juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 4 (Notch4) and similar proteins; Neurogenic locus notch homolog protein 4 (Notch4) functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. It affects the implementation of differentiation, proliferation and apoptotic programs. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch4, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958757751 1004 SPATRLPWPILCSPVVGVLLLALGALLVLQLIRRRRREHGALWLPPGFIRRPQTQqaPHRRRPPLGEDNIGLKALK 1079
Cdd:cd21705     19 LVAAQLPWPLVCSSVAGVLALVLGALLGVQLIRRRQREHGALWLPPGFARHRDPN--PHRRREPVGEDAIGLKPLK 92

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 1958757751  116 DMDECSSA-PCANGGHCQDQPGAFHCECLPGFEGPRCE 152
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 1958757751  534 DACQSG-PCHNHGTCTPRPGGFHCACPPGFVGLRCE 568
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 1958757751   79 INECAS-NPCLNQAACHDQLNGFLCLCLPGFTGARCE 114
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 1958757751  460 EISNLCQNGGLCIDTGSSYFCRCPPGFEGKLCQ 492
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 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 1958757751  156 DECRS-DPCPVGASCLDLPGAFLCLCRPGFTGQLCE 190
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 1958757751  333 VDHCASAS-CLNGGTCMSKPGTFFCHCATGFQGLHCE 368
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
                   ....*....|....*....|....*...
gi 1958757751  264 PCAHGGTCHPQPSGYNCSCLAGYTGLTC 291
Cdd:cd00054     10 PCQNGGTCVNTVGSYRCSCPPGYTGRNC 37

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 1958757751  298 CHSGPCLNGGSCSIHPEGYSCTCPPSHTGPH 328
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 4 (Notch4) and similar proteins; Neurogenic locus notch homolog protein 4 (Notch4) functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. It affects the implementation of differentiation, proliferation and apoptotic programs. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch4, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958757751 1004 SPATRLPWPILCSPVVGVLLLALGALLVLQLIRRRRREHGALWLPPGFIRRPQTQqaPHRRRPPLGEDNIGLKALK 1079
Cdd:cd21705     19 LVAAQLPWPLVCSSVAGVLALVLGALLGVQLIRRRQREHGALWLPPGFARHRDPN--PHRRREPVGEDAIGLKPLK 92

ankyrin repeat protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757751 1179 LLDRGACPQaHTVGTGETPLHLAARFSRPTAARRLLEAGANPNQPDRAGRTPLHTAVAADAREVCQLLLASRQTAVDART 1258
Cdd:PHA02875    21 LLDIGINPN-FEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFY 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757751 1259 DDGTTPLMLAARLAVEDLVEELIAARADVGARDKRGKTALHWAAAVNNARAARCLLQTGADKDAQDSREQTPLFLAAREG 1338
Cdd:PHA02875   100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          170
                   ....*....|...
gi 1958757751 1339 AVEVAQLLLEIGA 1351
Cdd:PHA02875   180 DIAICKMLLDSGA 192

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 1958757751   808 DCEIPPTCTpayDQYCRDHFHNGHCEKGCNNAQCGWDGGDC 848
Cdd:smart00004    1 PQDPWSRCE---DAQCWDKFGDGVCDEECNNAECLWDGGDC 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 1958757751  775 WKGCPPhSQCWLLFRDGRCHPQCDSEECLFDGYDCE 810
Cdd:pfam00066    1 WPNCPY-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 1958757751  534 DACQSG-PCHNHGTCTPRPGGFHCACPPGFVGLRCE 568
Cdd:cd00054      3 DECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 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 1958757751 1194 GETPLHLAARFSRPTAARRLLEAGanP---NQPDR----AGRTPLHTAVAADAREVCQLLLASRQTAVDARTDD------ 1260
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAA--PelvNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpg 128

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958757751 1261 -------GTTPLMLAARLAVEDLVEELIAARADVGARDKRGKTALH 1299
Cdd:cd22192    129 pknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1958757751   116 DMDECSSA-PCANGGHCQDQPGAFHCECLPGFE-GPRCE 152
Cdd:smart00179    1 DIDECASGnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|..
gi 1958757751     8 PSPCEHGGSCINTPGSFNCLCLPGYT-GSRCE 38
Cdd:smart00179    8 GNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 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 1958757751   40 DHNECLSQ-PCHPGSTCLDLLATFQCLCPPGLEGRLCE 76
Cdd:cd00054      1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1958757751    78 EINECAS-NPCLNQAACHDQLNGFLCLCLPGFT-GARCE 114
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1958757751   495 VNPCTSK-PCLHGATCVPQPNGYVCQCAPGYE-GQNC 529
Cdd:smart00179    2 IDECASGnPCQNGGTCVNTVGSYRCECPPGYTdGRNC 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 1958757751  570 DVDECLDR-PCHPSGTasCHSLANAFYCQCLPGHTGQRCE 608
Cdd:cd00054      1 DIDECASGnPCQNGGT--CVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1958757751    40 DHNECLS-QPCHPGSTCLDLLATFQCLCPPGLE-GRLCE 76
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 1958757751  378 NPCRNKATCQDTPRGARCLCSPGYTGSSCQ 407
Cdd:cd00054      9 NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 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
                   ....*....|....*....|....*...
gi 1958757751  264 PCAHGGTCHPQPSGYNCSCLAGYTGLTC 291
Cdd:cd00054     10 PCQNGGTCVNTVGSYRCSCPPGYTGRNC 37

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. Role of NOD domain remains to be elucidated.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958757751  859 PSLAL----LVVLSPPaldQQLLALA----RVLSLTLRVGLWVRKDSEGRNMVFPYPG 908
Cdd:pfam06816    2 EKLAEgvlvIVVLMDP---EELLNNSvqflRELSTVLRTNVRFKKDENGNPMIYPWYG 56

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 1958757751  120 CSSAPCANGGHCQDQPGAFHCECLPGFEGPR 150
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
                   ....*....|....*....|....*
gi 1958757751  465 CQNGGLCIDTGSSYFCRCPPGFEGK 489
Cdd:pfam00008    6 CSNGGTCVDTPGGYTCICPEGYTGK 30

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 1958757751  260 CLSTPCAHGGTCHPQPSGYNCSCLAGYTGLT 290
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 1958757751  298 CHSGPCLNGGSCSIHPEGYSCTCPPSHTGPH 328
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 1958757751   82 CASNPCLNQAACHDQLNGFLCLCLPGFTGAR 112
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 1958757751  301 GPCLNGGSCSIHPEGYSCTCPPSHTGPHCQ 330
Cdd:cd00054      9 NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.

                            10        20
                    ....*....|....*....|....*...
gi 1958757751  1194 GETPLHLAARFSRPTAARRLLEAGANPN 1221
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29

Ankyrin repeat [Signal transduction mechanisms];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757751 1146 DGVTPLMSAVFCGGVQstTVQRLglgnpepweplLDRGACPQAHTVGtGETPLHLAARFSRPTAARRLLEAGANPNQPDR 1225
Cdd:COG0666     86 GGNTLLHAAARNGDLE--IVKLL-----------LEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757751 1226 AGRTPLHTAVAADAREVCQLLLAsRQTAVDARTDDGTTPLMLAARLAVEDLVEELIAARADVGARDKRGKTALHWAAAVN 1305
Cdd:COG0666    152 DGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958757751 1306 NARAARCLLQTGADKDAQDSREQTPLFLAAREGAVEVAQLLLEIGAARGLRDQAGLAPA 1364
Cdd:COG0666    231 NLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289

Ankyrin repeat [Signal transduction mechanisms];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757751 1139 DSDTCGPDGVTPLMSAVFCGgvQSTTVQRlglgnpepwepLLDRGACPQAHTvGTGETPLHLAARFSRPTAARRLLEAGA 1218
Cdd:COG0666    112 DVNARDKDGETPLHLAAYNG--NLEIVKL-----------LLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAGA 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757751 1219 NPNQPDRAGRTPLHTAVAADAREVCQLLLAsrQTA-VDARTDDGTTPLMLAARLAVEDLVEELIAARADVGARDKRGKTA 1297
Cdd:COG0666    178 DVNARDNDGETPLHLAAENGHLEIVKLLLE--AGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958757751 1298 LHWAAAVNNARAARCLLQTGADKDAQDSREQTPL 1331
Cdd:COG0666    256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 4 (Notch4) and similar proteins; Neurogenic locus notch homolog protein 4 (Notch4) functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. It affects the implementation of differentiation, proliferation and apoptotic programs. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch4, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958757751 1004 SPATRLPWPILCSPVVGVLLLALGALLVLQLIRRRRREHGALWLPPGFIRRPQTQqaPHRRRPPLGEDNIGLKALK 1079
Cdd:cd21705     19 LVAAQLPWPLVCSSVAGVLALVLGALLGVQLIRRRQREHGALWLPPGFARHRDPN--PHRRREPVGEDAIGLKPLK 92

ankyrin repeat protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757751 1179 LLDRGACPQaHTVGTGETPLHLAARFSRPTAARRLLEAGANPNQPDRAGRTPLHTAVAADAREVCQLLLASRQTAVDART 1258
Cdd:PHA02875    21 LLDIGINPN-FEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFY 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757751 1259 DDGTTPLMLAARLAVEDLVEELIAARADVGARDKRGKTALHWAAAVNNARAARCLLQTGADKDAQDSREQTPLFLAAREG 1338
Cdd:PHA02875   100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          170
                   ....*....|...
gi 1958757751 1339 AVEVAQLLLEIGA 1351
Cdd:PHA02875   180 DIAICKMLLDSGA 192

ankyrin repeat protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757751 1179 LLDRGACPQAHTVGTGETPLHLAARFSRPTAARRLLEAGANPNQPDRAGRTPLHTAVAADAREVCQLLLASrQTAVDART 1258
Cdd:PHA02878   153 LLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-GASTDARD 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757751 1259 DDGTTPLMLA-ARLAVEDLVEELIAARADVGARDK-RGKTALHwaAAVNNARAARCLLQTGADKDAQDSREQTPLFLAAR 1336
Cdd:PHA02878   232 KCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALH--SSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVK 309

                   .
gi 1958757751 1337 E 1337
Cdd:PHA02878   310 Q 310

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
                   ....*....|....*....|....*....|....*....|....
gi 1958757751 1036 RRRRREHGALWLPPGFIrrpQTQQAPHRRRPPLGEDNIGLKALK 1079
Cdd:cd21702     39 RKRRREHGQLWFPEGFK---VSEPSKKKRREPVGEDSVGLKPLK 79

ankyrin-like protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757751 1144 GPDGVTPLMSAVFCGGVQSTTVQRLglgnpepwepLLDRGACPQAHTVgTGETPLHLAARFS-RPTAARRLLEAGANPNQ 1222
Cdd:PHA03095    44 GEYGKTPLHLYLHYSSEKVKDIVRL----------LLEAGADVNAPER-CGFTPLHLYLYNAtTLDVIKLLIKAGADVNA 112