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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847 134 PTISVPSSVTIGNRAVLTCSEHDGSPPSEYSWFKDGISMlTADAKKTRAFMNSSFTIDPKSGDLIFDPVTAFDSGEYYCQ 213
Cdd:cd20950   1 PTVNIPSSATIGNRAVLTCSEPDGSPPSEYTWFKDGVVM-PTNPKSTRAFSNSSYSLDPTTGELVFDPLSASDTGEYSCE 79

                        90
                ....*....|....*...
gi 27734847 214 AQNGYGTAMRSEAAHMDA 231
Cdd:cd20950  80 ARNGYGTPMRSNAVRMEA 97

Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF domains; The members here are composed of the second Ig-like domain of Junctional adhesion molecule-1 (JAM1). JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The 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 second Ig-like domain of JAM1 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, the A strand of the I-set is discontinuous but lacks 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847 134 PTISVPSSVTIGNRAVLTCSEHDGSPPSEYSWFKDGISMlTADAKKTRAFMNSSFTIDPKSGDLIFDPVTAFDSGEYYCQ 213
Cdd:cd20950   1 PTVNIPSSATIGNRAVLTCSEPDGSPPSEYTWFKDGVVM-PTNPKSTRAFSNSSYSLDPTTGELVFDPLSASDTGEYSCE 79

                        90
                ....*....|....*...
gi 27734847 214 AQNGYGTAMRSEAAHMDA 231
Cdd:cd20950  80 ARNGYGTPMRSNAVRMEA 97

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847   133 KPTISVPSS---VTIGNRAVLTCsEHDGSPPSEYSWFKDGISMLTADAkktrafmnSSFTIDPKSGDLIFDPVTAFDSGE 209
Cdd:pfam13927   1 KPVITVSPSsvtVREGETVTLTC-EATGSPPPTITWYKNGEPISSGST--------RSRSLSGSNSTLTISNVTRSDAGT 71

                  ....*..
gi 27734847   210 YYCQAQN 216
Cdd:pfam13927  72 YTCVASN 78

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847    141 SVTIGNRAVLTCsEHDGSPPSEYSWFKDGISMLTADAKKTRAFMNSSFTidpksgdLIFDPVTAFDSGEYYCQAQNGYGT 220
Cdd:smart00410   5 TVKEGESVTLSC-EASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTST-------LTISNVTPEDSGTYTCAATNSSGS 76

                   .
gi 27734847    221 A 221
Cdd:smart00410  77 A 77

Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF domains; The members here are composed of the second Ig-like domain of Junctional adhesion molecule-1 (JAM1). JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The 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 second Ig-like domain of JAM1 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, the A strand of the I-set is discontinuous but lacks 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847 134 PTISVPSSVTIGNRAVLTCSEHDGSPPSEYSWFKDGISMlTADAKKTRAFMNSSFTIDPKSGDLIFDPVTAFDSGEYYCQ 213
Cdd:cd20950   1 PTVNIPSSATIGNRAVLTCSEPDGSPPSEYTWFKDGVVM-PTNPKSTRAFSNSSYSLDPTTGELVFDPLSASDTGEYSCE 79

                        90
                ....*....|....*...
gi 27734847 214 AQNGYGTAMRSEAAHMDA 231
Cdd:cd20950  80 ARNGYGTPMRSNAVRMEA 97

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847   133 KPTISVPSS---VTIGNRAVLTCsEHDGSPPSEYSWFKDGISMLTADAkktrafmnSSFTIDPKSGDLIFDPVTAFDSGE 209
Cdd:pfam13927   1 KPVITVSPSsvtVREGETVTLTC-EATGSPPPTITWYKNGEPISSGST--------RSRSLSGSNSTLTISNVTRSDAGT 71

                  ....*..
gi 27734847   210 YYCQAQN 216
Cdd:pfam13927  72 YTCVASN 78

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847    141 SVTIGNRAVLTCsEHDGSPPSEYSWFKDGISMLTADAKKTRAFMNSSFTidpksgdLIFDPVTAFDSGEYYCQAQNGYGT 220
Cdd:smart00410   5 TVKEGESVTLSC-EASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTST-------LTISNVTPEDSGTYTCAATNSSGS 76

                   .
gi 27734847    221 A 221
Cdd:smart00410  77 A 77

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 27734847 148 AVLTCsEHDGSPPSEYSWFKDGismltadaKKTRAFMNSSFTIDPKSGDLIFDPVTAFDSGEYYCQAQNGYGTAMRSEA 226
Cdd:cd00096   1 VTLTC-SASGNPPPTITWYKNG--------KPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847    32 TAQSDVQVPENESIKLTCTYSGFSS---PRVEWKFVQ--GSTTALVCYNSQITAPYADRVTFSSSG--------ITFSSV 98
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSeasTSVYWYRQPpgKGPTFLIAYYSNGSEEGVKKGRFSGRGdpsngdgsLTIQNL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 27734847    99 TRKDNGEYTCMVSEEGGQNYGEvSIHLTVL 128
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGK-GTRLTVL 109

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second 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 the 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, and 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, 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 Slit-2 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 27734847 139 PSS--VTIGNRAVLTCSEHDGSPPSEYSWFKDGismltadakKTRAFMNSSFTIdPKSGDLIFDPVTAFDSGEYYCQAQN 216
Cdd:cd05724   4 PSDtqVAVGEMAVLECSPPRGHPEPTVSWRKDG---------QPLNLDNERVRI-VDDGNLLIAEARKSDEGTYKCVATN 73

                        90
                ....*....|.
gi 27734847 217 GYGTAmRSEAA 227
Cdd:cd05724  74 MVGER-ESRAA 83

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847    33 AQSDVQVPENESIKLTCTYSGFSS-PRVEWKFvQGSTtalvcYNSQITAPYADRVTFSSSgITFSSVTRKDNGEYTCMVS 111
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSASTGSPgPDVTWSK-EGGT-----LIESLKVKHDNGRTTQSS-LLISNVTKEDAGTYTCVVN 74

                          90
                  ....*....|..
gi 27734847   112 EEGGQNYGEVSI 123
Cdd:pfam00047  75 NPGGSATLSTSL 86

Sixth 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 sixth 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 27734847 143 TIGNRAVLTCSEHDGSPPSEYSWFKDGISMLTADAKKTRafmnssfTIDPKSGDLIFDPVTAFDSGEYYCQAQNGYGTA 221
Cdd:cd20959  15 QVGMRAQLHCGVPGGDLPLNIRWTLDGQPISDDLGITVS-------RLGRRSSILSIDSLEASHAGNYTCHARNSAGSA 86

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 27734847  45 IKLTCTYSGFSSPRVEWKFVQGSTtalvcynsQITAPYADRVTFSSSGITFSSVTRKDNGEYTCMVSEEGG 115
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPL--------PPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63

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 27734847 147 RAVLTCsEHDGSPPSEYSWFKDGismltadakkTRAFMNSSFTIDPKSGDLIF-DPVTAFDSGEYYCQAQNGYGTAMRSE 225
Cdd:cd04967  21 KVALNC-RARANPVPSYRWLMNG----------TEIDLESDYRYSLVDGTLVIsNPSKAKDAGHYQCLATNTVGSVLSRE 89

                .
gi 27734847 226 A 226
Cdd:cd04967  90 A 90

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847   133 KPTISVPSS-VTIGNRAVLTCSEhDGSPPSEYSWFKDGismltadakktrafmnssfTIDPKSGDLIFDPVTAFDSGEYY 211
Cdd:pfam13895   1 KPVLTPSPTvVTEGEPVTLTCSA-PGNPPPSYTWYKDG-------------------SAISSSPNFFTLSVSAEDSGTYT 60

                  ....*...
gi 27734847   212 CQAQNGYG 219
Cdd:pfam13895  61 CVARNGRG 68

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. 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. The Ig-like domain of the Twitchin is a member of the I-set 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. 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847 139 PSSVTI--GNRAVLTCsEHDGSPPSEYSWFKDG--ISMLTADAKKTRAFMNSsftidpksgdLIFDPVTAFDSGEYYCQA 214
Cdd:cd20949   6 AYVTTVkeGQSATILC-EVKGEPQPNVTWHFNGqpISASVADMSKYRILADG----------LLINKVTQDDTGEYTCRA 74

                        90       100
                ....*....|....*....|..
gi 27734847 215 QNGYGTAmrseaahMDAVELNV 236
Cdd:cd20949  75 YQVNSIA-------SDMQERTV 89

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third 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 27734847 141 SVTIGNRAVLTCsEHDGSPPSEYSWFKDGISMltadaKKTRAFMnssftIDPKSgdLIFDPVTAFDSGEYYCQAQNGYGT 220
Cdd:cd05725   8 VVLVDDSAEFQC-EVGGDPVPTVRWRKEDGEL-----PKGRYEI-----LDDHS--LKIRKVTAGDMGSYTCVAENMVGK 74

                .
gi 27734847 221 A 221
Cdd:cd05725  75 I 75

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). 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 27734847  36 DVQVPENESIKLTCTYSGFSSPRVEWKFvqgsttalvcYNSQITAPYADRVTFSSSG---ITFSSVTRKDNGEYTCMVSE 112
Cdd:cd05744   9 DLEVQEGRLCRFDCKVSGLPTPDLFWQL----------NGKPVRPDSAHKMLVRENGrhsLIIEPVTKRDAGIYTCIARN 78

                        90
                ....*....|....*
gi 27734847 113 EGGQNygEVSIHLTV 127
Cdd:cd05744  79 RAGEN--SFNAELVV 91

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 27734847 134 PTISVPSS-----VTIGNRAVLTCSEhDGSPPSEYSWFKDGISMLTADakkTRAFMNSSFTidpksgDLIFDPVTAFDSG 208
Cdd:cd20970   1 PVISTPQPsftvtAREGENATFMCRA-EGSPEPEISWTRNGNLIIEFN---TRYIVRENGT------TLTIRNIRRSDMG 70

                        90
                ....*....|....*....
gi 27734847 209 EYYCQAQNGYGTAMRSEAA 227
Cdd:cd20970  71 IYLCIASNGVPGSVEKRIT 89

First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord. This group belongs to the I-set of IgSF domains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847 147 RAVLTCSEHdGSPPSEYSWFKDGismltadakkTRAFMNSSFTIDPKSGDLIF-DPVTAFDSGEYYCQAQNGYGTAMRSE 225
Cdd:cd05848  21 KVILNCEAR-GNPVPTYRWLRNG----------TEIDTESDYRYSLIDGNLIIsNPSEVKDSGRYQCLATNSIGSILSRE 89

                .
gi 27734847 226 A 226
Cdd:cd05848  90 A 90

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 27734847 139 PSSVTI--GNRAVLTCSEHdGSPPSEYSWFKdGISMLTADAKKtrAFMnssftidpKSGDLIFDPVTAFDSGEYYCQAQN 216
Cdd:cd20968   6 PTNVTIieGLKAVLPCTTM-GNPKPSVSWIK-GDDLIKENNRI--AVL--------ESGSLRIHNVQKEDAGQYRCVAKN 73

                ....*
gi 27734847 217 GYGTA 221
Cdd:cd20968  74 SLGIA 78

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. 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, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -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, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -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 is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847 142 VTIGNRAVLTCSEhDGSPPSEYSWFKDGISMLTADakktrafmnSSFTIDPkSGDLIFDPVTAFDSGEYYCQAQNGYGTA 221
Cdd:cd20952  11 VAVGGTVVLNCQA-TGEPVPTISWLKDGVPLLGKD---------ERITTLE-NGSLQIKGAEKSDTGEYTCVALNLSGEA 79

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 27734847  35 SDVQVPENESIKLTCTYSGFSSPRVEWKfvqgsttalvcYNSQITAPYADRVTFSSSG--ITFSSVTRKDNGEYTCMVSE 112
Cdd:cd20970  10 FTVTAREGENATFMCRAEGSPEPEISWT-----------RNGNLIIEFNTRYIVRENGttLTIRNIRRSDMGIYLCIASN 78

                        90
                ....*....|....*..
gi 27734847 113 EGGqnyGEVSIHLTVLV 129
Cdd:cd20970  79 GVP---GSVEKRITLQV 92

Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also referred to as Z39Ig and V-set and Ig domain-containing 4 (VSIG4)) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. CRIg plays a role in the complement system, an inhibitor of the alternative pathway convertases, and a negative regulator of T cell activation. 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 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847 141 SVTIGNRAVLTCsEHDGSPPSEYSWFKDGismlTADAKKTRAFMNSSftidpksgdLIFDPVTAFDSGEYYCQAQNGYGT 220
Cdd:cd16082   9 TVPQGMRISLQC-QAWGSPPISYVWYKEQ----TNNQEPIKVAALST---------LLFKPAVVADSGSYFCTAKGRVGS 74

                ....*...
gi 27734847 221 AMRSEAAH 228
Cdd:cd16082  75 EQRSDIVK 82

First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. 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. 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-2 is also expressed in retinal amacrine cells in the developing chick retina, corresponding to the period of formation and maturation of AC processes. This group belongs to the I-set of IgSF domains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847 134 PTISVPSSVTIGNRAvltcsehDGSPPSEYSWFKDGISMLTADAKKTRAFmnssftidpkSGDL-IFDPVTAFDSGEYYC 212
Cdd:cd05850  15 PEGSAEEKVTLACRA-------RASPPATYRWKMNGTELKMEPDSRYRLV----------AGNLvISNPVKAKDAGSYQC 77

                        90
                ....*....|....
gi 27734847 213 QAQNGYGTAMRSEA 226
Cdd:cd05850  78 LASNRRGTVVSREA 91

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 27734847 136 ISVPSSVTI---GNRAVLTCSEhDGSPPSEYSWFKDGismltadakktRAFMNSSFTIDPKSGDLIFDPVTAFDSGEYYC 212
Cdd:cd20978   4 IQKPEKNVVvkgGQDVTLPCQV-TGVPQPKITWLHNG-----------KPLQGPMERATVEDGTLTIINVQPEDTGYYGC 71

                ....*...
gi 27734847 213 QAQNGYGT 220
Cdd:cd20978  72 VATNEIGD 79

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27734847 141 SVTIGNRAVLTCSEHDGSPPSEYSWFKDGISMltadAKKTRAfMNSSFTIDPKSGDLIFDPVTAFDSGEYYCQAQNGYG 219
Cdd:cd05895  10 EVAAGSKLVLRCETSSEYPSLRFKWFKNGKEI----NRKNKP-ENIKIQKKKKKSELRINKASLADSGEYMCKVSSKLG 83

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 or CADM3), Necl-2 (also known as CADM1), Necl-3 (also known as CADM2) and Necl-4 (also known as CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 27734847 128 LVPPSKPTISV-PSSVTIGNRAVLTCSEHDGSPPSEYSWFKD 168
Cdd:cd05761   1 LGVPEKPVITGfTSPVVEGDEITLTCTTSGSKPAADIRWFKN 42

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. 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 27734847  33 AQSDVQVPENESIKLTCTYSGFSSPRVEWKFvqgsttalvcYNSQITAPYADRVTFSSSGI---TFSSVTRKDNGEYTCM 109
Cdd:cd20990   6 APGDLTVQEGKLCRMDCKVSGLPTPDLSWQL----------DGKPIRPDSAHKMLVRENGVhslIIEPVTSRDAGIYTCI 75

                        90
                ....*....|....*...
gi 27734847 110 VSEEGGQNygEVSIHLTV 127
Cdd:cd20990  76 ATNRAGQN--SFNLELVV 91

First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1 (PVRL1) or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. In addition nectins heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls), nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734847  45 IKLTCTYSGFSSP----RVEW-KFVQGSTTALVCYNS----QITAPYADRVTF-----SSSGITFSSVTRKDNGEYTCMV 110
Cdd:cd05886  17 VVLHCSFANPLPSvkitQVTWqKSTNGSKQNVAIYNPsmgvSVLPPYRERVTFlnpsfTDGTIRLSRLELEDEGVYICEF 96

                        90
                ....*....|....*...
gi 27734847 111 SEEGGQNYgEVSIHLTVL 128
Cdd:cd05886  97 ATFPTGNR-ESQLNLTVM 113