Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605   172 PQIVSHPYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGLDIQlpgDDPHISVQFRGGPQRFEvtgwlqIQAVRPSDEGTY 251
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR---SSDRFKVTYEGGTYTLT------ISNVQPDDSGKY 71

                          90
                  ....*....|....*....
gi 68565605   252 RCLGRNALGQVEAPASLTV 270
Cdd:pfam07679  72 TCVATNSAGEAEASAELTV 90

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 68565605 129 RSQSPLCGSDGHTYSQICRLQEAARaRPDANLTVAHPGPC 168
Cdd:cd00104   3 KEYDPVCGSDGKTYSNECHLGCAAC-RSGRSITVAHNGPC 41

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605   172 PQIVSHPYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGLDIQlpgDDPHISVQFRGGPQRFEvtgwlqIQAVRPSDEGTY 251
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR---SSDRFKVTYEGGTYTLT------ISNVQPDDSGKY 71

                          90
                  ....*....|....*....
gi 68565605   252 RCLGRNALGQVEAPASLTV 270
Cdd:pfam07679  72 TCVATNSAGEAEASAELTV 90

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 172 PQIVSHPYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGLDIQLPGDDPHISVQfrggpqrfevTGWLQIQAVRPSDEGTY 251
Cdd:cd20976   2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAG----------VGELHIQDVLPEDHGTY 71

                        90
                ....*....|....*....
gi 68565605 252 RCLGRNALGQVEAPASLTV 270
Cdd:cd20976  72 TCLAKNAAGQVSCSAWVTV 90

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 68565605 129 RSQSPLCGSDGHTYSQICRLQEAARaRPDANLTVAHPGPC 168
Cdd:cd00104   3 KEYDPVCGSDGKTYSNECHLGCAAC-RSGRSITVAHNGPC 41

Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 68565605     53 CAPCRPEECAA-PRGCLAGRVRDACGCCWECANLEGQLCDLDpsahfYGHCGEQLECR 109
Cdd:smart00121   3 CPPCDPARCPPcPPGCAELVRLDGCGCCPVCARQEGEPCGVY-----TPRCAPGLRCQ 55

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605   172 PQIVSHPYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGLDIQlpgDDPHISVQFRGGPQRFEvtgwlqIQAVRPSDEGTY 251
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR---SSDRFKVTYEGGTYTLT------ISNVQPDDSGKY 71

                          90
                  ....*....|....*....
gi 68565605   252 RCLGRNALGQVEAPASLTV 270
Cdd:pfam07679  72 TCVATNSAGEAEASAELTV 90

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 172 PQIVSHPYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGLDIQLPGDDPHISVQfrggpqrfevTGWLQIQAVRPSDEGTY 251
Cdd:cd20976   2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAG----------VGELHIQDVLPEDHGTY 71

                        90
                ....*....|....*....
gi 68565605 252 RCLGRNALGQVEAPASLTV 270
Cdd:cd20976  72 TCLAKNAAGQVSCSAWVTV 90

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605   172 PQIVSHPYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGldiQLPGDDPHISVQFRGGpqrfevTGWLQIQAVRPSDEGTY 251
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNG---EPISSGSTRSRSLSGS------NSTLTISNVTRSDAGTY 72

                  ....*.
gi 68565605   252 RCLGRN 257
Cdd:pfam13927  73 TCVASN 78

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68565605 189 VIFGCEVFAYPMASIEWRKDGLDIQLPGDDPHISVQfrggpqrfeVTGWLQIQAVRPSDEGTYRCLGRNALG 260
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSEL---------GNGTLTISNVTLEDSGTYTCVASNSAG 63

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 177 HPYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGlDIQLPGDdphisvqfrggpqRFEVTGW--LQIQAVRPSDEGTYRCL 254
Cdd:cd05723   3 KPSNIYAHESMDIVFECEVTGKPTPTVKWVKNG-DVVIPSD-------------YFKIVKEhnLQVLGLVKSDEGFYQCI 68

                        90
                ....*....|....*.
gi 68565605 255 GRNALGQVEAPASLTV 270
Cdd:cd05723  69 AENDVGNAQASAQLII 84

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 172 PQIVSHP-YDTWNVTGQDVIFGCEVFAYPMASIEWRKDGLDIQlpgddphisvqfrGGPQRFEVT-GWLQIQAVRPSDEG 249
Cdd:cd20978   1 PKFIQKPeKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQ-------------GPMERATVEdGTLTIINVQPEDTG 67

                        90       100
                ....*....|....*....|.
gi 68565605 250 TYRCLGRNALGQVEAPASLTV 270
Cdd:cd20978  68 YYGCVATNEIGDIYTETLLHV 88

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68565605 184 VTGQDVIFGCEVFAYPMASIEWRKDGldIQLPgdDPHisvqfRggpQRFEVTGWLQIQAV-RPSDEGTYRCLGRNALGQ 261
Cdd:cd20958  13 VAGQTLRLHCPVAGYPISSITWEKDG--RRLP--LNH-----R---QRVFPNGTLVIENVqRSSDEGEYTCTARNQQGQ 79

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 172 PQIVSH-PYDTWNVTGQDVIFGCEVFAYPMASIEWRK-DGLdiQLPGDDPHISvqfrggpqrfevTGWLQIQAVRPSDEG 249
Cdd:cd04968   1 PSIKVRfPADTYALKGQTVTLECFALGNPVPQIKWRKvDGS--PSSQWEITTS------------EPVLEIPNVQFEDEG 66

                        90       100
                ....*....|....*....|.
gi 68565605 250 TYRCLGRNALGQVEAPASLTV 270
Cdd:cd04968  67 TYECEAENSRGKDTVQGRIIV 87

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 174 IVSHPYDTWNVT---GQDVIFGCEVFAYPMASIEWRKDGLDIQLpgddphisvqfrgGPQRFEVTGW---LQIQAVRPSD 247
Cdd:cd20970   2 VISTPQPSFTVTareGENATFMCRAEGSPEPEISWTRNGNLIIE-------------FNTRYIVRENgttLTIRNIRRSD 68

                        90       100
                ....*....|....*....|....
gi 68565605 248 EGTYRCLGRN-ALGQVEAPASLTV 270
Cdd:cd20970  69 MGIYLCIASNgVPGSVEKRITLQV 92

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 173 QIVSHPYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGLDIQL-PGDDPHISVQFRGGPqrfevTGWLQIQAVRPSDEGTY 251
Cdd:cd05726   1 QFVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNLLfPYQPPQPSSRFSVSP-----TGDLTITNVQRSDVGYY 75

                        90
                ....*....|....*....
gi 68565605 252 RCLGRNALGQVEAPASLTV 270
Cdd:cd05726  76 ICQALNVAGSILAKAQLEV 94

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 186 GQDVIFGCEVFAYPMASIEWRKDGldIQLPGDDPHISVQfrggpqrfevTGWLQIQAVRPSDEGTYRCLGRNALGQVEAP 265
Cdd:cd05745   2 GQTVDFLCEAQGYPQPVIAWTKGG--SQLSVDRRHLVLS----------SGTLRISRVALHDQGQYECQAVNIVGSQRTV 69

                ....*
gi 68565605 266 ASLTV 270
Cdd:cd05745  70 AQLTV 74

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 172 PQIVSH--PYDTWNvtGQDVIFGCEVFAYPMASIEWRKDGLDIQLPGDDPHISVQFRGGPQRfevtgwLQIQAVRPSDEG 249
Cdd:cd20951   1 PEFIIRlqSHTVWE--KSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHV------LHIRRVTVEDSA 72

                        90       100
                ....*....|....*....|.
gi 68565605 250 TYRCLGRNALGQVEAPASLTV 270
Cdd:cd20951  73 VYSAVAKNIHGEASSSASVVV 93

Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 68565605     53 CAPCRPEECAA-PRGCLAGRVRDACGCCWECANLEGQLCDLDpsahfYGHCGEQLECR 109
Cdd:smart00121   3 CPPCDPARCPPcPPGCAELVRLDGCGCCPVCARQEGEPCGVY-----TPRCAPGLRCQ 55

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 185 TGQDVIFGCEVFAYPMASIEWRKDGLDIQlPGDDPHIsvqFRggpqrfEVTGWLQIQAVRPSDEGTYRCLGRNALGQVEA 264
Cdd:cd05730  17 LGQSVTLACDADGFPEPTMTWTKDGEPIE-SGEEKYS---FN------EDGSEMTILDVDKLDEAEYTCIAENKAGEQEA 86

                ....*.
gi 68565605 265 PASLTV 270
Cdd:cd05730  87 EIHLKV 92

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 172 PQIVSHPYDTWNVTGQDVIFGCEVFAYPMASIEWRKdgldiQLPGDDPHISV--QFRGGpqrFEVT--GWLQIQAVRPSD 247
Cdd:cd05765   1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEK-----QVPGKENLIMRpnHVRGN---VVVTniGQLVIYNAQPQD 72

                        90       100
                ....*....|....*....|...
gi 68565605 248 EGTYRCLGRNALGQVEAPASLTV 270
Cdd:cd05765  73 AGLYTCTARNSGGLLRANFPLSV 95

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 171 GPQIVSHPYDTWNVTGQD---VIFGCEVFAYPMASIEWRKDGLDIQLPGDDphisvqfrggpqRFE-VTGWLQI-QAVRP 245
Cdd:cd04967   1 GPVFEEQPDDTIFPEDSDekkVALNCRARANPVPSYRWLMNGTEIDLESDY------------RYSlVDGTLVIsNPSKA 68

                        90
                ....*....|....*..
gi 68565605 246 SDEGTYRCLGRNALGQV 262
Cdd:cd04967  69 KDAGHYQCLATNTVGSV 85

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 178 PYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGldiqlpGDDphisvqFRGGPQR----FEVTGWLQIQAVRPSDEGTYRC 253
Cdd:cd05763   6 PHDITIRAGSTARLECAATGHPTPQIAWQKDG------GTD------FPAARERrmhvMPEDDVFFIVDVKIEDTGVYSC 73

                        90
                ....*....|....*...
gi 68565605 254 LGRNALGQVEAPASLTVL 271
Cdd:cd05763  74 TAQNSAGSISANATLTVL 91

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 173 QIVSHPYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGLDIQlpgDDPHISVqfrggpqrFEvTGWLQIQAVRPSDEGTYR 252
Cdd:cd20968   1 KITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIK---ENNRIAV--------LE-SGSLRIHNVQKEDAGQYR 68

                        90
                ....*....|....*....
gi 68565605 253 CLGRNALGQV-EAPASLTV 270
Cdd:cd20968  69 CVAKNSLGIAySKPVTIEV 87

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 174 IVSHPYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGldiqlpgddphisvQFRGGPQRFEVT-----GWLQIQAVRPSDE 248
Cdd:cd05747   6 ILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREG--------------QIIVSSQRHQITsteykSTFEISKVQMSDE 71

                        90       100
                ....*....|....*....|.
gi 68565605 249 GTYRCLGRNALGQVEAPASLT 269
Cdd:cd05747  72 GNYTVVVENSEGKQEAQFTLT 92

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68565605 193 CEVFAYPMASIEWRKDGLDIQLPGDDpHISVQfrggpqrfevtGWLQIQAVRPSDEGTYRCLGRNALGQVEAPASLT 269
Cdd:cd05746   5 CSAQGDPEPTITWNKDGVQVTESGKF-HISPE-----------GYLAIRDVGVADQGRYECVARNTIGYASVSMVLS 69

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 185 TGQDVIFGCEVFAYPMASIEWRKDGLDIQLPGDDPHISVqfRGGPQRFEvtgwlqiqAVRPSDEGTYRCLGRNALGQVEA 264
Cdd:cd04978  13 PGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTV--DGRTLIFS--------NLQPNDTAVYQCNASNVHGYLLA 82

                ....*..
gi 68565605 265 PASLTVL 271
Cdd:cd04978  83 NAFLHVL 89

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68565605 188 DVIFGCEVFAYPMASIEWRKDGLDIQlPGDDPHISVQFRGGpqrfevTGWLQIQAVRPSD-EGTYRCLGRNALG 260
Cdd:cd05733  18 NITIKCEAKGNPQPTFRWTKDGKFFD-PAKDPRVSMRRRSG------TLVIDNHNGGPEDyQGEYQCYASNELG 84

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 178 PYDTWNVTGQDVIFGCEVFAYPMASIEW----RKDGLDIQlPGDDPHISVQFRGG----PQRFEVtgwLQIQAVRPSDEG 249
Cdd:cd05858   8 PANTSVVVGTDAEFVCKVYSDAQPHIQWlkhvEKNGSKYG-PDGLPYVEVLKTAGvnttDKEIEV---LYLRNVTFEDAG 83

                        90       100
                ....*....|....*....|..
gi 68565605 250 TYRCLGRNALGQVEAPASLTVL 271
Cdd:cd05858  84 EYTCLAGNSIGISHHSAWLTVL 105

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 177 HPYDTWNVTGQDVIFGCEVFAYPMASIEWRK----DGlDIQLPGDDPHISVQFRGGPQRFEVTGWLQIQAVRPSDEGTYR 252
Cdd:cd04974   7 LPANQTVVLGSDVEFHCKVYSDAQPHIQWLKhvevNG-SKYGPDGLPYVTVLKVAGVNTTGEENTLTISNVTFDDAGEYI 85

                        90
                ....*....|....*..
gi 68565605 253 CLGRNALGQVEAPASLT 269
Cdd:cd04974  86 CLAGNSIGLSFHSAWLT 102

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 178 PYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGldiqlpgddphisvQFRGGPQRFEVT-GWLQIQAVRPSDEGTYRCLGR 256
Cdd:cd05728   6 ISDTEADIGSSLRWECKASGNPRPAYRWLKNG--------------QPLASENRIEVEaGDLRITKLSLSDSGMYQCVAE 71

                        90
                ....*....|....
gi 68565605 257 NALGQVEAPASLTV 270
Cdd:cd05728  72 NKHGTIYASAELAV 85

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565605 186 GQDVIFGCE-VFAYPMASIEWRKDGLDIQLPGDDPHISVqfRGGPQRFEvtgwLQIQAVRPSDEGTYRCLGRNALGQVEA 264
Cdd:cd05895  14 GSKLVLRCEtSSEYPSLRFKWFKNGKEINRKNKPENIKI--QKKKKKSE----LRINKASLADSGEYMCKVSSKLGNDSA 87

                ....*.
gi 68565605 265 PASLTV 270
Cdd:cd05895  88 SANVTI 93