NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|164420687|ref|NP_899045|]
View 

Fc receptor-like protein 5 isoform a precursor [Mus musculus]

Protein Classification

Ig and Ig_3 domain-containing protein( domain architecture ID 10310332)

protein containing domains Ig, Ig_2, and Ig_3

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
119-202 6.77e-18

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 cd05753:

Pssm-ID: 472250  Cd Length: 83  Bit Score: 78.50  E-value: 6.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 119 LVLQAPPAVF-EGDSVVLRCYAKKGIEAETLTFYKDGKALTLHPQSSEFYIHRANLKDNGQYKCTSkKKWSFgsLYTSNT 197
Cdd:cd05753    2 LLLQAPSAVVfEGEPLTLRCHGWKDKKVHKVTYYKDGKALKFSYENSNFSIPQATLSDSGSYHCSG-TVRIK--RRSSES 78

                 ....*
gi 164420687 198 VVVQV 202
Cdd:cd05753   79 VNITV 83
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
34-114 1.57e-16

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 cd05752:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 79  Bit Score: 74.71  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  34 SVVSLQPPWTTFFRGEVVTLTCYRFGFSVPQKTKWYQKRKTVKQTPGALVIKAHTLKvhESGEYWCQADSLLPSMHVNVE 113
Cdd:cd05752    1 AVVSLDPPWTTVFQGEKVTLTCQGFYSPEQNSTQWYHNGTLISSTSSSYRIVAATVN--DSGEYRCQTQGSSLSDPVHLE 78

                 .
gi 164420687 114 F 114
Cdd:cd05752   79 V 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
310-377 1.01e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.96  E-value: 1.01e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420687  310 PASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKDMLNKETKILK----SSNAEFKISQVNISDAGEYYCEANN 377
Cdd:pfam13927   8 PSSVTVREGETVTLTCEATGSPPP-TITWYKNGEPISSGSTRSrslsGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
397-484 2.77e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


:

Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.77  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  397 QPVLTLStgKTQALEGDLMTLHCQSQrGSPCILYEFFyenvslGNSSILSGGGAYFNFSMSTERSGNYYCTADNGLGAQC 476
Cdd:pfam13895   1 KPVLTPS--PTVVTEGEPVTLTCSAP-GNPPPSYTWY------KDGSAISSSPNFFTLSVSAEDSGTYTCVARNGRGGKV 71

                  ....*...
gi 164420687  477 SEAIRISI 484
Cdd:pfam13895  72 SNPVELTV 79
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
208-297 1.28e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


:

Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 40.84  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  208 RPVLRARPSHPIDGSPVTLTCQTqlsaqKSDARLQFCFFRNLQLLGSgcsrSSEFHIPAIWTEESKRYQCKAEtvNSQVS 287
Cdd:pfam13895   1 KPVLTPSPTVVTEGEPVTLTCSA-----PGNPPPSYTWYKDGSAISS----SPNFFTLSVSAEDSGTYTCVAR--NGRGG 69
                          90
                  ....*....|
gi 164420687  288 KQSTAFIIPV 297
Cdd:pfam13895  70 KVSNPVELTV 79
 
Name Accession Description Interval E-value
Ig2_FcgammaR_like cd05753
Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
119-202 6.77e-18

Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409411  Cd Length: 83  Bit Score: 78.50  E-value: 6.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 119 LVLQAPPAVF-EGDSVVLRCYAKKGIEAETLTFYKDGKALTLHPQSSEFYIHRANLKDNGQYKCTSkKKWSFgsLYTSNT 197
Cdd:cd05753    2 LLLQAPSAVVfEGEPLTLRCHGWKDKKVHKVTYYKDGKALKFSYENSNFSIPQATLSDSGSYHCSG-TVRIK--RRSSES 78

                 ....*
gi 164420687 198 VVVQV 202
Cdd:cd05753   79 VNITV 83
Ig1_FcgammaR_like cd05752
First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
34-114 1.57e-16

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409410 [Multi-domain]  Cd Length: 79  Bit Score: 74.71  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  34 SVVSLQPPWTTFFRGEVVTLTCYRFGFSVPQKTKWYQKRKTVKQTPGALVIKAHTLKvhESGEYWCQADSLLPSMHVNVE 113
Cdd:cd05752    1 AVVSLDPPWTTVFQGEKVTLTCQGFYSPEQNSTQWYHNGTLISSTSSSYRIVAATVN--DSGEYRCQTQGSSLSDPVHLE 78

                 .
gi 164420687 114 F 114
Cdd:cd05752   79 V 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
310-377 1.01e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.96  E-value: 1.01e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420687  310 PASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKDMLNKETKILK----SSNAEFKISQVNISDAGEYYCEANN 377
Cdd:pfam13927   8 PSSVTVREGETVTLTCEATGSPPP-TITWYKNGEPISSGSTRSrslsGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
310-393 4.67e-09

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: 53.66  E-value: 4.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687   310 PASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKD--MLNKETKIL---KSSNAEFKISQVNISDAGEYYCEANNSRRSFVS 384
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPP-EVTWYKQGgkLLAESGRFSvsrSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                   ....*....
gi 164420687   385 rafPITIKV 393
Cdd:smart00410  80 ---GTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
321-387 2.01e-08

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: 51.18  E-value: 2.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164420687 321 LLLNCSVKGVPGPlKFSWYKKDMLNKETKI----LKSSNAEFKISQVNISDAGEYYCEANNSRRSFVSRAF 387
Cdd:cd00096    1 VTLTCSASGNPPP-TITWYKNGKPLPPSSRdsrrSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
119-202 4.76e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 47.77  E-value: 4.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  119 LVLQAPPA-VFEGDSVVLRCYAKkGIEAETLTFYKDGKALtlhPQSSEFYIHRANLKDNGQYKCT-SKKKWSFgslyTSN 196
Cdd:pfam13895   2 PVLTPSPTvVTEGEPVTLTCSAP-GNPPPSYTWYKDGSAI---SSSPNFFTLSVSAEDSGTYTCVaRNGRGGK----VSN 73

                  ....*.
gi 164420687  197 TVVVQV 202
Cdd:pfam13895  74 PVELTV 79
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
397-484 2.77e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.77  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  397 QPVLTLStgKTQALEGDLMTLHCQSQrGSPCILYEFFyenvslGNSSILSGGGAYFNFSMSTERSGNYYCTADNGLGAQC 476
Cdd:pfam13895   1 KPVLTPS--PTVVTEGEPVTLTCSAP-GNPPPSYTWY------KDGSAISSSPNFFTLSVSAEDSGTYTCVARNGRGGKV 71

                  ....*...
gi 164420687  477 SEAIRISI 484
Cdd:pfam13895  72 SNPVELTV 79
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
208-297 1.28e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 40.84  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  208 RPVLRARPSHPIDGSPVTLTCQTqlsaqKSDARLQFCFFRNLQLLGSgcsrSSEFHIPAIWTEESKRYQCKAEtvNSQVS 287
Cdd:pfam13895   1 KPVLTPSPTVVTEGEPVTLTCSA-----PGNPPPSYTWYKDGSAISS----SPNFFTLSVSAEDSGTYTCVAR--NGRGG 69
                          90
                  ....*....|
gi 164420687  288 KQSTAFIIPV 297
Cdd:pfam13895  70 KVSNPVELTV 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
40-101 3.71e-04

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: 39.80  E-value: 3.71e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164420687    40 PPWTTFFRGEVVTLTCYRFGFSVPQKTkWY-QKRKTVKQTPGALVIK---AHTLKVHE-----SGEYWCQA 101
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVT-WYkQGGKLLAESGRFSVSRsgsTSTLTISNvtpedSGTYTCAA 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
127-200 4.42e-04

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: 39.41  E-value: 4.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687   127 VFEGDSVVLRCYAKkGIEAETLTFYKDGKALTLHPQ---------SSEFYIHRANLKDNGQYKCTSKKkwSFGSLYTSNT 197
Cdd:smart00410   6 VKEGESVTLSCEAS-GSPPPEVTWYKQGGKLLAESGrfsvsrsgsTSTLTISNVTPEDSGTYTCAATN--SSGSASSGTT 82

                   ...
gi 164420687   198 VVV 200
Cdd:smart00410  83 LTV 85
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
38-101 2.03e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 37.37  E-value: 2.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164420687   38 LQPPWTTFFRGEVVTLTCYRFGFSVPqKTKWYQKRKTVKQTPGALVIKAHtlkVHESGEYWCQA 101
Cdd:pfam13895   4 LTPSPTVVTEGEPVTLTCSAPGNPPP-SYTWYKDGSAISSSPNFFTLSVS---AEDSGTYTCVA 63
 
Name Accession Description Interval E-value
Ig2_FcgammaR_like cd05753
Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
119-202 6.77e-18

Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409411  Cd Length: 83  Bit Score: 78.50  E-value: 6.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 119 LVLQAPPAVF-EGDSVVLRCYAKKGIEAETLTFYKDGKALTLHPQSSEFYIHRANLKDNGQYKCTSkKKWSFgsLYTSNT 197
Cdd:cd05753    2 LLLQAPSAVVfEGEPLTLRCHGWKDKKVHKVTYYKDGKALKFSYENSNFSIPQATLSDSGSYHCSG-TVRIK--RRSSES 78

                 ....*
gi 164420687 198 VVVQV 202
Cdd:cd05753   79 VNITV 83
Ig1_FcgammaR_like cd05752
First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
34-114 1.57e-16

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409410 [Multi-domain]  Cd Length: 79  Bit Score: 74.71  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  34 SVVSLQPPWTTFFRGEVVTLTCYRFGFSVPQKTKWYQKRKTVKQTPGALVIKAHTLKvhESGEYWCQADSLLPSMHVNVE 113
Cdd:cd05752    1 AVVSLDPPWTTVFQGEKVTLTCQGFYSPEQNSTQWYHNGTLISSTSSSYRIVAATVN--DSGEYRCQTQGSSLSDPVHLE 78

                 .
gi 164420687 114 F 114
Cdd:cd05752   79 V 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
310-377 1.01e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.96  E-value: 1.01e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420687  310 PASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKDMLNKETKILK----SSNAEFKISQVNISDAGEYYCEANN 377
Cdd:pfam13927   8 PSSVTVREGETVTLTCEATGSPPP-TITWYKNGEPISSGSTRSrslsGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
308-391 1.10e-09

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 55.09  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  308 IIPASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKDMLNketkilkSSNAEFKISQVNISDAGEYYCEANNSRRSFVSRAF 387
Cdd:pfam13895   4 LTPSPTVVTEGEPVTLTCSAPGNPPP-SYTWYKDGSAI-------SSSPNFFTLSVSAEDSGTYTCVARNGRGGKVSNPV 75

                  ....
gi 164420687  388 PITI 391
Cdd:pfam13895  76 ELTV 79
I-set pfam07679
Immunoglobulin I-set domain;
303-378 3.87e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 53.80  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  303 RFQTHIIPASklVFEGQLLLLNCSVKGVPGPlKFSWYKKDMLNKETKILK----SSNAEFKISQVNISDAGEYYCEANNS 378
Cdd:pfam07679   2 KFTQKPKDVE--VQEGESARFTCTVTGTPDP-EVSWFKDGQPLRSSDRFKvtyeGGTYTLTISNVQPDDSGKYTCVATNS 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
310-393 4.67e-09

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: 53.66  E-value: 4.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687   310 PASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKD--MLNKETKIL---KSSNAEFKISQVNISDAGEYYCEANNSRRSFVS 384
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPP-EVTWYKQGgkLLAESGRFSvsrSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                   ....*....
gi 164420687   385 rafPITIKV 393
Cdd:smart00410  80 ---GTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
321-387 2.01e-08

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: 51.18  E-value: 2.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164420687 321 LLLNCSVKGVPGPlKFSWYKKDMLNKETKI----LKSSNAEFKISQVNISDAGEYYCEANNSRRSFVSRAF 387
Cdd:cd00096    1 VTLTCSASGNPPP-TITWYKNGKPLPPSSRdsrrSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
312-381 2.02e-07

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: 48.94  E-value: 2.02e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420687 312 SKLVFEGQLLLLNCSVKGVPGPlKFSWYKK--DMLNKETKiLKSSNAEFKISQVNISDAGEYYCEANNSRRS 381
Cdd:cd05731    4 STMVLRGGVLLLECIAEGLPTP-DIRWIKLggELPKGRTK-FENFNKTLKIENVSEADSGEYQCTASNTMGS 73
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
308-378 3.38e-07

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 48.35  E-value: 3.38e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164420687  308 IIPASKLVFEGQLLLLNCSVKGVPGPLKFSWYKKDMLNKE-----TKILKSSNAEFKISQVNISDAGEYYCEANNS 378
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIEslkvkHDNGRTTQSSLLISNVTKEDAGTYTCVVNNP 76
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
119-202 4.76e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 47.77  E-value: 4.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  119 LVLQAPPA-VFEGDSVVLRCYAKkGIEAETLTFYKDGKALtlhPQSSEFYIHRANLKDNGQYKCT-SKKKWSFgslyTSN 196
Cdd:pfam13895   2 PVLTPSPTvVTEGEPVTLTCSAP-GNPPPSYTWYKDGSAI---SSSPNFFTLSVSAEDSGTYTCVaRNGRGGK----VSN 73

                  ....*.
gi 164420687  197 TVVVQV 202
Cdd:pfam13895  74 PVELTV 79
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
310-379 6.99e-07

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: 47.54  E-value: 6.99e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 310 PASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKDMLNKETKILKSSNAEFKISQVNISDAGEYYCEANNSR 379
Cdd:cd04968    8 PADTYALKGQTVTLECFALGNPVP-QIKWRKVDGSPSSQWEITTSEPVLEIPNVQFEDEGTYECEAENSR 76
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
310-393 1.20e-06

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: 46.85  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 310 PASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKDMLNKETK---ILKSSNaeFKISQVNISDAGEYYCEANNSRRSFVSRa 386
Cdd:cd20968    6 PTNVTIIEGLKAVLPCTTMGNPKP-SVSWIKGDDLIKENNriaVLESGS--LRIHNVQKEDAGQYRCVAKNSLGIAYSK- 81

                 ....*..
gi 164420687 387 fPITIKV 393
Cdd:cd20968   82 -PVTIEV 87
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
312-377 2.71e-06

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.97  E-value: 2.71e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420687 312 SKLVFEGQLLLLNCSVKGVPGPLKFSWYK-----KDMLNKETKILKS-SNAEFKISQVNISDAGEYYCEANN 377
Cdd:cd05750    8 SQTVQEGSKLVLKCEATSENPSPRYRWFKdgkelNRKRPKNIKIRNKkKNSELQINKAKLEDSGEYTCVVEN 79
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
125-181 8.00e-06

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 44.42  E-value: 8.00e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164420687 125 PAVFEGDSVVLRCYAKKGIEAETLTFYKDGKALTLH----------PQSSEFYIHRANLKDNGQYKC 181
Cdd:cd05750    9 QTVQEGSKLVLKCEATSENPSPRYRWFKDGKELNRKrpknikirnkKKNSELQINKAKLEDSGEYTC 75
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
397-484 2.77e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.77  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  397 QPVLTLStgKTQALEGDLMTLHCQSQrGSPCILYEFFyenvslGNSSILSGGGAYFNFSMSTERSGNYYCTADNGLGAQC 476
Cdd:pfam13895   1 KPVLTPS--PTVVTEGEPVTLTCSAP-GNPPPSYTWY------KDGSAISSSPNFFTLSVSAEDSGTYTCVARNGRGGKV 71

                  ....*...
gi 164420687  477 SEAIRISI 484
Cdd:pfam13895  72 SNPVELTV 79
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
310-385 3.19e-05

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: 42.77  E-value: 3.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 310 PASKLVFEGQLLLLNCSV-KGVPGPlKFSWYKKD----MLNKETKILKSSNaeFKISQVNISDAGEYYCEANNS---RRS 381
Cdd:cd05724    4 PSDTQVAVGEMAVLECSPpRGHPEP-TVSWRKDGqplnLDNERVRIVDDGN--LLIAEARKSDEGTYKCVATNMvgeRES 80

                 ....
gi 164420687 382 FVSR 385
Cdd:cd05724   81 RAAR 84
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
310-393 3.64e-05

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: 42.50  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 310 PASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKDMLNKETK---ILKSSNAEFKISQVNISDAGEYYCEANNSRRSFVSRA 386
Cdd:cd20970    9 SFTVTAREGENATFMCRAEGSPEP-EISWTRNGNLIIEFNtryIVRENGTTLTIRNIRRSDMGIYLCIASNGVPGSVEKR 87

                 ....*..
gi 164420687 387 fpITIKV 393
Cdd:cd20970   88 --ITLQV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
124-182 5.57e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.78  E-value: 5.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164420687  124 PPAVFEGDSVVLRCYAKkGIEAETLTFYKDGKAL--------TLHPQSSEFYIHRANLKDNGQYKCT 182
Cdd:pfam13927  10 SVTVREGETVTLTCEAT-GSPPPTITWYKNGEPIssgstrsrSLSGSNSTLTISNVTRSDAGTYTCV 75
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
311-392 6.83e-05

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: 41.82  E-value: 6.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 311 ASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKD--MLNKETKILkSSNAEFKISQVNISDAGEYYCEANNSRRSfVSRAFP 388
Cdd:cd05876    3 SSLVALRGQSLVLECIAEGLPTP-TVKWLRPSgpLPPDRVKYQ-NHNKTLQLLNVGESDDGEYVCLAENSLGS-ARHAYY 79

                 ....
gi 164420687 389 ITIK 392
Cdd:cd05876   80 VTVE 83
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
127-181 8.93e-05

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


Pssm-ID: 409476  Cd Length: 93  Bit Score: 41.52  E-value: 8.93e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164420687 127 VFEGDSVVLRCYAKKGIEAETLTFYKDGKALTLH-----------PQSSEFYIHRANLKDNGQYKC 181
Cdd:cd05895   11 VAAGSKLVLRCETSSEYPSLRFKWFKNGKEINRKnkpenikiqkkKKKSELRINKASLADSGEYMC 76
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
208-297 1.28e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 40.84  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  208 RPVLRARPSHPIDGSPVTLTCQTqlsaqKSDARLQFCFFRNLQLLGSgcsrSSEFHIPAIWTEESKRYQCKAEtvNSQVS 287
Cdd:pfam13895   1 KPVLTPSPTVVTEGEPVTLTCSA-----PGNPPPSYTWYKDGSAISS----SPNFFTLSVSAEDSGTYTCVAR--NGRGG 69
                          90
                  ....*....|
gi 164420687  288 KQSTAFIIPV 297
Cdd:pfam13895  70 KVSNPVELTV 79
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
310-378 1.66e-04

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: 40.46  E-value: 1.66e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164420687 310 PASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKD--MLNKETKILKSSNaeFKISQVNISDAGEYYCEANNS 378
Cdd:cd05725    4 PQNQVVLVDDSAEFQCEVGGDPVP-TVRWRKEDgeLPKGRYEILDDHS--LKIRKVTAGDMGSYTCVAENM 71
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
398-470 1.86e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 40.24  E-value: 1.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164420687  398 PVLTLSTGKTQALEGDLMTLHCQSQrGSPCILYEFFYENVSLGNSSILSGGGAYFNFSM-----STERSGNYYCTADN 470
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEAT-GSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLtisnvTRSDAGTYTCVASN 78
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
310-393 1.89e-04

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


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 40.76  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 310 PASKLVFEGQLLLLNCSVKGVPGPlKFSWYK---------KDML-NKETKILksSNAEFKISQVNISDAGEYYCEANNSR 379
Cdd:cd20954    8 PVDANVAAGQDVMLHCQADGFPTP-TVTWKKatgstpgeyKDLLyDPNVRIL--PNGTLVFGHVQKENEGHYLCEAKNGI 84
                         90
                 ....*....|....
gi 164420687 380 RSFVSRAfpITIKV 393
Cdd:cd20954   85 GSGLSKV--IFLKV 96
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
310-377 2.46e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 40.17  E-value: 2.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164420687 310 PASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKDML---NKETKILKSSNAEFK--ISQVNISDAGEYYCEANN 377
Cdd:cd05744    7 PGDLEVQEGRLCRFDCKVSGLPTP-DLFWQLNGKPvrpDSAHKMLVRENGRHSliIEPVTKRDAGIYTCIARN 78
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
122-195 3.17e-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: 39.87  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687  122 QAPPAVFEGDSVVLRCYAKKGIEAETLTFYKDGKALTLHPQ---------SSEFYIHRANLKDNGQYKCTSKKKWSFGSL 192
Cdd:pfam00047   3 PPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKvkhdngrttQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82

                  ...
gi 164420687  193 YTS 195
Cdd:pfam00047  83 STS 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
317-378 3.34e-04

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: 39.68  E-value: 3.34e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164420687 317 EGQLLLLNCSVKGVPGPlKFSW-YKKDMLNKETKILKSSNAEFKISQVNISDAGEYYCEANNS 378
Cdd:cd20978   15 GGQDVTLPCQVTGVPQP-KITWlHNGKPLQGPMERATVEDGTLTIINVQPEDTGYYGCVATNE 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
40-101 3.71e-04

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: 39.80  E-value: 3.71e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164420687    40 PPWTTFFRGEVVTLTCYRFGFSVPQKTkWY-QKRKTVKQTPGALVIK---AHTLKVHE-----SGEYWCQA 101
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVT-WYkQGGKLLAESGRFSVSRsgsTSTLTISNvtpedSGTYTCAA 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
127-200 4.42e-04

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: 39.41  E-value: 4.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687   127 VFEGDSVVLRCYAKkGIEAETLTFYKDGKALTLHPQ---------SSEFYIHRANLKDNGQYKCTSKKkwSFGSLYTSNT 197
Cdd:smart00410   6 VKEGESVTLSCEAS-GSPPPEVTWYKQGGKLLAESGrfsvsrsgsTSTLTISNVTPEDSGTYTCAATN--SSGSASSGTT 82

                   ...
gi 164420687   198 VVV 200
Cdd:smart00410  83 LTV 85
IgI_2_JAM1 cd20950
Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF ...
309-377 6.23e-04

Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF domains; The members here are composed of the second Ig-like domain of Junctional adhesion molecule-1 (JAM1). JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The second Ig-like domain of JAM1 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, the A strand of the I-set is discontinuous but lacks a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409542  Cd Length: 97  Bit Score: 39.22  E-value: 6.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 309 IPASKLVfeGQLLLLNCSVKGVPGPLKFSWYKKDML-----------NKETKILKSSNAEFKISQVNISDAGEYYCEANN 377
Cdd:cd20950    5 IPSSATI--GNRAVLTCSEPDGSPPSEYTWFKDGVVmptnpkstrafSNSSYSLDPTTGELVFDPLSASDTGEYSCEARN 82
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
309-386 6.61e-04

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: 39.14  E-value: 6.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 309 IPASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKDMLN----KETKI-LKSSNAEFKISQVNISDAGEYYCEANNSRRSFV 383
Cdd:cd05763    5 TPHDITIRAGSTARLECAATGHPTP-QIAWQKDGGTDfpaaRERRMhVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSIS 83

                 ...
gi 164420687 384 SRA 386
Cdd:cd05763   84 ANA 86
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
312-377 6.68e-04

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


Pssm-ID: 409476  Cd Length: 93  Bit Score: 39.21  E-value: 6.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164420687 312 SKLVFEGQLLLLNCSVKGVPGPLKFSWYKKDM-LNKETKIL------KSSNAEFKISQVNISDAGEYYCEANN 377
Cdd:cd05895    8 SQEVAAGSKLVLRCETSSEYPSLRFKWFKNGKeINRKNKPEnikiqkKKKKSELRINKASLADSGEYMCKVSS 80
IgC2_D1_D2_LILR_KIR_like cd16843
Immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer ...
125-191 7.27e-04

Immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer inhibitory receptors (KIRs) and similar domains; member of Immunoglobulin Constant-2 set of IgSF domains; The members here are composed of the first and second immunoglobulin (Ig)-like domains found in Leukocyte Ig-like receptors (LILRs), Natural killer inhibitory receptors (KIRs, also known as also known as cluster of differentiation (CD) 158), and similar proteins. This group includes LILRB1 (also known as LIR-1), LILRA5 (also known as LIR9), an activating natural cytotoxicity receptor NKp46, the immune-type receptor glycoprotein VI (GPVI), and the IgA-specific receptor Fc-alphaRI (also known as cluster of differentiation (CD) 89). LILRs are a family of immunoreceptors expressed on expressed on T and B cells, on monocytes, dendritic cells, and subgroups of natural killer (NK) cells. The human LILR family contains nine proteins (LILRA1-3, and 5, and LILRB1-5). From functional assays, and as the cytoplasmic domains of various LILRs, for example LILRB1, LILRB2 (also known as LIR-2), and LILRB3 (also known as LIR-3) contain immunoreceptor tyrosine-based inhibitory motifs (ITIMs), it is thought that LIR proteins are inhibitory receptors. Of the eight LIR family proteins, only LILRB1, and LILRB2, show detectable binding to class I MHC molecules; ligands for the other members have yet to be determined. The extracellular portions of the different LIR proteins contain different numbers of Ig-like domains for example, four in the case of LILRB1, and LILRB2, and two in the case of LILRB4 (also known as LIR-5). The activating natural cytotoxicity receptor NKp46 is expressed in natural killer cells, and is organized as an extracellular portion having two Ig-like extracellular domains, a transmembrane domain, and a small cytoplasmic portion. GPVI, which also contains two Ig-like domains, participates in the processes of collagen-mediated platelet activation and arterial thrombus formation. Fc-alphaRI is expressed on monocytes, eosinophils, neutrophils, and macrophages; it mediates IgA-induced immune effector responses such as phagocytosis, antibody-dependent cell-mediated cytotoxicity and respiratory burst. Killer cell immunoglobulin-like receptors (KIRs; also known as CD158 for human KIR) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. KIRs are a family of highly polymorphic activating and inhibitory receptors that serve as key regulators of human NK cell function. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The major ligands for KIR are MHC class I (HLA-A, -B or -C) molecules.


Pssm-ID: 409518 [Multi-domain]  Cd Length: 90  Bit Score: 38.90  E-value: 7.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164420687 125 PAVFEGDSVVLRCYAkkGIEAETLTFYKDGKALTLHPQSS-------EFYIHRANLKDNGQYKCTSKKK--WSFGS 191
Cdd:cd16843   10 SVVPLGENVTIRCQG--PPEAVLFQLYKEGNSLSQGTVREkepqnkaEFYIPHMDRNHAGRYRCRYRSGtlWSEPS 83
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
310-385 7.57e-04

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


Pssm-ID: 409387  Cd Length: 97  Bit Score: 39.00  E-value: 7.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 310 PASKLVFEGQLLLLNCSVKGVPgPLKFSWyKKD----MLNKETKILKSSNAEFKISQV-----NISDAGEYYCEANN-SR 379
Cdd:cd05722    8 PSDIVAMRGGPVVLNCSAESDP-PPKIEW-KKDgvllNLVSDERRQQLPNGSLLITSVvhskhNKPDEGFYQCVAQNeSL 85

                 ....*.
gi 164420687 380 RSFVSR 385
Cdd:cd05722   86 GSIVSR 91
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
310-387 7.76e-04

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: 38.63  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 310 PASKLVFEGQLLLLNCSVKGVPGPLkFSWYKK--DMLNKETKILKSSNAEFKISQVNISDAGEYYCEANNSRRSFVSRAF 387
Cdd:cd20952    6 PQNQTVAVGGTVVLNCQATGEPVPT-ISWLKDgvPLLGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAV 84
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
296-377 8.10e-04

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: 38.78  E-value: 8.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 296 PVQRASARFQthiipASKLVFEGQLlllNCSVKGVPGPlKFSWYKKDM-----LNKETKiLKSSNAEFKISQVNISDAGE 370
Cdd:cd05736    1 PVIRVYPEFQ-----AKEPGVEASL---RCHAEGIPLP-RVQWLKNGMdinpkLSKQLT-LIANGSELHISNVRYEDTGA 70

                 ....*..
gi 164420687 371 YYCEANN 377
Cdd:cd05736   71 YTCIAKN 77
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
318-386 8.80e-04

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


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 38.74  E-value: 8.80e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 318 GQLLLLNCSVKGVPGPlKFSWYKK-DMLNKETKIlKSSNAEFKISQVNISDAGEYYCEANNSRRSFVSRA 386
Cdd:cd05728   14 GSSLRWECKASGNPRP-AYRWLKNgQPLASENRI-EVEAGDLRITKLSLSDSGMYQCVAENKHGTIYASA 81
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
314-379 9.24e-04

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: 38.44  E-value: 9.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164420687 314 LVFEGQLLLLNCSVKGVPGPlKFSWYK-KDMLNKETKILKSSNAEFKISQVNISDAGEYYCEANNSR 379
Cdd:cd05852   13 LAAKGGRVIIECKPKAAPKP-KFSWSKgTELLVNNSRISIWDDGSLEILNITKLDEGSYTCFAENNR 78
IgC_CRIg cd16082
Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin ...
315-375 1.33e-03

Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also referred to as Z39Ig and V-set and Ig domain-containing 4 (VSIG4)) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. CRIg plays a role in the complement system, an inhibitor of the alternative pathway convertases, and a negative regulator of T cell activation. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409504  Cd Length: 86  Bit Score: 38.20  E-value: 1.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420687 315 VFEGQLLLLNCSVKGVPgPLKFSWYKKDMLNKE-TKILKSSNAEFKISQVniSDAGEYYCEA 375
Cdd:cd16082   10 VPQGMRISLQCQAWGSP-PISYVWYKEQTNNQEpIKVAALSTLLFKPAVV--ADSGSYFCTA 68
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
318-381 1.67e-03

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


Pssm-ID: 409551  Cd Length: 94  Bit Score: 37.86  E-value: 1.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164420687 318 GQLLLLNCSVKGVPGPLKFSWYKK-----DMLNKETKILKSSNAEFKISQVNISDAGEYYCEANNSRRS 381
Cdd:cd20959   17 GMRAQLHCGVPGGDLPLNIRWTLDgqpisDDLGITVSRLGRRSSILSIDSLEASHAGNYTCHARNSAGS 85
Ig2_FcgammaR_like cd05753
Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
315-391 1.91e-03

Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409411  Cd Length: 83  Bit Score: 37.67  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 315 VFEGQLLLLNCSvkgvpgplkfSWYKKDMLN----KETKILKSS--NAEFKISQVNISDAGEYYCEANNSRRSFVSRAFP 388
Cdd:cd05753   11 VFEGEPLTLRCH----------GWKDKKVHKvtyyKDGKALKFSyeNSNFSIPQATLSDSGSYHCSGTVRIKRRSSESVN 80

                 ...
gi 164420687 389 ITI 391
Cdd:cd05753   81 ITV 83
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
38-101 2.03e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 37.37  E-value: 2.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164420687   38 LQPPWTTFFRGEVVTLTCYRFGFSVPqKTKWYQKRKTVKQTPGALVIKAHtlkVHESGEYWCQA 101
Cdd:pfam13895   4 LTPSPTVVTEGEPVTLTCSAPGNPPP-SYTWYKDGSAISSSPNFFTLSVS---AEDSGTYTCVA 63
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
117-201 2.45e-03

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: 37.40  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 117 DFLVLQAPPAVFEGDSVVLRCYAkKGIEAETLTFYKDGKALTLHPQS------SEFYIH-----RANLKDNGQYKCTSKK 185
Cdd:cd20951    2 EFIIRLQSHTVWEKSDAKLRVEV-QGKPDPEVKWYKNGVPIDPSSIPgkykieSEYGVHvlhirRVTVEDSAVYSAVAKN 80
                         90
                 ....*....|....*.
gi 164420687 186 kwSFGSLYTSNTVVVQ 201
Cdd:cd20951   81 --IHGEASSSASVVVE 94
Ig1_FcgammaR_like cd05752
First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
315-381 2.60e-03

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409410 [Multi-domain]  Cd Length: 79  Bit Score: 36.96  E-value: 2.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164420687 315 VFEGQLLLLNCSVKGVPGPLKFSWYKKDmlnketKILKSSNAEFKISQVNISDAGEYYCEANNSRRS 381
Cdd:cd05752   12 VFQGEKVTLTCQGFYSPEQNSTQWYHNG------TLISSTSSSYRIVAATVNDSGEYRCQTQGSSLS 72
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
315-378 2.74e-03

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: 37.23  E-value: 2.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420687 315 VFEGQLLLLNCSVKGVPGPlKFSW--------YKKDMLNKETKIlkssnAEFKISQVNISDAGEYYCEANNS 378
Cdd:cd20976   13 AVEGQDFVAQCSARGKPVP-RITWirnaqplqYAADRSTCEAGV-----GELHIQDVLPEDHGTYTCLAKNA 78
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
310-387 3.67e-03

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


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 37.24  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164420687 310 PASKLVFEGQLLLLNCSVKGVPGPLKFsWYKKDMLN---------KETKILKSSNAEFKISQVNISDAGEYYCEANNSRR 380
Cdd:cd05726    6 PRDQVVALGRTVTFQCETKGNPQPAIF-WQKEGSQNllfpyqppqPSSRFSVSPTGDLTITNVQRSDVGYYICQALNVAG 84

                 ....*..
gi 164420687 381 SFVSRAF 387
Cdd:cd05726   85 SILAKAQ 91
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
323-385 3.75e-03

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


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 37.22  E-value: 3.75e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164420687 323 LNCSVKGVPGPLkfswYKKDMLNKETKILKSS-----NAEFKISQ-VNISDAGEYYCEANNSRRSFVSR 385
Cdd:cd04967   24 LNCRARANPVPS----YRWLMNGTEIDLESDYryslvDGTLVISNpSKAKDAGHYQCLATNTVGSVLSR 88
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
317-377 6.22e-03

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


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 35.68  E-value: 6.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164420687 317 EGQLLLLNCSVKGVPGPLkFSWYKK-DMLNKETKILKSSNAEFKISQVNISDAGEYYCEANN 377
Cdd:cd05745    1 EGQTVDFLCEAQGYPQPV-IAWTKGgSQLSVDRRHLVLSSGTLRISRVALHDQGQYECQAVN 61
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
35-101 7.23e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 7.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164420687   35 VVSLQPPWTTFFRGEVVTLTCYRFGFSVPQKTkWY---QKRKTVKQTPGALVIKAHTLKVHE-----SGEYWCQA 101
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPTIT-WYkngEPISSGSTRSRSLSGSNSTLTISNvtrsdAGTYTCVA 76
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
133-182 8.31e-03

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: 35.38  E-value: 8.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164420687 133 VVLRCYAKkGIEAETLTFYKDGKALTLHPQ--------SSEFYIHRANLKDNGQYKCT 182
Cdd:cd00096    1 VTLTCSAS-GNPPPTITWYKNGKPLPPSSRdsrrselgNGTLTISNVTLEDSGTYTCV 57
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
309-371 8.49e-03

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 36.03  E-value: 8.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164420687 309 IPASKLVFEGQLLLLNCSVKGVPGPlKFSWYKKDMLNKET-----KILKSSNAEFKISQVNISDAGEY 371
Cdd:cd05737    7 LPDVVTIMEGKTLNLTCNVWGDPPP-EVSWLKNDQALAFLdhcnlKVEAGRTVYFTINGVSSEDSGKY 73
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH