Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 88758613   385 DVDECALGRSPCAQG--CTNTDGSFHCSCEEG 414
Cdd:pfam07645   1 DVDECATGTHNCPANtvCVNTIGSFECRCPDG 32

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 88758613   264 CNFNNGGCHQDCfEGGDGSFLCGCRPGFRLLDDLVTC 300
Cdd:pfam14670   1 CSVNNGGCSHLC-LNTPGGYTCSCPEGYELQDDGRTC 36

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.

                          10        20
                  ....*....|....*....|..
gi 88758613   327 TCRCPQGYQLDSSQLDCVDVDE 348
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.

                          10        20
                  ....*....|....*....|...
gi 88758613   408 HCSCEEGYVLAgEDGTQCQDVDE 430
Cdd:pfam12662   1 TCSCPPGYQLD-PDGRTCVDIDE 22

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758613     30 VCVGTACYTAHSGKLSAAEAQNHCNQNGGNLATVKSKEEaqhvQRVLAQLLRREAAltarMSKFWIGLQREKGKCldpsl 109
Cdd:smart00034   6 ISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAE----NDFVASLLKNSGS----SDYYWIGLSDPDSNG----- 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88758613    110 plkGFSWVGGGEDTPYSNWHKELRNScISKRCVSLLLDLSqpllpsrlpKWSEGPCGSPgspgsniEGFVCK 181
Cdd:smart00034  73 ---SWQWSDGSGPVSYSNWAPGEPNN-SSGDCVVLSTSGG---------KWNDVSCTSK-------LPFVCE 124

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 88758613   385 DVDECALGRSPCAQG--CTNTDGSFHCSCEEG 414
Cdd:pfam07645   1 DVDECATGTHNCPANtvCVNTIGSFECRCPDG 32

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 88758613 383 CQDVDECALGRSPCAQGCTNTDGSFHCSCEEGYVLAgEDG 422
Cdd:cd01475 184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALL-EDN 222

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 88758613   264 CNFNNGGCHQDCfEGGDGSFLCGCRPGFRLLDDLVTC 300
Cdd:pfam14670   1 CSVNNGGCSHLC-LNTPGGYTCSCPEGYELQDDGRTC 36

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.

                          10        20
                  ....*....|....*....|..
gi 88758613   327 TCRCPQGYQLDSSQLDCVDVDE 348
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|...
gi 88758613   427 DVDECVGPGGPlCDS--LCFNTQGSFHCGCLPG 457
Cdd:pfam07645   1 DVDECATGTHN-CPAntVCVNTIGSFECRCPDG 32

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

                        10        20        30
                ....*....|....*....|....*....|....
gi 88758613 427 DVDECVGPGGPLCDSLCFNTQGSFHCGCLPGWVL 460
Cdd:cd00054   1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTG 34

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758613  36 CYTAHSGKLSAAEAQNHCNQNGGNLATVKSKEEAQHVQRVLAQLLRREaaltarmskFWIGLQREKGKCldpslplkGFS 115
Cdd:cd00037   2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD---------VWIGLNDLSSEG--------TWK 64

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88758613 116 WVGGGEDTPYSNWHKELRNSCISKRCVsllldlsqPLLPSRLPKWSEGPCgspgspgSNIEGFVCKF 182
Cdd:cd00037  65 WSDGSPLVDYTNWAPGEPNPGGSEDCV--------VLSSSSDGKWNDVSC-------SSKLPFICEK 116

Lectin C-type domain; This family includes both long and short form C-type

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758613    43 KLSAAEAQNHCNQNGGNLATVKSKEEaqhvQRVLAQLLRREAaltarmSKFWIGLQREKgkcldpslPLKGFSWVGGGED 122
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEE----LDFLSSTLKKSN------KYFWIGLTDRK--------NEGTWKWVDGSPV 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758613   123 TpYSNWHKELRNSCISKRCVsllldlsqpLLPSRLPKWSEGPCGSPGspgsnieGFVCKF 182
Cdd:pfam00059  63 N-YTNWAPEPNNNGENEDCV---------ELSSSSGKWNDENCNSKN-------PFVCEK 105

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 88758613    385 DVDECALGrSPCAQG--CTNTDGSFHCSCEEGYvlagEDGTQCQ 426
Cdd:smart00179   1 DIDECASG-NPCQNGgtCVNTVGSYRCECPPGY----TDGRNCE 39

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 88758613 383 CQDVDECALGRSPCAQGCTNTDGSFHCSCEEGYVLAgEDG 422
Cdd:cd01475 184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALL-EDN 222

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758613  36 CYTAHSGKLSAAEAQNHCNQ--NGGNLATVKSKEEAQHVQRVLAQLLRREaaltarmSKFWIGLQRekgkcldpslPLKG 113
Cdd:cd03594  12 CYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYQKAY-------QPVWIGLHD----------PQQS 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88758613 114 FSWV-GGGEDTPYSNWHkelRNSCIS--KRCVsllldlsQPLLPSRLPKWSEGPCgspgspgSNIEGFVCKF 182
Cdd:cd03594  75 RGWEwSDGSKLDYRSWD---RNPPYArgGYCA-------ELSRSTGFLKWNDANC-------EERNPFICKY 129

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 88758613   389 CALGRSPCAQG--CTNTDGSFHCSCEEGYVLageDGTQC 425
Cdd:pfam12947   1 CSDNNGGCHPNatCTNTGGSFTCTCNDGYTG---DGVTC 36

Calcium-binding EGF-like domain;

                           10        20
                   ....*....|....*....|....*...
gi 88758613    345 DVDECQ-DSPCAQ--ECVNTPGGFRCEC 369
Cdd:smart00179   1 DIDECAsGNPCQNggTCVNTVGSYRCEC 28

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758613  48 EAQNHCNQNGGNLATVKSKEEAQHVQRVlaqllrreaaLTARMSKFWIGLQREKGkcldpslplkGFSWVGGGEDTpYSN 127
Cdd:cd03602  14 EAQQYCRENYTDLATVQNQEDNALLSNL----------SRVSNSAAWIGLYRDVD----------SWRWSDGSESS-FRN 72

                .
gi 88758613 128 W 128
Cdd:cd03602  73 W 73

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 88758613   389 CALGRSPCAQGCTNTDGSFHCSCEEGYVLAgEDGTQC 425
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQ-DDGRTC 36

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 88758613 345 DVDECQD-SPCA--QECVNTPGGFRCEC 369
Cdd:cd00054   1 DIDECASgNPCQngGTCVNTVGSYRCSC 28

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758613  30 VCVGTACYTAHSGKLSAAEAQNHCNQNGGNLATVKSKEEAQHVQRVLaqllrreaaltaRMSKFWIGLQREKGKcldpsl 109
Cdd:cd03593   6 ICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQI------------GSSSYWIGLSREKSE------ 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 88758613 110 plKGFSWVGGgedTPYSNWHkELRNSCISKRCV 142
Cdd:cd03593  68 --KPWKWIDG---SPLNNLF-NIRGSTKSGNCA 94

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758613  37 YTAHSGKLSAAEAQNHCNQNGGNLATVKSKEEAQHVQrvlaqllrrEAALTARMSKFWIGLQREKgkcldpslplKGFSW 116
Cdd:cd03592   3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLN---------GFALKYNLGYYWIDGNDIN----------NEGTW 63

                        90       100
                ....*....|....*....|....*..
gi 88758613 117 VG-GGEDTPYSNWHKELRNSCISKRCV 142
Cdd:cd03592  64 VDtDKKELEYKNWAPGEPNNGRNENCL 90