juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 3 (Notch3) and similar proteins; Neurogenic locus notch homolog protein 3 (Notch3) 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. The model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch3, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414885 1566 ERLDFPYPLRDVRGEPLEPPEPSVPLLPLLVAGAVLLLVILVLGVMVARRKREHSTLWFPEGFSLHKDVAsgHKGRREPV 1645
Cdd:cd21704     1 ERLEFPYPIKEVRGEKLEPPPPPVRLLPLLGVAAVILLVILVLGVLVARRKREHSTLWFPEGFFLKKESS--NKNRREPV 78

                          90
                  ....*....|..
gi 530414885 1646 GQDALGMKNMAK 1657
Cdd:cd21704    79 GQDALGMKHIAK 90

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        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530414885  1525 VIGSVVMLEIDNRLCLQSPenDHCFPDAQSAADYLGALSAVERLDFPYPLRDVRGEPLEPP 1585
Cdd:pfam07684    1 VIGSVVYLEIDNRKCSQSS--DECFSTAQSAADFLAALAAKGGLDLPYPIKEVRSEPPPPP 59

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 530414885  1332 EPRCPRAACQAKRGDQRCDRECNSPGCGWDGGDCS 1366
Cdd:pfam00066    1 WPNCPYPYCWDKFGNGVCDEECNNAECLWDGGDCS 35

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 530414885  1422 YCADHFADGRCDQGCNTEECGWDGLDC 1448
Cdd:pfam00066    8 YCWDKFGNGVCDEECNNAECLWDGGDC 34

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

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 530414885  469 DIDECQS-SPCVNGGVCKDRVNGFSCTCPSGFSGSTCQ 505
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 530414885  431 DVNECLSG-PCRNQATCLDRIGQFTCICMAGFTGTYCE 467
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 530414885  274 DVDECQlQPNACHNGGTCFNTLGGHSCVCVNGWTGESC 311
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 530414885  877 SPSSCFNGGTCVDGVNSFSCLCRPGYTGAHCQ 908
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 530414885 1070 DVDECASQ-PCQHGGSCIDLVARYLCSCPPGTLGVLCE 1106
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 530414885  545 NVDDC-SPDPC-HHGRCVDGIASFSCACAPGYTGTRCE 580
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 530414885 1033 VDPCL-AQPCQHGGTCRGYMGGYMCECLPGYNGDNCE 1068
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 530414885  658 INECAS-SPCGEGGSCVDGENGFRCLCPPG 686
Cdd:cd00054     2 IDECASgNPCQNGGTCVNTVGSYRCSCPPG 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 530414885  314 NIDDCATA-VCFHGATCHDRVASFYCACPMGKTGLLC 349
Cdd:cd00054     1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 3 (Notch3) and similar proteins; Neurogenic locus notch homolog protein 3 (Notch3) 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. The model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch3, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414885 1566 ERLDFPYPLRDVRGEPLEPPEPSVPLLPLLVAGAVLLLVILVLGVMVARRKREHSTLWFPEGFSLHKDVAsgHKGRREPV 1645
Cdd:cd21704     1 ERLEFPYPIKEVRGEKLEPPPPPVRLLPLLGVAAVILLVILVLGVLVARRKREHSTLWFPEGFFLKKESS--NKNRREPV 78

                          90
                  ....*....|..
gi 530414885 1646 GQDALGMKNMAK 1657
Cdd:cd21704    79 GQDALGMKHIAK 90

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        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530414885  1525 VIGSVVMLEIDNRLCLQSPenDHCFPDAQSAADYLGALSAVERLDFPYPLRDVRGEPLEPP 1585
Cdd:pfam07684    1 VIGSVVYLEIDNRKCSQSS--DECFSTAQSAADFLAALAAKGGLDLPYPIKEVRSEPPPPP 59

ankyrin-like protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414885 1727 GMDVNVRGPDGFTPL--MLASFCggalepmpteedeaddTSASIISDLICQGAQLGARtDRTGETALH--LAARYARADA 1802
Cdd:PHA03095  107 GADVNAKDKVGRTPLhvYLSGFN----------------INPKVIRLLLRKGADVNAL-DLYGMTPLAvlLKSRNANVEL 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414885 1803 AKRLLDAGADTNAQDHSGRTPLHT-AVTADA-QGVFQILIRnRSTDLDARMADGSTALILAARLAV--EGMVEELIASHA 1878
Cdd:PHA03095  170 LRLLIDAGADVYAVDDRFRSLLHHhLQSFKPrARIVRELIR-AGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGI 248

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530414885 1879 DVNAVDELGKSALHWAAAVNNVEATLALLKNGANKDMQDSKEETPLFLAAREGSYEAAKLLL 1940
Cdd:PHA03095  249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 530414885    158 DVDECRVGEPCRHGGTCLNTPGSFRCQCPAGYT-GPLCE 195
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

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

                           10        20        30
                   ....*....|....*....|....*....|....
gi 530414885  1373 WRQCEALQCWRLFNNSRCDPACSSPACLYDNFDC 1406
Cdd:pfam00066    1 WPNCPYPYCWDKFGNGVCDEECNNAECLWDGGDC 34

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 530414885  1422 YCADHFADGRCDQGCNTEECGWDGLDC 1448
Cdd:pfam00066    8 YCWDKFGNGVCDEECNNAECLWDGGDC 34

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414885 1999 PGLKAAQSGSKKSRRPPGKaglgPQGPRGRGKKLTLACPGPLADSSV-TLSPVDSLD-SPRPFGGPPASPGGfPLEGPYA 2076
Cdd:PHA03247 2686 RAARPTVGSLTSLADPPPP----PPTPEPAPHALVSATPLPPGPAAArQASPALPAApAPPAVPAGPATPGG-PARPARP 2760

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414885 2077 AATATAVSLAQLGGPGRAGLGRQPPGGCVLSLGLLNPVAVPLDWARLPPPAPPGPSFLLPLA------PGPQLLNPGTPV 2150
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspagplPPPTSAQPTAPP 2840

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414885 2151 SPQERPPPYLA-----VPG-----HGEEYPAAGAHSSPPKARFLRVPSehPYLTPSPESpehwaSPSPPSlsdwsESTPS 2220
Cdd:PHA03247 2841 PPPGPPPPSLPlggsvAPGgdvrrRPPSRSPAAKPAAPARPPVRRLAR--PAVSRSTES-----FALPPD-----QPERP 2908

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 530414885 2221 PATATGAMATTTGALPAQPLPLSVPSSLAQAQTQLGPQPEVTPKRQ 2266
Cdd:PHA03247 2909 PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE 2954

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 530414885  391 DVDECSIGaNPCEHLGRCVNTQGSFLCQCGRGYTGPRCE 429
Cdd:cd00054     1 DIDECASG-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        30
                  ....*....|....*....|....*....|....*...
gi 530414885  431 DVNECLSG-PCRNQATCLDRIGQFTCICMAGFTGTYCE 467
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 530414885 1119 DSGPRCLHNGTCVDLVGGFRCTCPPGYTGLRCE 1151
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 530414885  274 DVDECQlQPNACHNGGTCFNTLGGHSCVCVNGWTGESC 311
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 530414885  877 SPSSCFNGGTCVDGVNSFSCLCRPGYTGAHCQ 908
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 530414885  835 DVDECLS-NPCGP-GTCTDHVASFTCTCPPGYGGFHCE 870
Cdd:cd00054     1 DIDECASgNPCQNgGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 530414885   1070 DVDECAS-QPCQHGGSCIDLVARYLCSCPPG-TLGVLCE 1106
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 530414885  236 NVDDC-PGHRCLNGGTCVDGVNTYNCQCPPEWTGQFCT 272
Cdd:cd00054     1 DIDECaSGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....
gi 530414885   1119 DSGPRCLHNGTCVDLVGGFRCTCPPGYT-GLRCE 1151
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 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 530414885  545 NVDDC-SPDPC-HHGRCVDGIASFSCACAPGYTGTRCE 580
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 530414885 1820 GRTPLHTAVTADAQGVFQILIRNRSTDLDARMA----DGSTALILAARLAVEGMVEELIASHADVNA-----------VD 1884
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPK 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530414885 1885 EL---GKSALHWAAAVNNVEATLALLKNGANKDMQDSKEETPLFLAAREGSYEAAKLLLDHFANREITDH---LDRLP 1956
Cdd:cd22192   131 NLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDKEDDlqpLDLVP 208

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 530414885    835 DVDECLS-NPCGPG-TCTDHVASFTCTCPPGY-GGFHCE 870
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 530414885  658 INECAS-SPCGEGGSCVDGENGFRCLCPPG 686
Cdd:cd00054     2 IDECASgNPCQNGGTCVNTVGSYRCSCPPG 31

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|...
gi 530414885    877 SPSSCFNGGTCVDGVNSFSCLCRPGYT-GAHCQ 908
Cdd:smart00179    7 SGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 530414885   158 DVDECRVG-EPCRHGGTCLNTPGSFRCQCPAG 188
Cdd:pfam07645    1 DVDECATGtHNCPANTVCVNTIGSFECRCPDG 32

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530414885  2063 PASPGGFPLEGPYAAATATAVSLAQLGGPGRAGLGRQ------PPGGCVLSLGLLNPVAVPLDWARLpppappgpsfLLP 2136
Cdd:TIGR01645  291 PATVSAIPAAAAVAAAAATAKIMAAEAVAGAAVLGPRaqspatPSSSLPTDIGNKAVVSSAKKEAEE----------VPP 360

                           90       100
                   ....*....|....*....|....*...
gi 530414885  2137 LAPG-PQLLNPGTPVSPQERPPPYLAVP 2163
Cdd:TIGR01645  361 LPQAaPAVVKPGPMEIPTPVPPPGLAIP 388

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 530414885    545 NVDDC-SPDPCHHG-RCVDGIASFSCACAPGYT-GTRCE 580
Cdd:smart00179    1 DIDECaSGNPCQNGgTCVNTVGSYRCECPPGYTdGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 530414885    583 VDECRS-QPCRHGGKCLDLVDKYLCRCPSG-TTGVNCE 618
Cdd:smart00179    2 IDECASgNPCQNGGTCVNTVGSYRCECPPGyTDGRNCE 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 530414885  1036 CLAQPCQHGGTCRGYMGGYMCECLPGYNGDN 1066
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 530414885  1123 RCLHNGTCVDLVGGFRCTCPPGYTGLR 1149
Cdd:pfam00008    5 PCSNGGTCVDTPGGYTCICPEGYTGKR 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 530414885   511 CASTPCRNGAKCVDQPDGYECRCAEGFEG 539
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29

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 530414885  314 NIDDCATA-VCFHGATCHDRVASFYCACPMGKTGLLC 349
Cdd:cd00054     1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37