NCBI Conserved Domain Search

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 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-nonNCAM), 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 the Ig1, Ig2, and Ig3 domains. 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. 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.

Pssm-ID: 409451 Cd Length: 97 Bit Score: 207.97 E-value: 7.78e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   20 LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLSPNQQRISVVWNDDDSSTLTIYNANIDDAGIYKCVVT 99
Cdd:cd05865     1 LQVDIVPSQGEISVGESKFFLCQVAGEAKDKDISWFSPNGEKLTPNQQRISVVRNDDYSSTLTIYNANIDDAGIYKCVVS 80

                          90
                  ....*....|....*..
gi 568958938  100 AEDGTQSEATVNVKIFQ 116
Cdd:cd05865    81 NEDEGESEATVNVKIFQ 97

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(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. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.

Pssm-ID: 143277 [Multi-domain] Cd Length: 97 Bit Score: 196.35 E-value: 1.01e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  307 AKPKITYVENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNISSEEKaswtrpekqeTLDGHMVVRSHARVSSLTLKSI 386
Cdd:cd05869     1 AKPKITYVENQTAMELEEQITLTCEASGDPIPSITWRTSTRNISSEEK----------TLDGHIVVRSHARVSSLTLKYI 70

                          90       100
                  ....*....|....*....|....*..
gi 568958938  387 QYTDAGEYICTASNTIGQDSQSMYLEV 413
Cdd:cd05869    71 QYTDAGEYLCTASNTIGQDSQSMYLEV 97

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.

Pssm-ID: 143207 [Multi-domain] Cd Length: 95 Bit Score: 182.44 E-value: 6.79e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  211 PPTVQARQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEeddEKHIFSDDSSELTIRNVDKNDEAEYVCIA 290
Cdd:cd05730     1 PPTIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGE---EKYSFNEDGSEMTILDVDKLDEAEYTCIA 77

                          90
                  ....*....|....*...
gi 568958938  291 ENKAGEQDASIHLKVFAK 308
Cdd:cd05730    78 ENKAGEQEAEIHLKVFAK 95

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 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-nonNCAM) 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 the Ig1, Ig2, and Ig3 domains. 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. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). 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.

Pssm-ID: 409366 Cd Length: 95 Bit Score: 176.29 E-value: 1.18e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   20 LQVDIVPSQGEISVGESKFFLCQVAGDakDKDISWFSPNGEKLSPNQQRISVVWNDDDSSTLTIYNANIDDAGIYKCVVT 99
Cdd:cd04977     1 LQVKIIPSYAEISVGESKFFLCKVSGD--AKNINWVSPNGEKVLTKHGNLKVVNHGSVLSSLTIYNANINDAGIYKCVAT 78

                          90
                  ....*....|....*..
gi 568958938  100 AEDGTQSEATVNVKIFQ 116
Cdd:cd04977    79 NGKGTESEATVKLDIIQ 95

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth 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. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.

Pssm-ID: 409395 [Multi-domain] Cd Length: 96 Bit Score: 175.79 E-value: 1.62e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  307 AKPKITYVENQTAMELEeQVTLTCEASGDPIPSITWRTSTRNISSEEKaswtrpekqeTLDGHMVVRSHARVSSLTLKSI 386
Cdd:cd05732     1 VQPKITYLENQTAVELE-QITLTCEAEGDPIPEITWRRATRGISFEEG----------DLDGRIVVRGHARVSSLTLKDV 69

                          90       100
                  ....*....|....*....|....*..
gi 568958938  387 QYTDAGEYICTASNTIGQDSQSMYLEV 413
Cdd:cd05732    70 QLTDAGRYDCEASNRIGGDQQSMYLEV 96

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. 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.

Pssm-ID: 409452 Cd Length: 93 Bit Score: 97.04 E-value: 5.24e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   20 LQVDIVPSQGEISVGESKFFLCQVAGDAKDkdISWFSPNGEKLSPNQQriSVVWNDDDSSTLTIYNANIDDAGIYKCVVT 99
Cdd:cd05866     1 LQVSISLSKVELSVGESKFFTCTAIGEPES--IDWYNPQGEKIVSSQR--VVVQKEGVRSRLTIYNANIEDAGIYRCQAT 76

                          90
                  ....*....|....*..
gi 568958938  100 AEDGTQSEATVNVKIFQ 116
Cdd:cd05866    77 DAKGQTQEATVVLEIYQ 93

Immunoglobulin I-set domain;

Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 86.54 E-value: 2.24e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   218 QSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIEneeEDDEKHI-FSDDSSELTIRNVDKNDEAEYVCIAENKAGE 296
Cdd:pfam07679    5 QKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR---SSDRFKVtYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81


                   ....*....
gi 568958938   297 QDASIHLKV 305
Cdd:pfam07679   82 AEASAELTV 90

Immunoglobulin I-set domain;

Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 81.15 E-value: 2.09e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938    21 QVDIVPSQGEISVGESKFFLCQVAGDaKDKDISWFSpNGEKLSPNQqRISVVwNDDDSSTLTIYNANIDDAGIYKCVVTA 100
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTVTGT-PDPEVSWFK-DGQPLRSSD-RFKVT-YEGGTYTLTISNVQPDDSGKYTCVATN 77

                           90
                   ....*....|....
gi 568958938   101 EDGtQSEATVNVKI 114
Cdd:pfam07679   78 SAG-EAEASAELTV 90

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

Pssm-ID: 214653 [Multi-domain] Cd Length: 85 Bit Score: 79.47 E-value: 6.69e-18

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938    222 NATANLGQSVTLVCDADGFPEPTMSWTKDGePIENEEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASI 301
Cdd:smart00410    3 SVTVKEGESVTLSCEASGSPPPEVTWYKQG-GKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81


                    ....
gi 568958938    302 HLKV 305
Cdd:smart00410   82 TLTV 85

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.

Pssm-ID: 409562 [Multi-domain] Cd Length: 92 Bit Score: 78.70 E-value: 1.45e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  212 PTVQARQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIeneEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAE 291
Cdd:cd20970     1 PVISTPQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLI---IEFNTRYIVRENGTTLTIRNIRRSDMGIYLCIAS 77

                          90
                  ....*....|....*
gi 568958938  292 NKA-GEQDASIHLKV 305
Cdd:cd20970    78 NGVpGSVEKRITLQV 92

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.

Pssm-ID: 143278 [Multi-domain] Cd Length: 98 Bit Score: 78.48 E-value: 2.41e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  308 KPKITYVENQTAMElEEQVTLTCEASGDPIPSITWRTSTRNIsseekaswTRPEKQETLDGHMVVRSHARVSSLTLKSIQ 387
Cdd:cd05870     2 QPHIIQLKNETTVE-NGAATLSCKAEGEPIPEITWKRASDGH--------TFSEGDKSPDGRIEVKGQHGESSLHIKDVK 72

                          90       100
                  ....*....|....*....|....*.
gi 568958938  388 YTDAGEYICTASNTIGQDSQSMYLEV 413
Cdd:cd05870    73 LSDSGRYDCEAASRIGGHQKSMYLDI 98

Immunoglobulin domain; This family contains immunoglobulin-like domains.

Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 76.06 E-value: 9.40e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   211 PPTVQARQSivNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENeeEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIA 290
Cdd:pfam13927    1 KPVITVSPS--SVTVREGETVTLTCEATGSPPPTITWYKNGEPISS--GSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76


                   ..
gi 568958938   291 EN 292
Cdd:pfam13927   77 SN 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.

Pssm-ID: 409353 [Multi-domain] Cd Length: 70 Bit Score: 74.29 E-value: 3.10e-16

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568958938  231 VTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIfsDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASI 301
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSE--LGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69

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

Pssm-ID: 409544 [Multi-domain] Cd Length: 87 Bit Score: 69.45 E-value: 2.62e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  217 RQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEddekHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGE 296
Cdd:cd20952     3 LQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDE----RITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78


                  ....*....
gi 568958938  297 QDASIHLKV 305
Cdd:cd20952    79 ATWSAVLDV 87

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

Pssm-ID: 214653 [Multi-domain] Cd Length: 85 Bit Score: 67.53 E-value: 1.02e-13

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938    324 EQVTLTCEASGDPIPSITWRtstrnisseekasWTRPEKQETlDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTIG 403
Cdd:smart00410   10 ESVTLSCEASGSPPPEVTWY-------------KQGGKLLAE-SGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG 75

                            90
                    ....*....|
gi 568958938    404 QDSQSMYLEV 413
Cdd:smart00410   76 SASSGTTLTV 85

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.

Pssm-ID: 409389 [Multi-domain] Cd Length: 87 Bit Score: 67.04 E-value: 1.82e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  217 RQSIVNATANLGQSVTLVCDAD-GFPEPTMSWTKDGEPIEneeeDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAG 295
Cdd:cd05724     1 RVEPSDTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLN----LDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVG 76


                  ....*
gi 568958938  296 EQDAS 300
Cdd:cd05724    77 ERESR 81

Immunoglobulin domain; This family contains immunoglobulin-like domains.

Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 66.43 E-value: 1.87e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   308 KPKITYVENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNISSEEkaswtrpekqetldgHMVVRSHARVSSLTLKSIQ 387
Cdd:pfam13927    1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGS---------------TRSRSLSGSNSTLTISNVT 65

                           90
                   ....*....|...
gi 568958938   388 YTDAGEYICTASN 400
Cdd:pfam13927   66 RSDAGTYTCVASN 78

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

Pssm-ID: 214653 [Multi-domain] Cd Length: 85 Bit Score: 64.06 E-value: 1.55e-12

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938     26 PSQGEISVGESKFFLCQVAGDAKDKdISWFSPNGEKLSPNQqRISVVwNDDDSSTLTIYNANIDDAGIYKCVVTAEDGT- 104
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPE-VTWYKQGGKLLAESG-RFSVS-RSGSTSTLTISNVTPEDSGTYTCAATNSSGSa 77


                    ....*...
gi 568958938    105 QSEATVNV 112
Cdd:smart00410   78 SSGTTLTV 85

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

Pssm-ID: 214653 [Multi-domain] Cd Length: 85 Bit Score: 63.68 E-value: 2.48e-12

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938    422 PVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNySNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQES 500
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78

Immunoglobulin domain; This family contains immunoglobulin-like domains.

Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 62.58 E-value: 4.32e-12

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568958938   422 PVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPsaSYLEVTPDSENDFGNYNCTAVN 494
Cdd:pfam13927    8 PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSN--STLTISNVTRSDAGTYTCVASN 78

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.

Pssm-ID: 409570 [Multi-domain] Cd Length: 88 Bit Score: 63.18 E-value: 4.43e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  222 NATANLGQSVTLVCDADGFPEPTMSWTKDGEPIeneEEDDEKHIFSDDSseLTIRNVDKNDEAEYVCIAENKAGEQDASI 301
Cdd:cd20978    10 NVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL---QGPMERATVEDGT--LTIINVQPEDTGYYGCVATNEIGDIYTET 84


                  ....
gi 568958938  302 HLKV 305
Cdd:cd20978    85 LLHV 88

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.

Pssm-ID: 409390 [Multi-domain] Cd Length: 83 Bit Score: 62.80 E-value: 5.07e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  221 VNATANLGQSVTLVCDADGFPEPTMSWTKDgepiENEEEDDEKHIFSDDSseLTIRNVDKNDEAEYVCIAENKAGEQDAS 300
Cdd:cd05725     5 QNQVVLVDDSAEFQCEVGGDPVPTVRWRKE----DGELPKGRYEILDDHS--LKIRKVTAGDMGSYTCVAENMVGKIEAS 78


                  ....*
gi 568958938  301 IHLKV 305
Cdd:cd05725    79 ATLTV 83

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.

Pssm-ID: 409353 [Multi-domain] Cd Length: 70 Bit Score: 61.19 E-value: 1.40e-11

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  326 VTLTCEASGDPIPSITWrtstrnisseekaswTRPEKQETLDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTIG 403
Cdd:cd00096     1 VTLTCSASGNPPPTITW---------------YKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63

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.

Pssm-ID: 409543 [Multi-domain] Cd Length: 94 Bit Score: 60.90 E-value: 2.93e-11

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIFSDDS-SELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd20951    15 KSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGvHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASVVV 93

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) 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, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), 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 Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 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.

Pssm-ID: 409490 [Multi-domain] Cd Length: 99 Bit Score: 60.64 E-value: 4.07e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENEEED-DEKHIFSDDSSELTIRNV----DKNDEAEYVCIAENKAGE---QDA 299
Cdd:cd07693    15 GDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDpRSHRIVLPSGSLFFLRVVhgrkGRSDEGVYVCVAHNSLGEavsRNA 94


                  ....
gi 568958938  300 SIHL 303
Cdd:cd07693    95 SLEV 98

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.

Pssm-ID: 409550 [Multi-domain] Cd Length: 89 Bit Score: 59.50 E-value: 8.17e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  211 PPTVQarqSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENeeeDDEKHIFSDDSseLTIRNVDKN-DEAEYVCI 289
Cdd:cd20958     1 PPFIR---PMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPL---NHRQRVFPNGT--LVIENVQRSsDEGEYTCT 72

                          90
                  ....*....|....*..
gi 568958938  290 AENKAGEQD-ASIHLKV 305
Cdd:cd20958    73 ARNQQGQSAsRSVFVKV 89

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.

Pssm-ID: 395002 Cd Length: 86 Bit Score: 58.75 E-value: 1.32e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   420 QGPVAVYTWEGNQVNITCEV-FAYPSATISWFRDGQLLPSSNYSNIKIYNTPSASyLEVTPDSENDFGNYNCTAVNRIGQ 498
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSS-LLISNVTKEDAGTYTCVVNNPGGS 79


                   ....*..
gi 568958938   499 ESLEFIL 505
Cdd:pfam00047   80 ATLSTSL 86

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

Pssm-ID: 214653 [Multi-domain] Cd Length: 85 Bit Score: 58.67 E-value: 1.35e-10

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938    124 PTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDvRFIVLSNN---YLQIRGIKKTDEGTYRCE 190
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESG-RFSVSRSGstsTLTISNVTPEDSGTYTCA 69

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.58 E-value: 1.64e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   649 SAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVKYRAKLASEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQG 728
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 568958938   729 KSK 731
Cdd:pfam00041   81 EGP 83

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; 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. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.

Pssm-ID: 409406 [Multi-domain] Cd Length: 82 Bit Score: 57.98 E-value: 1.94e-10

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPI-ENEEEDDEKHifsDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd05748     7 GESLRLDIPIKGRPTPTVTWSKDGQPLkETGRVQIETT---ASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82

Immunoglobulin I-set domain;

Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 58.42 E-value: 2.07e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   309 PKITYV-ENQTAMElEEQVTLTCEASGDPIPSItwrtstrnisseekaSWTRPEKQETLDGHMVVRSHARVSSLTLKSIQ 387
Cdd:pfam07679    1 PKFTQKpKDVEVQE-GESARFTCTVTGTPDPEV---------------SWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQ 64

                           90       100
                   ....*....|....*....|....*.
gi 568958938   388 YTDAGEYICTASNTIGQDSQSMYLEV 413
Cdd:pfam07679   65 PDDSGKYTCVATNSAGEAEASAELTV 90

Immunoglobulin I-set domain;

Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 57.65 E-value: 3.21e-10

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568958938   429 EGNQVNITCEVFAYPSATISWFRDGQLLPSSNYsnIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQESLEFIL 505
Cdd:pfam07679   14 EGESARFTCTVTGTPDPEVSWFKDGQPLRSSDR--FKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

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.

Pssm-ID: 409570 [Multi-domain] Cd Length: 88 Bit Score: 57.02 E-value: 5.13e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  315 ENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNISSEEKaswtrpekqetldghmvvRSHARVSSLTLKSIQYTDAGEY 394
Cdd:cd20978     8 EKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPME------------------RATVEDGTLTIINVQPEDTGYY 69

                          90
                  ....*....|....*....
gi 568958938  395 ICTASNTIGQDSQSMYLEV 413
Cdd:cd20978    70 GCVATNEIGDIYTETLLHV 88

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. 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 telokin Ig domain 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.

Pssm-ID: 409565 [Multi-domain] Cd Length: 88 Bit Score: 56.43 E-value: 8.60e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  217 RQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIEneeedDEKHIFSDDSSE----LTIRNVDKNDEAEYVCIAEN 292
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIV-----ESRRFQIDQDEDglcsLIISDVCGDDSGKYTCKAVN 75

                          90
                  ....*....|...
gi 568958938  293 KAGEQDASIHLKV 305
Cdd:cd20973    76 SLGEATCSAELTV 88

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 56.27 E-value: 9.58e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   512 SSPSIDRVEP-YSSTAQVQFDEPEaTGGVPILKYKAEWKSLGEESWHfKWYDAKEAnmEGIVTIMGLKPETRYSVRLAAL 590
Cdd:pfam00041    1 SAPSNLTVTDvTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPW-NEITVPGT--TTSVTLTGLKPGTEYEVRVQAV 76


                   ....*....
gi 568958938   591 NGKGLGEIS 599
Cdd:pfam00041   77 NGGGEGPPS 85

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.

Pssm-ID: 143222 [Multi-domain] Cd Length: 74 Bit Score: 55.71 E-value: 1.10e-09

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENeeedDEKHIFSdDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd05745     2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSV----DRRHLVL-SSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.

Pssm-ID: 409399 [Multi-domain] Cd Length: 93 Bit Score: 56.50 E-value: 1.16e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  207 IVNVPPTVQARQsivnatanLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDdeKHIFSDDSSELTIRNVDKNDEAEY 286
Cdd:cd05736     2 VIRVYPEFQAKE--------PGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSK--QLTLIANGSELHISNVRYEDTGAY 71


                  ....*....
gi 568958938  287 VCIAENKAG 295
Cdd:cd05736    72 TCIAKNEGG 80

Immunoglobulin domain; This family contains immunoglobulin-like domains.

Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 55.65 E-value: 1.25e-09

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938   124 PTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRDVI-LKKDVRFIVLSNNYLQIRGIKKTDEGTYRCE 190
Cdd:pfam13927    8 PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISsGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 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.

Pssm-ID: 409405 [Multi-domain] Cd Length: 91 Bit Score: 55.96 E-value: 1.40e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIEneeEDDEKHIFSDDSS--ELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd05744    15 GRLCRFDCKVSGLPTPDLFWQLNGKPVR---PDSAHKMLVRENGrhSLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91

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.

Pssm-ID: 409353 [Multi-domain] Cd Length: 70 Bit Score: 55.41 E-value: 1.41e-09

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568958938  433 VNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPsaSYLEVTPDSENDFGNYNCTAVNRIG 497
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGN--GTLTISNVTLEDSGTYTCVASNSAG 63

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 55.97 E-value: 1.64e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  509 DTPSSPSIDRVEpySSTAQVQFDEPEATGGvPILKYKAEWKSLGEESWHFKWYDAKEANMegiVTIMGLKPETRYSVRLA 588
Cdd:cd00063     2 SPPTNLRVTDVT--STSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETS---YTLTGLKPGTEYEFRVR 75

                          90
                  ....*....|....*...
gi 568958938  589 ALNGKGLGEISAATEFKT 606
Cdd:cd00063    76 AVNGGGESPPSESVTVTT 93

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.

Pssm-ID: 409442 Cd Length: 92 Bit Score: 55.64 E-value: 1.96e-09

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  227 LGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHifsdDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd05856    18 VGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKK----KKWTLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92

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.

Pssm-ID: 143205 [Multi-domain] Cd Length: 85 Bit Score: 55.30 E-value: 2.17e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  218 QSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEddekhiFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQ 297
Cdd:cd05728     4 KVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENR------IEVEAGDLRITKLSLSDSGMYQCVAENKHGTI 77


                  ....*...
gi 568958938  298 DASIHLKV 305
Cdd:cd05728    78 YASAELAV 85

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.

Pssm-ID: 409367 [Multi-domain] Cd Length: 89 Bit Score: 55.53 E-value: 2.28e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  222 NATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKhifSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASI 301
Cdd:cd04978     8 SLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRR---TVDGRTLIFSNLQPNDTAVYQCNASNVHGYLLANA 84


                  ....*
gi 568958938  302 HLKVF 306
Cdd:cd04978    85 FLHVL 89

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.49 E-value: 3.25e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  905 APPATTVPDS-NSVPAGQATPSKGVTASSSSPASAPKVAPLVDLSDTPTSAPSASNLSSTVLANQGAVLSPSTPASAGET 983
Cdd:PHA03247 2617 LPPDTHAPDPpPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLT 2696

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  984 SKA-PPASKASPAPTP---------TPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKNPPeAATAPASP 1053
Cdd:PHA03247 2697 SLAdPPPPPPTPEPAPhalvsatplPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPP-APAPPAAP 2775

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1054 KSKAATTNPSQGEDlKMDEGNFKTPDIDLAKDVFAALGSPAPA-TGASGQASELAPSTadSAVPPAPAKTeKGPVETkSE 1132
Cdd:PHA03247 2776 AAGPPRRLTRPAVA-SLSESRESLPSPWDPADPPAAVLAPAAAlPPAASPAGPLPPPT--SAQPTAPPPP-PGPPPP-SL 2850


                  ....*...
gi 568958938 1133 PPESEAKP 1140
Cdd:PHA03247 2851 PLGGSVAP 2858

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.

Pssm-ID: 409393 [Multi-domain] Cd Length: 95 Bit Score: 54.53 E-value: 4.65e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENEE-----EDDEKHiFSddsseLTIRNVDKNDEAEYVCIAENKAGEQDASIH 302
Cdd:cd05729    19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHriggtKVEEKG-WS-----LIIERAIPRDKGKYTCIVENEYGSINHTYD 92


                  ...
gi 568958938  303 LKV 305
Cdd:cd05729    93 VDV 95

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. 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 Lingo-1 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.

Pssm-ID: 409561 Cd Length: 92 Bit Score: 54.70 E-value: 4.87e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  224 TANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIFSDDSseLTIRNVDKNDEAEYVCIAENKAGEQDASIHL 303
Cdd:cd20969    13 FVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGT--LEVRYAQVQDNGTYLCIAANAGGNDSMPAHL 90


                  ..
gi 568958938  304 KV 305
Cdd:cd20969    91 HV 92

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(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. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.

Pssm-ID: 143277 [Multi-domain] Cd Length: 97 Bit Score: 54.22 E-value: 6.77e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  222 NATA-NLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIFSDDS---SELTIRNVDKNDEAEYVCIAENKAGEQ 297
Cdd:cd05869    10 NQTAmELEEQITLTCEASGDPIPSITWRTSTRNISSEEKTLDGHIVVRSHarvSSLTLKYIQYTDAGEYLCTASNTIGQD 89


                  ....*...
gi 568958938  298 DASIHLKV 305
Cdd:cd05869    90 SQSMYLEV 97

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third 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. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.

Pssm-ID: 409549 [Multi-domain] Cd Length: 88 Bit Score: 54.07 E-value: 6.95e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  208 VNVPPTVQarqsivnaTANLGQSVTLVCDADGFPEPTMSWTKDGEPIENeeeDDEKHIFSDDSseLTIRNVDKNDEAEYV 287
Cdd:cd20957     4 ATIDPPVQ--------TVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGH---SSRVQILSEDV--LVIPSVKREDKGMYQ 70

                          90
                  ....*....|....*...
gi 568958938  288 CIAENKAGEQDASIHLKV 305
Cdd:cd20957    71 CFVRNDGDSAQATAELKL 88

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.

Pssm-ID: 409541 [Multi-domain] Cd Length: 89 Bit Score: 53.87 E-value: 7.06e-09

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  220 IVNA---TANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIFSDDSseLTIRNVDKNDEAEYVCIAENKAG 295
Cdd:cd20949     3 TENAyvtTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADG--LLINKVTQDDTGEYTCRAYQVNS 79

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

Pssm-ID: 409544 [Multi-domain] Cd Length: 87 Bit Score: 54.04 E-value: 7.07e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  326 VTLTCEASGDPIPSITWRTSTRNISseekaswTRPEKQETLDGhmvvrsharvSSLTLKSIQYTDAGEYICTASNTIGQD 405
Cdd:cd20952    17 VVLNCQATGEPVPTISWLKDGVPLL-------GKDERITTLEN----------GSLQIKGAEKSDTGEYTCVALNLSGEA 79


                  ....*...
gi 568958938  406 SQSMYLEV 413
Cdd:cd20952    80 TWSAVLDV 87

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 60.34 E-value: 8.63e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  906 PPATTVPDSNSVPAGQATPSKGVTASSSSPASAPKVAPLVDLSDTPTSAPSASNLSstvlanqgavlsPSTPASAGETSK 985
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARP------------ARPPTTAGPPAP 2769

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  986 APPASKASPAP--TPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKNPPEAATAPASPKSKAATTNPS 1063
Cdd:PHA03247 2770 APPAAPAAGPPrrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS 2849

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1064 qgedlkMDEGNFKTPDIDLAKDVFAALGSPAPATGASGQASELA-----PSTADSAVPPAPAKTEKGPvetksEPPESEA 1138
Cdd:PHA03247 2850 ------LPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLArpavsRSTESFALPPDQPERPPQP-----QAPPPPQ 2918

                         250
                  ....*....|....*..
gi 568958938 1139 KPAPTEVKTVPNDATQT 1155
Cdd:PHA03247 2919 PQPQPPPPPQPQPPPPP 2935

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 59.50 E-value: 1.16e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  920 GQATPSKGVTASSSSPASAPKVAPLVDLSDTPTSAPSAsnlsstvlanQGAVLSPSTPASAGETSKAPPASKASPAPTPT 999
Cdd:PRK12323  370 GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPA----------AAPAAAAAARAVAAAPARRSPAPEALAAARQA 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1000 PAGAASPLAAVAAPATDAPqakqeAPSTKGPDPEPTQPGTVKNPPEAATAPAsPKSKAATTNPSQGEDLKMDEGNFKTPD 1079
Cdd:PRK12323  440 SARGPGGAPAPAPAPAAAP-----AAAARPAAAGPRPVAAAAAAAPARAAPA-AAPAPADDDPPPWEELPPEFASPAPAQ 513

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568958938 1080 IDLAKDVFAALGSPAPATG-ASGQASELAPSTADSAVPPAPAKTEkgPVETKSEPPESEAKPAPT 1143
Cdd:PRK12323  514 PDAAPAGWVAESIPDPATAdPDDAFETLAPAPAAAPAPRAAAATE--PVVAPRPPRASASGLPDM 576

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.

Pssm-ID: 409353 [Multi-domain] Cd Length: 70 Bit Score: 52.72 E-value: 1.20e-08

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568958938  135 AVIVCDVVSSLPPTIIWKHKGRDVIL-KKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEIN 200
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPsSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67

IL-beta-binding protein; Provisional

Pssm-ID: 165149 [Multi-domain] Cd Length: 326 Bit Score: 58.10 E-value: 1.28e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   51 DISWfspngEKLSPNQQRISVVwndDDSSTLTIYNANIDDAGIYKCVVTAEDG-----------TQSEATVNVKIFqklm 119
Cdd:PHA02785   62 DILW-----EKRGADNDRIIPI---DNGSNMLILNPTQSDSGIYICITKNETYcdmmslnltivSVSESNIDLISY---- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  120 fknaptPQEFKEGEDAVIVCD-----VVSSLPPTIIWKHKGRdvilKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRIL 194
Cdd:PHA02785  130 ------PQIVNERSTGEMVCPninafIASNVNADIIWSGHRR----LRNKRLKQRTPGIITIEDVRKNDAGYYTCVLKYI 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  195 ARGEInfKDIQVIVN-------VPPTVQARQSIVNAtanLGQSVTLVC---------DADGFpeptmsWTKDGEPIENEE 258
Cdd:PHA02785  200 YGDKT--YNVTRIVKlevrdriIPPTMQLPEGVVTS---IGSNLTIACrvslrppttDADVF------WISNGMYYEEDD 268

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 568958938  259 EDDE------KHIFSDD-----SSELTIRNVDKNDEAEYVCIA 290
Cdd:PHA02785  269 EDGDgrisvaNKIYTTDkrrviTSRLNINPVKEEDATTFTCMA 311

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third 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, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.

Pssm-ID: 409394 [Multi-domain] Cd Length: 83 Bit Score: 52.80 E-value: 1.39e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENEeeddeKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd05731    10 GGVLLLECIAEGLPTPDIRWIKLGGELPKG-----RTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82

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.

Pssm-ID: 409562 [Multi-domain] Cd Length: 92 Bit Score: 52.90 E-value: 1.91e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  315 ENQTAMElEEQVTLTCEASGDPIPSITWRtstRNISSeekaswtrpekQETLDGHMVVRSHARvsSLTLKSIQYTDAGEY 394
Cdd:cd20970    10 FTVTARE-GENATFMCRAEGSPEPEISWT---RNGNL-----------IIEFNTRYIVRENGT--TLTIRNIRRSDMGIY 72

                          90       100
                  ....*....|....*....|
gi 568958938  395 ICTASNTI-GQDSQSMYLEV 413
Cdd:cd20970    73 LCIASNGVpGSVEKRITLQV 92

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth 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.

Pssm-ID: 409358 [Multi-domain] Cd Length: 89 Bit Score: 52.08 E-value: 3.44e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENEeeddeKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd04969    17 GGDVIIECKPKASPKPTISWSKGTELLTNS-----SRICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89

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

Pssm-ID: 409544 [Multi-domain] Cd Length: 87 Bit Score: 52.11 E-value: 3.47e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568958938  119 MFKNAPTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRdVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRC 189
Cdd:cd20952     1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGV-PLLGKDERITTLENGSLQIKGAEKSDTGEYTC 70

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.

Pssm-ID: 409568 [Multi-domain] Cd Length: 90 Bit Score: 51.87 E-value: 3.55e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  222 NATANLGQSVTLVCDADGFPEPTMSWTKDGEPIEneeEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASI 301
Cdd:cd20976    10 DLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQ---YAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSA 86


                  ....
gi 568958938  302 HLKV 305
Cdd:cd20976    87 WVTV 90

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.

Pssm-ID: 143224 [Multi-domain] Cd Length: 92 Bit Score: 51.97 E-value: 4.18e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  224 TANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEeeddEKHIFSDDS--SELTIRNVDKNDEAEYVCIAENKAGEQDASI 301
Cdd:cd05747    14 TVSEGESARFSCDVDGEPAPTVTWMREGQIIVSS----QRHQITSTEykSTFEISKVQMSDEGNYTVVVENSEGKQEAQF 89


                  ..
gi 568958938  302 HL 303
Cdd:cd05747    90 TL 91

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.

Pssm-ID: 409390 [Multi-domain] Cd Length: 83 Bit Score: 51.63 E-value: 4.28e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  316 NQTAMeLEEQVTLTCEASGDPIPSITWRTStrnisseekaswtrpekqetlDGHMVV-RSHARV-SSLTLKSIQYTDAGE 393
Cdd:cd05725     6 NQVVL-VDDSAEFQCEVGGDPVPTVRWRKE---------------------DGELPKgRYEILDdHSLKIRKVTAGDMGS 63

                          90       100
                  ....*....|....*....|
gi 568958938  394 YICTASNTIGQDSQSMYLEV 413
Cdd:cd05725    64 YTCVAENMVGKIEASATLTV 83

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.

Pssm-ID: 409443 [Multi-domain] Cd Length: 95 Bit Score: 51.78 E-value: 5.28e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDeKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd05857    19 ANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIG-GYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDV 95

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third 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, 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 the chicken neuron-glia cell adhesion molecule, Ng-CAM.

Pssm-ID: 409460 [Multi-domain] Cd Length: 83 Bit Score: 51.07 E-value: 5.63e-08

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENeeeddEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAG 295
Cdd:cd05876    10 GQSLVLECIAEGLPTPTVKWLRPSGPLPP-----DRVKYQNHNKTLQLLNVGESDDGEYVCLAENSLG 72

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains.

Pssm-ID: 409400 [Multi-domain] Cd Length: 91 Bit Score: 51.55 E-value: 5.71e-08

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568958938  229 QSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEkhIFSDDSSELTIRNVDKNDEAEYVCIAENKAG 295
Cdd:cd05738    15 RTATMLCAASGNPDPEISWFKDFLPVDTATSNGR--IKQLRSGALQIENSEESDQGKYECVATNSAG 79

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.

Pssm-ID: 409408 [Multi-domain] Cd Length: 92 Bit Score: 51.36 E-value: 5.73e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568958938  429 EGNQVNITCEVFA-YPSATISWFRDGQLLPSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQES 500
Cdd:cd05750    13 EGSKLVLKCEATSeNPSPRYRWFKDGKELNRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDT 85

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.

Pssm-ID: 395002 Cd Length: 86 Bit Score: 51.04 E-value: 7.32e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   218 QSIVNATANLGQSVTLVCDADGF-PEPTMSWTKDGEpiENEEEDDEKHIFSDDS-SELTIRNVDKNDEAEYVCIAENKAG 295
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSASTGsPGPDVTWSKEGG--TLIESLKVKHDNGRTTqSSLLISNVTKEDAGTYTCVVNNPGG 78


                   ....*.
gi 568958938   296 EQDASI 301
Cdd:pfam00047   79 SATLST 84

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 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, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.

Pssm-ID: 409453 [Multi-domain] Cd Length: 89 Bit Score: 51.05 E-value: 8.51e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIfsdDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd05867    14 GETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHV---SSGALILTDVQPSDTAVYQCEARNRHGNLLANAHVHV 88

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.

Pssm-ID: 143223 Cd Length: 69 Bit Score: 50.26 E-value: 8.54e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568958938  231 VTLVCDADGFPEPTMSWTKDGEPIeneEEDDEKHIFSDdsSELTIRNVDKNDEAEYVCIAENKAGEQDASIHL 303
Cdd:cd05746     1 VQIPCSAQGDPEPTITWNKDGVQV---TESGKFHISPE--GYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (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.

Pssm-ID: 409421 [Multi-domain] Cd Length: 88 Bit Score: 50.55 E-value: 1.02e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  228 GQSVTLVCDADGFPEPTMSW-TKDGEPIENeeeDDEKHIFSDDSSELTIRNVdkNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd05764    15 GQRATLRCKARGDPEPAIHWiSPEGKLISN---SSRTLVYDNGTLDILITTV--KDTGAFTCIASNPAGEATARVELHI 88

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.

Pssm-ID: 409396 [Multi-domain] Cd Length: 94 Bit Score: 50.87 E-value: 1.14e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  212 PTVQArQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIenEEEDDEKHIFSDDSSELTIRNVDKNDEA---EYVC 288
Cdd:cd05733     1 PTITE-QSPKDYIVDPRDNITIKCEAKGNPQPTFRWTKDGKFF--DPAKDPRVSMRRRSGTLVIDNHNGGPEDyqgEYQC 77


                  ....*..
gi 568958938  289 IAENKAG 295
Cdd:cd05733    78 YASNELG 84

Fourth 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 fourth 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.

Pssm-ID: 409548 [Multi-domain] Cd Length: 96 Bit Score: 50.64 E-value: 1.31e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  324 EQVTLTCEASGDPIPSITWRTSTRNISSEEKaswTRPEKQETLDGHMVvrSHARVSSLTLKsiqytDAGEYICTASNTIG 403
Cdd:cd20956    17 PSVSLKCVASGNPLPQITWTLDGFPIPESPR---FRVGDYVTSDGDVV--SYVNISSVRVE-----DGGEYTCTATNDVG 86


                  ....*
gi 568958938  404 QDSQS 408
Cdd:cd20956    87 SVSHS 91

First 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 first 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.

Pssm-ID: 409387 Cd Length: 97 Bit Score: 50.55 E-value: 1.32e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  221 VNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIeNEEEDDEKHIFSDDSseLTIRNV-----DKNDEAEYVCIAENK 293
Cdd:cd05722     9 SDIVAMRGGPVVLNCSAESDPPPKIEWKKDGVLL-NLVSDERRQQLPNGS--LLITSVvhskhNKPDEGFYQCVAQNE 83

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.

Pssm-ID: 409353 [Multi-domain] Cd Length: 70 Bit Score: 49.64 E-value: 1.41e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938   39 FLCQVAGDAKDKdISWFSPNGEKLSPNQQRISvvwNDDDSSTLTIYNANIDDAGIYKCVVTAEDGTQSEATV 110
Cdd:cd00096     3 LTCSASGNPPPT-ITWYKNGKPLPPSSRDSRR---SELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 55.56 E-value: 1.95e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  844 TEPNETTPLTEPELPADTTAtvedmlPSVTTVTTNSDTITETFATAQNSPTSETTTLTssiAPPATTVPDS--NSVPAGQ 921
Cdd:PHA03307   64 RFEPPTGPPPGPGTEAPANE------SRSTPTWSLSTLAPASPAREGSPTPPGPSSPD---PPPPTPPPASppPSPAPDL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  922 ATPSKGVTASSSSPASAPKVAPLVDlSDTPTSAPSASNLSSTVLANQGAVLSPSTPASAGETSKAPPASKA--------- 992
Cdd:PHA03307  135 SEMLRPVGSPGPPPAASPPAAGASP-AAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPrpprrsspi 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  993 -----SPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPtQPGTVKNPPEAATAPASPKSKAATTNPSQGEd 1067
Cdd:PHA03307  214 sasasSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRP-APITLPTRIWEASGWNGPSSRPGPASSSSSP- 291

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568958938 1068 lkmdegNFKTPDIDLAKDVFAALGSPAPATGA-SGQASELAPSTADSAVPPAPAKTEKGPVETKSEPPESEAKPAPT 1143
Cdd:PHA03307  292 ------RERSPSPSPSSPGSGPAPSSPRASSSsSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADP 362

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.

Pssm-ID: 143223 Cd Length: 69 Bit Score: 49.10 E-value: 2.30e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  326 VTLTCEASGDPIPSITWRTSTRNISSEEKASWTRpekqetlDGHmvvrsharvssLTLKSIQYTDAGEYICTASNTIGQD 405
Cdd:cd05746     1 VQIPCSAQGDPEPTITWNKDGVQVTESGKFHISP-------EGY-----------LAIRDVGVADQGRYECVARNTIGYA 62


                  ....*.
gi 568958938  406 SQSMYL 411
Cdd:cd05746    63 SVSMVL 68

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk 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. 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 titin Z1z2 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.

Pssm-ID: 409566 [Multi-domain] Cd Length: 93 Bit Score: 49.66 E-value: 2.85e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd20974    15 GSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAELLV 92

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.42 E-value: 2.94e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  662 NSIKVNLIKQDDGGSPIRHYLVKYRAKLASEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFV-FRT 739
Cdd:cd00063    15 TSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVtVTT 93

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third 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. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.

Pssm-ID: 409549 [Multi-domain] Cd Length: 88 Bit Score: 49.07 E-value: 3.45e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   20 LQVDIVPSQGEISVGESKFFLCQVAGDAKdKDISWFSpNGEKLsPNQQRISVVwnddDSSTLTIYNANIDDAGIYKCVVt 99
Cdd:cd20957     2 LSATIDPPVQTVDFGRTAVFNCSVTGNPI-HTVLWMK-DGKPL-GHSSRVQIL----SEDVLVIPSVKREDKGMYQCFV- 73

                          90
                  ....*....|....*
gi 568958938  100 AEDGTQSEATVNVKI 114
Cdd:cd20957    74 RNDGDSAQATAELKL 88

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 48.76 E-value: 3.73e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938    511 PSSPSIDRVEPYSST-AQVQFDEPEATGGV-PILKYKAEWKSLGEEswhfkWYDAKEANMEGIVTIMGLKPETRYSVRLA 588
Cdd:smart00060    1 PSPPSNLRVTDVTSTsVTLSWEPPPDDGITgYIVGYRVEYREEGSE-----WKEVNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ....*...
gi 568958938    589 ALNGKGLG 596
Cdd:smart00060   76 AVNGAGEG 83

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.

Pssm-ID: 143224 [Multi-domain] Cd Length: 92 Bit Score: 49.28 E-value: 3.79e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  419 LQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSnySNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQ 498
Cdd:cd05747     7 LTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSS--QRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGK 84


                  ....*..
gi 568958938  499 ESLEFIL 505
Cdd:cd05747    85 QEAQFTL 91

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The members here are composed of the fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM 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. NrCAM is primarily expressed in the nervous system.

Pssm-ID: 409454 Cd Length: 89 Bit Score: 48.82 E-value: 4.06e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIfsdDSSELTIRNVDKNDEAEYVCIAENKAG 295
Cdd:cd05868    14 GEDGTLICRANGNPKPSISWLTNGVPIEIAPTDPSRKV---DGDTIIFSKVQERSSAVYQCNASNEYG 78

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.

Pssm-ID: 409357 [Multi-domain] Cd Length: 88 Bit Score: 49.08 E-value: 4.07e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  324 EQVTLTCEASGDPIPSITWRtstrnisseekaswtrpekqeTLDGHMVVRSHARVSSLTLK--SIQYTDAGEYICTASNT 401
Cdd:cd04968    17 QTVTLECFALGNPVPQIKWR---------------------KVDGSPSSQWEITTSEPVLEipNVQFEDEGTYECEAENS 75


                  ....
gi 568958938  402 IGQD 405
Cdd:cd04968    76 RGKD 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.

Pssm-ID: 409357 [Multi-domain] Cd Length: 88 Bit Score: 48.70 E-value: 4.32e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  225 ANLGQSVTLVCDADGFPEPTMSWTK-DGEPIeneeeddEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAG 295
Cdd:cd04968    13 ALKGQTVTLECFALGNPVPQIKWRKvDGSPS-------SQWEITTSEPVLEIPNVQFEDEGTYECEAENSRG 77

Seventh 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 seventh 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.

Pssm-ID: 409546 [Multi-domain] Cd Length: 96 Bit Score: 49.23 E-value: 4.52e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  221 VNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEED----DEKHIFSDDSseLTIRNVDKNDEAEYVCIAENKAG 295
Cdd:cd20954     9 VDANVAAGQDVMLHCQADGFPTPTVTWKKATGSTPGEYKDllydPNVRILPNGT--LVFGHVQKENEGHYLCEAKNGIG 85

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.

Pssm-ID: 409397 [Multi-domain] Cd Length: 97 Bit Score: 49.03 E-value: 4.55e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  326 VTLTCEASGDPIPSITWRTStrnisseeKASwTRPEKQETldghmvVRSHARV-----SSLTLKSIQYTDAGEYICTASN 400
Cdd:cd05734    19 VVLNCSADGYPPPTIVWKHS--------KGS-GVPQFQHI------VPLNGRIqllsnGSLLIKHVLEEDSGYYLCKVSN 83

                          90
                  ....*....|....
gi 568958938  401 TIGQD-SQSMYLEV 413
Cdd:cd05734    84 DVGADiSKSMYLTV 97

DNA polymerase III subunit gamma/tau;

Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 54.09 E-value: 5.15e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  950 TPTSAPSASNLSSTVLANQGAVLSPSTPASAGETSKAPPASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKG 1029
Cdd:PRK07003  388 AAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERD 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1030 PDPePTQPGTVKNPpeAATAPASPKSKAATTNPSQGEDLKMDEGNFKTPDIDLAKDVFAALGSPAPATGASGQASELAPS 1109
Cdd:PRK07003  468 AQP-PADSGSASAP--ASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAA 544

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568958938 1110 TADSA--------------------VPPAPAKTEKGPVETKSEPPESEAKPAPT 1143
Cdd:PRK07003  545 RAGGAaaaldvlrnagmrvssdrgaRAAAAAKPAAAPAAAPKPAAPRVAVQVPT 598

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here are composed of the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.

Pssm-ID: 409417 Cd Length: 95 Bit Score: 48.77 E-value: 6.14e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568958938  231 VTLVCDADGFPEPTMSWTKDGEPIeneEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGE 296
Cdd:cd05760    19 VTLRCHIDGHPRPTYQWFRDGTPL---SDGQGNYSVSSKERTLTLRSAGPDDSGLYYCCAHNAFGS 81

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.

Pssm-ID: 409570 [Multi-domain] Cd Length: 88 Bit Score: 48.54 E-value: 6.20e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   32 SVGESKFFLCQVAGDAKDKdISWFSpNGEKLSPNQQRISVvwnddDSSTLTIYNANIDDAGIYKCVVTAEDGT-QSEATV 110
Cdd:cd20978    14 KGGQDVTLPCQVTGVPQPK-ITWLH-NGKPLQGPMERATV-----EDGTLTIINVQPEDTGYYGCVATNEIGDiYTETLL 86


                  ..
gi 568958938  111 NV 112
Cdd:cd20978    87 HV 88

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.

Pssm-ID: 395002 Cd Length: 86 Bit Score: 48.35 E-value: 6.34e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   322 LEEQVTLTCEAS-GDPIPSITW-RTSTRNISSEEKaswtrpekqetldGHMVVRShaRVSSLTLKSIQYTDAGEYICTAS 399
Cdd:pfam00047   10 EGDSATLTCSAStGSPGPDVTWsKEGGTLIESLKV-------------KHDNGRT--TQSSLLISNVTKEDAGTYTCVVN 74

                           90
                   ....*....|
gi 568958938   400 NTIGQDSQSM 409
Cdd:pfam00047   75 NPGGSATLST 84

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.

Pssm-ID: 409551 Cd Length: 94 Bit Score: 48.26 E-value: 8.69e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  225 ANLGQSVTLVCD-ADGFPEPTMSWTKDGEPIeNEEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHL 303
Cdd:cd20959    14 AQVGMRAQLHCGvPGGDLPLNIRWTLDGQPI-SDDLGITVSRLGRRSSILSIDSLEASHAGNYTCHARNSAGSASYTAPL 92


                  ..
gi 568958938  304 KV 305
Cdd:cd20959    93 TV 94

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. 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.

Pssm-ID: 143259 Cd Length: 88 Bit Score: 47.71 E-value: 1.06e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  322 LEEQVTLTCEASGDPIPSITWRTSTRNISSEEKASwtrpekqetldghmvvrsharVSSLTLK--SIQYTDAGEYICTAS 399
Cdd:cd05851    15 KGQNVTLECFALGNPVPVIRWRKILEPMPATAEIS---------------------MSGAVLKifNIQPEDEGTYECEAE 73

                          90
                  ....*....|....*
gi 568958938  400 NTIGQDSQSMYLEVQ 414
Cdd:cd05851    74 NIKGKDKHQARVYVQ 88

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth 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.

Pssm-ID: 409359 Cd Length: 102 Bit Score: 48.32 E-value: 1.09e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  222 NATANLGQSVTLVCDA--DGFPEPTMSWTKDGEPIENEEEDD--EKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQ 297
Cdd:cd04970    11 NADITVGENATLQCHAshDPTLDLTFTWSFNGVPIDLEKIEGhyRRRYGKDSNGDLEIVNAQLKHAGRYTCTAQTVVDSD 90

                          90
                  ....*....|..
gi 568958938  298 DASIHLKVFAKP 309
Cdd:cd04970    91 SASATLVVRGPP 102

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.02 E-value: 1.27e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  846 PNETTPltEPELPADTTATVEDMLPSVTTVTTNSDTITETfATAQNSPTSETTTLTSSIAPPATTVPDSNSVPAGQATPS 925
Cdd:PHA03247 2703 PPPPTP--EPAPHALVSATPLPPGPAAARQASPALPAAPA-PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP 2779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  926 KGVTAsssspasapkVAPLVDLSDTPTSAPSASNLSstvlanqgAVLSPSTPASAGETSKAPPASKASPAPTPTPAGaas 1005
Cdd:PHA03247 2780 PRRLT----------RPAVASLSESRESLPSPWDPA--------DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA--- 2838

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1006 plaavaapatdapqakqeAPSTKGPDPEPTqpgtvknPPEAATAPASPKSKAATTNPSQGEDlkmdegnfKTPDIDLAKD 1085
Cdd:PHA03247 2839 ------------------PPPPPGPPPPSL-------PLGGSVAPGGDVRRRPPSRSPAAKP--------AAPARPPVRR 2885

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938 1086 VFAALGSPAPATGASGQASELAPSTADSAVPPAPAKTEKGPVETKSEPPESEAKPAPTEVKTVPNDATQ 1154
Cdd:PHA03247 2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE 2954

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.

Pssm-ID: 409550 [Multi-domain] Cd Length: 89 Bit Score: 47.56 E-value: 1.27e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  309 PKITYVENQTameleeqVTLTCEASGDPIPSITWrtstrnisseEKASWTRPE--KQetldghmvvrshaRVSS---LTL 383
Cdd:cd20958     8 GNLTAVAGQT-------LRLHCPVAGYPISSITW----------EKDGRRLPLnhRQ-------------RVFPngtLVI 57

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568958938  384 KSIQ-YTDAGEYICTASNTIGQ-DSQSMYLEV 413
Cdd:cd20958    58 ENVQrSSDEGEYTCTARNQQGQsASRSVFVKV 89

Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes.

Pssm-ID: 143250 Cd Length: 109 Bit Score: 48.00 E-value: 1.44e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  230 SVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIFSD---DSSELTIRNVDK-NDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd05773    25 DANLVCQAQGVPRVQFRWAKNGVPLDLGNPRYEETTEHTgtvHTSILTIINVSAaLDYALFTCTAHNSLGEDSLDIQLVS 104


                  ....
gi 568958938  306 FAKP 309
Cdd:cd05773   105 TSRP 108

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. 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.

Pssm-ID: 143259 Cd Length: 88 Bit Score: 47.32 E-value: 1.44e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568958938  225 ANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEddekhiFSDDSSELTIRNVDKNDEAEYVCIAENKAG 295
Cdd:cd05851    13 ALKGQNVTLECFALGNPVPVIRWRKILEPMPATAE------ISMSGAVLKIFNIQPEDEGTYECEAENIKG 77

Immunoglobulin domain; This family contains immunoglobulin-like domains.

Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 47.18 E-value: 1.48e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938    21 QVDIVPSQGEISVGESKFFLCQVAGDAKDKdISWFSPNGEKLSpnqQRISVVWNDDDSSTLTIYNANIDDAGIYKCVVT 99
Cdd:pfam13927    3 VITVSPSSVTVREGETVTLTCEATGSPPPT-ITWYKNGEPISS---GSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

Seventh 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 seventh 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.

Pssm-ID: 409546 [Multi-domain] Cd Length: 96 Bit Score: 47.31 E-value: 1.86e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  326 VTLTCEASGDPIPSITWRtstrnisseeKASWTRPEKQETLDGHMVVRSHARvSSLTLKSIQYTDAGEYICTASNTIGQD 405
Cdd:cd20954    19 VMLHCQADGFPTPTVTWK----------KATGSTPGEYKDLLYDPNVRILPN-GTLVFGHVQKENEGHYLCEAKNGIGSG 87


                  ....*....
gi 568958938  406 -SQSMYLEV 413
Cdd:cd20954    88 lSKVIFLKV 96

Immunoglobulin I-set domain;

Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 46.87 E-value: 2.06e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938   124 PTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRDviLKKDVRFIVLSNNY---LQIRGIKKTDEGTYRC 189
Cdd:pfam07679    7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQP--LRSSDRFKVTYEGGtytLTISNVQPDDSGKYTC 73

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.

Pssm-ID: 409399 [Multi-domain] Cd Length: 93 Bit Score: 47.26 E-value: 2.16e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  313 YVENQtAMELEEQVTLTCEASGDPIPSITWRTSTRNISseekaswTRPEKQETLDGHMvvrsharvSSLTLKSIQYTDAG 392
Cdd:cd05736     6 YPEFQ-AKEPGVEASLRCHAEGIPLPRVQWLKNGMDIN-------PKLSKQLTLIANG--------SELHISNVRYEDTG 69

                          90       100
                  ....*....|....*....|....
gi 568958938  393 EYICTASNTIG--QDSQSMYLEVQ 414
Cdd:cd05736    70 AYTCIAKNEGGvdEDISSLFVEDS 93

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.

Pssm-ID: 409408 [Multi-domain] Cd Length: 92 Bit Score: 46.74 E-value: 3.13e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  222 NATANLGQSVTLVCDADG-FPEPTMSWTKDGEPIENEEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDAS 300
Cdd:cd05750     8 SQTVQEGSKLVLKCEATSeNPSPRYRWFKDGKELNRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVT 87


                  ....*
gi 568958938  301 IHLKV 305
Cdd:cd05750    88 GNVTV 92

DNA polymerase III subunit gamma/tau;

Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 51.39 E-value: 3.17e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  905 APPATTVPDSNSVPAGQATPSKGVTASSSSPASAPKVAPLVDLSDTPTSAPSASNLSSTVLANQGAVLSPSTPASAGETS 984
Cdd:PRK07003  382 APGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADS 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  985 KAPPAS---KASPAPTPTPAGAAsplaAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKNPPEAAtAPASPKSKAATTN 1061
Cdd:PRK07003  462 RCDERDaqpPADSGSASAPASDA----PPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPA-AAAPPAPEARPPT 536

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1062 PSQGEDLKMDEGnfktpdIDLAKDVFAALG----------SPAPATGASGQASELAPSTADSAVP-PAPAKTEKGPVETK 1130
Cdd:PRK07003  537 PAAAAPAARAGG------AAAALDVLRNAGmrvssdrgarAAAAAKPAAAPAAAPKPAAPRVAVQvPTPRARAATGDAPP 610

                         250       260
                  ....*....|....*....|....*
gi 568958938 1131 SE----PPESEAKPAPTEVKTVPND 1151
Cdd:PRK07003  611 NGaaraEQAAESRGAPPPWEDIPPD 635

Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.

Pssm-ID: 409438 Cd Length: 89 Bit Score: 46.53 E-value: 3.27e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENeeeDDEKHIFSDDSseLTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd05852    17 GGRVIIECKPKAAPKPKFSWSKGTELLVN---NSRISIWDDGS--LEILNITKLDEGSYTCFAENNRGKANSTGVLSV 89

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.

Pssm-ID: 409582 Cd Length: 91 Bit Score: 46.63 E-value: 3.30e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  218 QSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIeneeEDDEKH---IFSDDSSELTIRNVDKNDEAEYVCIAENKA 294
Cdd:cd20990     5 QAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPI----RPDSAHkmlVRENGVHSLIIEPVTSRDAGIYTCIATNRA 80

                          90
                  ....*....|.
gi 568958938  295 GEQDASIHLKV 305
Cdd:cd20990    81 GQNSFNLELVV 91

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. 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. 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 structures of the titin-A168169 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.

Pssm-ID: 409563 Cd Length: 93 Bit Score: 46.31 E-value: 4.01e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  218 QSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIeneeEDDEKHIFSD---DSSELTIRNVD-KNDEAEYVCIAENK 293
Cdd:cd20971     6 EELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEI----IADGLKYRIQefkGGYHQLIIASVtDDDATVYQVRATNQ 81


                  ..
gi 568958938  294 AG 295
Cdd:cd20971    82 GG 83

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.

Pssm-ID: 409541 [Multi-domain] Cd Length: 89 Bit Score: 46.17 E-value: 4.40e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  120 FKNAPTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRDVI--LKKDVRFIVLSNNyLQIRGIKKTDEGTYRC 189
Cdd:cd20949     2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISasVADMSKYRILADG-LLINKVTQDDTGEYTC 72

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.94 E-value: 4.93e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  810 EEGKAAFSKDESKEPIVEVRTEEERTPNHDGgKHTEPNETTPLTE-----PELPADTTAT-VEDMLPSVTTVTTNSDTIT 883
Cdd:PHA03307   74 GPGTEAPANESRSTPTWSLSTLAPASPAREG-SPTPPGPSSPDPPpptppPASPPPSPAPdLSEMLRPVGSPGPPPAASP 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  884 EtFATAQNSPTSETTTLTSSIAPPATTVPDS-NSVPAGQATPSKGVTASSSSPASAPKVAPLVDLSDTPTSAPSASNLSS 962
Cdd:PHA03307  153 P-AAGASPAAVASDAASSRQAALPLSSPEETaRAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADD 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  963 TVLANQGAVLSPSTPASAGETSKAPpasKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTvkn 1042
Cdd:PHA03307  232 AGASSSDSSSSESSGCGWGPENECP---LPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGS--- 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1043 PPEAATAPASPKSKaattnpSQGEDlkmdegnfktpDIDLAKDVFAALGSPAPATGASGQASELAPSTADSAVPPAPAKT 1122
Cdd:PHA03307  306 GPAPSSPRASSSSS------SSRES-----------SSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKR 368

                         330       340       350
                  ....*....|....*....|....*....|..
gi 568958938 1123 EKGPVETKSEPPESEAKPAPTEVKTVPNDATQ 1154
Cdd:PHA03307  369 PRPSRAPSSPAASAGRPTRRRARAAVAGRARR 400

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk 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. 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 titin Z1z2 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.

Pssm-ID: 409564 [Multi-domain] Cd Length: 91 Bit Score: 46.04 E-value: 5.49e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  429 EGNQVNITCEVFAYPSATISWFRDGQLLPSSnySNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQES 500
Cdd:cd20972    15 EGSKVRLECRVTGNPTPVVRWFCEGKELQNS--PDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDT 84

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.

Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 50.69 E-value: 5.92e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   872 VTTVTTNSDTITET--FATAQNSPTSETTTLTSSIAPPATT--VPDSNSVPAGQATPSKgvTASSSSPASAPKVAPLVDL 947
Cdd:pfam05109  405 ITRTATNATTTTHKviFSKAPESTTTSPTLNTTGFAAPNTTtgLPSSTHVPTNLTAPAS--TGPTVSTADVTSPTPAGTT 482

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   948 SDTPTSAPSASNLSSTVLANQGAVLSPSTPAsageTSKAPPASKASPA-PTPTPAGAASP---LAAVAAPATDAPQAKQE 1023
Cdd:pfam05109  483 SGASPVTPSPSPRDNGTESKAPDMTSPTSAV----TTPTPNATSPTPAvTTPTPNATSPTlgkTSPTSAVTTPTPNATSP 558

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  1024 APSTKGPDPEPTQPGTVKNPPEAATAPASPKSKAAT---TNPSQGEDLKMDEGNFKTPDI-DLAKDVFAALGSPAPATGA 1099
Cdd:pfam05109  559 TPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTvgeTSPQANTTNHTLGGTSSTPVVtSPPKNATSAVTTGQHNITS 638

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  1100 SGQAS----------ELAPSTADSAVPPAPAKTEKGPVE----TKSEPPE------SEAKPAP-----TEVKTVPNDATQ 1154
Cdd:pfam05109  639 SSTSSmslrpssiseTLSPSTSDNSTSHMPLLTSAHPTGgeniTQVTPAStsthhvSTSSPAPrpgttSQASGPGNSSTS 718


                   ....*
gi 568958938  1155 TKENE 1159
Cdd:pfam05109  719 TKPGE 723

hypothetical E4 protein; Provisional

Pssm-ID: 177646 [Multi-domain] Cd Length: 230 Bit Score: 48.97 E-value: 6.03e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  974 PSTPASAGETSKAPPASKASPAPTPTPAgaasplaavaAPATDAPQAKQEAPSTKGPDPEPTQPGTvkNPPEAATAPASP 1053
Cdd:PHA03418   34 PLLPAPHHPNPQEDPDKNPSPPPDPPLT----------PRPPAQPNGHNKPPVTKQPGGEGTEEDH--QAPLAADADDDP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1054 K----SKAATTNPSQGEdlkmdeGNFKTPDIDLAKDvfAALGSPAPATGASGQASELAPSTADSAVPPaPAKTEkGPVET 1129
Cdd:PHA03418  102 RpgkrSKADEHGPAPGR------AALAPFKLDLDQD--PLHGDPDPPPGATGGQGEEPPEGGEESQPP-LGEGE-GAVEG 171

                         170
                  ....*....|...
gi 568958938 1130 KSEPPESEAKPAP 1142
Cdd:PHA03418  172 HPPPLPPAPEPKP 184

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.

Pssm-ID: 395002 Cd Length: 86 Bit Score: 45.65 E-value: 6.07e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938    24 IVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKlsPNQQRISVVWNDDDSSTLTIYNANIDDAGIYKCVVTAEDG 103
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTL--IESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGG 78

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.55 E-value: 6.52e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  941 VAPLVDLSDTPTSAPSASNLSSTVLANQGAVLSPSTPASAGETSKAPPASKASPAPTPTPAGAASPLAAVAAPATDAPQA 1020
Cdd:PHA03307   25 PATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1021 KQEAPSTKGPDpeptqpgtvknPPEAATAPASPkskAATTNPSQGEDLKMDEGnfkTPDIDLAKDVFAALGSPAPATGA- 1099
Cdd:PHA03307  105 SPTPPGPSSPD-----------PPPPTPPPASP---PPSPAPDLSEMLRPVGS---PGPPPAASPPAAGASPAAVASDAa 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568958938 1100 -SGQASELAPSTADSAVPPAPAKTEKGPvetksEPPESEAKPAP 1142
Cdd:PHA03307  168 sSRQAALPLSSPEETARAPSSPPAEPPP-----STPPAAASPRP 206

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. 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 Lingo-1 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.

Pssm-ID: 409561 Cd Length: 92 Bit Score: 45.07 E-value: 1.05e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  326 VTLTCEASGDPIPSITWRTSTRNisseekaswtrPEKQETLDGHMVVRSharvSSLTLKSIQYTDAGEYICTASNTIGQD 405
Cdd:cd20969    20 VQFVCRADGDPPPAILWLSPRKH-----------LVSAKSNGRLTVFPD----GTLEVRYAQVQDNGTYLCIAANAGGND 84


                  ....*...
gi 568958938  406 SQSMYLEV 413
Cdd:cd20969    85 SMPAHLHV 92

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth 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.

Pssm-ID: 409358 [Multi-domain] Cd Length: 89 Bit Score: 45.14 E-value: 1.06e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  326 VTLTCEASGDPIPSITWRTSTRNISSEEKASWTRpekqetlDGhmvvrsharvsSLTLKSIQYTDAGEYICTASNTIGQD 405
Cdd:cd04969    20 VIIECKPKASPKPTISWSKGTELLTNSSRICILP-------DG-----------SLKIKNVTKSDEGKYTCFAVNFFGKA 81


                  ....*...
gi 568958938  406 SQSMYLEV 413
Cdd:cd04969    82 NSTGSLSV 89

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.

Pssm-ID: 409442 Cd Length: 92 Bit Score: 44.85 E-value: 1.08e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  296 EQDASIHLKVFAKPkityvenqtameLEEQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTRPEkqetldghmvvrsh 375
Cdd:cd05856     4 TQPAKMRRRVIARP------------VGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKK-------------- 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568958938  376 arvSSLTLKSIQYTDAGEYICTASNTIGQDSQSMYLEV 413
Cdd:cd05856    58 ---WTLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92

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.

Pssm-ID: 409570 [Multi-domain] Cd Length: 88 Bit Score: 45.08 E-value: 1.09e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568958938  129 FKEGEDAVIVCDVVSSLPPTIIWKHKGRDviLKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEG 191
Cdd:cd20978    13 VKGGQDVTLPCQVTGVPQPKITWLHNGKP--LQGPMERATVEDGTLTIINVQPEDTGYYGCVA 73

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.

Pssm-ID: 143205 [Multi-domain] Cd Length: 85 Bit Score: 44.90 E-value: 1.17e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   25 VPSQGEISVGESKFFLCQVAGDAKDKdISWFSpNGEKLsPNQQRISVvwnddDSSTLTIYNANIDDAGIYKCVVTAEDGT 104
Cdd:cd05728     5 VISDTEADIGSSLRWECKASGNPRPA-YRWLK-NGQPL-ASENRIEV-----EAGDLRITKLSLSDSGMYQCVAENKHGT 76

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.

Pssm-ID: 409543 [Multi-domain] Cd Length: 94 Bit Score: 45.10 E-value: 1.18e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568958938  428 WEGNQVNITCEVFAYPSATISWFRDGQLL-PSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQES 500
Cdd:cd20951    13 WEKSDAKLRVEVQGKPDPEVKWYKNGVPIdPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEAS 86

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.

Pssm-ID: 143299 Cd Length: 92 Bit Score: 44.90 E-value: 1.31e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  422 PVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPSASyLEVTPDSENDFGNYNCTAVNRIGQESL 501
Cdd:cd05891     8 PDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYAS-LTIKGVTSEDSGKYSINVKNKYGGETV 86


                  ....
gi 568958938  502 EFIL 505
Cdd:cd05891    87 DVTV 90

Fourth 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 fourth 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.

Pssm-ID: 409548 [Multi-domain] Cd Length: 96 Bit Score: 44.86 E-value: 1.32e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPI-ENEEEDDEKHIFSDDS--SELTIRNVDKNDEAEYVCIAENKAGE 296
Cdd:cd20956    16 GPSVSLKCVASGNPLPQITWTLDGFPIpESPRFRVGDYVTSDGDvvSYVNISSVRVEDGGEYTCTATNDVGS 87

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 49.49 E-value: 1.35e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  977 PASAGETSKAPPASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQeAPSTKGPDPEPTQPGTVKNP--PEAATAPAS-- 1052
Cdd:PRK12323  376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAA-APARRSPAPEALAAARQASArgPGGAPAPAPap 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1053 PKSKAATTNPSqgedlkmdegnfktpdidlakdvfAALGSPAPATGASGQASElAPSTADSAVPPAPAKTEKGPVETKSE 1132
Cdd:PRK12323  455 AAAPAAAARPA------------------------AAGPRPVAAAAAAAPARA-APAAAPAPADDDPPPWEELPPEFASP 509

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568958938 1133 PP-ESEAKPAPTEVKTVPNDATQTKENESKA 1162
Cdd:PRK12323  510 APaQPDAAPAGWVAESIPDPATADPDDAFET 540

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

Pssm-ID: 464026 [Multi-domain] Cd Length: 79 Bit Score: 44.31 E-value: 1.49e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938   228 GQSVTLVCDADGFPEPTMSWTKDGEPIEneeeddekhifsdDSSELTIRNVDKNDEAEYVCIAEN-KAGEQDASIHLKV 305
Cdd:pfam13895   14 GEPVTLTCSAPGNPPPSYTWYKDGSAIS-------------SSPNFFTLSVSAEDSGTYTCVARNgRGGKVSNPVELTV 79

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.

Pssm-ID: 409405 [Multi-domain] Cd Length: 91 Bit Score: 44.41 E-value: 1.56e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  429 EGNQVNITCEVFAYPSATISWFRDGQLLpsSNYSNIKIYNTPSASY-LEVTPDSENDFGNYNCTAVNRIGQESLEFILV 506
Cdd:cd05744    14 EGRLCRFDCKVSGLPTPDLFWQLNGKPV--RPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRAGENSFNAELV 90

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.

Pssm-ID: 409476 Cd Length: 93 Bit Score: 44.60 E-value: 1.59e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  417 PKLQGPVAVYTWEGNQVNITCE-VFAYPSATISWFRDGQLLPSSNY-SNIKIYNTPSASYLEVTPDSENDFGNYNCTAVN 494
Cdd:cd05895     1 PKLKEMKSQEVAAGSKLVLRCEtSSEYPSLRFKWFKNGKEINRKNKpENIKIQKKKKKSELRINKASLADSGEYMCKVSS 80


                  ....*.
gi 568958938  495 RIGQES 500
Cdd:cd05895    81 KLGNDS 86

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 49.10 E-value: 1.61e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  955 PSASNLSSTVLANQGAVLSPSTPASAGETSKAPPASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPdpeP 1034
Cdd:PRK12323  365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQAS---A 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1035 TQPGTVKNP---PEAATAP------ASPKSKAATTNPSQGEDLKMDEGNFKTPDIDLAKDVFAALGSPAPATGASGQASE 1105
Cdd:PRK12323  442 RGPGGAPAPapaPAAAPAAaarpaaAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGW 521

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568958938 1106 LAPSTADSAV-PPAPAKTEKGPVETKSEPPESEAKPAPTEVKTVP 1149
Cdd:PRK12323  522 VAESIPDPATaDPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPP 566

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 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-nonNCAM) 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 the Ig1, Ig2, and Ig3 domains. 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. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). 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.

Pssm-ID: 409366 Cd Length: 95 Bit Score: 44.55 E-value: 1.66e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  214 VQARQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENK 293
Cdd:cd04977     1 LQVKIIPSYAEISVGESKFFLCKVSGDAKNINWVSPNGEKVLTKHGNLKVVNHGSVLSSLTIYNANINDAGIYKCVATNG 80

                          90
                  ....*....|....
gi 568958938  294 AG-EQDASIHLKVF 306
Cdd:cd04977    81 KGtESEATVKLDII 94

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.

Pssm-ID: 409560 [Multi-domain] Cd Length: 88 Bit Score: 44.54 E-value: 1.69e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568958938  221 VNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIEneeedDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAG 295
Cdd:cd20968     7 TNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIK-----ENNRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLG 76

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 49.21 E-value: 1.80e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  970 AVLSPStPASAGETSKAPPASKASPAPTPTPAGAAsplaavaapatdaPQAKQEAPSTKGPDPEPTQPGTVKNPPEAatA 1049
Cdd:PRK07764  586 AVVGPA-PGAAGGEGPPAPASSGPPEEAARPAAPA-------------APAAPAAPAPAGAAAAPAEASAAPAPGVA--A 649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1050 PASPKSKAATTNPSQGEDLKMDEGNFKTPDIDLAKDvfAALGSPAPATGASGQASELAPSTADSAVPPAPAKTEKGPVET 1129
Cdd:PRK07764  650 PEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAP--APAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQG 727

                         170
                  ....*....|...
gi 568958938 1130 KSEPPESEAKPAP 1142
Cdd:PRK07764  728 ASAPSPAADDPVP 740

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.

Pssm-ID: 409391 [Multi-domain] Cd Length: 98 Bit Score: 44.56 E-value: 1.82e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  222 NATANLGQSVTLVCDADGFPEPTMSWTKDGEP---IENEEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQD 298
Cdd:cd05726     8 DQVVALGRTVTFQCETKGNPQPAIFWQKEGSQnllFPYQPPQPSSRFSVSPTGDLTITNVQRSDVGYYICQALNVAGSIL 87


                  ....*..
gi 568958938  299 ASIHLKV 305
Cdd:cd05726    88 AKAQLEV 94

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third 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. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.

Pssm-ID: 409549 [Multi-domain] Cd Length: 88 Bit Score: 44.44 E-value: 1.82e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568958938  124 PTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRDviLKKDVRFIVLSNNYLQIRGIKKTDEGTYRC 189
Cdd:cd20957     8 PPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKP--LGHSSRVQILSEDVLVIPSVKREDKGMYQC 71

DNA polymerase III subunits gamma and tau; Provisional

Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 48.94 E-value: 1.96e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  977 PASAGETskAPPASKASPAPTPTPAgaasplaavaapatdaPQAKQEAPSTKGPDPEPTQPGTVKNPPEAATAPASPKSK 1056
Cdd:PRK14951  366 PAAAAEA--AAPAEKKTPARPEAAA----------------PAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVA 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1057 AattnpsqgedlkmdegnfktpdidlakdvfAALGSPAPATGASGQASELAPstadSAVPPAPAKTEKGPVETKSEPPES 1136
Cdd:PRK14951  428 A------------------------------PAAAAPAAAPAAAPAAVALAP----APPAQAAPETVAIPVRVAPEPAVA 473


                  ....*..
gi 568958938 1137 EAKPAPT 1143
Cdd:PRK14951  474 SAAPAPA 480

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.

Pssm-ID: 409550 [Multi-domain] Cd Length: 89 Bit Score: 44.10 E-value: 2.02e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  430 GNQVNITCEVFAYPSATISWFRDGQLLPSSnySNIKIYNTPSASYLEVTPDSenDFGNYNCTAVNRIGQ 498
Cdd:cd20958    15 GQTLRLHCPVAGYPISSITWEKDGRRLPLN--HRQRVFPNGTLVIENVQRSS--DEGEYTCTARNQQGQ 79

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.

Pssm-ID: 143222 [Multi-domain] Cd Length: 74 Bit Score: 43.77 E-value: 2.21e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  324 EQVTLTCEASGDPIPSItwrtstrnisseekaSWTRPEKQETLDghmvvRSHARVSSLTLK--SIQYTDAGEYICTASNT 401
Cdd:cd05745     3 QTVDFLCEAQGYPQPVI---------------AWTKGGSQLSVD-----RRHLVLSSGTLRisRVALHDQGQYECQAVNI 62

                          90
                  ....*....|..
gi 568958938  402 IGQDSQSMYLEV 413
Cdd:cd05745    63 VGSQRTVAQLTV 74

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 48.55 E-value: 2.22e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  947 LSDTPTSAPSASnlSSTVLANQgAVLSPSTPASAGET-SKAP---PASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQ 1022
Cdd:PRK08691  356 LAFAPLAAASCD--ANAVIENT-ELQSPSAQTAEKETaAKKPqprPEAETAQTPVQTASAAAMPSEGKTAGPVSNQENND 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1023 EAPSTKGPDPEPTQPGTVKNP-------PEAATAPASPKSK-AATTNPSQGEDLKMDEGN--FKTPDIDLAKDVFAALGS 1092
Cdd:PRK08691  433 VPPWEDAPDEAQTAAGTAQTSaksiqtaSEAETPPENQVSKnKAADNETDAPLSEVPSENpiQATPNDEAVETETFAHEA 512

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938 1093 PAPATGASGQASELAPSTADSAVPP------APAKTEKGPVETKSEPPESEAKPAPTE 1144
Cdd:PRK08691  513 PAEPFYGYGFPDNDCPPEDGAEIPPpdwehaAPADTAGGGADEEAEAGGIGGNNTPSA 570

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.

Pssm-ID: 409388 Cd Length: 84 Bit Score: 43.72 E-value: 2.26e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  221 VNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIeneeeddekhIFSD-----DSSELTIRNVDKNDEAEYVCIAENKAG 295
Cdd:cd05723     5 SNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVV----------IPSDyfkivKEHNLQVLGLVKSDEGFYQCIAENDVG 74

                          90
                  ....*....|
gi 568958938  296 EQDASIHLKV 305
Cdd:cd05723    75 NAQASAQLII 84

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.

Pssm-ID: 409582 Cd Length: 91 Bit Score: 43.94 E-value: 2.28e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  419 LQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQ-LLPSSNYSNIKIYNtpSASYLEVTPDSENDFGNYNCTAVNRIG 497
Cdd:cd20990     4 LQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKpIRPDSAHKMLVREN--GVHSLIIEPVTSRDAGIYTCIATNRAG 81


                  ....*....
gi 568958938  498 QESLEFILV 506
Cdd:cd20990    82 QNSFNLELV 90

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

Pssm-ID: 464026 [Multi-domain] Cd Length: 79 Bit Score: 43.54 E-value: 2.79e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   416 APKLQGPVAVYtWEGNQVNITCEVFAYPSATISWFRDGQLLPSSnysnikiyntPSASYLEVTPDsenDFGNYNCTAVNR 495
Cdd:pfam13895    1 KPVLTPSPTVV-TEGEPVTLTCSAPGNPPPSYTWYKDGSAISSS----------PNFFTLSVSAE---DSGTYTCVARNG 66


                   ....*
gi 568958938   496 IGQES 500
Cdd:pfam13895   67 RGGKV 71

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.

Pssm-ID: 143220 Cd Length: 78 Bit Score: 43.25 E-value: 2.83e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  324 EQVTLTCEASGDPIPSITWRTstrnisseekaSWtrpekqetldGHmvVRSHARVSS--------LTLKSIQYTDAGEYI 395
Cdd:cd05743     2 ETVEFTCVATGVPTPIINWRL-----------NW----------GH--VPDSARVSItseggygtLTIRDVKESDQGAYT 58


                  ....*...
gi 568958938  396 CTASNTIG 403
Cdd:cd05743    59 CEAINTRG 66

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.

Pssm-ID: 409568 [Multi-domain] Cd Length: 90 Bit Score: 43.78 E-value: 3.02e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  309 PKITYVENQtameleeQVTLTCEASGDPIPSITWRTSTRNISSEEKASwtrpekqetldghmvvRSHARVSSLTLKSIQY 388
Cdd:cd20976     9 KDLEAVEGQ-------DFVAQCSARGKPVPRITWIRNAQPLQYAADRS----------------TCEAGVGELHIQDVLP 65

                          90       100
                  ....*....|....*....|....*
gi 568958938  389 TDAGEYICTASNTIGQDSQSMYLEV 413
Cdd:cd20976    66 EDHGTYTCLAKNAAGQVSCSAWVTV 90

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.

Pssm-ID: 409562 [Multi-domain] Cd Length: 92 Bit Score: 43.65 E-value: 3.02e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568958938  429 EGNQVNITCEVFAYPSATISWFRDGQLL--PSSNYsnikIYNTpSASYLEVTPDSENDFGNYNCTAVNRIGQE 499
Cdd:cd20970    16 EGENATFMCRAEGSPEPEISWTRNGNLIieFNTRY----IVRE-NGTTLTIRNIRRSDMGIYLCIASNGVPGS 83

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.

Pssm-ID: 409408 [Multi-domain] Cd Length: 92 Bit Score: 43.65 E-value: 3.11e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  309 PKITYVENQTAMELEEQVtLTCEASGD-PIPSITWRTSTRNISSEekaswtRPEkqetldgHMVVRSHARVSSLTLKSIQ 387
Cdd:cd05750     1 PKLKEMKSQTVQEGSKLV-LKCEATSEnPSPRYRWFKDGKELNRK------RPK-------NIKIRNKKKNSELQINKAK 66

                          90       100
                  ....*....|....*....|....*.
gi 568958938  388 YTDAGEYICTASNTIGQDSQSMYLEV 413
Cdd:cd05750    67 LEDSGEYTCVVENILGKDTVTGNVTV 92

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.

Pssm-ID: 409560 [Multi-domain] Cd Length: 88 Bit Score: 43.77 E-value: 3.16e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  121 KNAPTPQEFKEGEDAVIVCDVVSSLPPTIIWKhKGRDVIlKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGR 192
Cdd:cd20968     3 TRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWI-KGDDLI-KENNRIAVLESGSLRIHNVQKEDAGQYRCVAK 72

Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, classical Ig-like domains resembling the antibody constant domain. Members of the IgC1 family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, while the IgC domain is involved in oligomerization and molecular interactions. 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 strands by G, F, C, and C'.

Pssm-ID: 409354 Cd Length: 95 Bit Score: 43.60 E-value: 3.17e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568958938  422 PVAVYTWEGNQVNITCEV--FAYPSATISWFRDGQLLPSSNYSNIKIYNTPSA----SYLEVTPDSENDFGNYNCTA 492
Cdd:cd00098     6 PPSPEEKGGGKVTLVCLVsgFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGTysvtSSLTVPPSDWDEGATYTCVV 82

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.

Pssm-ID: 409420 [Multi-domain] Cd Length: 91 Bit Score: 43.76 E-value: 3.19e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  224 TANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIFSDDsSELTIRNVDKNDEAEYVCIAENKAGEQDASIHL 303
Cdd:cd05763    10 TIRAGSTARLECAATGHPTPQIAWQKDGGTDFPAARERRMHVMPED-DVFFIVDVKIEDTGVYSCTAQNSAGSISANATL 88


                  ..
gi 568958938  304 KV 305
Cdd:cd05763    89 TV 90

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.

Pssm-ID: 409367 [Multi-domain] Cd Length: 89 Bit Score: 43.59 E-value: 3.20e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  305 VFAKPKITYVENQTAmeleeqvTLTCEASGDPIPSITWRTSTRNIsseEKASwtrPEKQETLDGhmvvrsharvSSLTLK 384
Cdd:cd04978     3 IIEPPSLVLSPGETG-------ELICEAEGNPQPTITWRLNGVPI---EPAP---EDMRRTVDG----------RTLIFS 59

                          90
                  ....*....|....*....
gi 568958938  385 SIQYTDAGEYICTASNTIG 403
Cdd:cd04978    60 NLQPNDTAVYQCNASNVHG 78

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 43.39 E-value: 3.35e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938   224 TANLGQSVTLVCDADGF-PEP-TMSWTKDGEPIENEEEdDEKHIFSDD-----SSELTIRNVDKNDEAEYVCIAENKA 294
Cdd:pfam07654    8 PEELGKPNTLTCLVTGFyPPDiTVTWLKNGQEVTEGVK-TTPPSPNSDwtyqlSSYLTVTPSDWESGDEYTCRVEHEG 84

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.06 E-value: 3.82e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  954 APSASNLSSTVLANQGAVLSPSTPASAGETSKAPPASKASPAPTPTPAGaasplaavaAPATDAPQAKQEAPSTKGPDPE 1033
Cdd:PRK07764  364 LPSASDDERGLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAP---------AAAAPAAAAAPAPAAAPQPAPA 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1034 P---TQPGTVKNPPEAATAPASPKSKAATTNPSqgedlkmdegnfktpdidlakdvfAALGSPAPATGASGQASELAPST 1110
Cdd:PRK07764  435 PapaPAPPSPAGNAPAGGAPSPPPAAAPSAQPA------------------------PAPAAAPEPTAAPAPAPPAAPAP 490

                         170
                  ....*....|....*..
gi 568958938 1111 ADSAVPPAPAKTEKGPV 1127
Cdd:PRK07764  491 AAAPAAPAAPAAPAGAD 507

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.

Pssm-ID: 409541 [Multi-domain] Cd Length: 89 Bit Score: 43.09 E-value: 4.55e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  312 TYVENQTAMELEE--QVTLTCEASGDPIPSITWRTStrnisseekaswTRPEKQETLDGHmvvRSHARVSSLTLKSIQYT 389
Cdd:cd20949     1 TFTENAYVTTVKEgqSATILCEVKGEPQPNVTWHFN------------GQPISASVADMS---KYRILADGLLINKVTQD 65

                          90       100
                  ....*....|....*....|....
gi 568958938  390 DAGEYICTASNTIGQDSQSMYLEV 413
Cdd:cd20949    66 DTGEYTCRAYQVNSIASDMQERTV 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.

Pssm-ID: 409435 Cd Length: 96 Bit Score: 43.39 E-value: 5.02e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  323 EEQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTrpekqeTLDGHMVVRSHARVssltlksiqyTDAGEYICTASNTI 402
Cdd:cd05848    19 EKKVILNCEARGNPVPTYRWLRNGTEIDTESDYRYS------LIDGNLIISNPSEV----------KDSGRYQCLATNSI 82


                  .
gi 568958938  403 G 403
Cdd:cd05848    83 G 83

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.

Pssm-ID: 409356 [Multi-domain] Cd Length: 96 Bit Score: 43.39 E-value: 5.30e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  322 LEEQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTrpekqeTLDGHMVVRSharvssltlkSIQYTDAGEYICTASNT 401
Cdd:cd04967    18 DEKKVALNCRARANPVPSYRWLMNGTEIDLESDYRYS------LVDGTLVISN----------PSKAKDAGHYQCLATNT 81


                  ..
gi 568958938  402 IG 403
Cdd:cd04967    82 VG 83

First 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.

Pssm-ID: 409474 Cd Length: 92 Bit Score: 43.16 E-value: 5.33e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568958938  428 WEGNQVNITCEVFAYPSATISWFRDG-QLLPSSNYSNIKiYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQES 500
Cdd:cd05893    13 FEGMPVTFTCRVAGNPKPKIYWFKDGkQISPKSDHYTIQ-RDLDGTCSLHTTASTLDDDGNYTIMAANPQGRIS 85

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 47.45 E-value: 5.63e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   952 TSAPSASNLSSTVLANQGAVLSPSTPASAGETSKAPP-ASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPStkgP 1030
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSvPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPS---P 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  1031 DPePTQPGTVKNPPEAATAPASPKSKAATTNPSQGEDLKMDEGNFKTP----DIDLAKDVFAALGSPAPATGASGQASEL 1106
Cdd:pfam03154  246 HP-PLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPvppqPFPLTPQSSQSQVPPGPSPAAPGQSQQR 324

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 568958938  1107 A--PSTADSAVPPAPAKTEKGPVETKSEPpesEAKPAPT 1143
Cdd:pfam03154  325 IhtPPSQSQLQSQQPPREQPLPPAPLSMP---HIKPPPT 360

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.

Pssm-ID: 409582 Cd Length: 91 Bit Score: 42.78 E-value: 5.83e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  328 LTCEASGDPIPSITWRTSTRNIsseekaswtRPEKQETldghMVVRSHArVSSLTLKSIQYTDAGEYICTASNTIGQDSQ 407
Cdd:cd20990    20 MDCKVSGLPTPDLSWQLDGKPI---------RPDSAHK----MLVRENG-VHSLIIEPVTSRDAGIYTCIATNRAGQNSF 85


                  ....*.
gi 568958938  408 SMYLEV 413
Cdd:cd20990    86 NLELVV 91

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.

Pssm-ID: 409542 Cd Length: 97 Bit Score: 43.07 E-value: 5.91e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  223 ATANLGQSVTLVC-DADGFPEPTMSWTKDGEPIENEEE-----DDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAG 295
Cdd:cd20950     7 SSATIGNRAVLTCsEPDGSPPSEYTWFKDGVVMPTNPKstrafSNSSYSLDPTTGELVFDPLSASDTGEYSCEARNGYG 85

CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin constant domain (IgC) of mu heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.

Pssm-ID: 409513 Cd Length: 99 Bit Score: 43.15 E-value: 6.01e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  205 QVIVNVPPtvqaRQSIVNatanlGQSVTLVCDADGF-PEP-TMSWTKDGEPIE------NEEEDDEKHIFSDDSSELTIR 276
Cdd:cd16093     3 TVSLHAPS----REEFLG-----NRTATFVCLATGFsPKTiSFKWLRNGKEVTsstgavVEEPKEDGKTLYSATSFLTIT 73

                          90       100
                  ....*....|....*....|....*
gi 568958938  277 NVDKNDEAEYVCIAENKAGEQDASI 301
Cdd:cd16093    74 ESEWKSQTEFTCEFKHKGEIVEKNA 98

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.

Pssm-ID: 409422 [Multi-domain] Cd Length: 95 Bit Score: 42.92 E-value: 6.32e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568958938   26 PSQGEISVGESKFFLCQVAGDAKdKDISW--FSPNGEKL--SPNQQRISVVWNDddSSTLTIYNANIDDAGIYKC 96
Cdd:cd05765     7 PTHQTVKVGETASFHCDVTGRPQ-PEITWekQVPGKENLimRPNHVRGNVVVTN--IGQLVIYNAQPQDAGLYTC 78

First immunoglobulin (Ig)-like domain of Tyro3 receptor tyrosine kinase (RTK), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Tyro3 receptor tyrosine kinase (RTK). Tyro3 together with Axl and Mer form the Axl/Tyro3 family of receptor tyrosine kinases (RTKs). This family includes Axl (also known as Ark, Ufo, and Tyro7), Tyro3 (also known as Sky, Rse, Brt, Dtk, and Tif), and Mer (also known as Nyk, c-Eyk, and Tyro12). Axl/Tyro3 family receptors have an extracellular portion with two Ig-like domains followed by two fibronectin-types III (FNIII) domains, a membrane-spanning single helix, and a cytoplasmic tyrosine kinase domain. Axl, Tyro3 and Mer are widely expressed in adult tissues, though they show higher expression in the brain, in the lymphatic and vascular systems, and in the testis. Axl, Tyro3, and Mer bind the vitamin K dependent protein Gas6 with high affinity, and in doing so activate their tyrosine kinase activity. Axl/Gas6 signaling may play a part in cell adhesion processes, prevention of apoptosis, and cell proliferation.

Pssm-ID: 409553 Cd Length: 87 Bit Score: 42.82 E-value: 6.96e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  221 VNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEE----DDEKHIFsddsSELTIRNVDKNDEAEYVCIAENkAGE 296
Cdd:cd20961     1 VKLTVSQGQPVKLNCSVEGMEEPDIQWVKDGAVVQNLDQlyipVSEQHWI----GFLSLKSVERSDAGRYWCQVED-GGE 75


                  ....
gi 568958938  297 QDAS 300
Cdd:cd20961    76 TEIS 79

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

Pssm-ID: 409544 [Multi-domain] Cd Length: 87 Bit Score: 42.48 E-value: 7.09e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  419 LQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNySNIKIYNTPSasyLEVTPDSENDFGNYNCTAVNRIGQ 498
Cdd:cd20952     3 LQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKD-ERITTLENGS---LQIKGAEKSDTGEYTCVALNLSGE 78


                  ..
gi 568958938  499 ES 500
Cdd:cd20952    79 AT 80

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 47.17 E-value: 7.13e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  950 TPTSAPSASNLSSTVLANQGAVLSPSTPASAGETSKAPPASKASPAPTPTPAgaasPLAAVAAPATDAPQAKQEAPSTKG 1029
Cdd:PRK07994  363 APLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVP----LPETTSQLLAARQQLQRAQGATKA 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1030 PDPEPTQPGTvknPPEAATAPASPKSKAATTNPSQGEDLKMDEGNFKTPDIDLAKDVFAALGSPAPATGASGQASELAPS 1109
Cdd:PRK07994  439 KKSEPAAASR---ARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEKTPELAAK 515

                         170
                  ....*....|
gi 568958938 1110 TADSAVPPAP 1119
Cdd:PRK07994  516 LAAEAIERDP 525

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.90 E-value: 7.29e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  954 APSASNLSSTVlANQGAVLSPSTPASAGETSKAPPASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDPE 1033
Cdd:PRK07764  591 APGAAGGEGPP-APASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1034 PTqPGTVKNPPEAATAPASPKSKAATTNPSQGEDlkmdegnfktPDIDLAKDVFAALGSPAPATGASGQASELAPSTADS 1113
Cdd:PRK07764  670 PA-KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA----------PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568958938 1114 AVPPAPAKTEKGPVETKSEPPESEAKPAPTEVKTVPNDATQTKENES 1160
Cdd:PRK07764  739 VPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEM 785

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.

Pssm-ID: 409388 Cd Length: 84 Bit Score: 42.18 E-value: 8.57e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  122 NAPTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGrDVILKKDVRFIVLSNNyLQIRGIKKTDEGTYRC 189
Cdd:cd05723     2 KKPSNIYAHESMDIVFECEVTGKPTPTVKWVKNG-DVVIPSDYFKIVKEHN-LQVLGLVKSDEGFYQC 67

First 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 first 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.

Pssm-ID: 409387 Cd Length: 97 Bit Score: 42.47 E-value: 8.64e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568958938  132 GEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIK-----KTDEGTYRCEGRILARGEI 199
Cdd:cd05722    16 GGPVVLNCSAESDPPPKIEWKKDGVLLNLVSDERRQQLPNGSLLITSVVhskhnKPDEGFYQCVAQNESLGSI 88

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.

Pssm-ID: 409475 Cd Length: 86 Bit Score: 42.13 E-value: 8.79e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENEEedDEKHIFSD-DSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd05894    10 GNKLRLDVPISGEPAPTVTWSRGDKAFTATE--GRVRVESYkDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.70 E-value: 9.50e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  941 VAPLVDLSDTPTSAPSASNLSSTVLANQGAVLSPSTPASAGETSKAPPASKASPAPTPTPA--------GAASPLAAVAA 1012
Cdd:PHA03307   61 ACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPppaspppsPAPDLSEMLRP 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1013 PATDAPQAKQEAPSTkgPDPEPTQPGTVKNPPEAATAPASPKSkAATTNPSQGEDLKMDEGNFKTPDIDLAKDVFAALGS 1092
Cdd:PHA03307  141 VGSPGPPPAASPPAA--GASPAAVASDAASSRQAALPLSSPEE-TARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASA 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568958938 1093 PAPA-TGASGQASELAPSTADSAVPPAPAKTEKGPVETKSEPPESEAKPAPTEVKTVPNDATQTKENESKA 1162
Cdd:PHA03307  218 SSPApAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSS 288

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.

Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.83 E-value: 9.66e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   813 KAAFSK-DESKEPIVEVRTEEERTPNHDGGKHTEPNETTPLTEPELPADTTATVEDMLPSVTTVTTNSDTITETFATAQN 891
Cdd:pfam05109  418 KVIFSKaPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDN 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   892 SPTSETTTLTSSIAPPATTVPDSNSVPAGQATPSKGVTASS-SSPASAPKVAPLVDLSDTPTSAPSASNLSSTVlanqgA 970
Cdd:pfam05109  498 GTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTlGKTSPTSAVTTPTPNATSPTPAVTTPTPNATI-----P 572

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   971 VLSPSTPASAGET----SKAPPASKASPAPTPTpaGAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKNPPEA 1046
Cdd:pfam05109  573 TLGKTSPTSAVTTptpnATSPTVGETSPQANTT--NHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSS 650

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  1047 ATAPASPKSKAATTN---------PSQGEDLKMdegnfKTPDIDLAKDVfaALGSPAPATGASGQASelAPSTADSAVPP 1117
Cdd:pfam05109  651 ISETLSPSTSDNSTShmplltsahPTGGENITQ-----VTPASTSTHHV--STSSPAPRPGTTSQAS--GPGNSSTSTKP 721

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 568958938  1118 APAKTEKGpvetksEPPESEAKP-APTEVKTVPNDATQT 1155
Cdd:pfam05109  722 GEVNVTKG------TPPKNATSPqAPSGQKTAVPTVTST 754

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.

Pssm-ID: 409390 [Multi-domain] Cd Length: 83 Bit Score: 42.00 E-value: 9.99e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568958938  132 GEDAVIVCDVVSSLPPTIIWKHKGRDVilkKDVRFIVLSNNYLQIRGIKKTDEGTYRCE-----GRILARG 197
Cdd:cd05725    12 DDSAEFQCEVGGDPVPTVRWRKEDGEL---PKGRYEILDDHSLKIRKVTAGDMGSYTCVaenmvGKIEASA 79

CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];

Pssm-ID: 444384 [Multi-domain] Cd Length: 874 Bit Score: 46.58 E-value: 1.05e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  833 ERTPNHDGGKHTEPNETTPLTEPELPADTTatvedmlPSVTTVTTNSDTITETFATAQNsptsetttltssiaPPATTVP 912
Cdd:COG5665   243 LATPPATPATEEKSSQQPKSQPTSPSGGTT-------PPSTNQLTTSNTPTSTAKAQPQ--------------PPTKKQP 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  913 dsnsvpaGQATPSKGVTASSsspasapkVAPLVDL-SDTPTSAPSASNLSSTVlanqGAVLSPSTPASAGET--SKAPPA 989
Cdd:COG5665   302 -------AKEPPSDTASGNP--------SAPSVLInSDSPTSEDPATASVPTT----EETTAFTTPSSVPSTpaEKDTPA 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  990 SKASPAPTPTPAgAASPLAAVAAPATDAPQAKQEAPST-KGPDPEPTQPGtVKNPPEaATAPASPKSKAATTNPSQGEDL 1068
Cdd:COG5665   363 TDLATPVSPTPP-ETSVDKKVSPDSATSSTKSEKEGGTaSSPMPPNIAIG-AKDDVD-ATDPSQEAKEYTKNAPMTPEAD 439

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938 1069 KMDEGNFKTP----------DIDLAKDVFAALGSPAPATGASGQASELAPSTADSAVPPAPAktekgPVETKSEPPESE 1137
Cdd:COG5665   440 SAPESSVRTEaspsagsdlePENTTLRDPAPNAIPPPEDPSTIGRLSSGDKLANETGPPVIR-----RDSTPSSTADQS 513

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.

Pssm-ID: 409416 Cd Length: 98 Bit Score: 42.44 E-value: 1.08e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  421 GPVAVYTwEGNQVNITCEVF-AYPSATISWFRDGQLLPSSNYSNIKIYN---TPSASYLEVTPDSENDFGNYNCTAVN 494
Cdd:cd05759     7 GPVISLQ-AGVPYNLTCRARgAKPAAEIIWFRDGEQLEGAVYSKELLKDgkrETTVSTLLITPSDLDTGRTFTCRARN 83

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.

Pssm-ID: 319300 Cd Length: 92 Bit Score: 42.19 E-value: 1.20e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  422 PVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIyNTPSASYLEVTPDSENDFGNYNCTAVNRIGQESL 501
Cdd:cd05737     8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKV-EAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETS 86


                  ..
gi 568958938  502 EF 503
Cdd:cd05737    87 DV 88

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.

Pssm-ID: 395002 Cd Length: 86 Bit Score: 41.80 E-value: 1.26e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568958938   123 APTPQEFKEGEDAVIVCDVVSSLP-PTIIWKHKGRDVILKkdvRFIVLSNNY-----LQIRGIKKTDEGTYRCEGR 192
Cdd:pfam00047    2 APPTVTVLEGDSATLTCSASTGSPgPDVTWSKEGGTLIES---LKVKHDNGRttqssLLISNVTKEDAGTYTCVVN 74

Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, classical Ig-like domains resembling the antibody constant domain. Members of the IgC1 family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, while the IgC domain is involved in oligomerization and molecular interactions. 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 strands by G, F, C, and C'.

Pssm-ID: 409354 Cd Length: 95 Bit Score: 42.06 E-value: 1.31e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  223 ATANLGQSVTLVCDADGF--PEPTMSWTKDGEPIENEEEDDEKHIFSDD----SSELTIRNVDKNDEAEYVCIAENKAGE 296
Cdd:cd00098     9 PEEKGGGKVTLVCLVSGFypKDITVTWLKNGVPLTSGVSTSSPVEPNDGtysvTSSLTVPPSDWDEGATYTCVVTHESLK 88


                  ....*..
gi 568958938  297 QDASIHL 303
Cdd:cd00098    89 SPLSKTW 95

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth 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.

Pssm-ID: 409359 Cd Length: 102 Bit Score: 42.15 E-value: 1.35e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  310 KITYVENQTAMELEEQVTLTCEASGDPIPSIT--WRTSTRNIS-SEEKASWTRPEKQETldghmvvrsharVSSLTLKSI 386
Cdd:cd04970     4 RITLAPSNADITVGENATLQCHASHDPTLDLTftWSFNGVPIDlEKIEGHYRRRYGKDS------------NGDLEIVNA 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568958938  387 QYTDAGEYICTASNTIGQDSQSMYLEVQYAP 417
Cdd:cd04970    72 QLKHAGRYTCTAQTVVDSDSASATLVVRGPP 102

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.

Pssm-ID: 143278 [Multi-domain] Cd Length: 98 Bit Score: 42.27 E-value: 1.39e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  222 NATANLGQSVTLVCDADGFPEPTMSWTK--DGEPIENEEEDDEKHI---FSDDSSELTIRNVDKNDEAEYVCIAENKAGE 296
Cdd:cd05870    10 NETTVENGAATLSCKAEGEPIPEITWKRasDGHTFSEGDKSPDGRIevkGQHGESSLHIKDVKLSDSGRYDCEAASRIGG 89


                  ....*....
gi 568958938  297 QDASIHLKV 305
Cdd:cd05870    90 HQKSMYLDI 98

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.

Pssm-ID: 409391 [Multi-domain] Cd Length: 98 Bit Score: 42.25 E-value: 1.41e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  326 VTLTCEASGDPIPSITWRtstrnisseekaswtRPEKQETLDGHMVVRSHARVS-----SLTLKSIQYTDAGEYICTASN 400
Cdd:cd05726    17 VTFQCETKGNPQPAIFWQ---------------KEGSQNLLFPYQPPQPSSRFSvsptgDLTITNVQRSDVGYYICQALN 81

                          90
                  ....*....|...
gi 568958938  401 TIGQDSQSMYLEV 413
Cdd:cd05726    82 VAGSILAKAQLEV 94

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 1.43e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  905 APPATtvPDsNSVPAGQATPSKgvtasssspasapkVAPLVDLSDTPTSAPSASNLSSTVLANQGAVLSPSTPASAgets 984
Cdd:PHA03247 2559 APPAA--PD-RSVPPPRPAPRP--------------SEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPL---- 2617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  985 kaPPASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDP-----EPTQPGTVKNPPEAATAPASPKSKAAT 1059
Cdd:PHA03247 2618 --PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRprrarRLGRAAQASSPPQRPRRRAARPTVGSL 2695

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1060 TN----PSQGED-----LKMDEGNFKTPDIDLAKDVFAAL----GSPAPATGASGQASEL------APSTADSAVPPA-- 1118
Cdd:PHA03247 2696 TSladpPPPPPTpepapHALVSATPLPPGPAAARQASPALpaapAPPAVPAGPATPGGPArparppTTAGPPAPAPPAap 2775

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 568958938 1119 ----PAKTEKGPVETKSEPPESEAKPAPTEVKTVPNDATQTKENESKA 1162
Cdd:PHA03247 2776 aagpPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS 2823

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.32 E-value: 1.46e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  798 GKAGPGAKGKDMEEGkAAFSKDESKEPIVEVRTEEERTPNHDGGKHTEPNETTPLTEPELPADTTATVEDMLPSVTTVTT 877
Cdd:PHA03307  104 GSPTPPGPSSPDPPP-PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEET 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  878 nsdtiTETFATAQNSPTSETTTLTSSIAPPATTVPDSNSVPAGQATPSKGVTASSSSPASAPKVAPLVD-----LSDTPT 952
Cdd:PHA03307  183 -----ARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGcgwgpENECPL 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  953 SAPSASNLSSTVLANQGAVL--------SPSTPASAGETSKAPPASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEA 1024
Cdd:PHA03307  258 PRPAPITLPTRIWEASGWNGpssrpgpaSSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1025 PSTKGPDPEPTQPGTVKNPPEAATAPASPKSKAATTNPSQGEDLKMDEGNFKTpdidlAKDVfAALGSPAPATGASGQAS 1104
Cdd:PHA03307  338 GAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRA-----RAAV-AGRARRRDATGRFPAGR 411

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 568958938 1105 ELAPSTADSAVPPAPAKTEKgPVETKSEP-PESEAKPA 1141
Cdd:PHA03307  412 PRPSPLDAGAASGAFYARYP-LLTPSGEPwPGSPPPPP 448

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.

Pssm-ID: 143222 [Multi-domain] Cd Length: 74 Bit Score: 41.08 E-value: 1.54e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  429 EGNQVNITCEVFAYPSATISWFRDGQLLPSSnysniKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQES 500
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVD-----RRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQR 67

First immunoglobulin-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1), and similar domains; member of the I-set of IgSF domains; The members here include the first immunoglobulin-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1; also known as Cluster of Differentiation 106 (CD106)) and similar proteins. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. The interaction of VCAM-1 binding to the beta1 integrin very late antigen (VLA-4) expressed by lymphocytes and monocytes mediates the adhesion of leucocytes to blood vessel walls, and regulates migration across the endothelium. During metastasis, some circulating cancer cells extravasate to a secondary site by a similar process. VCAM-1 may be involved in organ targeted tumor metastasis and may also act as host receptors for viruses and parasites. VCAM-1 contains seven Ig domains. 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 first Ig-like domain of VCAM-1 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, the A strand of the I-set is discontinuous, but lacks a C" strand.

Pssm-ID: 409536 Cd Length: 89 Bit Score: 41.50 E-value: 1.55e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  315 ENQTAMELEEQVTLTCEASGDPIPSITWRTSTrnisseekaswtrpekQETLDGhmVVRSHARVSSLTLKSIQYTDAGEY 394
Cdd:cd20943     8 GSRYAAQIGDSVSLTCSTTGCESPSFSWRTQI----------------DSPLNG--KVRNEGTTSTLTLSPVSFENEHSY 69


                  ....*
gi 568958938  395 ICTAS 399
Cdd:cd20943    70 LCTVT 74

104 kDa microneme/rhoptry antigen; Provisional

Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 45.84 E-value: 1.65e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  974 PSTPasagETSKAP--PASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPD--PEPTQPGTVKNP--PEAA 1047
Cdd:PTZ00449  579 PEFP----KDPKHPkdPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKrpPPPQRPSSPERPegPKII 654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1048 TAPASPKSKAATTNPSQGEDLkMDEGNFKTPDIDLAKDVFAALGSPAPATGASGQASELAPSTADSAVPPAPAKTEKGPV 1127
Cdd:PTZ00449  655 KSPKPPKSPKPPFDPKFKEKF-YDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPF 733

                         170       180
                  ....*....|....*....|..
gi 568958938 1128 ETKSEPpeSEAKPAPTEVKTVP 1149
Cdd:PTZ00449  734 EPIGDP--DAEQPDDIEFFTPP 753

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. 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.

Pssm-ID: 409412 Cd Length: 85 Bit Score: 41.39 E-value: 1.70e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  204 IQVIVNVPPTVQARQsivnatanlGQSVTLVCDA-DGFPEPTMSWTKDGEPIENEEEDDekhifsddSSELTIRNVDKND 282
Cdd:cd05754     1 IQVTVEEPRSQEVRP---------GADVSFICRAkSKSPAYTLVWTRVNGTLPSRAMDF--------NGILTIRNVQLSD 63

                          90
                  ....*....|
gi 568958938  283 EAEYVCIAEN 292
Cdd:cd05754    64 AGTYVCTGSN 73

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.

Pssm-ID: 409397 [Multi-domain] Cd Length: 97 Bit Score: 41.71 E-value: 1.74e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568958938  120 FKNAPTPQEFKEGEDAVIVCDVVSSLPPTIIWKH-KGRDV-----ILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCE 190
Cdd:cd05734     4 FVVQPNDQDGIYGKAVVLNCSADGYPPPTIVWKHsKGSGVpqfqhIVPLNGRIQLLSNGSLLIKHVLEEDSGYYLCK 80

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 45.75 E-value: 1.79e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  905 APPATTVPDSNSVPAGQATPSKGVTASSSSPASAPKVAPLVDLSDTPTSAPSASNLSSTVLANQGAVLSPSTPASAGETS 984
Cdd:PRK07764  616 AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAG 695

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  985 KAPPASKASPAPTPTPAG----AASPLAAVAAPATDAPQAKQEAPSTKGPDPEPtQPGTVKNPPEAATAPASPKSKAATT 1060
Cdd:PRK07764  696 AAPAQPAPAPAATPPAGQaddpAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP-DPAGAPAQPPPPPAPAPAAAPAAAP 774


                  ....*..
gi 568958938 1061 NPSQGED 1067
Cdd:PRK07764  775 PPSPPSE 781

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth 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.

Pssm-ID: 409358 [Multi-domain] Cd Length: 89 Bit Score: 41.29 E-value: 1.84e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568958938  430 GNQVNITCEVFAYPSATISWFRDGQLLPSSNysniKIYNTPSASyLEVTPDSENDFGNYNCTAVNRIGQESLEFILV 506
Cdd:cd04969    17 GGDVIIECKPKASPKPTISWSKGTELLTNSS----RICILPDGS-LKIKNVTKSDEGKYTCFAVNFFGKANSTGSLS 88

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.

Pssm-ID: 409388 Cd Length: 84 Bit Score: 41.41 E-value: 1.86e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  419 LQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKiyntpSASYLEVTPDSENDFGNYNCTAVNRIG- 497
Cdd:cd05723     1 LKKPSNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIV-----KEHNLQVLGLVKSDEGFYQCIAENDVGn 75


                  ....*....
gi 568958938  498 -QESLEFIL 505
Cdd:cd05723    76 aQASAQLII 84

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; 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. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.

Pssm-ID: 409406 [Multi-domain] Cd Length: 82 Bit Score: 41.04 E-value: 2.04e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  324 EQVTLTCEASGDPIPSITWrtstrnisseekaswTRPEKQETLDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTIG 403
Cdd:cd05748     8 ESLRLDIPIKGRPTPTVTW---------------SKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAG 72


                  ...
gi 568958938  404 QDS 406
Cdd:cd05748    73 EKS 75

Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth 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 (AC) in the developing chick retina, corresponding to the period of formation and maturation of AC processes.

Pssm-ID: 409440 Cd Length: 102 Bit Score: 41.57 E-value: 2.07e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  310 KITYVENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNIS---SEEKASWTRPEKQETldghmvvrsharVSSLTLKSI 386
Cdd:cd05854     4 KITLAPSSADINQGENLTLQCHASHDPTMDLTFTWSLDDFPidlDKPNGHYRRMEVKET------------IGDLVIVNA 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568958938  387 QYTDAGEYICTASNTIGQDSQSMYLEVQYAP 417
Cdd:cd05854    72 QLSHAGTYTCTAQTVVDSASASATLVVRGPP 102

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 45.63 E-value: 2.09e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  974 PSTPASAGETSKAPPASKASPAPTPTPAGaasplaavaapatdapqakQEAPSTKGPDPEPTQPGTVKNPPEAATAPASP 1053
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTA-------------------AVAPPQAPAVPPPPASAPQQAPAVPLPETTSQ 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1054 KSKAATTNPSQgedlkmdEGNFKTPDIDlakdvfaALGSPAPATGASGQASELAPSTADSAVPPAPAKTEkgPVETKSEP 1133
Cdd:PRK07994  422 LLAARQQLQRA-------QGATKAKKSE-------PAAASRARPVNSALERLASVRPAPSALEKAPAKKE--AYRWKATN 485

                         170       180
                  ....*....|....*....|....*....
gi 568958938 1134 PESEAKPAPTEVKTVPNDATQTKENESKA 1162
Cdd:PRK07994  486 PVEVKKEPVATPKALKKALEHEKTPELAA 514

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.

Pssm-ID: 409568 [Multi-domain] Cd Length: 90 Bit Score: 41.47 E-value: 2.13e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  429 EGNQVNITCEVFAYPSATISWFRDGQLLpssNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQES 500
Cdd:cd20976    15 EGQDFVAQCSARGKPVPRITWIRNAQPL---QYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVS 83

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 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-nonNCAM) 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 the Ig1, Ig2, and Ig3 domains. 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. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). 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.

Pssm-ID: 409366 Cd Length: 95 Bit Score: 41.47 E-value: 2.22e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  310 KITYVENQTAMELEEQVTLTCEASGDPipsitwrtstrnisseEKASWTRP--EKQETLDGHMVVRSHARV-SSLTLKSI 386
Cdd:cd04977     2 QVKIIPSYAEISVGESKFFLCKVSGDA----------------KNINWVSPngEKVLTKHGNLKVVNHGSVlSSLTIYNA 65

                          90       100
                  ....*....|....*....|..
gi 568958938  387 QYTDAGEYICTASNTIGQDSQS 408
Cdd:cd04977    66 NINDAGIYKCVATNGKGTESEA 87

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk 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. 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 titin Z1z2 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.

Pssm-ID: 409566 [Multi-domain] Cd Length: 93 Bit Score: 41.18 E-value: 2.24e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  418 KLQGpvaVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIG 497
Cdd:cd20974     6 PLQS---VVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSG 82


                  .
gi 568958938  498 Q 498
Cdd:cd20974    83 Q 83

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 2.27e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  851 PLTEPElPADTTATVEDMLPSVTTVTTNSDTITETFA-TAQNSPTSETTTLTSSIAPPATTVPDSNSVPAGQATPSkgvt 929
Cdd:PHA03247 2775 PAAGPP-RRLTRPAVASLSESRESLPSPWDPADPPAAvLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS---- 2849

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  930 assssPASAPKVAPLVDLSDTPTSAPSASnlsstvlanqgavlSPSTPASAGETSKAPPASKASPAPTPTPAGAASPLAA 1009
Cdd:PHA03247 2850 -----LPLGGSVAPGGDVRRRPPSRSPAA--------------KPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQ 2910

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568958938 1010 VAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKNPPEAATAPASPKSKAA 1058
Cdd:PHA03247 2911 PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAV 2959

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;

Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 45.65 E-value: 2.31e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  965 LANQGAVLSPSTPASAGETSKAPPASKASPAPTPTPAgaasplaavaapatdaPQAKQEAPSTKGPDPEPTQPGTVKNPP 1044
Cdd:PRK12270   33 FADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAA----------------PAPAPPAAAAPAAPPKPAAAAAAAAAP 96

                          90       100
                  ....*....|....*....|....*
gi 568958938 1045 EAATAPASPKSKAATTNPSQGEDLK 1069
Cdd:PRK12270   97 AAPPAAAAAAAPAAAAVEDEVTPLR 121

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

Pssm-ID: 464026 [Multi-domain] Cd Length: 79 Bit Score: 40.84 E-value: 2.38e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   308 KPKITyVENQTAMELEEqVTLTCEASGDPIPSITWRtstrnisSEEKASWTRPEkqetldghmvvrsharvssLTLKSIQ 387
Cdd:pfam13895    1 KPVLT-PSPTVVTEGEP-VTLTCSAPGNPPPSYTWY-------KDGSAISSSPN-------------------FFTLSVS 52

                           90       100
                   ....*....|....*....|....*..
gi 568958938   388 YTDAGEYICTASNT-IGQDSQSMYLEV 413
Cdd:pfam13895   53 AEDSGTYTCVARNGrGGKVSNPVELTV 79

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). 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 human APEG-1 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.

Pssm-ID: 409567 Cd Length: 91 Bit Score: 41.30 E-value: 2.42e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  212 PTVQArqSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIfSDDSSELTIRNVDKNDEAEYVCIAE 291
Cdd:cd20975     1 PTFKV--SLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEA-EGGLCRLRILAAERGDAGFYTCKAV 77

                          90
                  ....*....|....
gi 568958938  292 NKAGEQDASIHLKV 305
Cdd:cd20975    78 NEYGARQCEARLEV 91

Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of human neurofascin (NF). NF 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 a cytoplasmic domain. NF has many alternatively spliced isoforms having different temporal expression patterns during development. NF participates in axon subcellular targeting and synapse formation, however little is known of the functions of the different isoforms. 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.

Pssm-ID: 409459 Cd Length: 95 Bit Score: 41.50 E-value: 2.42e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  324 EQVTLTCEASGDPIPSITWRTSTR--NISSEEKASWTRPEkqetldGHMVVRSHArvssltlKSIQYTDAGEYICTASNT 401
Cdd:cd05875    17 DNILIECEAKGNPVPTFHWTRNGKffNVAKDPRVSMRRRS------GTLVIDFRG-------GGRPEDYEGEYQCFARNK 83


                  ..
gi 568958938  402 IG 403
Cdd:cd05875    84 FG 85

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.

Pssm-ID: 409422 [Multi-domain] Cd Length: 95 Bit Score: 41.00 E-value: 3.04e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  324 EQVTLTCEASGDPIPSITWRtstRNISSEEKASwTRPEKqetLDGHMVVRSharVSSLTLKSIQYTDAGEYICTASNTIG 403
Cdd:cd05765    16 ETASFHCDVTGRPQPEITWE---KQVPGKENLI-MRPNH---VRGNVVVTN---IGQLVIYNAQPQDAGLYTCTARNSGG 85

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.

Pssm-ID: 409393 [Multi-domain] Cd Length: 95 Bit Score: 41.05 E-value: 3.29e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  326 VTLTCEASGDPIPSITWRTSTRNISSEEKASWTRPEKQETldghmvvrsharvsSLTLKSIQYTDAGEYICTASNTIGQD 405
Cdd:cd05729    22 VRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGW--------------SLIIERAIPRDKGKYTCIVENEYGSI 87


                  ....*...
gi 568958938  406 SQSMYLEV 413
Cdd:cd05729    88 NHTYDVDV 95

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.

Pssm-ID: 143220 Cd Length: 78 Bit Score: 40.17 E-value: 3.52e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHifSDDSSELTIRNVDKNDEAEYVCIAENKAGeqdasihlKVFA 307
Cdd:cd05743     1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITS--EGGYGTLTIRDVKESDQGAYTCEAINTRG--------MVFG 70


                  ..
gi 568958938  308 KP 309
Cdd:cd05743    71 IP 72

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 44.70 E-value: 3.65e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  995 APTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPTqpgtvknpPEAATAPASPKSKAATTNPSQGEDLK--MDE 1072
Cdd:PRK08691  357 AFAPLAAASCDANAVIENTELQSPSAQTAEKETAAKKPQPR--------PEAETAQTPVQTASAAAMPSEGKTAGpvSNQ 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1073 GNFKTPDIDLAKDVFAALGSPAPATGASGQASelapstADSAVPPAPAKTEKGPVETKSEPPESEAkPAPTEVKTVPND- 1151
Cdd:PRK08691  429 ENNDVPPWEDAPDEAQTAAGTAQTSAKSIQTA------SEAETPPENQVSKNKAADNETDAPLSEV-PSENPIQATPNDe 501

                         170
                  ....*....|...
gi 568958938 1152 --ATQTKENESKA 1162
Cdd:PRK08691  502 avETETFAHEAPA 514

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.

Pssm-ID: 409405 [Multi-domain] Cd Length: 91 Bit Score: 40.56 E-value: 3.66e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  326 VTLTCEASGDPIPSITWRTSTRNISSEEKASwtrpekqetldghMVVRSHARVSsLTLKSIQYTDAGEYICTASNTIGQD 405
Cdd:cd05744    18 CRFDCKVSGLPTPDLFWQLNGKPVRPDSAHK-------------MLVRENGRHS-LIIEPVTKRDAGIYTCIARNRAGEN 83


                  ....*...
gi 568958938  406 SQSMYLEV 413
Cdd:cd05744    84 SFNAELVV 91

Seventh 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 seventh 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.

Pssm-ID: 409546 [Multi-domain] Cd Length: 96 Bit Score: 40.76 E-value: 3.93e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568958938  124 PTPQEFKEGEDAVIVCDVVSSLPPTIIWKH-------KGRDVILKKDVRFivLSNNYLQIRGIKKTDEGTYRCE 190
Cdd:cd20954     8 PVDANVAAGQDVMLHCQADGFPTPTVTWKKatgstpgEYKDLLYDPNVRI--LPNGTLVFGHVQKENEGHYLCE 79

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.

Pssm-ID: 409363 Cd Length: 102 Bit Score: 40.87 E-value: 4.06e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  221 VNATANLGQSVTLVCDADGFPEPTMSWTK-----------DGEPieNEEEDDEKHIFSD-DSSELTIRNVDKNDEAEYVC 288
Cdd:cd04974     9 ANQTVVLGSDVEFHCKVYSDAQPHIQWLKhvevngskygpDGLP--YVTVLKVAGVNTTgEENTLTISNVTFDDAGEYIC 86

                          90
                  ....*....|....*.
gi 568958938  289 IAENKAGEQDASIHLK 304
Cdd:cd04974    87 LAGNSIGLSFHSAWLT 102

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.

Pssm-ID: 409562 [Multi-domain] Cd Length: 92 Bit Score: 40.57 E-value: 4.14e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  131 EGEDAVIVCDVVSSLPPTIIWKHKGRDVILkKDVRFIVLSNN-YLQIRGIKKTDEGTYRC 189
Cdd:cd20970    16 EGENATFMCRAEGSPEPEISWTRNGNLIIE-FNTRYIVRENGtTLTIRNIRRSDMGIYLC 74

DNA polymerase III subunits gamma and tau; Provisional

Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 44.42 E-value: 4.49e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  970 AVLSPST-PASAGETSKAPPASKASPAPTPTPagaasPLAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKNPPEAAT 1048
Cdd:PRK14950  358 ALLVPVPaPQPAKPTAAAPSPVRPTPAPSTRP-----KAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLT 432

                          90
                  ....*....|....
gi 568958938 1049 APASPKSKAATTNP 1062
Cdd:PRK14950  433 RAAIPVDEKPKYTP 446

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.

Pssm-ID: 143224 [Multi-domain] Cd Length: 92 Bit Score: 40.42 E-value: 4.54e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  324 EQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTRPEKQETLDghmvvrsharvssltLKSIQYTDAGEYICTASNTIG 403
Cdd:cd05747    19 ESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFE---------------ISKVQMSDEGNYTVVVENSEG 83


                  .
gi 568958938  404 Q 404
Cdd:cd05747    84 K 84

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.

Pssm-ID: 409542 Cd Length: 97 Bit Score: 40.76 E-value: 4.62e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568958938  430 GNQVNITC-EVFAYPSATISWFRDGQLLP-----SSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIG 497
Cdd:cd20950    12 GNRAVLTCsEPDGSPPSEYTWFKDGVVMPtnpksTRAFSNSSYSLDPTTGELVFDPLSASDTGEYSCEARNGYG 85

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth 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.

Pssm-ID: 409359 Cd Length: 102 Bit Score: 40.61 E-value: 4.97e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   26 PSQGEISVGESKFFLCQVAGD-AKDKDISWfSPNG-----EKLSPNQQRISVVwndDDSSTLTIYNANIDDAGIYKCVV- 98
Cdd:cd04970     9 PSNADITVGENATLQCHASHDpTLDLTFTW-SFNGvpidlEKIEGHYRRRYGK---DSNGDLEIVNAQLKHAGRYTCTAq 84

                          90
                  ....*....|....*
gi 568958938   99 TAEDGTQSEATVNVK 113
Cdd:cd04970    85 TVVDSDSASATLVVR 99

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.39 E-value: 5.03e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  941 VAPLVDLS-DTPTSAPSASNLSSTVLANQG----------AVLSPSTPASAGETSKaPPASKASPAPTPTPAGAASPLAA 1009
Cdd:PHA03307  733 VAPLVRYSpRRARARASAWDITDALFSNPSlvpaklaealALLEPAEPQRGAGSSP-PVRAEAAFRRPGRLRRSGPAADA 811

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1010 VAAPATDApQAKQEAPSTKGPDPEPTQPGTVKNPPEAATAPASPKSKAATTNPSQGEDLKMDEGNFKTPDidlakdvfAA 1089
Cdd:PHA03307  812 ASRTASKR-KSRSHTPDGGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPR--------AR 882

                         170       180       190
                  ....*....|....*....|....*....|
gi 568958938 1090 LGSPAPATGASGQASELAPSTADSAVPPAP 1119
Cdd:PHA03307  883 PGAAAPPKAAAAAPPAGAPAPRPRPAPRVK 912

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. 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 telokin Ig domain 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.

Pssm-ID: 409565 [Multi-domain] Cd Length: 88 Bit Score: 40.25 E-value: 5.16e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  429 EGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIkIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQ 498
Cdd:cd20973    11 EGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQI-DQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGE 79

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.

Pssm-ID: 409475 Cd Length: 86 Bit Score: 39.82 E-value: 5.75e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  325 QVTLTCEASGDPIPSITWRTSTRNISSEEkaswtrpekqetldGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTIGQ 404
Cdd:cd05894    12 KLRLDVPISGEPAPTVTWSRGDKAFTATE--------------GRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGE 77


                  ....*....
gi 568958938  405 DSQSMYLEV 413
Cdd:cd05894    78 DHASLFVKV 86

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.

Pssm-ID: 409405 [Multi-domain] Cd Length: 91 Bit Score: 40.17 E-value: 5.91e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   26 PSQGEISVGESKFFLCQVAGDAKdKDISWfSPNGEKLSPNQqRISVVWNDDDSSTLTIYNANIDDAGIYKCVVTAEDG-T 104
Cdd:cd05744     7 PGDLEVQEGRLCRFDCKVSGLPT-PDLFW-QLNGKPVRPDS-AHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGeN 83


                  ....*...
gi 568958938  105 QSEATVNV 112
Cdd:cd05744    84 SFNAELVV 91

DNA polymerase III subunit gamma/tau;

Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.07 E-value: 6.14e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  965 LANQGAVLSPSTPASAGEtskaPPASKASPAPTPTPAGAASPLAAVaapatdaPQAKQEAPSTKGPDPEPTQPGTVKNPP 1044
Cdd:PRK07003  356 LAFEPAVTGGGAPGGGVP----ARVAGAVPAPGARAAAAVGASAVP-------AVTAVTGAAGAALAPKAAAAAAATRAE 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1045 EAATAPASPKSKAATTNPSqgedlkmdegnfktpdidlAKDVFAALGSPAPATGASGQASELAPSTADSAVPPAPAKTEK 1124
Cdd:PRK07003  425 APPAAPAPPATADRGDDAA-------------------DGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAP 485

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568958938 1125 GPVETKSEPPESEAKPAPTEVKTVPNDATQTKENESKA 1162
Cdd:PRK07003  486 PDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPA 523

Fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR); The members here are composed of the fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR; also known as cluster of differentiation (CD) 140a) alpha and beta. PDGF is a potent mitogen for connective tissue cells. PDGF-stimulated processes are mediated by three different PDGFs (PDGF-A,PDGF-B, and PDGF-C). PDGFR alpha binds to all three PDGFs, whereas the PDGFR beta binds only to PDGF-B. PDGF alpha is organized as an extracellular component having five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. In mice, PDGFR alpha and PDGFR beta are essential for normal development.

Pssm-ID: 409445 Cd Length: 101 Bit Score: 40.23 E-value: 6.18e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  222 NATANLGQSVTLVCDADGFPEPTMSWTKDGEP-IENEEE---DDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQ 297
Cdd:cd05859    12 LEFANLHEVKEFVVEVEAYPPPQIRWLKDNRTlIENLTEittSTRNVQETRYVSKLKLIRAKEEDSGLYTALAQNEDAVK 91


                  ....*...
gi 568958938  298 DASIHLKV 305
Cdd:cd05859    92 SYTFALQI 99

Treacher Collins syndrome protein Treacle;

Pssm-ID: 460967 [Multi-domain] Cd Length: 531 Bit Score: 43.52 E-value: 6.76e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   905 APPATTVPDSNS---VPAGQATPSKG--VTASSSSPASAPKVAPLVDLSDTPTSAPSASNLSSTVLANQGAVLSPSTPAS 979
Cdd:pfam03546  245 APAAATPAQAKPalkTPQTKASPRKGtpITPTSAKVPPVRVGTPAPWKAGTVTSPACASSPAVARGAQRPEEDSSSSEES 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   980 AGETSKAPPAS-------------KASPAPTPTPAGAASPLAAVAAPATDAPQAKQEA----------PSTKGPDPEPTQ 1036
Cdd:pfam03546  325 ESEEETAPAAAvgqaksvgkglqgKAASAPTKGPSGQGTAPVPPGKTGPAVAQVKAEAqedsesseeeSDSEEAAATPAQ 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  1037 PGTVKNPPEAATAPASPKSKAATTNPSqgedlkmdegnfkTPDIDLAKDVFAALGSPAP-----------ATGASGQASE 1105
Cdd:pfam03546  405 VKASGKTPQAKANPAPTKASSAKGAAS-------------APGKVVAAAAQAKQGSPAKvkppartpqnsAISVRGQASV 471

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 568958938  1106 LAPSTADSAVPPAPAKTEKGPVETKSEPPESEA---KPAPTEVK 1146
Cdd:pfam03546  472 PAVGKAVATAAQAQKGPVGGPQEEDSESSEEESdseEEAPAQAK 515

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.

Pssm-ID: 409405 [Multi-domain] Cd Length: 91 Bit Score: 39.79 E-value: 6.78e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  119 MFKNAPTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRDVilKKDVRFIVLSNN----YLQIRGIKKTDEGTYRCEGR 192
Cdd:cd05744     2 HFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPV--RPDSAHKMLVREngrhSLIIEPVTKRDAGIYTCIAR 77

60S ribosomal protein L19-like protein; Provisional

Pssm-ID: 185616 [Multi-domain] Cd Length: 357 Bit Score: 43.40 E-value: 6.80e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  969 GAVLSPSTPASAGETSKAPPASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDPeptqPGTVKNPPEAAT 1048
Cdd:PTZ00436  193 AAAAAAAKQKAAAKKAAAPSGKKSAKAAAPAKAAAAPAKAAAPPAKAAAAPAKAAAAPAKAAAP----PAKAAAPPAKAA 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1049 AP----ASPKSKAATTnpsqgedlkmdegnfktpdidlakdvfAALGSPAPATGASGQASELAPSTADSAVP----PAPA 1120
Cdd:PTZ00436  269 APpakaAAPPAKAAAP---------------------------PAKAAAPPAKAAAAPAKAAAAPAKAAAAPakaaAPPA 321

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568958938 1121 KTEKGPVETKSEPPESEAKPAPTEVKTVPNDATQTK 1156
Cdd:PTZ00436  322 KAAAPPAKAATPPAKAAAPPAKAAAAPVGKKAGGKK 357

EBNA-3B; Provisional

Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.90 E-value: 6.86e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  906 PPATTVPDSN-SVPAGQATPSKGVTasssspasapkvAPLVDLSDTPTSAPSASNLSSTVLANQGAVLSPSTPASAGETS 984
Cdd:PHA03378  697 PPRAPTPMRPpAAPPGRAQRPAAAT------------GRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA 764

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  985 KAPPASKASPAPTPTPAGAASPLAAVAAPATDAPQ----------AKQEAPSTKGPDPEPTQ---PGTVKNPPEAATAPA 1051
Cdd:PHA03378  765 RPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPpqagptsmqlMPRAAPGQQGPTKQILRqllTGGVKRGRPSLKKPA 844

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1052 SPKSKAA---TTNPSQGEDLKMDEGNFKTPDIDLAKDVFAALGSPAPA---------TGASGQASELAPSTADSAVPPAP 1119
Cdd:PHA03378  845 ALERQAAagpTPSPGSGTSDKIVQAPVFYPPVLQPIQVMRQLGSVRAAaastvtqapTEYTGERRGVGPMHPTDIPPSKR 924

                         250       260
                  ....*....|....*....|....
gi 568958938 1120 AKTEKGPvetKSEPPESEAKPAPT 1143
Cdd:PHA03378  925 AKTDAYV---ESQPPHGGQSHSFS 945

Third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R), and similar domains; member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the hematopoietic colony-stimulating factor 1 receptor (CSF-1R) and similar proteins. CSF-1R, a class III receptor tyrosine kinase (RTKIII), is critical to the survival, proliferation, and differentiation of mononuclear phagocytic cells such as monocytes, tissue macrophages, muscularis macrophages, microglia, osteoclasts, Paneth cells, and myeloid dendritic cells. Human colony-stimulating factor 1 receptor (hCSF-1R) is unique among the hematopoietic receptors because it is activated by two distinct cytokines, CSF-1 and interleukin-34 (IL-34). The Ig superfamily (IgSF) 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. 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. This group belongs to the I-set of IgSF domains.

Pssm-ID: 409530 Cd Length: 93 Bit Score: 39.94 E-value: 7.12e-04

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568958938  375 HARVSSLTLKSIQYTDAGEYICTASNTIGQDSQSMYLEV 413
Cdd:cd20936    55 YQKVLTLNLDQVDFQDAGNYSCVASNVQGKHSASMFFRV 93

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third 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, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.

Pssm-ID: 409394 [Multi-domain] Cd Length: 83 Bit Score: 39.70 E-value: 7.29e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  318 TAMELEEQV-TLTCEASGDPIPSITWRtstrnisseekaswtrPEKQETLDGHMVVRSHARVssLTLKSIQYTDAGEYIC 396
Cdd:cd05731     4 STMVLRGGVlLLECIAEGLPTPDIRWI----------------KLGGELPKGRTKFENFNKT--LKIENVSEADSGEYQC 65


                  ....*..
gi 568958938  397 TASNTIG 403
Cdd:cd05731    66 TASNTMG 72

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.

Pssm-ID: 409240 [Multi-domain] Cd Length: 163 Bit Score: 41.21 E-value: 8.64e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1020 AKQEAPSTKGP-DPEPTQPGTVKNPPEAATApASPKSKAATTNPSQGEDLKMDEGNFKTPDIDLAKDVFAALGSPAPATG 1098
Cdd:cd21975    36 VRATREVAKGPgPPGPAWKPDGADSPGLVTA-APHLLAANVLAPLRGPSVEGSSLESGDADMGSDSDVAPASGAAASTSP 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568958938 1099 ASGQASELAPSTADSAVPPAPAKTEKGPVETKSEPPESEAKPAP 1142
Cdd:cd21975   115 ESSSDAASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPA 158

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (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.

Pssm-ID: 409421 [Multi-domain] Cd Length: 88 Bit Score: 39.38 E-value: 8.67e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  322 LEEQ-VTLTCEASGDPIPSITWRTSTRNISSeeKASWTRPEKQETLDghmvvrsharVSSLTLKsiqytDAGEYICTASN 400
Cdd:cd05764    13 LEGQrATLRCKARGDPEPAIHWISPEGKLIS--NSSRTLVYDNGTLD----------ILITTVK-----DTGAFTCIASN 75

                          90
                  ....*....|...
gi 568958938  401 TIGQDSQSMYLEV 413
Cdd:cd05764    76 PAGEATARVELHI 88

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.

Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 43.22 E-value: 9.49e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  949 DTPTSAPSASNLSSTVLANQGAV-------LSPSTPASAGetSKAPPASKASPAPTPTPAGAASPLAAVAAPATDAPQAK 1021
Cdd:NF033839  249 DNVNTKVEIENTVHKIFADMDAVvtkfkkgLTQDTPKEPG--NKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLE 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1022 QEAPSTKgPDPEPTQPGTvknPPEAATAPASPKSKAATTNPSQGEDLKMDEGNFKTPDIDLAKDVFAALGSPAPATGASg 1101
Cdd:NF033839  327 KPKPEVK-PQPEKPKPEV---KPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQ- 401

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568958938 1102 qaselaPSTADSAVPPAPaKTEKGPVETKSEPPESEAKPAPTEVKTVPNDATQTKENESKA 1162
Cdd:NF033839  402 ------PEKPKPEVKPQP-EKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKP 455

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.

Pssm-ID: 409389 [Multi-domain] Cd Length: 87 Bit Score: 39.31 E-value: 9.55e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568958938  442 YPSATISWFRDGQLLpssNYSNIKIYnTPSASYLEVTPDSENDFGNYNCTAVNRIG 497
Cdd:cd05724    25 HPEPTVSWRKDGQPL---NLDNERVR-IVDDGNLLIAEARKSDEGTYKCVATNMVG 76

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.

Pssm-ID: 409435 Cd Length: 96 Bit Score: 39.54 E-value: 9.55e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  211 PPTVQARQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEedDEKHIFSDDSseLTIRNVDK-NDEAEYVCI 289
Cdd:cd05848     2 PVFVQEPDDAIFPTDSDEKKVILNCEARGNPVPTYRWLRNGTEIDTES--DYRYSLIDGN--LIISNPSEvKDSGRYQCL 77


                  ....*.
gi 568958938  290 AENKAG 295
Cdd:cd05848    78 ATNSIG 83

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.

Pssm-ID: 409389 [Multi-domain] Cd Length: 87 Bit Score: 39.31 E-value: 9.93e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  132 GEDAVIVCDVVSSLP-PTIIWKHKGRDVILKKDVRFIVLSNNyLQIRGIKKTDEGTYRC 189
Cdd:cd05724    12 GEMAVLECSPPRGHPePTVSWRKDGQPLNLDNERVRIVDDGN-LLIAEARKSDEGTYKC 69

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.

Pssm-ID: 409368 Cd Length: 88 Bit Score: 39.36 E-value: 1.02e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  123 APTPQEFKEGEDAVIVCDVVSSLPPtIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEG 191
Cdd:cd04979     2 SFKQISVKEGDTVILSCSVKSNNAP-VTWIHNGKKVPRYRSPRLVLKTERGLLIRSAQEADAGVYECHS 69

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; 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. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.

Pssm-ID: 409406 [Multi-domain] Cd Length: 82 Bit Score: 39.11 E-value: 1.05e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568958938   52 ISWFSPNGEKLSPNQQRISVVwndDDSSTLTIYNANIDDAGIYKCVVTAEDGTQSeATVNVKI 114
Cdd:cd05748    24 VTWSKDGQPLKETGRVQIETT---ASSTSLVIKNAKRSDSGKYTLTLKNSAGEKS-ATINVKV 82

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.44 E-value: 1.05e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  906 PPATTVPDSNSVPAGQATPSKGVTASssspasapkvaplvdlsdTPTSAPSASNLSSTVLANQGAVLSPSTPASAGETSK 985
Cdd:PRK07764  609 PEEAARPAAPAAPAAPAAPAPAGAAA------------------APAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  986 APPASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGtvknppeAATAPASPKSKAATTNPSQg 1065
Cdd:PRK07764  671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQ-------AAQGASAPSPAADDPVPLP- 742

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1066 edlkmdegnfktPDIDLAKDVFAALGSPAPATGASGQASELAPSTADSAVPPAPAktekgpVETKSEPPESEAKPAPTEV 1145
Cdd:PRK07764  743 ------------PEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEM------AEDDAPSMDDEDRRDAEEV 804

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.

Pssm-ID: 409560 [Multi-domain] Cd Length: 88 Bit Score: 39.15 E-value: 1.08e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  310 KITYVENQTAMELEEQVTLTCEASGDPIPSITWrtstrnisseekaswtrpekqetLDGHMVVRSHARVS-----SLTLK 384
Cdd:cd20968     1 KITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSW-----------------------IKGDDLIKENNRIAvlesgSLRIH 57

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568958938  385 SIQYTDAGEYICTASNTIGQD-SQSMYLEVQ 414
Cdd:cd20968    58 NVQKEDAGQYRCVAKNSLGIAySKPVTIEVE 88

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;

Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 43.34 E-value: 1.16e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  944 LVDLSDTPTSAPSASN-LSSTVLANQGAVLSPSTPASAGETSKAPPASKASPAPTPTPAGaasplaavaapaTDAPQAKQ 1022
Cdd:PRK12270   33 FADYGPGSTAAPTAAAaAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAA------------AAAPAAPP 100

                          90       100
                  ....*....|....*....|....*...
gi 568958938 1023 EAPSTKGPDPEPTQPGTVK-NPPEAATA 1049
Cdd:PRK12270  101 AAAAAAAPAAAAVEDEVTPlRGAAAAVA 128

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.

Pssm-ID: 409396 [Multi-domain] Cd Length: 94 Bit Score: 39.31 E-value: 1.24e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  324 EQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTRPEKQETLdghmVVRSHARVSSltlksiQYTdaGEYICTASNTIG 403
Cdd:cd05733    17 DNITIKCEAKGNPQPTFRWTKDGKFFDPAKDPRVSMRRRSGTL----VIDNHNGGPE------DYQ--GEYQCYASNELG 84

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 38.75 E-value: 1.32e-03

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568958938    670 KQDDGGSPIRHYLVKYRAKlASEWKpEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKS 730
Cdd:smart00060   25 PDDGITGYIVGYRVEYREE-GSEWK-EVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83

Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of human neurofascin (NF). NF 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 a cytoplasmic domain. NF has many alternatively spliced isoforms having different temporal expression patterns during development. NF participates in axon subcellular targeting and synapse formation, however little is known of the functions of the different isoforms. 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.

Pssm-ID: 409459 Cd Length: 95 Bit Score: 39.19 E-value: 1.36e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  212 PTVqARQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEedDEKHIFSDDSSELTIRNVDKND----EAEYV 287
Cdd:cd05875     1 PTI-TKQSAKDYIVDPRDNILIECEAKGNPVPTFHWTRNGKFFNVAK--DPRVSMRRRSGTLVIDFRGGGRpedyEGEYQ 77

                          90
                  ....*....|....*...
gi 568958938  288 CIAENKAGEQDAS-IHLK 304
Cdd:cd05875    78 CFARNKFGTALSNkIRLQ 95

NADH-quinone oxidoreductase subunit E;

Pssm-ID: 237082 [Multi-domain] Cd Length: 400 Bit Score: 42.48 E-value: 1.41e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  953 SAPSASNLSSTVLANQGAVLsPSTPASAGETSKAPPASKASPAPTP---TPAGAASPLAAVAAPATDAPQAKQEAPSTKG 1029
Cdd:PRK12373  209 SKALAEDIGDTVKRIDGTEV-PLLAPWQGDAAPVPPSEAARPKSADaetNAALKTPATAPKAAAKNAKAPEAQPVSGTAA 287

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568958938 1030 PDPEPTQPGTVKNPPEAATAPASPKSkAATTNPSQGEDLKMDEG 1073
Cdd:PRK12373  288 AEPAPKEAAKAAAAAAKPALEDKPRP-LGIARPGGADDLKLISG 330

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 1.49e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  966 ANQGAVLSPSTPASAGETSKAPPASK---ASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKN 1042
Cdd:PRK07764  404 AAPAAAPAPAAAAPAAAAAPAPAAAPqpaPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPA 483

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568958938 1043 P---PEAATAPASPKSKAATTNPSQGEDLKM 1070
Cdd:PRK07764  484 PpaaPAPAAAPAAPAAPAAPAGADDAATLRE 514

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.

Pssm-ID: 143207 [Multi-domain] Cd Length: 95 Bit Score: 39.14 E-value: 1.50e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   33 VGESKFFLCQVAGdAKDKDISWfSPNGEKLSPNQQRISVvwnDDDSSTLTIYNANIDDAGIYKCVVTAEDGtQSEATVNV 112
Cdd:cd05730    17 LGQSVTLACDADG-FPEPTMTW-TKDGEPIESGEEKYSF---NEDGSEMTILDVDKLDEAEYTCIAENKAG-EQEAEIHL 90


                  ....*
gi 568958938  113 KIFQK 117
Cdd:cd05730    91 KVFAK 95

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.

Pssm-ID: 143222 [Multi-domain] Cd Length: 74 Bit Score: 38.38 E-value: 1.59e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  131 EGEDAVIVCDVVSSLPPTIIWKHKGRDviLKKDVRFIVLSNNYLQIRGIKKTDEGTYRCE 190
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAWTKGGSQ--LSVDRRHLVLSSGTLRISRVALHDQGQYECQ 58

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. 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 Lingo-1 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.

Pssm-ID: 409561 Cd Length: 92 Bit Score: 38.91 E-value: 1.73e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  131 EGEDAVIVCDVVSSLPPTIIWKHKGRD-VILKKDVRFIVLSNNYLQIRGIKKTDEGTYRC 189
Cdd:cd20969    16 EGHTVQFVCRADGDPPPAILWLSPRKHlVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLC 75

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.

Pssm-ID: 409355 [Multi-domain] Cd Length: 111 Bit Score: 39.24 E-value: 1.80e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   26 PSQGEISVGESKFFLCQVAGDAKDKDISWF--------------SPNGEKLSPN-QQRISVVWNDDDSSTLTIYNANIDD 90
Cdd:cd00099     5 PRSLSVQEGESVTLSCEVSSSFSSTYIYWYrqkpgqgpefliylSSSKGKTKGGvPGRFSGSRDGTSSFSLTISNLQPED 84


                  ....*....
gi 568958938   91 AGIYKCVVT 99
Cdd:cd00099    85 SGTYYCAVS 93

Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of the collagenase stimulatory factor, basigin-1 (BSG1; also known as Cluster of Differentiation 147 (CD147) and Extracellular Matrix Metalloproteinase Inducer (EMMPRIN)) and similar proteins. CD147 is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It is expressed in nearly all cells including platelets and fibroblasts and is involved in inflammatory diseases, and cancer progression. CD147 is highly expressed in several cancers and used as a prognostic marker. The two primary isoforms of CD147 that are related to cancer progression have been identified: CD147 Ig1-Ig2 (also called Basigin-2) that is ubiquitously expressed in most tissues and CD147 Ig0-Ig1-Ig2 (also called Basigin-1) that is retinal specific and implicated in retinoblastoma. Studies showed that CD147 Ig0 domain is a potent stimulator of interleukin-6 and suggest that the CD147 Ig0 dimer is the functional unit required for activity.

Pssm-ID: 409534 Cd Length: 116 Bit Score: 39.56 E-value: 1.81e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  419 LQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDG--------QLLPSSNYSNIKI---YNTPSASYLEVTPDSENDFGN 487
Cdd:cd20940     4 IKSPLSQQRLVGDSVELHCEAVGSPIPEIQWWFEGqepneicsQLWDGARLDRVHInatYHQHATSTISIDNLTEEDTGT 83


                  ....*..
gi 568958938  488 YNCTAVN 494
Cdd:cd20940    84 YECRASN 90

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth 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.

Pssm-ID: 409358 [Multi-domain] Cd Length: 89 Bit Score: 38.60 E-value: 1.83e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  130 KEGEDAVIVCDVVSSLPPTIIWKhKGrDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEG 191
Cdd:cd04969    15 AKGGDVIIECKPKASPKPTISWS-KG-TELLTNSSRICILPDGSLKIKNVTKSDEGKYTCFA 74

flagellar biosynthesis protein FlhF;

Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 42.28 E-value: 1.84e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  909 TTVPDSNSVPAGQATPSKGVTASSSSPASAPKVAPLVDLSDTPTSAPSASNLSSTVLANQGAVLSPSTPASA---GETSK 985
Cdd:PRK12727   57 TARSDTPATAAAPAPAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAAEDMIAAMALRQPVSVPRQAPAAApvrAASIP 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  986 APPASKASPAPTPTPAgaasplAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKNPPeaATAPASPKSKAATTNPSQG 1065
Cdd:PRK12727  137 SPAAQALAHAAAVRTA------PRQEHALSAVPEQLFADFLTTAPVPRAPVQAPVVAAP--APVPAIAAALAAHAAYAQD 208

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568958938 1066 EDLKMDEgnfktPDIDLAKDVFAALGSPA--PATGASGQASELApstADSAVPPAPAKTEK 1124
Cdd:PRK12727  209 DDEQLDD-----DGFDLDDALPQILPPAAlpPIVVAPAAPAALA---AVAAAAPAPQNDEE 261

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.

Pssm-ID: 409419 Cd Length: 99 Bit Score: 38.78 E-value: 1.87e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGEPIEneEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKVFA 307
Cdd:cd05762    16 GESVELFCKVTGTQPITCTWMKFRKQIQ--EGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVVD 93


                  ..
gi 568958938  308 KP 309
Cdd:cd05762    94 KP 95

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.

Pssm-ID: 409550 [Multi-domain] Cd Length: 89 Bit Score: 38.32 E-value: 1.98e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   34 GESKFFLCQVAGDAKDKdISWFSpNGEKLsPNQQRISVVWNdddsSTLTIYNAN-IDDAGIYKCVVTAEDGTQSEATVNV 112
Cdd:cd20958    15 GQTLRLHCPVAGYPISS-ITWEK-DGRRL-PLNHRQRVFPN----GTLVIENVQrSSDEGEYTCTARNQQGQSASRSVFV 87


                  ..
gi 568958938  113 KI 114
Cdd:cd20958    88 KV 89

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.

Pssm-ID: 409355 [Multi-domain] Cd Length: 111 Bit Score: 39.24 E-value: 2.04e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  217 RQSIVNATANLGQSVTLVCDADG-FPEPTMSW--TKDGEPIE----------NEEEDDEKHI----FSDDSSELTIRNVD 279
Cdd:cd00099     2 TQSPRSLSVQEGESVTLSCEVSSsFSSTYIYWyrQKPGQGPEfliylssskgKTKGGVPGRFsgsrDGTSSFSLTISNLQ 81

                          90
                  ....*....|.
gi 568958938  280 KNDEAEYVCIA 290
Cdd:cd00099    82 PEDSGTYYCAV 92

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 2.08e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  968 QGAVLSPS-TPASAGETSKAPPASKASPAPTPTPAgAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKNPPEA 1046
Cdd:PHA03247  249 RGDIAAPApPPVVGEGADRAPETARGATGPPPPPE-AAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAEEE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1047 A--------TAPAS----------PKSKAAT-TNPSQGEDLKMDEGNFKTPDIDL--------AKDVFAALG----SPAP 1095
Cdd:PHA03247  328 DdedgamevVSPLPrprqhyplgfPKRRRPTwTPPSSLEDLSAGRHHPKRASLPTrkrrsarhAATPFARGPggddQTRP 407

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938 1096 ATGASGQASELAPSTADSAVPPAPAktekGPVETkSEPPESEAkPAPTEVKTVPNDATQTKE 1157
Cdd:PHA03247  408 AAPVPASVPTPAPTPVPASAPPPPA----TPLPS-AEPGSDDG-PAPPPERQPPAPATEPAP 463

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.

Pssm-ID: 409391 [Multi-domain] Cd Length: 98 Bit Score: 38.78 E-value: 2.16e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  120 FKNAPTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRDVIL------KKDVRFIVLSNNYLQIRGIKKTDEGTYRCE--- 190
Cdd:cd05726     2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNLLfpyqppQPSSRFSVSPTGDLTITNVQRSDVGYYICQaln 81

                          90
                  ....*....|....*.
gi 568958938  191 --GRILARGEINFKDI 204
Cdd:cd05726    82 vaGSILAKAQLEVTDV 97

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.

Pssm-ID: 409444 Cd Length: 105 Bit Score: 38.79 E-value: 2.46e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  326 VTLTCEASGDPIPSITWrtsTRNIssEEKASWTRPEKQ---ETLDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTI 402
Cdd:cd05858    19 AEFVCKVYSDAQPHIQW---LKHV--EKNGSKYGPDGLpyvEVLKTAGVNTTDKEIEVLYLRNVTFEDAGEYTCLAGNSI 93

                          90
                  ....*....|.
gi 568958938  403 GQDSQSMYLEV 413
Cdd:cd05858    94 GISHHSAWLTV 104

First immunoglobulin (Ig) domain of contactin-1; 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-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. 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.

Pssm-ID: 409436 [Multi-domain] Cd Length: 95 Bit Score: 38.40 E-value: 2.65e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  322 LEEQVTLTCEASGDPIPSITWRTSTRNISSEEkaswtrpEKQETLDGHMVVRSHARvssltlksiqYTDAGEYICTASNT 401
Cdd:cd05849    18 TEGKVSVNCRARANPFPIYKWRKNNLDIDLTN-------DRYSMVGGNLVINNPDK----------YKDAGRYVCIVSNI 80


                  ..
gi 568958938  402 IG 403
Cdd:cd05849    81 YG 82

Class I major histocompatibility complex (MHC) alpha chain, alpha3 immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class I alpha chain. Class I MHC proteins bind antigenic peptide fragments and present them to CD8+ T lymphocytes. Class I molecules consist of a transmembrane alpha chain and a small chain called the beta-2-microglobulin. The alpha chain contains three extracellular domains, two of which fold together to form the peptide-binding cleft (alpha1 and alpha2), and one which has an Ig fold (alpha3). Peptide binding to class I molecules occurs in the endoplasmic reticulum (ER) and involves both chaperones and dedicated factors to assist in peptide loading. Class I MHC molecules are expressed on most nucleated cells.

Pssm-ID: 409495 Cd Length: 92 Bit Score: 37.98 E-value: 2.89e-03

                          10        20        30
                  ....*....|....*....|....*....|..
gi 568958938  230 SVTLVCDADGF--PEPTMSWTKDGEPIENEEE 259
Cdd:cd07698    16 ESTLRCWALGFypAEITLTWQRDGEDQTQDME 47

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.

Pssm-ID: 409541 [Multi-domain] Cd Length: 89 Bit Score: 38.08 E-value: 2.93e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  429 EGNQVNITCEVFAYPSATISWFRDGQLLpSSNYSNIKIYNTpSASYLEVTPDSENDFGNYNCTAVNRIGQES 500
Cdd:cd20949    13 EGQSATILCEVKGEPQPNVTWHFNGQPI-SASVADMSKYRI-LADGLLINKVTQDDTGEYTCRAYQVNSIAS 82

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

Pssm-ID: 462230 Cd Length: 109 Bit Score: 38.59 E-value: 3.01e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   322 LEEQVTLTCEASG---DPIPSITW-RTSTRNISSEEKASWTRPEKQETLDGHMVVRSHARVS--SLTLKSIQYTDAGEYI 395
Cdd:pfam07686   10 LGGSVTLPCTYSSsmsEASTSVYWyRQPPGKGPTFLIAYYSNGSEEGVKKGRFSGRGDPSNGdgSLTIQNLTLSDSGTYT 89

                           90
                   ....*....|....*....
gi 568958938   396 C-TASNTIGQDSQSMYLEV 413
Cdd:pfam07686   90 CaVIPSGEGVFGKGTRLTV 108

Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of the collagenase stimulatory factor, basigin-1 (BSG1; also known as Cluster of Differentiation 147 (CD147) and Extracellular Matrix Metalloproteinase Inducer (EMMPRIN)) and similar proteins. CD147 is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It is expressed in nearly all cells including platelets and fibroblasts and is involved in inflammatory diseases, and cancer progression. CD147 is highly expressed in several cancers and used as a prognostic marker. The two primary isoforms of CD147 that are related to cancer progression have been identified: CD147 Ig1-Ig2 (also called Basigin-2) that is ubiquitously expressed in most tissues and CD147 Ig0-Ig1-Ig2 (also called Basigin-1) that is retinal specific and implicated in retinoblastoma. Studies showed that CD147 Ig0 domain is a potent stimulator of interleukin-6 and suggest that the CD147 Ig0 dimer is the functional unit required for activity.

Pssm-ID: 409534 Cd Length: 116 Bit Score: 38.79 E-value: 3.08e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  322 LEEQVTLTCEASGDPIPSITWRTSTrNISSEEKASWTRPEKQETLDGHMVVRSHArVSSLTLKSIQYTDAGEYICTASN 400
Cdd:cd20940    14 VGDSVELHCEAVGSPIPEIQWWFEG-QEPNEICSQLWDGARLDRVHINATYHQHA-TSTISIDNLTEEDTGTYECRASN 90

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (also known as Flt-1), VEGFR-2 (also known as KDR or Flk-1) and VEGFR-3 (also known as Flt-4). VEGF_A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF, VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-2 and -1 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth.

Pssm-ID: 409448 Cd Length: 102 Bit Score: 38.19 E-value: 3.09e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568958938  357 WTRPEKQETLDGHMVVR-----SHAR--VSSLTLKSIQYTDAGEYICTASNTIGQDSQSMYLEV 413
Cdd:cd05862    37 WDYPGKKEQRRASVRRRrkqqsSEATefSSTLTIDNVTLSDKGLYTCAASSGPMFKKNSTSVIV 100

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.79 E-value: 3.32e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  905 APPATTVPDSNSVPAGQATPSKGVTASSSSPASAPKVAPLVDLSDTPTSAPSASNLSSTVLANQGAVLSPSTPASAGets 984
Cdd:PRK12323  400 AAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAA--- 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  985 kAPPASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPT-QPGTVKNPPEAATAPASPKSKAATTNPS 1063
Cdd:PRK12323  477 -AAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIpDPATADPDDAFETLAPAPAAAPAPRAAA 555

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568958938 1064 QGEDL----KMDEGNFKTPDIDLAKdvFAALGSPAPATGASGQ---ASELAPSTADSAV--PPAPAKTEKGPVE 1128
Cdd:PRK12323  556 ATEPVvaprPPRASASGLPDMFDGD--WPALAARLPVRGLAQQlarQSELAGVEGDTVRlrVPVPALAEAEVVE 627

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 41.62 E-value: 3.34e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  905 APPATTVPDSNSVPAGQATPSKGV-TASSSSPASAPKVAPLVDLSDTPTSAPSASNLSSTVLANQGAVLSPSTPASAGET 983
Cdd:PRK08691  359 APLAAASCDANAVIENTELQSPSAqTAEKETAAKKPQPRPEAETAQTPVQTASAAAMPSEGKTAGPVSNQENNDVPPWED 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  984 SKAPPASKASPAPTPTP----AGAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKNPPEAAT-APASPKSKAA 1058
Cdd:PRK08691  439 APDEAQTAAGTAQTSAKsiqtASEAETPPENQVSKNKAADNETDAPLSEVPSENPIQATPNDEAVETETfAHEAPAEPFY 518

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568958938 1059 TTNPSQGEDLKMDEGNFKTPDIDLAKDVFAALGSP---APATGASGQASELAPS 1109
Cdd:PRK08691  519 GYGFPDNDCPPEDGAEIPPPDWEHAAPADTAGGGAdeeAEAGGIGGNNTPSAPP 572

DNA translocase FtsK; Provisional

Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.61 E-value: 3.38e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  951 PTSAPSASNLSSTVLANQGAVLSPSTPASAGETSKAPPASKASPAP---TPTPAGAASPLAAVAAPATDAPQAKQEAPST 1027
Cdd:PRK10263  319 PVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPgpqTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQ 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1028 kgpdpEPTQPGTVKNPPEAATAPASPKSKAATTNPSQGEDLKMDEGNFKTPDIDLAKDvfaalGSPAPATGASGQASELA 1107
Cdd:PRK10263  399 -----QPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEE-----QQSTFAPQSTYQTEQTY 468

                         170       180       190
                  ....*....|....*....|....*....|....
gi 568958938 1108 PSTADSAVPPAPAKTEKGPVETKSEPPESEAKPA 1141
Cdd:PRK10263  469 QQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPA 502

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.

Pssm-ID: 143224 [Multi-domain] Cd Length: 92 Bit Score: 38.11 E-value: 3.43e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  131 EGEDAVIVCDVVSSLPPTIIWKHKGRdvILKKDVRFIVLSNNY---LQIRGIKKTDEGTY 187
Cdd:cd05747    17 EGESARFSCDVDGEPAPTVTWMREGQ--IIVSSQRHQITSTEYkstFEISKVQMSDEGNY 74

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-2 (KDR/Flk-1) is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A; VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGF-A also interacts with VEGFR-1, which it binds more strongly than VEGFR-2. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. 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.

Pssm-ID: 409450 Cd Length: 89 Bit Score: 37.99 E-value: 3.45e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  430 GNQVNITCEVFAYPSATISWFRDGQLLPssnySNIKIYntpSASYLEVTPDSENDFGNYNCTAVNRIGQE 499
Cdd:cd05864    17 GERVRIPVKYLGYPPPEIKWYKNGIPIE----SNHTIK---AGHVLTIMEVTEKDAGNYTVVLTNPISKE 79

CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, and delta chains, and CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, epsilon, and mu chains; member of the C1-set of I; The members here are composed of the third and fourth immunoglobulin constant domain (IgC) of alpha, delta, gamma and alpha, epsilon, and mu heavy chains, respectively. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.

Pssm-ID: 409425 Cd Length: 105 Bit Score: 38.09 E-value: 3.69e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568958938  225 ANLGQSVTLVCDADGF--PEPTMSWTKDGEPIE-------NEEEDDEKHIFSddSSELTIRNVDKNDEAEYVCIA 290
Cdd:cd05768    13 LSLNETVTLTCLVKGFypEDIFVSWLQNGEPLPsadykttAPVPESDGSFFV--YSKLNVSTADWNSGDVFSCVV 85

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 41.39 E-value: 3.69e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  904 IAPPATTVPDSNSVPAGQATPSKGVTASSSSPASAPKVAplvdlSDTPTSAPSASNLSSTV-LANQGAVLSPSTPASAGE 982
Cdd:PRK07994  365 LPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPP-----ASAPQQAPAVPLPETTSqLLAARQQLQRAQGATKAK 439

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  983 TSKAPPASKASPAPTPTPAgaaSPLAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKNPPEAATAPASPK 1054
Cdd:PRK07994  440 KSEPAAASRARPVNSALER---LASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEK 508

DNA polymerase III subunits gamma and tau; Provisional

Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 41.24 E-value: 3.96e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  961 SSTVLANQGAVLSPSTPASAGETSKAPPASKAS-PAPTPTPAGAASPLAAVAAPAtdaPQAKQEAPSTKGPDPEPTQPGT 1039
Cdd:PRK14951  367 AAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAaPAPAAAPAAAASAPAAPPAAA---PPAPVAAPAAAAPAAAPAAAPA 443

                          90
                  ....*....|....*...
gi 568958938 1040 VKNPPEAATAPASPKSKA 1057
Cdd:PRK14951  444 AVALAPAPPAQAAPETVA 461

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

Pssm-ID: 464026 [Multi-domain] Cd Length: 79 Bit Score: 37.37 E-value: 3.98e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938    24 IVPSQGEISVGESKFFLCQVAGDAKDKdISWFSPNgeklspnqqriSVVWNDDDSSTLtiyNANIDDAGIYKCVVTAEDG 103
Cdd:pfam13895    4 LTPSPTVVTEGEPVTLTCSAPGNPPPS-YTWYKDG-----------SAISSSPNFFTL---SVSAEDSGTYTCVARNGRG 68

                           90
                   ....*....|.
gi 568958938   104 TQSEATVNVKI 114
Cdd:pfam13895   69 GKVSNPVELTV 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.

Pssm-ID: 409476 Cd Length: 93 Bit Score: 37.66 E-value: 4.06e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   30 EISVGESKFFLCQVAGDAKDKDISWFSPNGEKLSPNQQRISVVWNDDDSSTLTIYNANIDDAGIYKCVVTAEDGTQSeAT 109
Cdd:cd05895    10 EVAAGSKLVLRCETSSEYPSLRFKWFKNGKEINRKNKPENIKIQKKKKKSELRINKASLADSGEYMCKVSSKLGNDS-AS 88


                  ....*
gi 568958938  110 VNVKI 114
Cdd:cd05895    89 ANVTI 93

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.

Pssm-ID: 409562 [Multi-domain] Cd Length: 92 Bit Score: 37.87 E-value: 4.07e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938   25 VPSQGE---ISVGESKFFLCQVAGdAKDKDISWFSPNGEKLSPNQQRISVVWNDddssTLTIYNANIDDAGIYKCVVT-- 99
Cdd:cd20970     5 TPQPSFtvtAREGENATFMCRAEG-SPEPEISWTRNGNLIIEFNTRYIVRENGT----TLTIRNIRRSDMGIYLCIASng 79

                          90
                  ....*....|...
gi 568958938  100 AEDGTQSEATVNV 112
Cdd:cd20970    80 VPGSVEKRITLQV 92

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. 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.

Pssm-ID: 409412 Cd Length: 85 Bit Score: 37.54 E-value: 4.27e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  324 EQVTLTCEA-SGDPIPSITWrtsTRNisseekaswtrpekqetlDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTI 402
Cdd:cd05754    17 ADVSFICRAkSKSPAYTLVW---TRV------------------NGTLPSRAMDFNGILTIRNVQLSDAGTYVCTGSNML 75


                  ...
gi 568958938  403 GQD 405
Cdd:cd05754    76 DTD 78

IL-1 receptor-like protein; Provisional

Pssm-ID: 165173 [Multi-domain] Cd Length: 227 Bit Score: 39.90 E-value: 4.54e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  170 SNNyLQIRGIKKTDEGTYRCE---GRILARGEINFkdiqvivnvpptvQARQSIVNATANLGQSVTLVC-DADG----FP 241
Cdd:PHA02826   97 SEN-LWIGNVINIDEGIYICTissGNICEESTIRL-------------TFDSGTINYQFNSGKDSKLHCyGTDGisstFK 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568958938  242 EPTMSWTKDGEPIENeeedDEKHIFSDDSSELTIRNVDKNDEAEYVC 288
Cdd:PHA02826  163 DYTLTWYKNGNIVLY----TDRIQLRNNNSTLVIKSATHDDSGIYTC 205

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.

Pssm-ID: 409356 [Multi-domain] Cd Length: 96 Bit Score: 37.61 E-value: 4.57e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938  432 QVNITCEVFAYPSATISWFRDG---QLLPSSNYSNIkiyntpSASYLEVTPDSENDFGNYNCTAVNRIG 497
Cdd:cd04967    21 KVALNCRARANPVPSYRWLMNGteiDLESDYRYSLV------DGTLVISNPSKAKDAGHYQCLATNTVG 83

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.

Pssm-ID: 409443 [Multi-domain] Cd Length: 95 Bit Score: 37.53 E-value: 4.78e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  326 VTLTCEASGDPIPSITWRTSTRNISSEEKaswtrpekqetLDGHMVVRSHarvSSLTLKSIQYTDAGEYICTASNTIGQD 405
Cdd:cd05857    22 VKFRCPAAGNPTPTMRWLKNGKEFKQEHR-----------IGGYKVRNQH---WSLIMESVVPSDKGNYTCVVENEYGSI 87


                  ....*...
gi 568958938  406 SQSMYLEV 413
Cdd:cd05857    88 NHTYHLDV 95

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. 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.

Pssm-ID: 409412 Cd Length: 85 Bit Score: 37.15 E-value: 4.99e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  122 NAPTPQEFKEGEDAVIVCDVVSSLP-PTIIW-KHKGRDVILKKDvrfivlSNNYLQIRGIKKTDEGTYRCEG 191
Cdd:cd05754     6 EEPRSQEVRPGADVSFICRAKSKSPaYTLVWtRVNGTLPSRAMD------FNGILTIRNVQLSDAGTYVCTG 71

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.

Pssm-ID: 409570 [Multi-domain] Cd Length: 88 Bit Score: 37.37 E-value: 5.04e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  429 EGNQVNITCEVFAYPSATISWFRDGQLLpSSNYSNIKIYNtpsaSYLEVTPDSENDFGNYNCTAVNRIGQESLEFILV 506
Cdd:cd20978    15 GGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVED----GTLTIINVQPEDTGYYGCVATNEIGDIYTETLLH 87

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.

Pssm-ID: 143278 [Multi-domain] Cd Length: 98 Bit Score: 37.65 E-value: 5.22e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  425 VYTWEGNQVNITCEVFAYPSATISWFR--DGQLLPSSNYS---NIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIG-- 497
Cdd:cd05870    11 ETTVENGAATLSCKAEGEPIPEITWKRasDGHTFSEGDKSpdgRIEVKGQHGESSLHIKDVKLSDSGRYDCEAASRIGgh 90


                  ....
gi 568958938  498 QESL 501
Cdd:cd05870    91 QKSM 94

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.

Pssm-ID: 409551 Cd Length: 94 Bit Score: 37.47 E-value: 5.29e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  324 EQVTLTCEAS-GDPIPSITWRTSTRNISSEEKASWTRpekqetLDghmvvrshARVSSLTLKSIQYTDAGEYICTASNTI 402
Cdd:cd20959    18 MRAQLHCGVPgGDLPLNIRWTLDGQPISDDLGITVSR------LG--------RRSSILSIDSLEASHAGNYTCHARNSA 83

                          90
                  ....*....|.
gi 568958938  403 GQDSQSMYLEV 413
Cdd:cd20959    84 GSASYTAPLTV 94

Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F (also known as LAR), type IIa; member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains. Included in this group is Drosophila LAR (DLAR).

Pssm-ID: 409401 Cd Length: 82 Bit Score: 37.19 E-value: 5.41e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  210 VPPTvqarqsivNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEddekhiFSDDSSELTIRNVdkNDEAEYVCI 289
Cdd:cd05739     2 IPPS--------NHEVMPGGSVNLTCVAVGAPMPYVKWMKGGEELTKEDE------MPVGRNVLELTNI--YESANYTCV 65

                          90
                  ....*....|....*.
gi 568958938  290 AENKAGEQDASIHLKV 305
Cdd:cd05739    66 AISSLGMIEATAQVTV 81

Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains; The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.

Pssm-ID: 409402 [Multi-domain] Cd Length: 89 Bit Score: 37.37 E-value: 5.73e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568958938  229 QSVTLVCDADGfPEPTMSWTKDGEPIEneeeDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAEN 292
Cdd:cd05740    16 DAVTLTCEPET-QNTSYLWWFNGQSLP----VTPRLTLSNGNRTLTLLNVTREDAGAYQCEISN 74

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.

Pssm-ID: 409476 Cd Length: 93 Bit Score: 37.28 E-value: 5.95e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  309 PKITYVENQTAMELEEQVtLTCEASGD-PIPSITWRTSTRNISSEEKaswtrPEkqetldgHMVVRSHARVSSLTLKSIQ 387
Cdd:cd05895     1 PKLKEMKSQEVAAGSKLV-LRCETSSEyPSLRFKWFKNGKEINRKNK-----PE-------NIKIQKKKKKSELRINKAS 67

                          90       100
                  ....*....|....*....|.
gi 568958938  388 YTDAGEYICTASNTIGQDSQS 408
Cdd:cd05895    68 LADSGEYMCKVSSKLGNDSAS 88

sporozoite surface protein 2 (SSP2); Provisional

Pssm-ID: 240420 [Multi-domain] Cd Length: 576 Bit Score: 40.72 E-value: 6.43e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1025 PSTKGPDPEPTQPGT------VKNPPEAATAPASPKSKAAttNPSQGEDLKMDEGNFKTPDIDLAKDVFAALgsPAPATG 1098
Cdd:PTZ00441  292 PAPVPPTPEDDNPRPtddefaVPNFNEGLDVPDNPQDPVP--PPNEGKDGNPNEENLFPPGDDEVPDESNVP--PNPPNV 367

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568958938 1099 ASGQASELAPSTADSAVPPAPAKTEKGPvetksEPPESEAKPAPTEVKTVPNDATQTKENESK 1161
Cdd:PTZ00441  368 PGGSNSEFSSDVENPPNPPNPDIPEQEP-----NIPEDSNKEVPEDVPMEPEDDRDNNFNEPK 425

capsid maturational protease; Provisional

Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 40.75 E-value: 6.62e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  944 LVDLSDTPTSAPSASNLSSTVLANQGAVLSPS--TPASAGETSK-APPASKASPAPTPTPAGAASPLAAVAAPATDAPQA 1020
Cdd:PHA03369  348 LKTASLTAPSRVLAAAAKVAVIAAPQTHTGPAdrQRPQRPDGIPySVPARSPMTAYPPVPQFCGDPGLVSPYNPQSPGTS 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1021 KQEAPSTKGPdPEPTQPGTVKNPPEAATAPASPKSKAATTNPSQGEDLKMDEGNFKTpDIDLAKDVFAALGSPAPATGAS 1100
Cdd:PHA03369  428 YGPEPVGPVP-PQPTNPYVMPISMANMVYPGHPQEHGHERKRKRGGELKEELIETLK-LVKKLKEEQESLAKELEATAHK 505

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568958938 1101 GQASELAPSTADSAVPPAPAKTEKGPVETKSEPPESEAKPAPT 1143
Cdd:PHA03369  506 SEIKKIAESEFKNAGAKTAAANIEPNCSADAAAPATKRARPET 548

Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains; The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.

Pssm-ID: 409402 [Multi-domain] Cd Length: 89 Bit Score: 36.99 E-value: 6.90e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  308 KPKITyVENQTAMELEEQVTLTCEASgDPIPSITWRTSTRNISSEEKASWTRPEKQetldghmvvrsharvssLTLKSIQ 387
Cdd:cd05740     1 KPFIS-SNNSNPVEDKDAVTLTCEPE-TQNTSYLWWFNGQSLPVTPRLTLSNGNRT-----------------LTLLNVT 61

                          90
                  ....*....|....*
gi 568958938  388 YTDAGEYICTASNTI 402
Cdd:cd05740    62 REDAGAYQCEISNPV 76

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.

Pssm-ID: 409422 [Multi-domain] Cd Length: 95 Bit Score: 37.14 E-value: 7.11e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568958938  122 NAPTPQEFKEGEDAVIVCDVVSSLPPTIIWK---HKGRDVILKKD-VR--FIVLSNNYLQIRGIKKTDEGTYRCEGR 192
Cdd:cd05765     5 NSPTHQTVKVGETASFHCDVTGRPQPEITWEkqvPGKENLIMRPNhVRgnVVVTNIGQLVIYNAQPQDAGLYTCTAR 81

Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule). NrCAM 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. NrCAM is primarily expressed in the nervous system.

Pssm-ID: 409458 Cd Length: 95 Bit Score: 37.27 E-value: 7.31e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  212 PTVqARQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEedDEKHIFSDDSSELTIR--NVDKND--EAEYV 287
Cdd:cd05874     1 PTI-THQSPKDYIVDPRENIVIQCEAKGKPPPSFSWTRNGTHFDIDK--DPKVTMKPNTGTLVINimNGEKAEayEGVYQ 77


                  ....*...
gi 568958938  288 CIAENKAG 295
Cdd:cd05874    78 CTARNERG 85

Immunoglobulin domain of Cluster of Differentiation (CD) 1; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin domain of Cluster of Differentiation (CD) 1. CD1 family of transmembrane glycoproteins, are structurally related to the major histocompatibility complex (MHC) proteins and form heterodimers with beta-2-microglobulin. They mediate the presentation of primarily lipid and glycolipid antigens of self or microbial origin to T cells. The human genome contains five CD1 family genes (CD1a, CD1b, CD1c, CD1d, and CD1e) organized in a cluster on chromosome 1. The CD1 family members are thought to differ in their cellular localization and specificity for particular lipid ligands. CD1a localizes to the plasma membrane and to recycling vesicles of the early endocytic system. Alternative splicing results in multiple transcript variants. Immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class I alpha chain. Class I MHC proteins bind antigenic peptide fragments and present them to CD8+ T lymphocytes. Class I molecules consist of a transmembrane alpha chain and a small chain called the beta-2-microglobulin. The alpha chain contains three extracellular domains, two of which fold together to form the peptide-binding cleft (alpha1 and alpha2), and one which has an Ig fold (alpha3). Peptide binding to class I molecules occurs in the endoplasmic reticulum (ER) and involves both chaperones and dedicated factors to assist in peptide loading. Class I MHC molecules are expressed on most nucleated cells. C1-set Ig domains have one beta sheet that is formed by strands A, B, E, and D and the other strands by G, F, C, and C'.

Pssm-ID: 409620 Cd Length: 93 Bit Score: 36.92 E-value: 7.36e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  210 VPPTVqarqSIVNATANLGQSVTLVCDADGF-PEPT-MSWTKDGEPIENEEEDDEKHIFSDDSSELTIR-NVDKNDEAEY 286
Cdd:cd21029     1 VKPRV----RLSSRPSPGDGHLQLSCHVTGFyPRPIeVTWLRDGQEQMDGTQSGGILPNHDGTYQLRKTlDIAPGEGAGY 76


                  ..
gi 568958938  287 VC 288
Cdd:cd21029    77 SC 78

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.

Pssm-ID: 409437 [Multi-domain] Cd Length: 97 Bit Score: 37.21 E-value: 7.44e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  323 EEQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTRpekqetLDGHMVVRSharvssltlkSIQYTDAGEYICTASNTI 402
Cdd:cd05850    20 EEKVTLACRARASPPATYRWKMNGTELKMEPDSRYRL------VAGNLVISN----------PVKAKDAGSYQCLASNRR 83


                  .
gi 568958938  403 G 403
Cdd:cd05850    84 G 84

translocon at the inner envelope of chloroplast subunit 62; Provisional

Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 40.29 E-value: 7.70e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  964 VLANQGAVLSPSTPASAGETSK--APPASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGP----------- 1030
Cdd:PLN03209  305 VIAETTAPLTPMEELLAKIPSQrvPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPytayedlkppt 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938 1031 DPEPTQPGTVK---NPPEAATAPASPKSKAATTNPSQGEDLKMDEGNFKT-----PDIDLAKDVFAALGSPAPATGASGQ 1102
Cdd:PLN03209  385 SPIPTPPSSSPassKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKtrplsPYARYEDLKPPTSPSPTAPTGVSPS 464

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938 1103 ASELAPSTADSAVPPAPAKTEKGPVETKSEPPES------EAKP--APTEVKTVPNDATQTKENESKA 1162
Cdd:PLN03209  465 VSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSpyavydDLKPptSPSPAAPVGKVAPSSTNEVVKV 532

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 36.52 E-value: 7.81e-03

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568958938    230 SVTLVCDADGF-PEP-TMSWTKDGEPIENEEEDDEKhIFSDD-----SSELTIRNVDKNDEAEYVCIAE 291
Cdd:smart00407    1 KATLVCLVSGFyPPDiTVTWLRNGQEVTEGVSTTDP-LKNSDgtyflSSYLTVPASTWESGDVYTCQVT 68

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.

Pssm-ID: 409422 [Multi-domain] Cd Length: 95 Bit Score: 37.14 E-value: 7.99e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  224 TANLGQSVTLVCDADGFPEPTMSWtkdgepiENEEEDDEKHIFSDDS----------SELTIRNVDKNDEAEYVCIAENK 293
Cdd:cd05765    11 TVKVGETASFHCDVTGRPQPEITW-------EKQVPGKENLIMRPNHvrgnvvvtniGQLVIYNAQPQDAGLYTCTARNS 83

                          90
                  ....*....|..
gi 568958938  294 AGEQDASIHLKV 305
Cdd:cd05765    84 GGLLRANFPLSV 95

Fourth 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 fourth 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.

Pssm-ID: 409548 [Multi-domain] Cd Length: 96 Bit Score: 36.77 E-value: 8.54e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958938  430 GNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPSA---SYLEVTPDSENDFGNYNCTAVNRIGQ 498
Cdd:cd20956    16 GPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDYVTSDGdvvSYVNISSVRVEDGGEYTCTATNDVGS 87

DNA polymerase III subunits gamma and tau; Validated

Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.35 E-value: 8.77e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  905 APPATTVPDSNSVPAGQATPSKGVTASSSSPASAPKVAPLVDLSDT----PTSAPSASNLSSTVLANQGAVLSPSTPA-- 978
Cdd:PRK07764  620 APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGgdgwPAKAGGAAPAAPPPAPAPAAPAAPAGAApa 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  979 --SAGETSKAPPASKASPAPTPTPAGAASPLAAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVkNPPEAATAPASPksk 1056
Cdd:PRK07764  700 qpAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPA-PAPAAAPAAAPP--- 775

                         170       180       190
                  ....*....|....*....|....*....|....
gi 568958938 1057 aATTNPSQGEDLKMDEGNFKTPDIDLAKDVFAAL 1090
Cdd:PRK07764  776 -PSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMEL 808

IL-1 receptor-like protein; Provisional

Pssm-ID: 165173 [Multi-domain] Cd Length: 227 Bit Score: 39.13 E-value: 8.79e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568958938   48 KDKDISWFSpNGEKLsPNQQRISVvwnDDDSSTLTIYNANIDDAGIYKC 96
Cdd:PHA02826  162 KDYTLTWYK-NGNIV-LYTDRIQL---RNNNSTLVIKSATHDDSGIYTC 205

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-3 (Flt-4) binds two members of the VEGF family (VEGF-C and VEGF-D) and is involved in tumor angiogenesis and growth. 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.

Pssm-ID: 409449 Cd Length: 88 Bit Score: 36.45 E-value: 9.17e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568958938  419 LQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNysnikiyntpSASYLEVTPDSENDFGNYNCTAVNR 495
Cdd:cd05863     8 RKGPVIEATAGDELVKLPVKVAAYPPPEFQWYKDGKLISGKH----------SPHSLQIKDVTEASAGTYTLVLWNS 74

Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains; member of the C2-set IgSF domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), also known as CD66e (Cluster of Differentiation 66e), is a cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. Diseases associated with CEACAM5 include lung cancer and rectum cancer. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.

Pssm-ID: 409540 Cd Length: 76 Bit Score: 36.32 E-value: 9.37e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958938  228 GQSVTLVCDADGFPEPTMSWTKDGepieneeeddekhIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKV 305
Cdd:cd20948    10 GENLNLSCHAASNPPAQYSWTING-------------TFQTSSQELFLPAITENNEGTYTCSAHNSLTGKNISLVLSV 74

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.

Pssm-ID: 409355 [Multi-domain] Cd Length: 111 Bit Score: 37.31 E-value: 9.63e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958938  124 PTPQEFKEGEDAVIVCDVVSSLPPT----------------IIWKHKGRDVILKKDVRFIVLSNN----YLQIRGIKKTD 183
Cdd:cd00099     5 PRSLSVQEGESVTLSCEVSSSFSSTyiywyrqkpgqgpeflIYLSSSKGKTKGGVPGRFSGSRDGtssfSLTISNLQPED 84


                  ....*.
gi 568958938  184 EGTYRC 189
Cdd:cd00099    85 SGTYYC 90