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 17380387 1719 DFQIHSVRGIKNPGDEDNgEPPANVKYVITGIILVIIALAFFGMVLSTQRKRAHGVTWFPEGF---RAPAAVMSRRRRDP 1795
Cdd:cd21706    1 DFPIYQVRGEDPPDPPPE-PPPSNLTYVVIGVVVVLLIGLLLGVLVTTQRKRARGITWFPEGFfttSSSQRRRRSRRRGP 79

                         90
                 ....*....|.
gi 17380387 1796 HGQEMRNLNKQ 1806
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 17380387  449 DIDECDQGSPCEHNGICVNTPGSYRCNCSQGFTGPRCE 486
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 17380387  907 DIDECSLSSPCRNGASCLNVPGSYRCLCTKGYEGRDC 943
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 17380387  677 NVNECHS-NPCNNGATCIDGINSYKCQCVPGFTGQHCE 713
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 17380387  526 DIDECQS-NPCLNDGTCHDKINGFKCSCALGFTGARCQ 562
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 17380387 1184 IDECQSQ-PCQNGGTCRDLIGAYECQCRQGFQGQNCE 1219
Cdd:cd00054    2 IDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 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 17380387   1565 AYCQKHYGDGFCDYGCNNAECSWDGLDCE 1593
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 17380387  984 DINECLSQ-PCQNGATCSQYVNSYTCTCPLGFSGINCQ 1020
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 17380387  640 INECES-NPCQFDGHCQDRVGSYYCQCQAGTSGKNCE 675
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 17380387  946 NTDDCASF-PCQNGGTCLDGIGDYSCLCVDGFDGKHCE 982
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 17380387 1221 NIDDCA-PNPCQNGGTCHDRVMNFSCSCPPGTMGIICE 1257
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 17380387  715 NVDEC-ISSPCANNGVCIDQVNGYKCECPRGFYDAHC 750
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 17380387  295 DDCL-GHLCQNGGTCIDGISDYTCRCPPNFTGRFCQ 329
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 17380387 1027 TESSCLNGGSCIDGINGYNCSCLAGYSGANCQ 1058
Cdd:cd00054    7 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 17380387  260 SPSPCQNGGICRSNGLSYECKCPKGFEGKNCE 291
Cdd:cd00054    7 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 17380387  179 NLCAS-SPCRNGATCTALAGSssFTCSCPPGFTGDTC 214
Cdd:cd00054    3 DECASgNPCQNGGTCVNTVGS--YRCSCPPGYTGRNC 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 17380387 1338 VDFCAQ-SPCQNGGNCNIRQSGHHCICNNGFYGKNCE 1373
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 17380387 1719 DFQIHSVRGIKNPGDEDNgEPPANVKYVITGIILVIIALAFFGMVLSTQRKRAHGVTWFPEGF---RAPAAVMSRRRRDP 1795
Cdd:cd21706    1 DFPIYQVRGEDPPDPPPE-PPPSNLTYVVIGVVVVLLIGLLLGVLVTTQRKRARGITWFPEGFfttSSSQRRRRSRRRGP 79

                         90
                 ....*....|.
gi 17380387 1796 HGQEMRNLNKQ 1806
Cdd:cd21706   80 DGQEMRNLKKQ 90

Ankyrin repeats (3 copies);

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380387   2022 LILAARLAIEGMVEDLITADADINAADNSGKTALHWAAAVNNTEAVNILLMhHANRDAQDDkDETPLFLAAREGSYEACK 2101
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 17380387   2102 ALLDNFANREITD 2114
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 17380387  449 DIDECDQGSPCEHNGICVNTPGSYRCNCSQGFTGPRCE 486
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 17380387     449 DIDECDQGSPCEHNGICVNTPGSYRCNCSQGFT-GPRCE 486
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 17380387  907 DIDECSLSSPCRNGASCLNVPGSYRCLCTKGYEGRDC 943
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 17380387  677 NVNECHS-NPCNNGATCIDGINSYKCQCVPGFTGQHCE 713
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 17380387  526 DIDECQS-NPCLNDGTCHDKINGFKCSCALGFTGARCQ 562
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 17380387  753 DVDECAS-NPCVNEGRCEDGINEFICHCPPGYTGKRCE 789
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 17380387  488 NINECES-HPCQNEGSCLDDPGTFRCVCMPGFTGTQCE 524
Cdd:cd00054    1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 17380387     677 NVNECHS-NPCNNGATCIDGINSYKCQCVPGFT-GQHCE 713
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 17380387  984 DINECLSQ-PCQNGATCSQYVNSYTCTCPLGFSGINCQ 1020
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 17380387 1935 DLLAQGAelnatmdkTGETSLHLAARFARADAAKRLLDAGADANCQDNT-----GRTPLHAAVAADAMGVFQILLRNRAT 2009
Cdd:cd22192   43 DLFQRGA--------LGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVNQNLNLVRELIARGAD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380387 2010 NLNAR-------------MHDGTTPLILAARLAIEGMVEDLITADADINAADNSGKTALHWAAAVNNT----EAVNILLm 2072
Cdd:cd22192  115 VVSPRatgtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKtfacQMYDLIL- 193

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17380387 2073 hhaNRDAQDD----------KDETPLFLAAREGSYEA 2099
Cdd:cd22192  194 ---SYDKEDDlqpldlvpnnQGLTPFKLAAKEGNIVM 227

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 17380387    1476 EQQRAMCDKRGCTEKQGNGICDSDCNTYACNFDGNDC 1512
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 17380387  640 INECES-NPCQFDGHCQDRVGSYYCQCQAGTSGKNCE 675
Cdd:cd00054    2 IDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 17380387     753 DVDECAS-NPCVNEGRCEDGINEFICHCPPGYT-GKRCE 789
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 17380387     526 DIDECQS-NPCLNDGTCHDKINGFKCSCALGFT-GARCQ 562
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 17380387  331 DVDECAQRDhpVCQNGATCTNTHGSYSCICVNGWAGLDC 369
Cdd:cd00054    1 DIDECASGN--PCQNGGTCVNTVGSYRCSCPPGYTGRNC 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 17380387 1221 NIDDCA-PNPCQNGGTCHDRVMNFSCSCPPGTMGIICE 1257
Cdd:cd00054    1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 17380387     640 INECES-NPCQFDGHCQDRVGSYYCQCQAG-TSGKNCE 675
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
                 ....*....|....*....|....*....|....*..
gi 17380387  715 NVDEC-ISSPCANNGVCIDQVNGYKCECPRGFYDAHC 750
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 17380387 1259 NKDDCKPGA-CHNNGSCIDRVGGFECVCQPGFVGARCE 1295
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 17380387  295 DDCL-GHLCQNGGTCIDGISDYTCRCPPNFTGRFCQ 329
Cdd:cd00054    3 DECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 17380387     331 DVDECAQRDhpVCQNGATCTNTHGSYSCICVNGW-AGLDC 369
Cdd:smart00179    1 DIDECASGN--PCQNGGTCVNTVGSYRCECPPGYtDGRNC 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 17380387     946 NTDDCASF-PCQNGGTCLDGIGDYSCLCVDGF-DGKHCE 982
Cdd:smart00179    1 DIDECASGnPCQNGGTCVNTVGSYRCECPPGYtDGRNCE 39

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 17380387    681 CHSNPCNNGATCIDGINSYKCQCVPGFTGQH 711
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 17380387  602 NINDCDS-NPCHR-GKCIDDVNSFKCLCDPGYTGYICQ 637
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 17380387 1027 TESSCLNGGSCIDGINGYNCSCLAGYSGANCQ 1058
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 17380387    757 CASNPCVNEGRCEDGINEFICHCPPGYTGKR 787
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31