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Conserved domains on  [gi|9055246|ref|NP_061211|]
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insulin-like growth factor-binding protein-like 1 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 147-252 3.54e-14

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.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 66.51  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246    147 PVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspegtEGLEELPGDHVNIAVqvrggpsDHETTSwILINPLR 226
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK--------DGQPLRSSDRFKVTY-------EGGTYT-LTISNVQ 64

                          90       100
                  ....*....|....*....|....*.
gi 9055246    227 KEDEGVYHCHAANAIGEAQSHGTVTV 252
Cdd:pfam07679  65 PDDSGKYTCVATNSAGEAEASAELTV 90
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 106-143 4.42e-06

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 42.67  E-value: 4.42e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 9055246     106 VCGSDGRSYSSICALRLRARHapraHHGHLHKARDGPC 143
Cdd:smart00280  13 VCGSDGVTYSNECHLCKAACE----SGKSIEVKHDGPC 46
IGFBP pfam00219
Insulin-like growth factor binding protein;
52-83 4.53e-05

Insulin-like growth factor binding protein;


:

Pssm-ID: 459717  Cd Length: 53  Bit Score: 40.00  E-value: 4.53e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 9055246     52 RDECGCCARCLGAEGASCGGPVGsRCGPGLVC 83
Cdd:pfam00219  23 LDGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
 
Name Accession Description Interval E-value
I-set pfam07679
Immunoglobulin I-set domain;
147-252 3.54e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.51  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246    147 PVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspegtEGLEELPGDHVNIAVqvrggpsDHETTSwILINPLR 226
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK--------DGQPLRSSDRFKVTY-------EGGTYT-LTISNVQ 64

                          90       100
                  ....*....|....*....|....*.
gi 9055246    227 KEDEGVYHCHAANAIGEAQSHGTVTV 252
Cdd:pfam07679  65 PDDSGKYTCVATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 161-252 1.18e-11

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: 59.44  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246     161 GTQVFLSCEVKAVPTPVITWKKVKHSPegtegleelpgdhvnIAVQVRGGPSDHETTSWILINPLRKEDEGVYHCHAANA 240
Cdd:smart00410   9 GESVTLSCEASGSPPPEVTWYKQGGKL---------------LAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNS 73

                           90
                   ....*....|..
gi 9055246     241 IGEAQSHGTVTV 252
Cdd:smart00410  74 SGSASSGTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 164-247 6.47e-10

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: 54.26  E-value: 6.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  164 VFLSCEVKAVPTPVITWKKvkhspegtegleelpgDHVNIAVQVRGGPSDHETTSWILINPLRKEDEGVYHCHAANAIGE 243
Cdd:cd00096   1 VTLTCSASGNPPPTITWYK----------------NGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGG 64


                ....
gi 9055246  244 AQSH 247
Cdd:cd00096  65 SASA 68
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 106-143 4.42e-06

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 42.67  E-value: 4.42e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 9055246     106 VCGSDGRSYSSICALRLRARHapraHHGHLHKARDGPC 143
Cdd:smart00280  13 VCGSDGVTYSNECHLCKAACE----SGKSIEVKHDGPC 46
IGFBP pfam00219
Insulin-like growth factor binding protein;
52-83 4.53e-05

Insulin-like growth factor binding protein;


Pssm-ID: 459717  Cd Length: 53  Bit Score: 40.00  E-value: 4.53e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 9055246     52 RDECGCCARCLGAEGASCGGPVGsRCGPGLVC 83
Cdd:pfam00219  23 LDGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 106-143 1.88e-04

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 38.02  E-value: 1.88e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 9055246  106 VCGSDGRSYSSICALRLRARHapraHHGHLHKARDGPC 143
Cdd:cd00104   8 VCGSDGKTYSNECHLGCAACR----SGRSITVAHNGPC 41
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
 30-99 7.84e-04

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


Pssm-ID: 197525  Cd Length: 75  Bit Score: 37.45  E-value: 7.84e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9055246      30 CSPCQQDRCPAPSPCPAPwISARDECGCCARCLGAEGASCGGPVGsRCGPGLVCASRASGTAP-----EGTGLCV 99
Cdd:smart00121   3 CPPCDPARCPPCPPGCAE-LVRLDGCGCCPVCARQEGEPCGVYTP-RCAPGLRCQPPPGEERPlrallHGQGVCM 75
 
Name Accession Description Interval E-value
I-set pfam07679
Immunoglobulin I-set domain;
147-252 3.54e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.51  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246    147 PVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspegtEGLEELPGDHVNIAVqvrggpsDHETTSwILINPLR 226
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK--------DGQPLRSSDRFKVTY-------EGGTYT-LTISNVQ 64

                          90       100
                  ....*....|....*....|....*.
gi 9055246    227 KEDEGVYHCHAANAIGEAQSHGTVTV 252
Cdd:pfam07679  65 PDDSGKYTCVATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 161-252 1.18e-11

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: 59.44  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246     161 GTQVFLSCEVKAVPTPVITWKKVKHSPegtegleelpgdhvnIAVQVRGGPSDHETTSWILINPLRKEDEGVYHCHAANA 240
Cdd:smart00410   9 GESVTLSCEASGSPPPEVTWYKQGGKL---------------LAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNS 73

                           90
                   ....*....|..
gi 9055246     241 IGEAQSHGTVTV 252
Cdd:smart00410  74 SGSASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 147-239 1.36e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.42  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246    147 PVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspegtEGLEELPGDHVNIAVQvrggpsdhETTSWILINPLR 226
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYK--------NGEPISSGSTRSRSLS--------GSNSTLTISNVT 65

                          90
                  ....*....|...
gi 9055246    227 KEDEGVYHCHAAN 239
Cdd:pfam13927  66 RSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 164-247 6.47e-10

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: 54.26  E-value: 6.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  164 VFLSCEVKAVPTPVITWKKvkhspegtegleelpgDHVNIAVQVRGGPSDHETTSWILINPLRKEDEGVYHCHAANAIGE 243
Cdd:cd00096   1 VTLTCSASGNPPPTITWYK----------------NGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGG 64


                ....
gi 9055246  244 AQSH 247
Cdd:cd00096  65 SASA 68
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 153-242 1.40e-07

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: 48.46  E-value: 1.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  153 PRDIHNVTGTQVFLSCEVKAVPTPVITWKKVKHSPEGtEGLEELPGDHVNIavqvrggpsdHETTSwILINPLRKEDEGV 232
Cdd:cd20954   8 PVDANVAAGQDVMLHCQADGFPTPTVTWKKATGSTPG-EYKDLLYDPNVRI----------LPNGT-LVFGHVQKENEGH 75

                        90
                ....*....|
gi 9055246  233 YHCHAANAIG 242
Cdd:cd20954  76 YLCEAKNGIG 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 152-252 2.06e-07

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: 47.77  E-value: 2.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  152 PPRDIHNVTGTQVFLSCEVKAVPTPVITWKkvkhspegtegleelpgdHVNIAVQVRGGPSDHETTSwILINPLRKEDEG 231
Cdd:cd20978   7 PEKNVVVKGGQDVTLPCQVTGVPQPKITWL------------------HNGKPLQGPMERATVEDGT-LTIINVQPEDTG 67

                        90       100
                ....*....|....*....|.
gi 9055246  232 VYHCHAANAIGEAQSHGTVTV 252
Cdd:cd20978  68 YYGCVATNEIGDIYTETLLHV 88
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 153-246 4.00e-07

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: 47.01  E-value: 4.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  153 PRDIHNVTGTQVFLSCEV-KAVPTPVITWKKvkhspegteglEELPGDHVNIAVQVRGGPSdhettswILINPLRKEDEG 231
Cdd:cd05724   4 PSDTQVAVGEMAVLECSPpRGHPEPTVSWRK-----------DGQPLNLDNERVRIVDDGN-------LLIAEARKSDEG 65

                        90
                ....*....|....*
gi 9055246  232 VYHCHAANAIGEAQS 246
Cdd:cd05724  66 TYKCVATNMVGERES 80
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 159-252 8.85e-07

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: 45.91  E-value: 8.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  159 VTGTQVFLSCEVKAVPTPVITWKKvkhspeGTEGLEELPgdhvNIAVQVRGgpsdhettSWILINpLRKEDEGVYHCHAA 238
Cdd:cd04969  15 AKGGDVIIECKPKASPKPTISWSK------GTELLTNSS----RICILPDG--------SLKIKN-VTKSDEGKYTCFAV 75

                        90
                ....*....|....
gi 9055246  239 NAIGEAQSHGTVTV 252
Cdd:cd04969  76 NFFGKANSTGSLSV 89
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 153-253 1.23e-06

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: 45.69  E-value: 1.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  153 PRDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspegtEGLEELPGdhvniAVQVRGG--PSDHEttswILINPLRKEDE 230
Cdd:cd05763   6 PHDITIRAGSTARLECAATGHPTPQIAWQK--------DGGTDFPA-----ARERRMHvmPEDDV----FFIVDVKIEDT 68

                        90       100
                ....*....|....*....|...
gi 9055246  231 GVYHCHAANAIGEAQSHGTVTVL 253
Cdd:cd05763  69 GVYSCTAQNSAGSISANATLTVL 91
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 150-246 3.70e-06

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: 44.11  E-value: 3.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  150 LMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspegtEGLEELPGDHVNIA----VQVRGgpsdhettswilinpL 225
Cdd:cd05723   1 LKKPSNIYAHESMDIVFECEVTGKPTPTVKWVK--------NGDVVIPSDYFKIVkehnLQVLG---------------L 57

                        90       100
                ....*....|....*....|.
gi 9055246  226 RKEDEGVYHCHAANAIGEAQS 246
Cdd:cd05723  58 VKSDEGFYQCIAENDVGNAQA 78
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 153-252 3.90e-06

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: 44.08  E-value: 3.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  153 PRDIHNVTGTQVFLSCEVKAVPTPVITWKKVKHSPEGTegleelpgdhvniAVQVRGGPSDHettswilINPLRKEDEGV 232
Cdd:cd04968   8 PADTYALKGQTVTLECFALGNPVPQIKWRKVDGSPSSQ-------------WEITTSEPVLE-------IPNVQFEDEGT 67

                        90       100
                ....*....|....*....|
gi 9055246  233 YHCHAANAIGEAQSHGTVTV 252
Cdd:cd04968  68 YECEAENSRGKDTVQGRIIV 87
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 106-143 4.42e-06

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 42.67  E-value: 4.42e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 9055246     106 VCGSDGRSYSSICALRLRARHapraHHGHLHKARDGPC 143
Cdd:smart00280  13 VCGSDGVTYSNECHLCKAACE----SGKSIEVKHDGPC 46
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 161-252 7.27e-06

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: 43.70  E-value: 7.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  161 GTQVFLSCEVKAVPTPVITWKkvkhspegtegLEELP---------GDHVNiavqvrggpSDHETTSWILINPLRKEDEG 231
Cdd:cd20956  16 GPSVSLKCVASGNPLPQITWT-----------LDGFPipesprfrvGDYVT---------SDGDVVSYVNISSVRVEDGG 75

                        90       100
                ....*....|....*....|.
gi 9055246  232 VYHCHAANAIGEAQSHGTVTV 252
Cdd:cd20956  76 EYTCTATNDVGSVSHSARINV 96
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 152-253 7.45e-06

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: 43.99  E-value: 7.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246    152 PPRDIHNVTGTQVFLSCEVK---AVPTPVITWKKVKHSPEGTE-GLEELPGDHVNI---AVQVRGGPSDHETTswILINP 224
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSssmSEASTSVYWYRQPPGKGPTFlIAYYSNGSEEGVkkgRFSGRGDPSNGDGS--LTIQN 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 9055246    225 LRKEDEGVYHCHAA-NAIGEAQSHGTVTVL 253
Cdd:pfam07686  80 LTLSDSGTYTCAVIpSGEGVFGKGTRLTVL 109
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 156-245 9.88e-06

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: 43.28  E-value: 9.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  156 IHNVT---GTQVFLSCEVKAVPTPVITWKKvkhspeGTEGLEELPGDhVNIAVQVRGgpsdHETTSWILINPLRKEDEGV 232
Cdd:cd05732   8 LENQTaveLEQITLTCEAEGDPIPEITWRR------ATRGISFEEGD-LDGRIVVRG----HARVSSLTLKDVQLTDAGR 76

                        90
                ....*....|...
gi 9055246  233 YHCHAANAIGEAQ 245
Cdd:cd05732  77 YDCEASNRIGGDQ 89
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 150-252 1.33e-05

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: 42.38  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  150 LMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspegTEGleELPGDHVNIAvqvrggpSDHEttswILINPLRKED 229
Cdd:cd05725   1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRK-------EDG--ELPKGRYEIL-------DDHS----LKIRKVTAGD 60

                        90       100
                ....*....|....*....|...
gi 9055246  230 EGVYHCHAANAIGEAQSHGTVTV 252
Cdd:cd05725  61 MGSYTCVAENMVGKIEASATLTV 83
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
 154-245 1.65e-05

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: 42.66  E-value: 1.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  154 RDIHNVTGTQVFLSCEVKAVPTPVITWKKVKHSPEGTEGLEELPGdhvniAVQVRGgpsdHETTSWILINPLRKEDEGVY 233
Cdd:cd05870   9 KNETTVENGAATLSCKAEGEPIPEITWKRASDGHTFSEGDKSPDG-----RIEVKG----QHGESSLHIKDVKLSDSGRY 79

                        90
                ....*....|..
gi 9055246  234 HCHAANAIGEAQ 245
Cdd:cd05870  80 DCEAASRIGGHQ 91
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 148-252 1.70e-05

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: 1.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  148 VVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKVKHSPEGT-EGLEELPgdhvNIAVQVRGgpsdhettswilinpLR 226
Cdd:cd20952   1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKdERITTLE----NGSLQIKG---------------AE 61

                        90       100
                ....*....|....*....|....*.
gi 9055246  227 KEDEGVYHCHAANAIGEAQSHGTVTV 252
Cdd:cd20952  62 KSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 161-252 1.78e-05

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: 42.41  E-value: 1.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  161 GTQVFLSCEVKAVPTPVITWKK--VKHSPEGTEG---LEELPGDHVniavqvrggpsdhettswILINPLRKEDEGVYHC 235
Cdd:cd20951  15 KSDAKLRVEVQGKPDPEVKWYKngVPIDPSSIPGkykIESEYGVHV------------------LHIRRVTVEDSAVYSA 76

                        90
                ....*....|....*..
gi 9055246  236 HAANAIGEAQSHGTVTV 252
Cdd:cd20951  77 VAKNIHGEASSSASVVV 93
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
 159-252 1.80e-05

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: 1.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  159 VTGTQVFLSCEVKAVPTPVITWKKvkhspegtegleelpGDHVNIAVQVRGGPSDHETTSWILINPLRKEDEGVYHCHAA 238
Cdd:cd05894   8 VAGNKLRLDVPISGEPAPTVTWSR---------------GDKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVT 72

                        90
                ....*....|....
gi 9055246  239 NAIGEAQSHGTVTV 252
Cdd:cd05894  73 NPVGEDHASLFVKV 86
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 152-253 2.88e-05

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: 41.67  E-value: 2.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  152 PPRDIHNVTGTQVFLsCEVKAVPTPVITWkKVKHSPegtegLEELPGDHVNIavqvrggpsDHETTswILINPLRKEDEG 231
Cdd:cd04978   6 PPSLVLSPGETGELI-CEAEGNPQPTITW-RLNGVP-----IEPAPEDMRRT---------VDGRT--LIFSNLQPNDTA 67

                        90       100
                ....*....|....*....|..
gi 9055246  232 VYHCHAANAIGEAQSHGTVTVL 253
Cdd:cd04978  68 VYQCNASNVHGYLLANAFLHVL 89
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 147-244 3.47e-05

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: 41.71  E-value: 3.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  147 PVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKVKHSPEgtegleelPGDHVNIAVQVRGGPSdhettswILINPLR 226
Cdd:cd05744   1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVR--------PDSAHKMLVRENGRHS-------LIIEPVT 65

                        90
                ....*....|....*...
gi 9055246  227 KEDEGVYHCHAANAIGEA 244
Cdd:cd05744  66 KRDAGIYTCIARNRAGEN 83
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 147-252 3.78e-05

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: 41.52  E-value: 3.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  147 PVVLMPP--RDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspeGTEGLeeLPGDHVNIavqvrggpsdhettsW----I 220
Cdd:cd05852   1 PTFEFNPmkKKILAAKGGRVIIECKPKAAPKPKFSWSK------GTELL--VNNSRISI---------------WddgsL 57

                        90       100       110
                ....*....|....*....|....*....|..
gi 9055246  221 LINPLRKEDEGVYHCHAANAIGEAQSHGTVTV 252
Cdd:cd05852  58 EILNITKLDEGSYTCFAENNRGKANSTGVLSV 89
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 146-252 3.79e-05

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: 3.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  146 APVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKVKHSPEgtegleeLPGDHVNIAVQVrggpsdhettSWILINPL 225
Cdd:cd20976   1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQ-------YAADRSTCEAGV----------GELHIQDV 63

                        90       100
                ....*....|....*....|....*..
gi 9055246  226 RKEDEGVYHCHAANAIGEAQSHGTVTV 252
Cdd:cd20976  64 LPEDHGTYTCLAKNAAGQVSCSAWVTV 90
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 161-252 3.96e-05

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: 3.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  161 GTQVFLSCEVKAVPTPVITWKKvkhspegtEGLEELPGDHVNIAVqvrggpsdHETTSWILINPLRKEDEGVYHCHAANA 240
Cdd:cd05748   7 GESLRLDIPIKGRPTPTVTWSK--------DGQPLKETGRVQIET--------TASSTSLVIKNAKRSDSGKYTLTLKNS 70

                        90
                ....*....|..
gi 9055246  241 IGEAQSHGTVTV 252
Cdd:cd05748  71 AGEKSATINVKV 82
IGFBP pfam00219
Insulin-like growth factor binding protein;
52-83 4.53e-05

Insulin-like growth factor binding protein;


Pssm-ID: 459717  Cd Length: 53  Bit Score: 40.00  E-value: 4.53e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 9055246     52 RDECGCCARCLGAEGASCGGPVGsRCGPGLVC 83
Cdd:pfam00219  23 LDGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 147-252 4.89e-05

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: 41.16  E-value: 4.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  147 PVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKVkhspegtegLEELPGDhvniavqvrggpSDHETTSWIL-INPL 225
Cdd:cd05851   2 ADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKI---------LEPMPAT------------AEISMSGAVLkIFNI 60

                        90       100
                ....*....|....*....|....*..
gi 9055246  226 RKEDEGVYHCHAANAIGEAQSHGTVTV 252
Cdd:cd05851  61 QPEDEGTYECEAENIKGKDKHQARVYV 87
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 146-252 5.55e-05

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: 41.03  E-value: 5.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  146 APVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITW----KKVKHSPEgtegleelpgdhvniaVQVRGGPSDHEttswIL 221
Cdd:cd20972   1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWfcegKELQNSPD----------------IQIHQEGDLHS----LI 60

                        90       100       110
                ....*....|....*....|....*....|.
gi 9055246  222 INPLRKEDEGVYHCHAANAIGEAQSHGTVTV 252
Cdd:cd20972  61 IAEAFEEDTGRYSCLATNSVGSDTTSAEIFV 91
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 149-235 7.74e-05

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: 41.17  E-value: 7.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  149 VLMPPRDIHNVTGTQVFLSCEVK-AVPTPVITW--KKVKHSPEGtegLEELPGDHVNIAVQVRGG--PSDHETTSWIL-I 222
Cdd:cd00099   1 VTQSPRSLSVQEGESVTLSCEVSsSFSSTYIYWyrQKPGQGPEF---LIYLSSSKGKTKGGVPGRfsGSRDGTSSFSLtI 77

                        90
                ....*....|...
gi 9055246  223 NPLRKEDEGVYHC 235
Cdd:cd00099  78 SNLQPEDSGTYYC 90
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 153-253 1.65e-04

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: 39.94  E-value: 1.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  153 PRDIHNVTGTQVFLSCEVKAVPTPVITWKK------VKHSPEGTEGLEELPGDHVNIavqvrggpSDHETTSWILINpLR 226
Cdd:cd05858   8 PANTSVVVGTDAEFVCKVYSDAQPHIQWLKhvekngSKYGPDGLPYVEVLKTAGVNT--------TDKEIEVLYLRN-VT 78

                        90       100
                ....*....|....*....|....*..
gi 9055246  227 KEDEGVYHCHAANAIGEAQSHGTVTVL 253
Cdd:cd05858  79 FEDAGEYTCLAGNSIGISHHSAWLTVL 105
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 106-143 1.88e-04

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 38.02  E-value: 1.88e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 9055246  106 VCGSDGRSYSSICALRLRARHapraHHGHLHKARDGPC 143
Cdd:cd00104   8 VCGSDGKTYSNECHLGCAACR----SGRSITVAHNGPC 41
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 147-246 1.90e-04

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: 39.53  E-value: 1.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  147 PVVLMPPRDIHNVTGT---QVFLSCEVKAVPTPVITWKKvkhspEGTEgleelpgdhvniavqVRGGPSDHETT---SWI 220
Cdd:cd04967   2 PVFEEQPDDTIFPEDSdekKVALNCRARANPVPSYRWLM-----NGTE---------------IDLESDYRYSLvdgTLV 61

                        90       100
                ....*....|....*....|....*.
gi 9055246  221 LINPLRKEDEGVYHCHAANAIGEAQS 246
Cdd:cd04967  62 ISNPSKAKDAGHYQCLATNTVGSVLS 87
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 161-246 2.13e-04

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: 39.10  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246    161 GTQVFLSCEVKAVPTPV-ITWKKvkhspEGTEGLEELPGDHVNiavqvrggpsDHETTSWILINPLRKEDEGVYHCHAAN 239
Cdd:pfam00047  11 GDSATLTCSASTGSPGPdVTWSK-----EGGTLIESLKVKHDN----------GRTTQSSLLISNVTKEDAGTYTCVVNN 75


                  ....*..
gi 9055246    240 AIGEAQS 246
Cdd:pfam00047  76 PGGSATL 82
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 161-252 2.46e-04

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: 39.12  E-value: 2.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  161 GTQVFLSCEVKAVPTPVITWKKVKhSPegtegleeLPGDhvniavqvRGGPSDHetTSWILINPLRKEDEGVYHCHAANA 240
Cdd:cd05876  10 GQSLVLECIAEGLPTPTVKWLRPS-GP--------LPPD--------RVKYQNH--NKTLQLLNVGESDDGEYVCLAENS 70

                        90
                ....*....|..
gi 9055246  241 IGEAQSHGTVTV 252
Cdd:cd05876  71 LGSARHAYYVTV 82
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 160-246 3.32e-04

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: 38.76  E-value: 3.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  160 TGTQVFLSCEVKAVPTPVITWKKvkhspeGTEGLEELPGDHvniavqvrggpSDHETTSWILINPLRKEDEGVYHCHAAN 239
Cdd:cd05730  17 LGQSVTLACDADGFPEPTMTWTK------DGEPIESGEEKY-----------SFNEDGSEMTILDVDKLDEAEYTCIAEN 79


                ....*..
gi 9055246  240 AIGEAQS 246
Cdd:cd05730  80 KAGEQEA 86
Ig0_BSG1 cd20940
Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are ...
 160-239 3.65e-04

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: 39.18  E-value: 3.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  160 TGTQVFLSCEVKAVPTPVITWKKVKHSPEgtEGLEELPGDHVNIAVQVRGGPSDHETTSWILINpLRKEDEGVYHCHAAN 239
Cdd:cd20940  14 VGDSVELHCEAVGSPIPEIQWWFEGQEPN--EICSQLWDGARLDRVHINATYHQHATSTISIDN-LTEEDTGTYECRASN 90
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 147-252 5.81e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. 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: 409473  Cd Length: 92  Bit Score: 38.21  E-value: 5.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  147 PVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKK----VKHSPEGTEGLEELPGDHVniavqvrggpsdhettswILI 222
Cdd:cd05892   1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKnnemLQYNTDRISLYQDNCGRIC------------------LLI 62

                        90       100       110
                ....*....|....*....|....*....|
gi 9055246  223 NPLRKEDEGVYHCHAANAIGEAQSHGTVTV 252
Cdd:cd05892  63 QNANKKDAGWYTVSAVNEAGVVSCNARLDV 92
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 161-252 6.12e-04

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: 37.77  E-value: 6.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  161 GTQVFLSCEVKAVPTPVITWKKVkhspegtegLEELPGDhvniavqvRGGPSDHETTswILINPLRKEDEGVYHCHAANA 240
Cdd:cd05731  10 GGVLLLECIAEGLPTPDIRWIKL---------GGELPKG--------RTKFENFNKT--LKIENVSEADSGEYQCTASNT 70

                        90
                ....*....|..
gi 9055246  241 IGEAQSHGTVTV 252
Cdd:cd05731  71 MGSARHTISVTV 82
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
 30-99 7.84e-04

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


Pssm-ID: 197525  Cd Length: 75  Bit Score: 37.45  E-value: 7.84e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9055246      30 CSPCQQDRCPAPSPCPAPwISARDECGCCARCLGAEGASCGGPVGsRCGPGLVCASRASGTAP-----EGTGLCV 99
Cdd:smart00121   3 CPPCDPARCPPCPPGCAE-LVRLDGCGCCPVCARQEGEPCGVYTP-RCAPGLRCQPPPGEERPlrallHGQGVCM 75
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 151-243 8.99e-04

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: 37.53  E-value: 8.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  151 MPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspEGTEGLEELPGdhvniavqvrggpsDHETTSWIL-INPLRKED 229
Cdd:cd05856   9 MRRRVIARPVGSSVRLKCVASGNPRPDITWLK-----DNKPLTPPEIG--------------ENKKKKWTLsLKNLKPED 69

                        90
                ....*....|....
gi 9055246  230 EGVYHCHAANAIGE 243
Cdd:cd05856  70 SGKYTCHVSNRAGE 83
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
 159-237 9.87e-04

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


Pssm-ID: 409455  Cd Length: 92  Bit Score: 37.33  E-value: 9.87e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9055246  159 VTGTQVFLSCEVKAvPTPVITWKKvkhSPEGTEGLEELPGDhVNIAVQVRGgpsdhettswILINPLRKEDEGVYHCHA 237
Cdd:cd05871  10 VEGNSTFLECLPKS-PQATVKWLF---QRGGDQRKEEVKSE-ERLIVTDRG----------LLLRSLQRSDAGVYTCQA 73
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 152-252 1.11e-03

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: 37.17  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  152 PPRDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspegtEGLEELPGDHVNIAvqvrggpSDHETTSWILINPLRKEDEG 231
Cdd:cd20973   3 TLRDKEVVEGSAARFDCKVEGYPDPEVKWMK--------DDNPIVESRRFQID-------QDEDGLCSLIISDVCGDDSG 67

                        90       100
                ....*....|....*....|.
gi 9055246  232 VYHCHAANAIGEAQSHGTVTV 252
Cdd:cd20973  68 KYTCKAVNSLGEATCSAELTV 88
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
 163-243 1.20e-03

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: 37.27  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  163 QVFLSCEVKAVPTPVITWKKVKHSPEGTEglEELPGdhvNIAVQvrggpsDHETTSWILINPLRKEDEGVYHCHAANAIG 242
Cdd:cd05869  19 QITLTCEASGDPIPSITWRTSTRNISSEE--KTLDG---HIVVR------SHARVSSLTLKYIQYTDAGEYLCTASNTIG 87


                .
gi 9055246  243 E 243
Cdd:cd05869  88 Q 88
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 161-252 1.46e-03

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: 36.70  E-value: 1.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  161 GTQVFLSCEVKAVPTPVITWK-KVKHSPegtegleelpgDHVNIAVQVRGGpsdhetTSWILINPLRKEDEGVYHCHAAN 239
Cdd:cd05743   1 GETVEFTCVATGVPTPIINWRlNWGHVP-----------DSARVSITSEGG------YGTLTIRDVKESDQGAYTCEAIN 63

                        90
                ....*....|....*
gi 9055246  240 AIGE--AQSHGTVTV 252
Cdd:cd05743  64 TRGMvfGIPDGILTV 78
IgI_1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; ...
 163-246 1.53e-03

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: 37.24  E-value: 1.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  163 QVFLSCEVKAVPTPVITWKKvkhspegTEGLEELPGDHVNIAvqvrGGpsdhettSWILINPLRKEDEGVYHCHAANAIG 242
Cdd:cd05849  21 KVSVNCRARANPFPIYKWRK-------NNLDIDLTNDRYSMV----GG-------NLVINNPDKYKDAGRYVCIVSNIYG 82


                ....
gi 9055246  243 EAQS 246
Cdd:cd05849  83 KVRS 86
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 147-242 1.53e-03

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: 37.09  E-value: 1.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  147 PVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKVKhspeGTEGLEELPGDHVNIAVQVRGGPSdhettswILINPLR 226
Cdd:cd05734   2 PRFVVQPNDQDGIYGKAVVLNCSADGYPPPTIVWKHSK----GSGVPQFQHIVPLNGRIQLLSNGS-------LLIKHVL 70

                        90
                ....*....|....*.
gi 9055246  227 KEDEGVYHCHAANAIG 242
Cdd:cd05734  71 EEDSGYYLCKVSNDVG 86
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
 149-247 1.76e-03

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: 37.00  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  149 VLMPPRDihnvtgtQVFLSCEVKAVPTPVITWKKvkhspegtEGLEELPGDHVNIAVQVRGGpsdhetTSWILINPLRKE 228
Cdd:cd05733  11 YIVDPRD-------NITIKCEAKGNPQPTFRWTK--------DGKFFDPAKDPRVSMRRRSG------TLVIDNHNGGPE 69

                        90       100
                ....*....|....*....|
gi 9055246  229 D-EGVYHCHAANAIGEAQSH 247
Cdd:cd05733  70 DyQGEYQCYASNELGTAISN 89
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 147-242 1.95e-03

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: 36.86  E-value: 1.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  147 PVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspegtEGLEELPGDHVNIAVQVRGgpsdhettSWILINPLR 226
Cdd:cd05736   1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLK--------NGMDINPKLSKQLTLIANG--------SELHISNVR 64

                        90
                ....*....|....*.
gi 9055246  227 KEDEGVYHCHAANAIG 242
Cdd:cd05736  65 YEDTGAYTCIAKNEGG 80
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 147-252 2.67e-03

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: 36.33  E-value: 2.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  147 PVVLMPPR--DIHNVTGTQVFLSCEVKAVPTPVITWKKVKHSPEgtegleelpgdHVNIAVQVRGGPSDHETTSwilinp 224
Cdd:cd20970   1 PVISTPQPsfTVTAREGENATFMCRAEGSPEPEISWTRNGNLII-----------EFNTRYIVRENGTTLTIRN------ 63

                        90       100
                ....*....|....*....|....*....
gi 9055246  225 LRKEDEGVYHCHAAN-AIGEAQSHGTVTV 252
Cdd:cd20970  64 IRRSDMGIYLCIASNgVPGSVEKRITLQV 92
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 152-246 4.95e-03

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: 35.30  E-value: 4.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  152 PPRDIHNVTGTQVFLSCEVKAVPTPVITWKKvkhspeGTEGLEElpgdHVNIAVQVRGGpsdhettswILINPLRKEDEG 231
Cdd:cd20968   5 PPTNVTIIEGLKAVLPCTTMGNPKPSVSWIK------GDDLIKE----NNRIAVLESGS---------LRIHNVQKEDAG 65

                        90
                ....*....|....*
gi 9055246  232 VYHCHAANAIGEAQS 246
Cdd:cd20968  66 QYRCVAKNSLGIAYS 80
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 159-235 6.43e-03

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


Pssm-ID: 409433  Cd Length: 108  Bit Score: 35.40  E-value: 6.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  159 VTGTQVFLSCEVKAVPTPV-ITWKKVKHSPEGTEG---------LEELPGDHVNIAvqvrggPSDHETTSwILINPLRKE 228
Cdd:cd05846  11 VLGGNATLSCNLTLPEEVLqVTWQKIKASSPENIVtyskkygvkIQPSYVRRISFT------SSGLNSTS-ITIWNVTLE 83


                ....*..
gi 9055246  229 DEGVYHC 235
Cdd:cd05846  84 DEGCYKC 90
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 147-243 7.57e-03

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: 35.08  E-value: 7.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  147 PVVLMPPRDIHNVTGTQVFLSCEVKAVPTPVITWKkvkhspegTEGLEELPGDHVNIAVQVRGGPSdhettswILINPLR 226
Cdd:cd20990   1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQ--------LDGKPIRPDSAHKMLVRENGVHS-------LIIEPVT 65

                        90
                ....*....|....*..
gi 9055246  227 KEDEGVYHCHAANAIGE 243
Cdd:cd20990  66 SRDAGIYTCIATNRAGQ 82
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 161-252 8.05e-03

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: 34.83  E-value: 8.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055246  161 GTQVFLSCEVKAVPTPVITWKkvKHSPeGTEGLEELPgDHV--NIAVQvrggpsdheTTSWILINPLRKEDEGVYHCHAA 238
Cdd:cd05765  15 GETASFHCDVTGRPQPEITWE--KQVP-GKENLIMRP-NHVrgNVVVT---------NIGQLVIYNAQPQDAGLYTCTAR 81

                        90
                ....*....|....
gi 9055246  239 NAIGEAQSHGTVTV 252
Cdd:cd05765  82 NSGGLLRANFPLSV 95
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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