheral nervous system, eye, wing disk, muscles and segmental appendages such as antennae and legs, through lateral inhibition or induction. It also regulates neuroblast self-renewal, identity and proliferation through the regulation of bHLH-O proteins; in larval brains, it is involved in the maintenance of type II neuroblast self-renewal and identity by suppressing erm expression together with pnt. It might also regulate dpn expression through the activation of the transcriptional regulator Su(H). This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of dNotch, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036756858 1717 DFPIYSVRGIKNPGDEDNgEPPANVKYVITGIILVILVLAFFGMVLSTQRKRAHGVTWFPEGF---RAPAAVMSRRRRDP 1793
Cdd:cd21706      1 DFPIYQVRGEDPPDPPPE-PPPSNLTYVVIGVVVVLLIGLLLGVLVTTQRKRARGITWFPEGFfttSSSQRRRRSRRRGP 79

                           90
                   ....*....|.
gi 1036756858 1794 HGQEMRNLNKQ 1804
Cdd:cd21706     80 DGQEMRNLKKQ 90

Ankyrin repeats (3 copies);

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036756858 2021 LILAARLAIEGMVEDLITADADINAADNSGKTALHWAAAVNNTEAVNILLMhHANRDAQDDkDETPLFLAAREGSYEACK 2100
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1036756858 2101 ALLDNFANREITD 2113
Cdd:pfam12796   79 LLLEKGADINVKD 91

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 1036756858  450 DIDECGQGSPCEHNGICVNTPGSYRCNCSQGFTGPRCE 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 1036756858  908 DIDECALSSPCRNGASCLNVPGSYRCLCTKGYEGRDC 944
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 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
                    ....*....|....*....|....*....|....*.
gi 1036756858  1515 NPWANCSAHECWNKFKNGKCNEECNNAACHYDGHDC 1550
Cdd:smart00004    3 DPWSRCEDAQCWDKFGDGVCDEECNNAECLWDGGDC 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 1036756858  218 DVEECQS-NPCKYGGTCVNTHGSYQCMCPTGYTGKDC 253
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 1036756858  792 DIDECSS-NPCQHGGTCYDKLNAFSCQCMPGYTGQKCE 828
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 1036756858 1185 IDECQSQ-PCQNGGTCRDLIGAYKCDCRQGFQGQNCE 1220
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 1036756858  489 NINECES-HPCQNEGSCLDDPGTFRCVCMPGFTGTQCE 525
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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
                    ....*....|....*....|....*....|....*..
gi 1036756858  1474 QQQRAMCDKRGCAEKQGNGFCDTECNSYACNFDGNDC 1510
Cdd:smart00004    2 QDPWSRCEDAQCWDKFGDGVCDEECNNAECLWDGGDC 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 1036756858  565 NIDDCQSQ-PCRNRGICHDSIAGYSCECPPGYTGTSCE 601
Cdd:cd00054      1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036756858 1934 DLLAQGAelnatmdkTGETSLHLAARFARADAAKRLLDAGADANCQDNT-----GRTPLHAAVAADAMGVFQILLRNRAT 2008
Cdd:cd22192     43 DLFQRGA--------LGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVNQNLNLVRELIARGAD 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036756858 2009 NLNAR-------------MHDGTTPLILAARLAIEGMVEDLITADADINAADNSGKTALHWAAAVNNT----EAVNILLm 2071
Cdd:cd22192    115 VVSPRatgtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKtfacQMYDLIL- 193

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1036756858 2072 hhaNRDAQDD----------KDETPLFLAAREGSYEA 2098
Cdd:cd22192    194 ---SYDKEDDlqpldlvpnnQGLTPFKLAAKEGNIVM 227

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1036756858   792 DIDECSS-NPCQHGGTCYDKLNAFSCQCMPGYT-GQKCE 828
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1036756858   218 DVEECQS-NPCKYGGTCVNTHGSYQCMCPTGYT-GKDCD 254
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 1036756858  332 DVDECAqrEHPVCQNGATCTNTHGSYSCICVNGWEGPDC 370
Cdd:cd00054      1 DIDECA--SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 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 1036756858  985 DINEC-ISQPCQNGATCSQYVNSYTCTCPLGFSGINCQ 1021
Cdd:cd00054      1 DIDECaSGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1036756858   527 DIDECQS-NPCLNDGTCHDKINGFKCSCALGFT-GARCQ 563
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1036756858   641 INECES-NPCQFDGHCQDRVGSYFCHCQPG-TSGKNCE 676
Cdd:smart00179    2 IDECASgNPCQNGGTCVNTVGSYRCECPPGyTDGRNCE 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 1036756858 1298 DINECLS-NPCSNAGTldCVQLVNNYHCNCRPGHMGRHCE 1336
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 1036756858  716 NVDEC-ISSPCANNGVCIDQVNGYKCECPRGFYDAHC 751
Cdd:cd00054      1 DIDECaSGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1036756858   332 DVDECAqrEHPVCQNGATCTNTHGSYSCICVNGWE-GPDC 370
Cdd:smart00179    1 DIDECA--SGNPCQNGGTCVNTVGSYRCECPPGYTdGRNC 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1036756858   985 DINECIS-QPCQNGATCSQYVNSYTCTCPLGFS-GINCQ 1021
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 1036756858  294 NFDDCV-GHLCQNGATCIDGISDYSCSCPPNFTGRYCQ 330
Cdd:cd00054      1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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 1036756858 1677 QTGIQIYLEIDNRKCT----ECFTHAVEAAEFLAATAAKHQLLDDFPIYSVRGIKNP 1729
Cdd:pfam07684    1 VIGSVVYLEIDNRKCSqssdECFSTAQSAADFLAALAAKGGLDLPYPIKEVRSEPPP 57

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 1036756858  682 CHSNPCNNGATCIDGINSYKCQCVPGFTGQH 712
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31

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 1036756858  758 CASNPCVNGGRCEDGINEFICHCPPGYAGKR 788
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 1036756858  603 NINDCDS-NPCHR-GKCIDDVNSFKCLCDPGYTGYICQ 638
Cdd:cd00054      1 DIDECASgNPCQNgGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1036756858  1260 NKDDCE-PGACHNNGSCIDRVGGFECVCQPGFV-GARCE 1296
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39