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Conserved domains on  [gi|42821116|ref|NP_981954|]
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neural cell adhesion molecule 2 precursor [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ig1_NCAM-2 cd05866
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: ...
21-112 1.64e-60

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule.


:

Pssm-ID: 143274  Cd Length: 92  Bit Score: 201.03  E-value: 1.64e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116  21 LQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKG 100
Cdd:cd05866   1 LQVSISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIVSSQRVVVQKEGVRSRLTIYNANIEDAGIYRCQATDAKG 80
                        90
                ....*....|..
gi 42821116 101 QTQEATVVLEIY 112
Cdd:cd05866  81 QTQEATVVLEIY 92
Ig super family cl11960
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
300-397 6.33e-59

Immunoglobulin domain; 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, 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.


The actual alignment was detected with superfamily member cd05870:

Pssm-ID: 325142  Cd Length: 98  Bit Score: 196.74  E-value: 6.33e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 300 VQPHILQLKNETTSENGHVTLICEAEGEPVPEITWKRAIDGVTFSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYD 379
Cdd:cd05870   1 VQPHIIQLKNETTVENGAATLSCKAEGEPIPEITWKRASDGHTFSEGDKSPDGRIEVKGQHGESSLHIKDVKLSDSGRYD 80
                        90
                ....*....|....*...
gi 42821116 380 CEAASRIGGHQRSMHLDI 397
Cdd:cd05870  81 CEAASRIGGHQKSMYLDI 98
Ig super family cl11960
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
208-301 1.12e-21

Immunoglobulin domain; 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, 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.


The actual alignment was detected with superfamily member cd05730:

Pssm-ID: 325142  Cd Length: 95  Bit Score: 92.30  E-value: 1.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 208 PPAIVMPQKSFNATAERGEEMTLTCKASGSPDPAISWFRNGKLIE-ENEKYILKGSNTELTVRNIINKDGGSYVCKATNK 286
Cdd:cd05730   1 PPTIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIEsGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENK 80
                        90
                ....*....|....*
gi 42821116 287 AGEDQKQAFLQVFVQ 301
Cdd:cd05730  81 AGEQEAEIHLKVFAK 95
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
496-588 8.17e-20

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


:

Pssm-ID: 238020  Cd Length: 93  Bit Score: 87.17  E-value: 8.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 496 PSSPRGVKIIELSQTTAKISFNKPESHGGvPIHHYQVDVMEETSETWKIVRSHGV-QTTVVLSSLEPNTTYEVRVAAVNG 574
Cdd:cd00063   1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNG 79
                        90
                ....*....|....
gi 42821116 575 KGQGDYSKIEIFQT 588
Cdd:cd00063  80 GGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
594-678 8.54e-11

Fibronectin type III domain;


:

Pssm-ID: 306538  Cd Length: 85  Bit Score: 60.89  E-value: 8.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   594 PSPPSIHGQPSSGKSFKISITKQDDGGAPILEYIVKYRSKDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAANRLG 673
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                  ....*
gi 42821116   674 YSEPT 678
Cdd:pfam00041  81 EGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
413-491 2.03e-10

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


:

Pssm-ID: 214653  Cd Length: 85  Bit Score: 59.83  E-value: 2.03e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116    413 WEGNPINISCDVKANPPASIHWRREKLVLPAENtTHLKTHSVGRKMILEIARTSDNDFGRYNCTATNRLGTRFQEYILE 491
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
122-187 2.97e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 316449  Cd Length: 76  Bit Score: 44.03  E-value: 2.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116   122 SPQEFKQGEDAEVVCRVSSSPAPAVSWlYHNEEVTTIPDNRFAVLANNNLQILNINKSDEGIYRCE 187
Cdd:pfam13927   9 SSVVVLEGESVTLTCEATGGPPPTITW-YKNGKPGPTSSRISLSGSNSTLTISNVTREDSGTYTCV 73
 
Name Accession Description Interval E-value
Ig1_NCAM-2 cd05866
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: ...
21-112 1.64e-60

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule.


Pssm-ID: 143274  Cd Length: 92  Bit Score: 201.03  E-value: 1.64e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116  21 LQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKG 100
Cdd:cd05866   1 LQVSISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIVSSQRVVVQKEGVRSRLTIYNANIEDAGIYRCQATDAKG 80
                        90
                ....*....|..
gi 42821116 101 QTQEATVVLEIY 112
Cdd:cd05866  81 QTQEATVVLEIY 92
Ig_NCAM-2 cd05870
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM ...
300-397 6.33e-59

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM); Ig_NCAM-2: immunoglobulin (Ig)-like domain similar to the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM , including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule.


Pssm-ID: 143278  Cd Length: 98  Bit Score: 196.74  E-value: 6.33e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 300 VQPHILQLKNETTSENGHVTLICEAEGEPVPEITWKRAIDGVTFSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYD 379
Cdd:cd05870   1 VQPHIIQLKNETTVENGAATLSCKAEGEPIPEITWKRASDGHTFSEGDKSPDGRIEVKGQHGESSLHIKDVKLSDSGRYD 80
                        90
                ....*....|....*...
gi 42821116 380 CEAASRIGGHQRSMHLDI 397
Cdd:cd05870  81 CEAASRIGGHQKSMYLDI 98
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
208-301 1.12e-21

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig3_NCAM-1_like: domain similar to the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1,and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207  Cd Length: 95  Bit Score: 92.30  E-value: 1.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 208 PPAIVMPQKSFNATAERGEEMTLTCKASGSPDPAISWFRNGKLIE-ENEKYILKGSNTELTVRNIINKDGGSYVCKATNK 286
Cdd:cd05730   1 PPTIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIEsGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENK 80
                        90
                ....*....|....*
gi 42821116 287 AGEDQKQAFLQVFVQ 301
Cdd:cd05730  81 AGEQEAEIHLKVFAK 95
I-set pfam07679
Immunoglobulin I-set domain;
22-111 6.73e-21

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 90.01  E-value: 6.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    22 QVTISLSKVELSVGESKFFTCTAIGEPE-SIDWYNPqGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKG 100
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDpEVSWFKD-GQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                          90
                  ....*....|.
gi 42821116   101 QtQEATVVLEI 111
Cdd:pfam07679  81 E-AEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
496-588 8.17e-20

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


Pssm-ID: 238020  Cd Length: 93  Bit Score: 87.17  E-value: 8.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 496 PSSPRGVKIIELSQTTAKISFNKPESHGGvPIHHYQVDVMEETSETWKIVRSHGV-QTTVVLSSLEPNTTYEVRVAAVNG 574
Cdd:cd00063   1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNG 79
                        90
                ....*....|....
gi 42821116 575 KGQGDYSKIEIFQT 588
Cdd:cd00063  80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
212-298 1.26e-19

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 86.54  E-value: 1.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   212 VMPQKSFNATAERGEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILK--GSNTELTVRNIINKDGGSYVCKATNKAGE 289
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTyeGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                  ....*....
gi 42821116   290 DQKQAFLQV 298
Cdd:pfam07679  82 AEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
496-578 4.77e-16

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


Pssm-ID: 214495  Cd Length: 83  Bit Score: 76.11  E-value: 4.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    496 PSSPRGVKIIELSQTTAKISFNKPESHGGV-PIHHYQVdVMEETSETWKIVRSHGVQTTVVLSSLEPNTTYEVRVAAVNG 574
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRV-EYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                   ....
gi 42821116    575 KGQG 578
Cdd:smart00060  80 AGEG 83
IG smart00409
Immunoglobulin;
219-298 9.59e-15

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 72.15  E-value: 9.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    219 NATAERGEEMTLTCKASGSPDPAISWFRNG-KLIEENEKYILKGSNTE--LTVRNIINKDGGSYVCKATNKAGEDQKQAF 295
Cdd:smart00409   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                   ...
gi 42821116    296 LQV 298
Cdd:smart00409  83 LTV 85
fn3 pfam00041
Fibronectin type III domain;
497-581 1.31e-14

Fibronectin type III domain;


Pssm-ID: 306538  Cd Length: 85  Bit Score: 71.68  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   497 SSPRGVKIIELSQTTAKISFNKPESHGGvPIHHYQVDV-MEETSETWKIVRSHGVQTTVVLSSLEPNTTYEVRVAAVNGK 575
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYrPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                  ....*.
gi 42821116   576 GQGDYS 581
Cdd:pfam00041  80 GEGPPS 85
IG smart00409
Immunoglobulin;
28-111 1.80e-14

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 71.38  E-value: 1.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116     28 SKVELSVGESKFFTCTAIGEPE-SIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTqEAT 106
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPpEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSA-SSG 80

                   ....*
gi 42821116    107 VVLEI 111
Cdd:smart00409  81 TTLTV 85
IG smart00409
Immunoglobulin;
308-395 6.90e-13

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 66.76  E-value: 6.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    308 KNETTSENGHVTLICEAEGEPVPEITWKRaidgvtfsEGDK--SPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASR 385
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTWYK--------QGGKllAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNS 73
                           90
                   ....*....|
gi 42821116    386 IGGHQRSMHL 395
Cdd:smart00409  74 SGSASSGTTL 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
302-382 5.77e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 64.06  E-value: 5.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   302 PHI-LQLKNETTSENGHVTLICEAEGEPVPEITWKRaidgvtfseGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDC 380
Cdd:pfam13927   2 PVItVSPSSVVVLEGESVTLTCEATGGPPPTITWYK---------NGKPGPTSSRISLSGSNSTLTISNVTREDSGTYTC 72

                  ..
gi 42821116   381 EA 382
Cdd:pfam13927  73 VA 74
fn3 pfam00041
Fibronectin type III domain;
594-678 8.54e-11

Fibronectin type III domain;


Pssm-ID: 306538  Cd Length: 85  Bit Score: 60.89  E-value: 8.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   594 PSPPSIHGQPSSGKSFKISITKQDDGGAPILEYIVKYRSKDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAANRLG 673
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                  ....*
gi 42821116   674 YSEPT 678
Cdd:pfam00041  81 EGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
413-491 2.03e-10

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 59.83  E-value: 2.03e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116    413 WEGNPINISCDVKANPPASIHWRREKLVLPAENtTHLKTHSVGRKMILEIARTSDNDFGRYNCTATNRLGTRFQEYILE 491
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
401-479 2.89e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 59.05  E-value: 2.89e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116   401 PKFVSNQTMYYSWEGNPINISCDVKANPPASIHWRREKlvlpAENTTHLKTHSVGRKMILEIARTSDNDFGRYNCTATN 479
Cdd:pfam13927   2 PVITVSPSSVVVLEGESVTLTCEATGGPPPTITWYKNG----KPGPTSSRISLSGSNSTLTISNVTREDSGTYTCVASN 76
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
418-484 9.96e-08

Immunoglobulin domain; 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, 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: 319273  Cd Length: 70  Bit Score: 51.47  E-value: 9.96e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42821116 418 INISCDVKANPPASIHWRREKLVLPaeNTTHLKTHSVGRKMILEIARTSDNDFGRYNCTATNRLGTR 484
Cdd:cd00096   1 VTLTCSASGNPPPTITWLKNGKPLP--SSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSA 65
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
594-678 1.09e-07

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


Pssm-ID: 238020  Cd Length: 93  Bit Score: 51.73  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 594 PSPPS-IHGQPSSGKSFKISITKQDDGGAPILEYIVKYRSKDkEDQWLE-KKVQGNKDHIILEHLQWTMGYEVQITAANR 671
Cdd:cd00063   1 PSPPTnLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKG-SGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                ....*..
gi 42821116 672 LGYSEPT 678
Cdd:cd00063  80 GGESPPS 86
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
594-675 9.08e-07

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


Pssm-ID: 214495  Cd Length: 83  Bit Score: 48.76  E-value: 9.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    594 PSPPS-IHGQPSSGKSFKISIT--KQDDGGAPILEYIVKYRskDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAAN 670
Cdd:smart00060   1 PSPPSnLRVTDVTSTSVTLSWEppPDDGITGYIVGYRVEYR--EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                   ....*
gi 42821116    671 RLGYS 675
Cdd:smart00060  79 GAGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
122-187 2.97e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 44.03  E-value: 2.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116   122 SPQEFKQGEDAEVVCRVSSSPAPAVSWlYHNEEVTTIPDNRFAVLANNNLQILNINKSDEGIYRCE 187
Cdd:pfam13927   9 SSVVVLEGESVTLTCEATGGPPPTITW-YKNGKPGPTSSRISLSGSNSTLTISNVTREDSGTYTCV 73
IGc2 smart00408
Immunoglobulin C-2 Type;
128-189 4.24e-05

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 43.55  E-value: 4.24e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42821116    128 QGEDAEVVCRVSSSPAPAVSWLYHNEEvttIPDNRFAVLANNNLQILNINKSDEGIYRCEGR 189
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKDGKP---LPESNRFVASGSTLTIKSVSLEDSGLYTCVAE 59
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
178-281 5.80e-04

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173  Cd Length: 227  Bit Score: 42.21  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116  178 KSDEGIYRCE---GRVEARGEIDFrdiivivnvppaiVMPQKSFNATAERGEEMTLTCK-----ASGSPDPAISWFRNGK 249
Cdd:PHA02826 107 NIDEGIYICTissGNICEESTIRL-------------TFDSGTINYQFNSGKDSKLHCYgtdgiSSTFKDYTLTWYKNGN 173
                         90       100       110
                 ....*....|....*....|....*....|..
gi 42821116  250 LIEENEKYILKGSNTELTVRNIINKDGGSYVC 281
Cdd:PHA02826 174 IVLYTDRIQLRNNNSTLVIKSATHDDSGIYTC 205
Ig4_Neogenin cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth ...
136-186 5.81e-04

Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC, which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain.


Pssm-ID: 212460  Cd Length: 71  Bit Score: 40.33  E-value: 5.81e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 42821116 136 CRVSSSPAPAVSWLYHNEEVttIPDNRFAVLANNNLQILNINKSDEGIYRC 186
Cdd:cd05723   6 CEVTGKPTPTVKWVKNGDMV--IPSDYFKIVKEHNLQVLGLVKSDEGFYQC 54
 
Name Accession Description Interval E-value
Ig1_NCAM-2 cd05866
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: ...
21-112 1.64e-60

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule.


Pssm-ID: 143274  Cd Length: 92  Bit Score: 201.03  E-value: 1.64e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116  21 LQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKG 100
Cdd:cd05866   1 LQVSISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIVSSQRVVVQKEGVRSRLTIYNANIEDAGIYRCQATDAKG 80
                        90
                ....*....|..
gi 42821116 101 QTQEATVVLEIY 112
Cdd:cd05866  81 QTQEATVVLEIY 92
Ig_NCAM-2 cd05870
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM ...
300-397 6.33e-59

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM); Ig_NCAM-2: immunoglobulin (Ig)-like domain similar to the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM , including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule.


Pssm-ID: 143278  Cd Length: 98  Bit Score: 196.74  E-value: 6.33e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 300 VQPHILQLKNETTSENGHVTLICEAEGEPVPEITWKRAIDGVTFSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYD 379
Cdd:cd05870   1 VQPHIIQLKNETTVENGAATLSCKAEGEPIPEITWKRASDGHTFSEGDKSPDGRIEVKGQHGESSLHIKDVKLSDSGRYD 80
                        90
                ....*....|....*...
gi 42821116 380 CEAASRIGGHQRSMHLDI 397
Cdd:cd05870  81 CEAASRIGGHQKSMYLDI 98
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
300-397 8.66e-49

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar proteins; Ig_NCAM-1 like: domain similar to the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE).


Pssm-ID: 143209  Cd Length: 96  Bit Score: 168.86  E-value: 8.66e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 300 VQPHILQLKNETTSENGHVTLICEAEGEPVPEITWKRAIdgVTFSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYD 379
Cdd:cd05732   1 VQPKITYLENQTAVELEQITLTCEAEGDPIPEITWRRAT--RNFSEGDKSLDGRIVVRGHARVSSLTLKDVQLTDAGRYD 78
                        90
                ....*....|....*...
gi 42821116 380 CEAASRIGGHQRSMHLDI 397
Cdd:cd05732  79 CEASNRIGGDQQSMYLEV 96
Ig1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1 and similar ...
21-111 1.61e-45

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1 and similar proteins; Ig1_NCAM-1 like: first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-nonNCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE).


Pssm-ID: 319283  Cd Length: 93  Bit Score: 159.72  E-value: 1.61e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116  21 LQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIIS--TQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDA 98
Cdd:cd04977   1 LQVKIIPSYAEISVGESKFFLCKVSGDAKNINWVSPNGEKVLTkhGNLKVVNHGSVLSSLTIYNANINDAGIYKCVATNG 80
                        90
                ....*....|...
gi 42821116  99 KGQTQEATVVLEI 111
Cdd:cd04977  81 KGTESEATVKLDI 93
Ig1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1; Ig1_NCAM-1: ...
21-112 4.68e-23

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1; Ig1_NCAM-1: first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143273  Cd Length: 96  Bit Score: 96.63  E-value: 4.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116  21 LQVTISLSKVELSVGESKFFTCTAIGEPES--IDWYNPQGEKIISTQR--VMLQKEGVRSRLTIYNANIEDAGIYRCQAT 96
Cdd:cd05865   1 LQVDIVPSQGEISVGESKFFLCQVAGEAKDkdISWFSPNGEKLTPNQQriSVVRNDDYSSTLTIYNANIDDAGIYKCVVS 80
                        90
                ....*....|....*.
gi 42821116  97 DAKGQTQEATVVLEIY 112
Cdd:cd05865  81 NEDEGESEATVNVKIF 96
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
208-301 1.12e-21

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig3_NCAM-1_like: domain similar to the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1,and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207  Cd Length: 95  Bit Score: 92.30  E-value: 1.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 208 PPAIVMPQKSFNATAERGEEMTLTCKASGSPDPAISWFRNGKLIE-ENEKYILKGSNTELTVRNIINKDGGSYVCKATNK 286
Cdd:cd05730   1 PPTIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIEsGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENK 80
                        90
                ....*....|....*
gi 42821116 287 AGEDQKQAFLQVFVQ 301
Cdd:cd05730  81 AGEQEAEIHLKVFAK 95
I-set pfam07679
Immunoglobulin I-set domain;
22-111 6.73e-21

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 90.01  E-value: 6.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    22 QVTISLSKVELSVGESKFFTCTAIGEPE-SIDWYNPqGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKG 100
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDpEVSWFKD-GQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
                          90
                  ....*....|.
gi 42821116   101 QtQEATVVLEI 111
Cdd:pfam07679  81 E-AEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
496-588 8.17e-20

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


Pssm-ID: 238020  Cd Length: 93  Bit Score: 87.17  E-value: 8.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 496 PSSPRGVKIIELSQTTAKISFNKPESHGGvPIHHYQVDVMEETSETWKIVRSHGV-QTTVVLSSLEPNTTYEVRVAAVNG 574
Cdd:cd00063   1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNG 79
                        90
                ....*....|....
gi 42821116 575 KGQGDYSKIEIFQT 588
Cdd:cd00063  80 GGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
212-298 1.26e-19

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 86.54  E-value: 1.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   212 VMPQKSFNATAERGEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILK--GSNTELTVRNIINKDGGSYVCKATNKAGE 289
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTyeGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                  ....*....
gi 42821116   290 DQKQAFLQV 298
Cdd:pfam07679  82 AEASAELTV 90
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
300-397 1.44e-17

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


Pssm-ID: 143277  Cd Length: 97  Bit Score: 80.79  E-value: 1.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 300 VQPHILQLKNETTSE-NGHVTLICEAEGEPVPEITWKRAIDgvTFSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRY 378
Cdd:cd05869   1 AKPKITYVENQTAMElEEQITLTCEASGDPIPSITWRTSTR--NISSEEKTLDGHIVVRSHARVSSLTLKYIQYTDAGEY 78
                        90
                ....*....|....*....
gi 42821116 379 DCEAASRIGGHQRSMHLDI 397
Cdd:cd05869  79 LCTASNTIGQDSQSMYLEV 97
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
496-578 4.77e-16

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


Pssm-ID: 214495  Cd Length: 83  Bit Score: 76.11  E-value: 4.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    496 PSSPRGVKIIELSQTTAKISFNKPESHGGV-PIHHYQVdVMEETSETWKIVRSHGVQTTVVLSSLEPNTTYEVRVAAVNG 574
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRV-EYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                   ....
gi 42821116    575 KGQG 578
Cdd:smart00060  80 AGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
208-285 1.05e-15

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 74.84  E-value: 1.05e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116   208 PPAIVMPQKsfNATAERGEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILKGSNTELTVRNIINKDGGSYVCKATN 285
Cdd:pfam13927   1 KPVITVSPS--SVVVLEGESVTLTCEATGGPPPTITWYKNGKPGPTSSRISLSGSNSTLTISNVTREDSGTYTCVASN 76
IG smart00409
Immunoglobulin;
219-298 9.59e-15

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 72.15  E-value: 9.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    219 NATAERGEEMTLTCKASGSPDPAISWFRNG-KLIEENEKYILKGSNTE--LTVRNIINKDGGSYVCKATNKAGEDQKQAF 295
Cdd:smart00409   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                   ...
gi 42821116    296 LQV 298
Cdd:smart00409  83 LTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
219-298 9.59e-15

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 72.15  E-value: 9.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    219 NATAERGEEMTLTCKASGSPDPAISWFRNG-KLIEENEKYILKGSNTE--LTVRNIINKDGGSYVCKATNKAGEDQKQAF 295
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                   ...
gi 42821116    296 LQV 298
Cdd:smart00410  83 LTV 85
fn3 pfam00041
Fibronectin type III domain;
497-581 1.31e-14

Fibronectin type III domain;


Pssm-ID: 306538  Cd Length: 85  Bit Score: 71.68  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   497 SSPRGVKIIELSQTTAKISFNKPESHGGvPIHHYQVDV-MEETSETWKIVRSHGVQTTVVLSSLEPNTTYEVRVAAVNGK 575
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNG-PITGYEVEYrPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                  ....*.
gi 42821116   576 GQGDYS 581
Cdd:pfam00041  80 GEGPPS 85
IG smart00409
Immunoglobulin;
28-111 1.80e-14

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 71.38  E-value: 1.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116     28 SKVELSVGESKFFTCTAIGEPE-SIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTqEAT 106
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPpEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSA-SSG 80

                   ....*
gi 42821116    107 VVLEI 111
Cdd:smart00409  81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
28-111 1.80e-14

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 71.38  E-value: 1.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116     28 SKVELSVGESKFFTCTAIGEPE-SIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTqEAT 106
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPpEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSA-SSG 80

                   ....*
gi 42821116    107 VVLEI 111
Cdd:smart00410  81 TTLTV 85
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
229-294 2.99e-14

Immunoglobulin domain; 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, 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: 319273  Cd Length: 70  Bit Score: 70.35  E-value: 2.99e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 229 TLTCKASGSPDPAISWFRNGKLIEENEKY--ILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQA 294
Cdd:cd00096   2 TLTCSASGNPPPTITWLKNGKPLPSSSRFrrRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASV 69
IG smart00409
Immunoglobulin;
308-395 6.90e-13

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 66.76  E-value: 6.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    308 KNETTSENGHVTLICEAEGEPVPEITWKRaidgvtfsEGDK--SPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASR 385
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTWYK--------QGGKllAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNS 73
                           90
                   ....*....|
gi 42821116    386 IGGHQRSMHL 395
Cdd:smart00409  74 SGSASSGTTL 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
308-395 6.90e-13

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 66.76  E-value: 6.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    308 KNETTSENGHVTLICEAEGEPVPEITWKRaidgvtfsEGDK--SPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASR 385
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYK--------QGGKllAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNS 73
                           90
                   ....*....|
gi 42821116    386 IGGHQRSMHL 395
Cdd:smart00410  74 SGSASSGTTL 83
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
318-394 1.31e-12

Immunoglobulin domain; 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, 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: 319273  Cd Length: 70  Bit Score: 65.73  E-value: 1.31e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42821116 318 VTLICEAEGEPVPEITWKRaidgvtfSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIGGHQRSMH 394
Cdd:cd00096   1 VTLTCSASGNPPPTITWLK-------NGKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
IGc2 smart00408
Immunoglobulin C-2 Type;
225-288 1.42e-12

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 65.51  E-value: 1.42e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42821116    225 GEEMTLTCKASGSPDPAISWFRNGKLIEENekYILKGSNTELTVRNIINKDGGSYVCKATNKAG 288
Cdd:smart00408   2 GQSVTLTCPAEGNPVPNITWLKDGKPLPES--NRFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
IGc2 smart00408
Immunoglobulin C-2 Type;
314-387 3.12e-12

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 64.35  E-value: 3.12e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42821116    314 ENGHVTLICEAEGEPVPEITWKRaiDGVTFSEGDKSpdgrievkgQHGRSSLHIRDVKLSDSGRYDCEAASRIG 387
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLK--DGKPLPESNRF---------VASGSTLTIKSVSLEDSGLYTCVAENSAG 63
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
302-382 5.77e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 64.06  E-value: 5.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   302 PHI-LQLKNETTSENGHVTLICEAEGEPVPEITWKRaidgvtfseGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDC 380
Cdd:pfam13927   2 PVItVSPSSVVVLEGESVTLTCEATGGPPPTITWYK---------NGKPGPTSSRISLSGSNSTLTISNVTREDSGTYTC 72

                  ..
gi 42821116   381 EA 382
Cdd:pfam13927  73 VA 74
I-set pfam07679
Immunoglobulin I-set domain;
302-387 7.62e-12

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 63.82  E-value: 7.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   302 PHILQ-LKNETTSENGHVTLICEAEGEPVPEITWKRaiDGVTFSegdksPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDC 380
Cdd:pfam07679   1 PKFTQkPKDVEVQEGESARFTCTVTGTPDPEVSWFK--DGQPLR-----SSDRFKVTYEGGTYTLTISNVQPDDSGKYTC 73

                  ....*..
gi 42821116   381 EAASRIG 387
Cdd:pfam07679  74 VATNSAG 80
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth ...
318-395 6.51e-11

Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells, which have undergone programmed cell death, and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 60.66  E-value: 6.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 318 VTLICEAEGEPVPEITWKRaiDGVTFSEGDK---SPDGrievkgqhgrsSLHIRDVKLSDSGRYDCEAASRIGGHQRSMH 394
Cdd:cd05746   1 VQIPCSAQGDPEPTITWNK--DGVQVTESGKfhiSPEG-----------YLAIRDVGVADQGRYECVARNTIGYASVSMV 67

                .
gi 42821116 395 L 395
Cdd:cd05746  68 L 68
fn3 pfam00041
Fibronectin type III domain;
594-678 8.54e-11

Fibronectin type III domain;


Pssm-ID: 306538  Cd Length: 85  Bit Score: 60.89  E-value: 8.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   594 PSPPSIHGQPSSGKSFKISITKQDDGGAPILEYIVKYRSKDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAANRLG 673
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                  ....*
gi 42821116   674 YSEPT 678
Cdd:pfam00041  81 EGPPS 85
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
219-298 8.74e-11

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


Pssm-ID: 143277  Cd Length: 97  Bit Score: 61.15  E-value: 8.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 219 NATA-ERGEEMTLTCKASGSPDPAISWFRNGKLIEENEK----YILKGSN---TELTVRNIINKDGGSYVCKATNKAGED 290
Cdd:cd05869  10 NQTAmELEEQITLTCEASGDPIPSITWRTSTRNISSEEKtldgHIVVRSHarvSSLTLKYIQYTDAGEYLCTASNTIGQD 89

                ....*...
gi 42821116 291 QKQAFLQV 298
Cdd:cd05869  90 SQSMYLEV 97
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
318-388 1.49e-10

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar to 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, -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.


Pssm-ID: 143202  Cd Length: 69  Bit Score: 59.73  E-value: 1.49e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42821116 318 VTLICEAEGEPVPEITWKRaidgvtfsEGDKSPDGRIEVKGQHgrsSLHIRDVKLSDSGRYDCEAASRIGG 388
Cdd:cd05725   1 VEFQCEVGGDPVPTVLWRK--------EDGELPKGRAEILDDK---SLKIRNVTAGDEGSYTCEAENMVGK 60
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
413-491 2.03e-10

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 59.83  E-value: 2.03e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116    413 WEGNPINISCDVKANPPASIHWRREKLVLPAENtTHLKTHSVGRKMILEIARTSDNDFGRYNCTATNRLGTRFQEYILE 491
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
IG smart00409
Immunoglobulin;
413-491 2.03e-10

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 59.83  E-value: 2.03e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116    413 WEGNPINISCDVKANPPASIHWRREKLVLPAENtTHLKTHSVGRKMILEIARTSDNDFGRYNCTATNRLGTRFQEYILE 491
Cdd:smart00409   7 KEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
401-479 2.89e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 59.05  E-value: 2.89e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116   401 PKFVSNQTMYYSWEGNPINISCDVKANPPASIHWRREKlvlpAENTTHLKTHSVGRKMILEIARTSDNDFGRYNCTATN 479
Cdd:pfam13927   2 PVITVSPSSVVVLEGESVTLTCEATGGPPPTITWYKNG----KPGPTSSRISLSGSNSTLTISNVTREDSGTYTCVASN 76
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
22-96 7.19e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 57.89  E-value: 7.19e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116    22 QVTISLSKVELSVGESKFFTCTAIGEPE-SIDWYNPQGEkiiSTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQAT 96
Cdd:pfam13927   3 VITVSPSSVVVLEGESVTLTCEATGGPPpTITWYKNGKP---GPTSSRISLSGSNSTLTISNVTREDSGTYTCVAS 75
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
308-393 2.55e-09

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: 278476  Cd Length: 86  Bit Score: 56.43  E-value: 2.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   308 KNETTSENGHVTLICEA-EGEPVPEITWKRaiDGVTFSEGDKSPDGRievkGQHGRSSLHIRDVKLSDSGRYDCEAASRI 386
Cdd:pfam00047   4 PTVTVLEGDSATLTCSAsTGSPGPDVTWSK--EGGTLIESLKVKHDN----GRTTQSSLLISNVTKEDAGTYTCVVNNPG 77

                  ....*..
gi 42821116   387 GGHQRSM 393
Cdd:pfam00047  78 GPATLST 84
Ig2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; ...
229-291 3.97e-09

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; Ig2_Follistatin_like: domain similar to 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: 143213  Cd Length: 76  Bit Score: 55.70  E-value: 3.97e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42821116 229 TLTCKASGSPDPAISWFRNGKLI--EENEKYILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQ 291
Cdd:cd05736   2 SLRCHAEGIPLPRLTWLKNGMDItpKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEAGVDE 66
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; ...
215-298 4.10e-09

Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; Ig4_Contactin-2-like: 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 (aliases 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  Cd Length: 85  Bit Score: 55.68  E-value: 4.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 215 QKSFNATAERGEEMTLTCKASGSPDPAISWFRNGK-LIEENEKYILKGsntELTVRNIINKDGGSYVCKATNKAGEDQKQ 293
Cdd:cd05728   4 KVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQpLASENRIEVEAG---DLRITKLSLSDSGMYQCVAENKHGTIYAS 80

                ....*
gi 42821116 294 AFLQV 298
Cdd:cd05728  81 AELAV 85
Ig_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2); ...
221-288 5.56e-09

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 55.69  E-value: 5.56e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42821116 221 TAERGEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILK---GSNTELTVRNIINKDGGSYVCKATNKAG 288
Cdd:cd05891  12 TIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKleqGKYASLTIKGVTSEDSGKYSINVKNKYG 82
Ig2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain ...
225-298 6.02e-09

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain similar to 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 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.


Pssm-ID: 143201  Cd Length: 86  Bit Score: 55.48  E-value: 6.02e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 225 GEEMTLTCKAS-GSPDPAISWFRNGK-LIEENEKY-ILKGSNteLTVRNIINKDGGSYVCKATNKAGE-DQKQAFLQV 298
Cdd:cd05724  11 GEMAVLECSPPrGHPEPTVSWRKDGQpLNLDNERVrIVDDGN--LLIAEARKSDEGTYKCVATNMVGErESAAARLSV 86
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
225-299 7.37e-09

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); Ig4_L1-NrCAM_like: fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 319284  Cd Length: 76  Bit Score: 54.77  E-value: 7.37e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116 225 GEEMTLTCKASGSPDPAISWFRNGKLIEE-NEKYILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVF 299
Cdd:cd04978   1 GETGELICEAEGNPQPTITWRLNGVPIEPaPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHGYLLANAFLHVL 76
Ig_2 cd05764
Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: subgroup of the immunoglobulin (Ig) ...
225-298 9.91e-09

Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: 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. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 143241  Cd Length: 74  Bit Score: 54.41  E-value: 9.91e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116 225 GEEMTLTCKASGSPDPAISW-FRNGKLIEENEKYILKGSNT-ELTVRNIinKDGGSYVCKATNKAGEDQKQAFLQV 298
Cdd:cd05764   1 GQRATLRCKARGDPEPAIHWiSPDGKLISNSSRTLVYDNGTlDILITTV--KDTGSFTCIASNAAGEATATVELHI 74
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
318-382 1.21e-08

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


Pssm-ID: 143220  Cd Length: 78  Bit Score: 54.42  E-value: 1.21e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42821116 318 VTLICEAEGEPVPEITWKraidgvtFSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEA 382
Cdd:cd05743   4 VEFTCVATGVPTPIINWR-------LNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEA 61
Ig1_Robo cd07693
First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; ...
208-289 1.76e-08

First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; Ig1_Robo: domain similar to the first 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, -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.


Pssm-ID: 143317  Cd Length: 100  Bit Score: 54.09  E-value: 1.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 208 PPAIVMPQKSFnaTAERGEEMTLTCKASGSPDPAISWFRNGKLIEENE-----KYILKGSNTELTVRNIINK----DGGS 278
Cdd:cd07693   1 PPRIVEHPSDL--IVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKddprsHRIVLPSGSLFFLRVVHGRkgrsDEGV 78
                        90
                ....*....|.
gi 42821116 279 YVCKATNKAGE 289
Cdd:cd07693  79 YVCVAHNSLGE 89
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
219-292 1.97e-08

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: 278476  Cd Length: 86  Bit Score: 53.74  E-value: 1.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116   219 NATAERGEEMTLTCKAS-GSPDPAISWFRNGKLIEENEKY---ILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQK 292
Cdd:pfam00047   5 TVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVkhdNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGPATL 82
IGc2 smart00408
Immunoglobulin C-2 Type;
414-482 2.13e-08

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 53.18  E-value: 2.13e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116    414 EGNPINISCDVKANPPASIHWRREKLVLPAENTTHlktHSVGRkmiLEIARTSDNDFGRYNCTATNRLG 482
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKDGKPLPESNRFV---ASGST---LTIKSVSLEDSGLYTCVAENSAG 63
Ig_Myomesin_like_C cd05737
C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein; Ig_Myomesin_like_C: ...
220-298 2.35e-08

C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein; Ig_Myomesin_like_C: domain similar to the C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein. 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: 53.75  E-value: 2.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 220 ATAERGEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILK---GSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFL 296
Cdd:cd05737  11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKveaGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTV 90

                ..
gi 42821116 297 QV 298
Cdd:cd05737  91 SV 92
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
40-108 5.45e-08

Immunoglobulin domain; 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, 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: 319273  Cd Length: 70  Bit Score: 52.24  E-value: 5.45e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116  40 FTCTAIGEPE-SIDWYNPqGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGqTQEATVV 108
Cdd:cd00096   3 LTCSASGNPPpTITWLKN-GKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAG-SASASVT 70
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
418-484 9.96e-08

Immunoglobulin domain; 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, 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: 319273  Cd Length: 70  Bit Score: 51.47  E-value: 9.96e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42821116 418 INISCDVKANPPASIHWRREKLVLPaeNTTHLKTHSVGRKMILEIARTSDNDFGRYNCTATNRLGTR 484
Cdd:cd00096   1 VTLTCSASGNPPPTITWLKNGKPLP--SSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSA 65
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
594-678 1.09e-07

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


Pssm-ID: 238020  Cd Length: 93  Bit Score: 51.73  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 594 PSPPS-IHGQPSSGKSFKISITKQDDGGAPILEYIVKYRSKDkEDQWLE-KKVQGNKDHIILEHLQWTMGYEVQITAANR 671
Cdd:cd00063   1 PSPPTnLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKG-SGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                ....*..
gi 42821116 672 LGYSEPT 678
Cdd:cd00063  80 GGESPPS 86
Ig2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
225-289 1.76e-07

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); Ig2_FGFRL1-like: second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 143264  Cd Length: 82  Bit Score: 50.99  E-value: 1.76e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42821116 225 GEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILKGSNTELTVRNIINKDGGSYVCKATNKAGE 289
Cdd:cd05856   9 GSSVRLKCVASGNPRPDITWLKDNKPLTPTEIGESRKKKWTLSLKNLKPEDSGKYTCHVSNRAGE 73
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
225-302 2.73e-07

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


Pssm-ID: 143220  Cd Length: 78  Bit Score: 50.18  E-value: 2.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 225 GEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILKGSNTE--LTVRNIINKDGGSYVCKATNKAGedqkqaflQVFVQP 302
Cdd:cd05743   1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYgtLTIRDVKESDQGAYTCEAINTRG--------MVFGIP 72
Ig2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, ...
319-387 3.65e-07

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR; Ig2_RPTP_IIa_LAR_like: domain similar to the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions, comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains, and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 319301  Cd Length: 74  Bit Score: 50.05  E-value: 3.65e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116 319 TLICEAEGEPVPEITWKRaidgvTFSEGDKSPDGRIEvkgQHGRSSLHIRDVKLSDSGRYDCEAASRIG 387
Cdd:cd05738   2 TMLCAASGNPDPEITWFK-----DFLPVDTTSNGRIK---QLRSGALQIENSEESDQGKYECVATNSAG 62
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth Ig domain of ...
225-298 3.99e-07

Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth 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 act ivity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319278  Cd Length: 73  Bit Score: 49.75  E-value: 3.99e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42821116 225 GEEMTLTCKASGSPDPAISWFRNGKLIEENeKYILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQV 298
Cdd:cd04969   1 GGDVIIECKPKASPKPTISWSKGTELLTNS-SRICILPDGSLKIKNVSKSDEGKYTCFAVNFFGKANSTGSLSV 73
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
224-288 3.99e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 316418  Cd Length: 78  Bit Score: 49.68  E-value: 3.99e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42821116   224 RGEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILKGSNTeltvrniinkDGGSYVCKATNKAG 288
Cdd:pfam13895  13 EGEPVTLTCSAPGNPPANYTWYKGGEALNSSPNFISSVSAE----------DSGTYTCVARNGRG 67
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin ...
235-298 4.01e-07

Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin (Ig)-like domain found in titin-like proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin, and similar to titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle, which also have repeated Ig-like and FN-III domains.


Pssm-ID: 319305  Cd Length: 74  Bit Score: 49.53  E-value: 4.01e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116 235 SGSPDPAISWFRNGKLIEENEKYILK--GSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQV 298
Cdd:cd05748   9 SGRPTPTVTWSKDGQPLKLSGRVQIEttATSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATVNVKV 74
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: ...
318-387 4.75e-07

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, 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: 143275  Cd Length: 76  Bit Score: 49.50  E-value: 4.75e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 318 VTLICEAEGEPVPEITWKraIDGVTFSEGDKSPDGRIEvkgqhgRSSLHIRDVKLSDSGRYDCEAASRIG 387
Cdd:cd05867   4 ARLDCQVEGIPTPNITWS--INGAPIEGTDPDPRRHVS------SGALILTDVQPSDTAVYQCEARNRHG 65
Ig3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of ...
318-382 6.24e-07

Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third 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 act ivity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319277  Cd Length: 88  Bit Score: 49.47  E-value: 6.24e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42821116 318 VTLICEAEGEPVPEITWKRAiDGVTFSEGDKSPDGRIevkgqhgrssLHIRDVKLSDSGRYDCEA 382
Cdd:cd04968  19 VTLECFALGNPVPQIKWRKV-DGSPSSQWTTSTSEPV----------LEIPNVQFEDEGTYECEA 72
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); Ig4_ ...
225-299 7.75e-07

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); Ig4_ NrCAM: fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six IG-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 143276  Cd Length: 76  Bit Score: 48.84  E-value: 7.75e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 225 GEEMTLTCKASGSPDPAISWFRNGKLIE---ENEKYILKGSNteLTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVF 299
Cdd:cd05868   1 GEDGTLICRANGNPKPSISWLTNGVPIEiapTDPSRKVDGDT--IIFSKVQERSSAVYQCNASNEYGYLLANAFVNVL 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
594-675 9.08e-07

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


Pssm-ID: 214495  Cd Length: 83  Bit Score: 48.76  E-value: 9.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    594 PSPPS-IHGQPSSGKSFKISIT--KQDDGGAPILEYIVKYRskDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAAN 670
Cdd:smart00060   1 PSPPSnLRVTDVTSTSVTLSWEppPDDGITGYIVGYRVEYR--EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                   ....*
gi 42821116    671 RLGYS 675
Cdd:smart00060  79 GAGEG 83
Ig4_Robo cd05726
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig4_Robo: domain similar ...
225-298 1.12e-06

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig4_Robo: domain similar to 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, -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.


Pssm-ID: 143203  Cd Length: 90  Bit Score: 48.80  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 225 GEEMTLTCKASGSPDPAISWFRNG--------KLIEENEKYILKGSNtELTVRNIINKDGGSYVCKATNKAGEDQKQAFL 296
Cdd:cd05726   1 GRTVTFQCEATGNPQPAIFWQKEGsqnllfsyQPPQSSSRFSVSQTG-DLTITNVQRSDVGYYICQTLNVAGSILTKAYL 79

                ..
gi 42821116 297 QV 298
Cdd:cd05726  80 EV 81
IGc2 smart00408
Immunoglobulin C-2 Type;
35-100 1.30e-06

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 48.17  E-value: 1.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42821116     35 GESKFFTCTAIGEPE-SIDWYNpQGEKIISTQRVMLQkegvRSRLTIYNANIEDAGIYRCQATDAKG 100
Cdd:smart00408   2 GQSVTLTCPAEGNPVpNITWLK-DGKPLPESNRFVAS----GSTLTIKSVSLEDSGLYTCVAENSAG 63
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
410-482 1.63e-06

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: 278476  Cd Length: 86  Bit Score: 47.96  E-value: 1.63e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116   410 YYSWEGNPINISCDVK-ANPPASIHWRREKLVLPaenTTHLKTHSVGRKMI--LEIARTSDNDFGRYNCTATNRLG 482
Cdd:pfam00047   6 VTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLI---ESLKVKHDNGRTTQssLLISNVTKEDAGTYTCVVNNPGG 78
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
208-301 1.72e-06

Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third 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: 143259  Cd Length: 88  Bit Score: 48.09  E-value: 1.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 208 PPAIVMPQKsfNATAERGEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILKGSntELTVRNIINKDGGSYVCKATNKA 287
Cdd:cd05851   1 PADINVKFK--DTYALKGQNVTLECFALGNPVPVIRWRKILEPMPATAEISMSGA--VLKIFNIQPEDEGTYECEAENIK 76
                        90
                ....*....|....
gi 42821116 288 GEDQKQAFlqVFVQ 301
Cdd:cd05851  77 GKDKHQAR--VYVQ 88
Ig1_Contactin-2 cd05850
First immunoglobulin (Ig) domain of contactin-2; Ig1_Contactin-2: First Ig domain of the ...
208-288 2.22e-06

First immunoglobulin (Ig) domain of contactin-2; Ig1_Contactin-2: First Ig domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module by contacts between IG domains 1 and 4, and domains 2 and 3. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-2 is also expressed in retinal amacrine cells in the developing chick retina, corresponding to the period of formation and maturation of AC processes.


Pssm-ID: 143258  Cd Length: 94  Bit Score: 47.62  E-value: 2.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 208 PPAIVMPQKSfnatAErgEEMTLTCKASGSPDPAISWFRNGKLI--EENEKYILKGSNteLTVRNIIN-KDGGSYVCKAT 284
Cdd:cd05850   8 PSSLLFPEGS----PE--EKVTLGCRARASPPATYRWKMNGTEIkfAPESRYTLVAGN--LVINNPQKaRDAGSYQCLAI 79

                ....
gi 42821116 285 NKAG 288
Cdd:cd05850  80 NRCG 83
Ig1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First Ig domain of contactins. ...
203-288 2.37e-06

First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First Ig domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319276  Cd Length: 91  Bit Score: 47.59  E-value: 2.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 203 VIVNVPPAIVMPQKSFNataergEEMTLTCKASGSPDPAISWFRNGKLI--EENEKYILKGSNteLTVRNIIN-KDGGSY 279
Cdd:cd04967   3 VFEEQPDDTIFPEESDE------EKVALNCRARANPPPTYRWKMNGTEIklEPDSRYSLVGGN--LVISNPSKaKDAGHY 74

                ....*....
gi 42821116 280 VCKATNKAG 288
Cdd:cd04967  75 QCLATNTVG 83
Ig2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, ...
229-288 2.49e-06

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR; Ig2_RPTP_IIa_LAR_like: domain similar to the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions, comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains, and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 319301  Cd Length: 74  Bit Score: 47.35  E-value: 2.49e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42821116 229 TLTCKASGSPDPAISWFRNGKLIEENEKYILKGSNT-ELTVRNIINKDGGSYVCKATNKAG 288
Cdd:cd05738   2 TMLCAASGNPDPEITWFKDFLPVDTTSNGRIKQLRSgALQIENSEESDQGKYECVATNSAG 62
Ig2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar ...
315-397 2.85e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar proteins; Ig2_FGFR_like: domain similar to the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor_like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 319297  Cd Length: 85  Bit Score: 47.21  E-value: 2.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 315 NGHVTLICEAEGEPVPEITWKRaiDGVTFSEGDKSPDGRIEVKGQhgrsSLHIRDVKLSDSGRYDCEAASRIGGHQRSMH 394
Cdd:cd05729   9 NTKVRLECGARGNPTPNITWLK--DGKQKWKINVIRPTRVEEKGW----VLIIRRAIPRDTGKYTCIVSNQYGTINHTYD 82

                ...
gi 42821116 395 LDI 397
Cdd:cd05729  83 VKV 85
IgV cd00099
Immunoglobulin variable domain (IgV); IgV: Immunoglobulin variable domain (IgV). Members of ...
220-295 3.48e-06

Immunoglobulin variable domain (IgV); IgV: Immunoglobulin variable domain (IgV). Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 319275  Cd Length: 103  Bit Score: 47.39  E-value: 3.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 220 ATAERGEEMTLTCKASGS-PDPAISWFRN--GKlieeNEKYILKGSNTE--------------------LTVRNIINKDG 276
Cdd:cd00099   1 VSVSTGESVTLNCVLSGSfSLYSISWYRQkpGK----QPQFLISGSSTGkpgipgrfsgtrnggsssfsLTISNLRPEDS 76
                        90
                ....*....|....*....
gi 42821116 277 GSYVCKATNKAGEDQKQAF 295
Cdd:cd00099  77 GTYYCAVSEGPGGGDKLVF 95
Ig3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of ...
222-299 3.81e-06

Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third 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 act ivity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319277  Cd Length: 88  Bit Score: 47.16  E-value: 3.81e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116 222 AERGEEMTLTCKASGSPDPAISWFR-NGKLIEeneKYILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVF 299
Cdd:cd04968  13 ALKGQTVTLECFALGNPVPQIKWRKvDGSPSS---QWTTSTSEPVLEIPNVQFEDEGTYECEAENSRGKDTVQGRIIVQ 88
Ig2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar ...
225-289 4.39e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar proteins; Ig2_FGFR_like: domain similar to the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor_like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 319297  Cd Length: 85  Bit Score: 46.83  E-value: 4.39e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 225 GEEMTLTCKASGSPDPAISWFRNGK-LIEEN--EKYILKGSNTELTVRNIINKDGGSYVCKATNKAGE 289
Cdd:cd05729   9 NTKVRLECGARGNPTPNITWLKDGKqKWKINviRPTRVEEKGWVLIIRRAIPRDTGKYTCIVSNQYGT 76
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
309-397 4.56e-06

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig3_NCAM-1_like: domain similar to the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1,and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207  Cd Length: 95  Bit Score: 46.85  E-value: 4.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 309 NETTSENGHVTLICEAEGEPVPEITWKRaiDGVTFSEGDK----SPDGrievkgqhgrSSLHIRDVKLSDSGRYDCEAAS 384
Cdd:cd05730  12 NATANLGQSVTLACDADGFPEPTMTWTK--DGEPIESGEEkysfNEDG----------SEMTILDVDKLDEAEYTCIAEN 79
                        90
                ....*....|...
gi 42821116 385 RIGGHQRSMHLDI 397
Cdd:cd05730  80 KAGEQEAEIHLKV 92
Ig2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: ...
232-288 5.72e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 143265  Cd Length: 85  Bit Score: 46.39  E-value: 5.72e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 232 CKASGSPDPAISWFRNGKLIEENEK---YILKGSNTELTVRNIINKDGGSYVCKATNKAG 288
Cdd:cd05857  16 CPAAGNPTPTMRWLKNGKEFKQEHRiggYKVRNQHWSLIMESVVPSDKGNYTCVVENEYG 75
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth ...
230-288 6.83e-06

Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells, which have undergone programmed cell death, and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 46.02  E-value: 6.83e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116 230 LTCKASGSPDPAISWFRNGKLIEENEKYILKGSNTeLTVRNIINKDGGSYVCKATNKAG 288
Cdd:cd05746   3 IPCSAQGDPEPTITWNKDGVQVTESGKFHISPEGY-LAIRDVGVADQGRYECVARNTIG 60
Ig2_KIRREL3-like cd05759
Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known ...
230-287 8.62e-06

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2); Ig2_KIRREL3-like: domain similar to the second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 143236  Cd Length: 82  Bit Score: 45.90  E-value: 8.62e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116 230 LTCKASGS-PDPAISWFRNGKLIEE--NEKYILKGSNTELTVRNII-----NKDGGSYVCKATNKA 287
Cdd:cd05759   4 LTCRARGAkPAAEIIWFRDGEVLDGatYSKELLKDGKRETTVSTLPitpsdHDTGRTFTCRARNEA 69
Ig4_Neogenin cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth ...
227-296 1.08e-05

Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC, which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain.


Pssm-ID: 212460  Cd Length: 71  Bit Score: 45.34  E-value: 1.08e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42821116 227 EMTLTCKASGSPDPAISWFRNGKLIEENEKY-ILKGSNteLTVRNIINKDGGSYVCKATNKAGEDQKQAFL 296
Cdd:cd05723   1 DIVFECEVTGKPTPTVKWVKNGDMVIPSDYFkIVKEHN--LQVLGLVKSDEGFYQCIAENDVGNVQAGAQL 69
Ig_TrkABC_d4 cd04972
Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d4: the ...
220-298 1.25e-05

Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d4: the fourth domain of Trk receptors TrkA, TrkB and TrkC, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors. They are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkA, TrkB, and TrkC share significant sequence homology and domain organization. The first three domains are leucine-rich domains. The fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrkA, B, and C mediate the trophic effects of the neurotrophin Nerve growth factor (NGF) family. TrkA is recognized by NGF. TrKB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. TrkC is recognized by NT-3. NT-3 is promiscuous as in some cell systems it activates TrkA and TrkB receptors. TrkA is a receptor found in all major NGF targets, including the sympathetic, trigeminal, and dorsal root ganglia, cholinergic neurons of the basal forebrain and the striatum. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. The TrkC gene is expressed throughout the mammalian nervous system.


Pssm-ID: 143173  Cd Length: 90  Bit Score: 45.59  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 220 ATAERGEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILKGSNT--ELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQ 297
Cdd:cd04972  10 TVVYEGGTATIRCTAEGSPLPKVEWIIAGLIVIQTRTDTLETTVDiyNLQLSNITSETQTTVTCTAENPVGQANVSVQVT 89

                .
gi 42821116 298 V 298
Cdd:cd04972  90 V 90
Ig1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; Ig1_Contactin-5: First Ig domain of the ...
203-297 1.87e-05

First immunoglobulin (Ig) domain of contactin-5; Ig1_Contactin-5: First Ig domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord.


Pssm-ID: 143256  Cd Length: 94  Bit Score: 44.92  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 203 VIVNVPPAIVMPQKSfnataeRGEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILKGSNTELTVRNIIN-KDGGSYVC 281
Cdd:cd05848   3 VFVQEPDDAIFPTDS------DEKKVILNCEARGNPVPTYRWLRNGTEIDTESDYRYSLIDGNLIISNPSEvKDSGRYQC 76
                        90
                ....*....|....*..
gi 42821116 282 KATNKAGED-QKQAFLQ 297
Cdd:cd05848  77 LATNSIGSIlSREALLQ 93
Ig_VEGFR-2 cd05864
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); ...
233-300 1.88e-05

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); Ig_VEGF-2: immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-2 (KDR/Flk-1) is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A; VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGF-A also interacts with VEGFR-1, which it binds more strongly than VEGFR-2. VEGFR-2 and -1 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells.


Pssm-ID: 143272  Cd Length: 70  Bit Score: 44.54  E-value: 1.88e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 233 KASGSPDPAISWFRNGKLIEENEKYILkgsNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVFV 300
Cdd:cd05864   6 KYYGYPPPEVKWYKNGQLIVLNHTFKR---GVHLTIYEVTEKDAGNYTVVLTNPITKEEQRHTFQLVV 70
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig) ...
228-290 1.94e-05

Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: 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 (NRG1, -2, -3, and -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; 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. 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 -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: 143227  Cd Length: 75  Bit Score: 44.83  E-value: 1.94e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116 228 MTLTCKA-SGSPDPAISWFRNGKLIE-----ENEKYILKGSNTELTVRNIINKDGGSYVCKATNKAGED 290
Cdd:cd05750   1 LVLKCEAtSEYPSLRFKWFKDGKELNrknkpRNIKIRNKKKNSELQINKAKLADSGEYTCVVENILGND 69
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
319-387 2.22e-05

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); Ig4_L1-NrCAM_like: fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 319284  Cd Length: 76  Bit Score: 44.37  E-value: 2.22e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116 319 TLICEAEGEPVPEITWKraIDGVTFSegDKSPDGRIEVKGQhgrsSLHIRDVKLSDSGRYDCEAASRIG 387
Cdd:cd04978   5 ELICEAEGNPQPTITWR--LNGVPIE--PAPEDMRRTVDGR----TLIFSNLQPNDTAVYQCNASNVHG 65
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
30-103 2.41e-05

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: 278476  Cd Length: 86  Bit Score: 44.49  E-value: 2.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116    30 VELSVGESKFFTCTAIG--EPESIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTQ 103
Cdd:pfam00047   6 VTVLEGDSATLTCSASTgsPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGPAT 81
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
314-397 2.56e-05

Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: 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  Cd Length: 74  Bit Score: 44.16  E-value: 2.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 314 ENGHVTLICEAEGEPVPEITWKRAidgvtfseGDKSPDGRIEVKGQHGrsSLHIRDVKLSDSGRYDCEAASRIGGHQRSM 393
Cdd:cd05745   1 EGQTVDFLCEAQGYPQPVIAWTKG--------GSQLSVDRRHLVLSSG--TLRISRVALHDQGQYECQAVNIVGSQRTVA 70

                ....
gi 42821116 394 HLDI 397
Cdd:cd05745  71 QLTV 74
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
305-382 2.75e-05

Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third 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: 143259  Cd Length: 88  Bit Score: 44.24  E-value: 2.75e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 305 LQLKNETTSENGHVTLICEAEGEPVPEITWKRAIDGVTFSegdkspdGRIEVKGqhgrSSLHIRDVKLSDSGRYDCEA 382
Cdd:cd05851   6 VKFKDTYALKGQNVTLECFALGNPVPVIRWRKILEPMPAT-------AEISMSG----AVLKIFNIQPEDEGTYECEA 72
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
122-187 2.97e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 44.03  E-value: 2.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116   122 SPQEFKQGEDAEVVCRVSSSPAPAVSWlYHNEEVTTIPDNRFAVLANNNLQILNINKSDEGIYRCE 187
Cdd:pfam13927   9 SSVVVLEGESVTLTCEATGGPPPTITW-YKNGKPGPTSSRISLSGSNSTLTISNVTREDSGTYTCV 73
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
311-378 3.11e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: domain similar to the M5, fifth immunoglobulin (Ig)-like domain from the human titin C terminus. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone, and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching.


Pssm-ID: 143224  Cd Length: 92  Bit Score: 44.27  E-value: 3.11e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 311 TTSENGHVTLICEAEGEPVPEITWKRAIDGVTFSEgdkspdgRIEVKGQHGRSSLHIRDVKLSDSGRY 378
Cdd:cd05747  14 TVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQ-------RHQITSTEYKSTFEISKVQMSDEGNY 74
Ig2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, ...
420-485 3.24e-05

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR; Ig2_RPTP_IIa_LAR_like: domain similar to the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions, comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains, and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 319301  Cd Length: 74  Bit Score: 43.89  E-value: 3.24e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116 420 ISCDVKANPPASIHWRREklVLPAENTTHLKThSVGRKMILEIARTSDNDFGRYNCTATNRLGTRF 485
Cdd:cd05738   3 MLCAASGNPDPEITWFKD--FLPVDTTSNGRI-KQLRSGALQIENSEESDQGKYECVATNSAGTRY 65
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
225-298 3.25e-05

Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: 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  Cd Length: 74  Bit Score: 44.16  E-value: 3.25e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42821116 225 GEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILKGSNTeLTVRNIINKDGGSYVCKATNKAGEDQKQAFLQV 298
Cdd:cd05745   2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSGT-LRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
318-398 3.88e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: domain similar to 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, or 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: 319298  Cd Length: 71  Bit Score: 43.57  E-value: 3.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 318 VTLICEAEGEPVPEITWKRaidgvtfsEGDKSPDGRIeVKGQHGRSsLHIRDVKLSDSGRYDCEAASRIGGHQRSMHLDI 397
Cdd:cd05731   1 LLLECIAEGLPTPDIRWIK--------LGGELPKGRT-KFENFNKT-LKIENVSEADSGEYQCTASNTMGSARHTISVTV 70

                .
gi 42821116 398 E 398
Cdd:cd05731  71 E 71
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
209-293 4.04e-05

Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: domain similar to the M5, fifth immunoglobulin (Ig)-like domain from the human titin C terminus. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone, and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching.


Pssm-ID: 143224  Cd Length: 92  Bit Score: 43.88  E-value: 4.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 209 PAIVMpQKSFNATAERGEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILKGSNTELTVRniINK----DGGSYVCKAT 284
Cdd:cd05747   3 PATIL-TKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFE--ISKvqmsDEGNYTVVVE 79

                ....*....
gi 42821116 285 NKAGEDQKQ 293
Cdd:cd05747  80 NSEGKQEAQ 88
IGc2 smart00408
Immunoglobulin C-2 Type;
128-189 4.24e-05

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 43.55  E-value: 4.24e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42821116    128 QGEDAEVVCRVSSSPAPAVSWLYHNEEvttIPDNRFAVLANNNLQILNINKSDEGIYRCEGR 189
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKDGKP---LPESNRFVASGSTLTIKSVSLEDSGLYTCVAE 59
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); Ig_C5_MyBP_C: the ...
326-397 4.34e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); Ig_C5_MyBP_C: the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP_C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP_C exist and are included in this group: cardiac(c), and fast and slow skeletal muscle (s) MyBP_C. cMYBP_C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 143302  Cd Length: 86  Bit Score: 43.68  E-value: 4.34e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42821116 326 GEPVPEITWKRAIDGVTFSEgdkspdGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIGGHQRSMHLDI 397
Cdd:cd05894  21 GEPAPTVTWSRGDKAFTETE------GRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
Ig4_Robo cd05726
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig4_Robo: domain similar ...
318-387 4.41e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig4_Robo: domain similar to 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, -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.


Pssm-ID: 143203  Cd Length: 90  Bit Score: 43.79  E-value: 4.41e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42821116 318 VTLICEAEGEPVPEITWKR-AIDGVTFSEGDKSPDGRIEVKgqhGRSSLHIRDVKLSDSGRYDCEAASRIG 387
Cdd:cd05726   4 VTFQCEATGNPQPAIFWQKeGSQNLLFSYQPPQSSSRFSVS---QTGDLTITNVQRSDVGYYICQTLNVAG 71
Ig_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
318-387 4.42e-05

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; Ig_L1-CAM_like: domain similar to the first immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin.


Pssm-ID: 319299  Cd Length: 77  Bit Score: 43.58  E-value: 4.42e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42821116 318 VTLICEAEGEPVPEITWKRaiDGVTFsegDKSPDGRIEVKGQHGRSSLHIRD-VKLSD-SGRYDCEAASRIG 387
Cdd:cd05733   1 IVLKCEAKGNPPPTFSWTK--DGKHF---DPEKDPSVSMKRDSGTFVISNHNgNAAKDyQGKYRCYASNELG 67
Ig2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; ...
319-387 5.31e-05

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; Ig2_Follistatin_like: domain similar to 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: 143213  Cd Length: 76  Bit Score: 43.37  E-value: 5.31e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116 319 TLICEAEGEPVPEITWKRaidgvtfSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIG 387
Cdd:cd05736   2 SLRCHAEGIPLPRLTWLK-------NGMDITPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEAG 63
Ig1_Neogenin cd05722
First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: first ...
311-382 5.44e-05

First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: 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.


Pssm-ID: 143199  Cd Length: 95  Bit Score: 43.62  E-value: 5.44e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42821116 311 TTSENGHVTLICEAEGEPVPEITWKRaiDGVTFSEGDKS-----PDGRIEVKgqhgrSSLHIRDVKlSDSGRYDCEA 382
Cdd:cd05722  10 VAVRGGPVVLNCSAEGEPPPKIEWKK--DGVLLNLVSDErrqqlPNGSLLIT-----SVVHSKHNK-PDEGFYQCVA 78
Ig4_Robo cd05726
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig4_Robo: domain similar ...
415-495 6.27e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig4_Robo: domain similar to 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, -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.


Pssm-ID: 143203  Cd Length: 90  Bit Score: 43.41  E-value: 6.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 415 GNPINISCDVKANPPASIHWRRE---KLVLPAENTTHLKTHSVGRKMILEIARTSDNDFGRYNCTATNRLGTRFQEYILE 491
Cdd:cd05726   1 GRTVTFQCEATGNPQPAIFWQKEgsqNLLFSYQPPQSSSRFSVSQTGDLTITNVQRSDVGYYICQTLNVAGSILTKAYLE 80

                ....
gi 42821116 492 LADV 495
Cdd:cd05726  81 VTDV 84
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
311-395 6.94e-05

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


Pssm-ID: 311561  Cd Length: 109  Bit Score: 43.23  E-value: 6.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   311 TTSENGHVTLICEA---EGEPVPEITW---------KRAIDGVTFSEGDKSPDGRIEVKGQHGRS--SLHIRDVKLSDSG 376
Cdd:pfam07686   7 TVAEGGSVTLPCTYsssMSEASYYIYWyrqppgggpEELIAYYSNGYEEGKKKGRFSLRGDPSRSdfSLTIQNLTPSDSG 86
                          90       100
                  ....*....|....*....|
gi 42821116   377 RYDCEAASR-IGGHQRSMHL 395
Cdd:pfam07686  87 TYFCAVIPSgEGVFGSGTRL 106
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: ...
225-298 9.23e-05

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, 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: 143275  Cd Length: 76  Bit Score: 42.56  E-value: 9.23e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42821116 225 GEEMTLTCKASGSPDPAISWFRNGKLIEE---NEKYILKGSNTELTvrNIINKDGGSYVCKATNKAGEDQKQAFLQV 298
Cdd:cd05867   1 GETARLDCQVEGIPTPNITWSINGAPIEGtdpDPRRHVSSGALILT--DVQPSDTAVYQCEARNRHGNLLANAHVHV 75
I-set pfam07679
Immunoglobulin I-set domain;
117-193 9.49e-05

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 42.63  E-value: 9.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   117 FREVLSPQEFKQGEDAEVVCRVSSSPAPAVSWLYHNEEVTtiPDNRFAVLANNNLQI---LNINKSDEGIYRCE-----G 188
Cdd:pfam07679   3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR--SSDRFKVTYEGGTYTltiSNVQPDDSGKYTCVatnsaG 80

                  ....*
gi 42821116   189 RVEAR 193
Cdd:pfam07679  81 EAEAS 85
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; Ig5_Contactin-1: fifth Ig domain of the ...
225-298 1.09e-04

Fifth immunoglobulin (Ig) domain of contactin-1; Ig5_Contactin-1: fifth 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: 143260  Cd Length: 73  Bit Score: 42.32  E-value: 1.09e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42821116 225 GEEMTLTCKASGSPDPAISWFRNGKLIEENEKyILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQV 298
Cdd:cd05852   1 GGRVIIECKPKAAPKPKFSWSKGTELLVNNSR-ISIWDDGSLEILNITKLDEGSYTCFAENNRGKANSTGVLSV 73
Ig_3 cd05765
Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: subgroup of the immunoglobulin (Ig) ...
35-103 1.11e-04

Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: 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. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 143242  Cd Length: 81  Bit Score: 42.53  E-value: 1.11e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42821116  35 GESKFFTCTAIGEPE-SIDW--YNPQGEKIISTQRVMLQKEGVRS--RLTIYNANIEDAGIYRCQATDAKGQTQ 103
Cdd:cd05765   1 GETASFHCDVTGRPPpEITWekQVHGKENLIMRPNHVRGNVVVTNigQLVIYNAQPQDAGLYTCTARNSGGLLR 74
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: ...
318-395 1.12e-04

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


Pssm-ID: 143211  Cd Length: 79  Bit Score: 42.61  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 318 VTLICEAEGEPVPEITWKraidgvtFSEGDKSP--------DGRIEVKGQhgrSSLHIRDVKLSDSGRYDCEAASRIGGH 389
Cdd:cd05734   1 VTLNCSAEGYPPPTIVWK-------HSKGRGHPqhthtcclAGRIQLLSN---GSLLIKHVLEEDSGYYLCKVSNDVGAD 70

                ....*..
gi 42821116 390 -QRSMHL 395
Cdd:cd05734  71 aSKSMVL 77
I-set pfam07679
Immunoglobulin I-set domain;
414-483 1.24e-04

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 42.24  E-value: 1.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   414 EGNPINISCDVKANPPASIHWRREKLVLPAENttHLKTHSVGRKMILEIARTSDNDFGRYNCTATNRLGT 483
Cdd:pfam07679  14 EGESARFTCTVTGTPDPEVSWFKDGQPLRSSD--RFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81
Ig_VEGFR cd04976
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); ...
230-300 1.31e-04

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); Ig_VEGFR: immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4). VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-2 and -1 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth.


Pssm-ID: 319282  Cd Length: 70  Bit Score: 42.16  E-value: 1.31e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42821116 230 LTCKASGSPDPAISWFRNGKLIEENeKYILKGSNteLTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVFV 300
Cdd:cd04976   3 LPVKVKAYPPPEFKWYKNGKPITEN-HTKKSGYS--LQIKDVTEHDAGNYTVVLTNPLSKLEKRHTLTLIV 70
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
35-100 1.33e-04

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


Pssm-ID: 143220  Cd Length: 78  Bit Score: 42.09  E-value: 1.33e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42821116  35 GESKFFTCTAIGEPES-IDWYNPQGEkIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKG 100
Cdd:cd05743   1 GETVEFTCVATGVPTPiINWRLNWGH-VPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRG 66
Ig1_FcgammaR_like cd05752
Frst immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs) and similar proteins; ...
225-283 1.33e-04

Frst immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs) and similar proteins; Ig1_FcgammaR_like: domain similar to 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: 143229  Cd Length: 78  Bit Score: 42.33  E-value: 1.33e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 225 GEEMTLTCKASGSP-DPAISWFRNGKLIEEnekyilkgSNTELTVRNIINkDGGSYVCKA 283
Cdd:cd05752  15 GEKVTLTCNGFNSPeQNSTQWYHNGKLLET--------TTNSYRIRAANN-DSGEYRCQT 65
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig) ...
320-387 1.35e-04

Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: 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 (NRG1, -2, -3, and -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; 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. 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 -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: 143227  Cd Length: 75  Bit Score: 42.13  E-value: 1.35e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 320 LICEAEGE-PVPEITWKRaiDGvtfSEGDKSPDGR-IEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIG 387
Cdd:cd05750   3 LKCEATSEyPSLRFKWFK--DG---KELNRKNKPRnIKIRNKKKNSELQINKAKLADSGEYTCVVENILG 67
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
24-107 1.50e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 316418  Cd Length: 78  Bit Score: 41.97  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116    24 TISLSKVELSVGESKFFTCTA-IGEPESIDWYNpQGEKIISTQRVmlqkegvrsrltIYNANIEDAGIYRCQATDAKGQT 102
Cdd:pfam13895   3 VLTPSPTVVTEGEPVTLTCSApGNPPANYTWYK-GGEALNSSPNF------------ISSVSAEDSGTYTCVARNGRGGK 69

                  ....*
gi 42821116   103 QEATV 107
Cdd:pfam13895  70 VSNPV 74
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; Ig6_Contactin_like: Sixth Ig domain of ...
226-298 1.54e-04

Sixth immunoglobulin (Ig) domain of contactin; Ig6_Contactin_like: Sixth 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 neur onal act ivity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319279  Cd Length: 85  Bit Score: 42.15  E-value: 1.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 226 EEMTLTCKASGSP--DPAISWFRNGKLIEENEKYI------LKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQ 297
Cdd:cd04970   1 ENATLQCHASHDPtlDLTFTWSFNGVPIDLEKINGhyrrryGKDSNGDLEIVNAQLKHAGRYTCTAQTVVDSDSASATLV 80

                .
gi 42821116 298 V 298
Cdd:cd04970  81 V 81
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
422-483 1.65e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar to 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, -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.


Pssm-ID: 143202  Cd Length: 69  Bit Score: 41.62  E-value: 1.65e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42821116 422 CDVKANPPASIHWRREKLVLPAENTTHLKTHSvgrkmiLEIARTSDNDFGRYNCTATNRLGT 483
Cdd:cd05725   5 CEVGGDPVPTVLWRKEDGELPKGRAEILDDKS------LKIRNVTAGDEGSYTCEAENMVGK 60
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
401-492 1.88e-04

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


Pssm-ID: 143277  Cd Length: 97  Bit Score: 41.89  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 401 PK--FVSNQTMYYSWEgnPINISCDVKANPPASIHWRREKLVLPAENTT---HLKTHSVGRKMILEIARTSDNDFGRYNC 475
Cdd:cd05869   3 PKitYVENQTAMELEE--QITLTCEASGDPIPSITWRTSTRNISSEEKTldgHIVVRSHARVSSLTLKYIQYTDAGEYLC 80
                        90
                ....*....|....*..
gi 42821116 476 TATNRLGTRFQEYILEL 492
Cdd:cd05869  81 TASNTIGQDSQSMYLEV 97
IG smart00409
Immunoglobulin;
122-187 1.92e-04

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 41.72  E-value: 1.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116    122 SPQEFKQGEDAEVVCRVSSSPAPAVSWlYHNEEVTTIPDNRFAVLANNNLQI---LNINKSDEGIYRCE 187
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTW-YKQGGKLLAESGRFSVSRSGSTSTltiSNVTPEDSGTYTCA 69
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
122-187 1.92e-04

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 41.72  E-value: 1.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116    122 SPQEFKQGEDAEVVCRVSSSPAPAVSWlYHNEEVTTIPDNRFAVLANNNLQI---LNINKSDEGIYRCE 187
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTW-YKQGGKLLAESGRFSVSRSGSTSTltiSNVTPEDSGTYTCA 69
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
230-288 1.93e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: domain similar to 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, or 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: 319298  Cd Length: 71  Bit Score: 41.65  E-value: 1.93e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 230 LTCKASGSPDPAISWFR-NGKLIeeNEKYILKGSNTELTVRNIINKDGGSYVCKATNKAG 288
Cdd:cd05731   3 LECIAEGLPTPDIRWIKlGGELP--KGRTKFENFNKTLKIENVSEADSGEYQCTASNTMG 60
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; Ig_Pro_neuregulin-1: ...
320-387 2.19e-04

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; Ig_Pro_neuregulin-1: 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: 143303  Cd Length: 76  Bit Score: 41.53  E-value: 2.19e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 320 LICEAEGEpVPEITWKRAIDGVTFSEGDKsPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIG 387
Cdd:cd05895   3 LRCETVSE-YPSLRFKWFKNGKEIGAKNK-PDNKIKIRKKKKSSELQISKASLADNGEYKCMVSSKLG 68
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
414-484 2.47e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: 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  Cd Length: 74  Bit Score: 41.46  E-value: 2.47e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42821116 414 EGNPINISCDVKANPPASIHWRREKLVLPAEntthlKTHSVGRKMILEIARTSDNDFGRYNCTATNRLGTR 484
Cdd:cd05745   1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVD-----RRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQ 66
Ig1_Neogenin cd05722
First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: first ...
219-286 2.66e-04

First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: 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.


Pssm-ID: 143199  Cd Length: 95  Bit Score: 41.31  E-value: 2.66e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42821116 219 NATAERGEEMTLTCKASGSPDPAISWFRNGKLIEE--NEKYILKgSNTELTVRNII----NK-DGGSYVCKATNK 286
Cdd:cd05722   8 DIVAVRGGPVVLNCSAEGEPPPKIEWKKDGVLLNLvsDERRQQL-PNGSLLITSVVhskhNKpDEGFYQCVAQND 81
Ig_2 cd05764
Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: subgroup of the immunoglobulin (Ig) ...
42-111 2.71e-04

Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: 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. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 143241  Cd Length: 74  Bit Score: 41.32  E-value: 2.71e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42821116  42 CTAIGEPE-SIDWYNPQGEKIISTQRVMLQKEGVrsrLTIYNANIEDAGIYRCQATDAKGqtqEATVVLEI 111
Cdd:cd05764   8 CKARGDPEpAIHWISPDGKLISNSSRTLVYDNGT---LDILITTVKDTGSFTCIASNAAG---EATATVEL 72
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7, also known as CCK4; ...
228-289 2.81e-04

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7, also known as CCK4; Ig2_PTK7: domain similar to the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane, and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.


Pssm-ID: 143237  Cd Length: 77  Bit Score: 41.05  E-value: 2.81e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42821116 228 MTLTCKASGSPDPAISWFRNGK-LIEENEKYILKGSNTELTVRNIINKDGGSYVCKATNKAGE 289
Cdd:cd05760   1 VTLRCHIDGHPRPTYQWFRDGTpLSDGQGNYSVSSKERTLTLRSAGPDDSGLYYCCAHNAFGS 63
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: ...
229-298 2.89e-04

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


Pssm-ID: 143211  Cd Length: 79  Bit Score: 41.07  E-value: 2.89e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 229 TLTCKASGSPDPAISW-FRNGKLIEENEK------YILKGSNTELTVRNIINKDGGSYVCKATNKAGED-QKQAFLQV 298
Cdd:cd05734   2 TLNCSAEGYPPPTIVWkHSKGRGHPQHTHtcclagRIQLLSNGSLLIKHVLEEDSGYYLCKVSNDVGADaSKSMVLTV 79
Ig_1 cd05763
Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: subgroup of the immunoglobulin (Ig) ...
320-387 3.25e-04

Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: 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. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 143240  Cd Length: 75  Bit Score: 41.07  E-value: 3.25e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 320 LICEAEGEPVPEITWKRAiDGVTFSEGDKSpdgRIEVKGQHgrSSLHIRDVKLSDSGRYDCEAASRIG 387
Cdd:cd05763   3 LECAATGHPTPQIAWQKD-GGTDFPAARER---RMHVMPED--DVFFIVDVKIEDTGVYSCTAQNTAG 64
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
32-109 3.52e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: domain similar to the M5, fifth immunoglobulin (Ig)-like domain from the human titin C terminus. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone, and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching.


Pssm-ID: 143224  Cd Length: 92  Bit Score: 41.19  E-value: 3.52e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116  32 LSVGESKFFTCTAIGEP-ESIDWYNpQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQtQEATVVL 109
Cdd:cd05747  15 VSEGESARFSCDVDGEPaPTVTWMR-EGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGK-QEAQFTL 91
Ig_TrkB_d5 cd05855
Fifth domain (immunoglobulin-like) of Trk receptor TrkB; TrkB_d5: the fifth domain of Trk ...
236-293 3.52e-04

Fifth domain (immunoglobulin-like) of Trk receptor TrkB; TrkB_d5: the fifth domain of Trk receptor TrkB, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors, which mediate the trophic effects of the neurotrophin Nerve growth factor (NGF) family. The Trks are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkB shares significant sequence homology and domain organization with TrkA, and TrkC. The first three domains are leucine-rich domains. The fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrKB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. In some cell systems NT-3 can activate TrkA and TrkB receptors. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems.


Pssm-ID: 143263  Cd Length: 79  Bit Score: 40.98  E-value: 3.52e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116 236 GSPDPAISWFRNGKLIEENEkYILKG----SNTE----LTVRNIINKDGGSYVCKATNKAGEDQKQ 293
Cdd:cd05855   9 GNPKPTLQWFHEGAILNESE-YICTKihviNNTEyhgcLQLDNPTHLNNGIYTLVAKNEYGEDEKN 73
Ig_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; Ig_Myotilin_like_C: ...
318-397 4.48e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; Ig_Myotilin_like_C: 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: all three bind 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).


Pssm-ID: 319304  Cd Length: 75  Bit Score: 40.67  E-value: 4.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 318 VTLICEAEGEPVPEITWKRAIDGVTFsegdkSPDgRIEV-KGQHGRSSLHIRDVKLSDSGRYDCEAASRIGGHQRSMHLD 396
Cdd:cd05744   1 VKLECQVLAIPPPQIFWKKENEMLQF-----NTD-RISLyQDNHGRICLLIKDVTKEDAGWYTVSAKNEAGITSCNARLD 74

                .
gi 42821116 397 I 397
Cdd:cd05744  75 V 75
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin ...
326-378 4.64e-04

Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin (Ig)-like domain found in titin-like proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin, and similar to titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle, which also have repeated Ig-like and FN-III domains.


Pssm-ID: 319305  Cd Length: 74  Bit Score: 40.67  E-value: 4.64e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 42821116 326 GEPVPEITWKRAidgvtfsEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRY 378
Cdd:cd05748  10 GRPTPTVTWSKD-------GQPLKLSGRVQIETTATSTSLVIKNAKRSDSGKY 55
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
229-298 4.95e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar to 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, -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.


Pssm-ID: 143202  Cd Length: 69  Bit Score: 40.47  E-value: 4.95e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 229 TLTCKASGSPDPAISWFRNGKLIEENEKYILkgSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQV 298
Cdd:cd05725   2 EFQCEVGGDPVPTVLWRKEDGELPKGRAEIL--DDKSLKIRNVTAGDEGSYTCEAENMVGKIEASASLTV 69
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth Ig domain of ...
316-397 5.45e-04

Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth 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 act ivity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319278  Cd Length: 73  Bit Score: 40.12  E-value: 5.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 316 GHVTLICEAEGEPVPEITWKRAIDGVTFSeGDKS--PDGrievkgqhgrsSLHIRDVKLSDSGRYDCEAASRIGGHQRSM 393
Cdd:cd04969   2 GDVIIECKPKASPKPTISWSKGTELLTNS-SRICilPDG-----------SLKIKNVSKSDEGKYTCFAVNFFGKANSTG 69

                ....
gi 42821116 394 HLDI 397
Cdd:cd04969  70 SLSV 73
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
178-281 5.80e-04

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173  Cd Length: 227  Bit Score: 42.21  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116  178 KSDEGIYRCE---GRVEARGEIDFrdiivivnvppaiVMPQKSFNATAERGEEMTLTCK-----ASGSPDPAISWFRNGK 249
Cdd:PHA02826 107 NIDEGIYICTissGNICEESTIRL-------------TFDSGTINYQFNSGKDSKLHCYgtdgiSSTFKDYTLTWYKNGN 173
                         90       100       110
                 ....*....|....*....|....*....|..
gi 42821116  250 LIEENEKYILKGSNTELTVRNIINKDGGSYVC 281
Cdd:PHA02826 174 IVLYTDRIQLRNNNSTLVIKSATHDDSGIYTC 205
Ig4_Neogenin cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth ...
136-186 5.81e-04

Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC, which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain.


Pssm-ID: 212460  Cd Length: 71  Bit Score: 40.33  E-value: 5.81e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 42821116 136 CRVSSSPAPAVSWLYHNEEVttIPDNRFAVLANNNLQILNINKSDEGIYRC 186
Cdd:cd05723   6 CEVTGKPTPTVKWVKNGDMV--IPSDYFKIVKEHNLQVLGLVKSDEGFYQC 54
Ig_Perlecan_like cd05754
Igmmunoglobulin (Ig)-like domain found in Perlecan and similar proteins; Ig_Perlecan_like: ...
225-296 6.26e-04

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


Pssm-ID: 143231  Cd Length: 85  Bit Score: 40.22  E-value: 6.26e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42821116 225 GEEMTLTCKA-SGSPDPAISWFRNGKLIEENEKyilkGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFL 296
Cdd:cd05754  16 GADVSFICRAkSKSPAYTLVWTRVGGGLPSRAM----DFNGILTIRNVQLSDAGTYVCTGSNMLDTDEATATL 84
Ig_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; Ig_Myotilin_C: C-terminal ...
230-288 6.69e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; Ig_Myotilin_C: C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle, and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin and actin. Mutations in myotilin lead to muscle disorders.


Pssm-ID: 143300  Cd Length: 75  Bit Score: 39.93  E-value: 6.69e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42821116 230 LTCKASGSPDPAISWFRNGKLIEENEKYI-LKGSNT---ELTVRNIINKDGGSYVCKATNKAG 288
Cdd:cd05892   3 LECQISAIPPPKIFWKRNNEMVQYNTDRIsLYQDNSgrvTLLIKNVNKKDAGWYTVSAVNEAG 65
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
413-479 7.17e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 316418  Cd Length: 78  Bit Score: 40.05  E-value: 7.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42821116   413 WEGNPINISCDVKANPPASIHWRREKLVLPaENTTHLKTHSVGrkmileiartsdnDFGRYNCTATN 479
Cdd:pfam13895  12 TEGEPVTLTCSAPGNPPANYTWYKGGEALN-SSPNFISSVSAE-------------DSGTYTCVARN 64
Ig1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; Ig1_Contactin-1: First Ig domain of the ...
208-288 7.18e-04

First immunoglobulin (Ig) domain of contactin-1; Ig1_Contactin-1: First 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: 143257  Cd Length: 93  Bit Score: 39.94  E-value: 7.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 208 PPAIVMPQKSFNAtaergeEMTLTCKASGSPDPAISWFRNGKLIE-ENEKYILKGSNteLTVRNI-INKDGGSYVCKATN 285
Cdd:cd05849   8 PIDTIYPEESTEG------KVSVNCRARANPFPIYKWRKNNLDIDlTNDRYSMVGGN--LVINNPdKYKDAGRYVCIVSN 79

                ...
gi 42821116 286 KAG 288
Cdd:cd05849  80 IYG 82
Ig5_KIRREL3-like cd05758
Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known ...
400-483 7.19e-04

Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2) and similar proteins; Ig5_KIRREL3-like: domain similar to the fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 319310  Cd Length: 98  Bit Score: 40.21  E-value: 7.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 400 APKFVSNQTMYYSWEGNPINISCDVKANP-PASIHWRREKLVLPAENTTHLKTHSV----GRKMILEIARTSDNDFGR-Y 473
Cdd:cd05758   1 GPPIITAEATQPAILGEKARLECLVFSSPpPDRIVWSWDEGFLESGSSGRFSVETFptepGVISVLHISGTQRSDFQTsF 80
                        90
                ....*....|
gi 42821116 474 NCTATNRLGT 483
Cdd:cd05758  81 NCSAWNRFGE 90
Ig_CEACAM cd05740
Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion ...
209-285 7.87e-04

Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM); Ig_CEACAM: Immunoglobulin (Ig)-like domain 4 in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions, it is a cell adhesion molecule, and a signaling molecule that regulates the growth of tumor cells, it is an angiogenic factor, and is a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.


Pssm-ID: 143217  Cd Length: 91  Bit Score: 39.95  E-value: 7.87e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42821116 209 PAIVMPQKSFNATAERGEEMTLTCKASGSPDpAISWFRNGKLIEENeKYILKGSNTELTVRNIINKDGGSYVCKATN 285
Cdd:cd05740   2 PVINSNNSVGNQPPEDNQPVTLTCEAEGQAT-YIWWVNNGSLLVPP-RLQLSNDNRTLTFNNVTRSDTGHYQCEASN 76
Ig2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
315-387 8.51e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); Ig2_FGFRL1-like: second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 143264  Cd Length: 82  Bit Score: 39.82  E-value: 8.51e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42821116 315 NGHVTLICEAEGEPVPEITWkraidgvtfsEGDKSPDGRIEV-KGQHGRSSLHIRDVKLSDSGRYDCEAASRIG 387
Cdd:cd05856   9 GSSVRLKCVASGNPRPDITW----------LKDNKPLTPTEIgESRKKKWTLSLKNLKPEDSGKYTCHVSNRAG 72
Ig_NrCAM cd05874
Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); ...
228-288 9.74e-04

Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); Ig_NrCAM: domain similar to the first immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule). NrCAM belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 143282  Cd Length: 77  Bit Score: 39.55  E-value: 9.74e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 228 MTLTCKASGSPDPAISWFRNGKL--IEENEKYILKgSNTELTVRNIINKDG-----GSYVCKATNKAG 288
Cdd:cd05874   1 IVIQCEAKGKPPPSFSWTRNGTHfdIDKDPKVTMK-PNTGTLVINIMNGEKaeayeGVYQCTARNERG 67
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth Ig domain of ...
415-483 1.08e-03

Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth 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 act ivity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319278  Cd Length: 73  Bit Score: 39.35  E-value: 1.08e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116 415 GNPINISCDVKANPPASIHWRREKlvlpaENTTHLKTHSVGRKMILEIARTSDNDFGRYNCTATNRLGT 483
Cdd:cd04969   1 GGDVIIECKPKASPKPTISWSKGT-----ELLTNSSRICILPDGSLKIKNVSKSDEGKYTCFAVNFFGK 64
Ig_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
228-288 1.09e-03

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; Ig_L1-CAM_like: domain similar to the first immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin.


Pssm-ID: 319299  Cd Length: 77  Bit Score: 39.34  E-value: 1.09e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 228 MTLTCKASGSPDPAISWFRNGKL--IEENEKYILKGSNTELTvrnIINKDG-------GSYVCKATNKAG 288
Cdd:cd05733   1 IVLKCEAKGNPPPTFSWTKDGKHfdPEKDPSVSMKRDSGTFV---ISNHNGnaakdyqGKYRCYASNELG 67
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; ...
27-100 1.24e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; Ig4_Contactin-2-like: 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 (aliases 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  Cd Length: 85  Bit Score: 39.12  E-value: 1.24e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42821116  27 LSKVELSVGESKFFTCTAIGEPE-SIDWYNpQGEKIISTQRVMLQKegvrSRLTIYNANIEDAGIYRCQATDAKG 100
Cdd:cd05728   6 ISDTEADIGSSLRWECKASGNPRpAYRWLK-NGQPLASENRIEVEA----GDLRITKLSLSDSGMYQCVAENKHG 75
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); Ig_C5_MyBP_C: the ...
225-298 1.35e-03

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); Ig_C5_MyBP_C: the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP_C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP_C exist and are included in this group: cardiac(c), and fast and slow skeletal muscle (s) MyBP_C. cMYBP_C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 143302  Cd Length: 86  Bit Score: 39.06  E-value: 1.35e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42821116 225 GEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILKGSNTEL---TVRNIINKDGGSYVCKATNKAGEDQKQAFLQV 298
Cdd:cd05894  10 GNKLRLDVPISGEPAPTVTWSRGDKAFTETEGRVRVESYKDLssfVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
508-588 1.50e-03

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 318794  Cd Length: 92  Bit Score: 38.92  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116   508 SQTTAKISFNKPESHGGvpihhYQVDVMEETSETWKIV-----------RSHGVQTTVVLSSLEPNTTYEVRVaavnGKG 576
Cdd:pfam16656  10 PSTSMTVTWVTPADVTS-----PVVQYGTSPDALTSTAngtsstyttgnGTSGYIHRATLTGLEPGTTYYYRV----GDG 80
                          90
                  ....*....|..
gi 42821116   577 QGDYSKIEIFQT 588
Cdd:pfam16656  81 NGGWSEVYSFTT 92
Ig1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First Ig domain of contactins. ...
126-186 1.52e-03

First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First Ig domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319276  Cd Length: 91  Bit Score: 39.12  E-value: 1.52e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42821116 126 FKQGEDAEVV---CRVSSSPAPAVSWLYHNEEVTTIPDNRFAVLANNNLQILNINKSDEGIYRC 186
Cdd:cd04967  13 FPEESDEEKValnCRARANPPPTYRWKMNGTEIKLEPDSRYSLVGGNLVISNPSKAKDAGHYQC 76
Ig2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain ...
318-392 1.86e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain similar to 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 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.


Pssm-ID: 143201  Cd Length: 86  Bit Score: 38.53  E-value: 1.86e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116 318 VTLICEA-EGEPVPEITWKRaiDGVTFSEGDKspdGRIEVKGqhgrSSLHIRDVKLSDSGRYDCeAASRIGGHQRS 392
Cdd:cd05724  14 AVLECSPpRGHPEPTVSWRK--DGQPLNLDNE---RVRIVDD----GNLLIAEARKSDEGTYKC-VATNMVGERES 79
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
34-114 1.88e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig3_NCAM-1_like: domain similar to the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1,and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207  Cd Length: 95  Bit Score: 38.76  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116  34 VGESKFFTCTAIGEPESIDWYNPQGEKIIS-TQRVMLQKEGvrSRLTIYNANIEDAGIYRCQATDAKGQtQEATVVLEIY 112
Cdd:cd05730  17 LGQSVTLACDADGFPEPTMTWTKDGEPIESgEEKYSFNEDG--SEMTILDVDKLDEAEYTCIAENKAGE-QEAEIHLKVF 93

                ..
gi 42821116 113 QK 114
Cdd:cd05730  94 AK 95
Ig1_Necl-3 cd07701
First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3, also ...
308-380 1.92e-03

First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3, also known as cell adhesion molecule 2 (CADM2)); Ig1_Necl-3: domain similar to the N-terminal immunoglobulin (Ig)-like domain of nectin-like molecule-3, Necl-3 (also known as cell adhesion molecule 2 (CADM2), SynCAM2, IGSF4D). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region, belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-3 accumulates in central and peripheral nervous system tissue, and has been shown to selectively interact with oligodendrocytes.


Pssm-ID: 319327  Cd Length: 95  Bit Score: 38.54  E-value: 1.92e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42821116 308 KNETTSENGHVTLICEAEGEPVPEITWKRAIDGVTFSeGDKSP--DGRIE-VKGQHGRSSLHIRDVKLSDSGRYDC 380
Cdd:cd07701   5 QNVTVVEGGTANLTCRVDQNDNTSLQWSNPAQQTLYF-DDKKAlrDNRIElVRASWHELSISISDVSLSDEGQYTC 79
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
132-194 2.06e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar to 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, -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.


Pssm-ID: 143202  Cd Length: 69  Bit Score: 38.54  E-value: 2.06e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 132 AEVVCRVSSSPAPAVSWlyhNEEVTTIPDNRFAVLANNNLQILNINKSDEGIYRCE-----GRVEARG 194
Cdd:cd05725   1 VEFQCEVGGDPVPTVLW---RKEDGELPKGRAEILDDKSLKIRNVTAGDEGSYTCEaenmvGKIEASA 65
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; Ig6_Contactin_like: Sixth Ig domain of ...
318-401 2.06e-03

Sixth immunoglobulin (Ig) domain of contactin; Ig6_Contactin_like: Sixth 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 neur onal act ivity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319279  Cd Length: 85  Bit Score: 38.69  E-value: 2.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 318 VTLICEAEGEPVPEITWKRAIDGVTFsEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIGGHQRSMHLDI 397
Cdd:cd04970   3 ATLQCHASHDPTLDLTFTWSFNGVPI-DLEKINGHYRRRYGKDSNGDLEIVNAQLKHAGRYTCTAQTVVDSDSASATLVV 81

                ....
gi 42821116 398 EYAP 401
Cdd:cd04970  82 RGPP 85
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: ...
228-288 2.55e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: 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: 143284  Cd Length: 71  Bit Score: 38.37  E-value: 2.55e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42821116 228 MTLTCKASGSPDPAISWFR-NGKLIEENEKYilKGSNTELTVRNIINKDGGSYVCKATNKAG 288
Cdd:cd05876   1 LVLECIAEGLPTPEVHWDRiDGPLSPNRTKK--LNNNKTLQLDNVLESDDGEYVCTAENSEG 60
Ig_3 cd05765
Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: subgroup of the immunoglobulin (Ig) ...
225-288 2.55e-03

Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: 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. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 143242  Cd Length: 81  Bit Score: 38.29  E-value: 2.55e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42821116 225 GEEMTLTCKASGSPDPAISWfrnGKLIEENEKYILKGSNT----------ELTVRNIINKDGGSYVCKATNKAG 288
Cdd:cd05765   1 GETASFHCDVTGRPPPEITW---EKQVHGKENLIMRPNHVrgnvvvtnigQLVIYNAQPQDAGLYTCTARNSGG 71
Ig2_Necl-3 cd05884
Second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3, also known as cell ...
228-298 2.60e-03

Second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3, also known as cell adhesion molecule 2 (CADM2)); Ig2_Necl-3: second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3, also known as cell adhesion molecule 2 (CADM2)). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Ig domains are likely to participate in ligand binding and recognition.


Pssm-ID: 319320  Cd Length: 83  Bit Score: 38.44  E-value: 2.60e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116 228 MTLTCKASGS-PDPAISWFRNGKLIEENEKYILKGSNTE-LTVRNII------NKDGGSYVCKATNKAGEDQKQAFLQV 298
Cdd:cd05884   2 MQLTCKTSGSkPAADIRWFKNDKEIKDVKYLKEEDANRKtFTVSSTLdfrvdrSDDGVAIICRVDHESLNATPQIAMQV 80
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); Ig4_ ...
129-161 2.91e-03

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); Ig4_ NrCAM: fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six IG-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 143276  Cd Length: 76  Bit Score: 38.06  E-value: 2.91e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 42821116 129 GEDAEVVCRVSSSPAPAVSWLYHNEEVTTIPDN 161
Cdd:cd05868   1 GEDGTLICRANGNPKPSISWLTNGVPIEIAPTD 33
Ig2_Necl-1-4_like cd05761
Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4 (also ...
227-298 3.59e-03

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4 (also known as cell adhesion molecules CADM3, CADM1, CADM2, and CADM4, respectively); Ig2_Necl-1-4_like: domain similar to the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 (CADM3)), Necl-2 (CADM1), Necl-3 (CADM2) and Necl-4 (CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.


Pssm-ID: 319311  Cd Length: 83  Bit Score: 37.93  E-value: 3.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 227 EMTLTCKASGSPDPA-ISWFRNGKLIEENEKYILKGSN-------TELTVRNIINKDGGSYVCKATNKA---GEDQKQAF 295
Cdd:cd05761   1 EVELTCTSSGSKPAAtLRWYKDDQELKGVPDVSESDENgktytvtSSLTFQVDRKDDGAPIICQVDHPSltsHDKQTQQV 80

                ...
gi 42821116 296 LQV 298
Cdd:cd05761  81 LEV 83
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: ...
318-398 4.41e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: 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: 143284  Cd Length: 71  Bit Score: 37.60  E-value: 4.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 318 VTLICEAEGEPVPEITWKRAidgvtfsEGDKSPDgriEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIGGHQRSMHLDI 397
Cdd:cd05876   1 LVLECIAEGLPTPEVHWDRI-------DGPLSPN---RTKKLNNNKTLQLDNVLESDDGEYVCTAENSEGSARHHYTVTV 70

                .
gi 42821116 398 E 398
Cdd:cd05876  71 E 71
Ig3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of ...
34-101 4.51e-03

Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third 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 act ivity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319277  Cd Length: 88  Bit Score: 37.53  E-value: 4.51e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42821116  34 VGESKFFTCTAIGEP-ESIDWYNPQGEKIisTQRVMLQKEGVrsrLTIYNANIEDAGIYRCQATDAKGQ 101
Cdd:cd04968  15 KGQTVTLECFALGNPvPQIKWRKVDGSPS--SQWTTSTSEPV---LEIPNVQFEDEGTYECEAENSRGK 78
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2); Ig2_IL1R2_like: ...
242-282 4.81e-03

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2); Ig2_IL1R2_like: domain similar to the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with an accessory protein, IL1RAP. IL-1 also binds the type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of Mature IL1R1, and does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 143305  Cd Length: 95  Bit Score: 37.44  E-value: 4.81e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 42821116 242 ISWFRNGKLIEENEK--YILKGSnTELTVRNIINKDGGSYVCK 282
Cdd:cd05897  32 LQWYKDSVLLDKDNEkfYSLKGS-TYLHIIDVSLNDSGYYTCK 73
Ig_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
418-483 5.57e-03

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; Ig_L1-CAM_like: domain similar to the first immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin.


Pssm-ID: 319299  Cd Length: 77  Bit Score: 37.03  E-value: 5.57e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42821116 418 INISCDVKANPPASIHWRREKLVLPAENTTHLKTHSVGRKMILEI--ARTSDNDFGRYNCTATNRLGT 483
Cdd:cd05733   1 IVLKCEAKGNPPPTFSWTKDGKHFDPEKDPSVSMKRDSGTFVISNhnGNAAKDYQGKYRCYASNELGT 68
Ig_1 cd05763
Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: subgroup of the immunoglobulin (Ig) ...
230-298 5.75e-03

Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: 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. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 143240  Cd Length: 75  Bit Score: 37.22  E-value: 5.75e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42821116 230 LTCKASGSPDPAISWFRNG--KLIEENEKYI-LKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQV 298
Cdd:cd05763   3 LECAATGHPTPQIAWQKDGgtDFPAARERRMhVMPEDDVFFIVDVKIEDTGVYSCTAQNTAGSISANATLTV 74
Ig2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: ...
318-397 5.91e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 143265  Cd Length: 85  Bit Score: 37.15  E-value: 5.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 318 VTLICEAEGEPVPEITWKRaiDGVTFSEGDKSpdGRIEVKGQHgrSSLHIRDVKLSDSGRYDCEAASRIGGHQRSMHLDI 397
Cdd:cd05857  12 VKFRCPAAGNPTPTMRWLK--NGKEFKQEHRI--GGYKVRNQH--WSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDV 85
Ig3_FGFR-2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); ...
225-298 6.06e-03

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); Ig3_FGFR-2-like; domain similar to the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination.


Pssm-ID: 143266  Cd Length: 90  Bit Score: 37.22  E-value: 6.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116 225 GEEMTLTCKASGSPDPAISWFR----NG-KLIEENEKY--ILK--GSNTE------LTVRNIINKDGGSYVCKATNKAGE 289
Cdd:cd05858   1 GSTVEFVCKVYSDAQPHIQWLKhvekNGsKYGPDGLPYvtVLKtaGVNTTdkemevLYLRNVTFEDAGEYTCLAGNSIGI 80

                ....*....
gi 42821116 290 DQKQAFLQV 298
Cdd:cd05858  81 SHHSAWLTV 89
Ig_hNephrin_like cd05773
Immunoglobulin-like domain of nephrin and similar domains; Ig_hNephrin_like: ...
229-291 6.15e-03

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


Pssm-ID: 143250  Cd Length: 109  Bit Score: 37.22  E-value: 6.15e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42821116 229 TLTCKASGSPDPAISWFRNGKLI-------EENEKYILKGSNTELTVRNI-INKDGGSYVCKATNKAGEDQ 291
Cdd:cd05773  27 NLVCQAQGVPRVQFRWAKNGVPLdlgnpryEETTEHTGTVHTSILTIINVsAALDYALFTCTAHNSLGEDS 97
Ig_VEGFR-3 cd05863
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3); ...
230-300 6.27e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3); Ig_VEGFR-3: immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-3 (Flt-4) binds two members of the VEGF family (VEGF-C and -D) and is involved in tumor angiogenesis and growth.


Pssm-ID: 143271  Cd Length: 67  Bit Score: 36.84  E-value: 6.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42821116 230 LTCKASGSPDPAISWFRNGKLIEenekyiLKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVFV 300
Cdd:cd05863   3 LPVKVAAYPPPEFQWYKDGKLIS------GKHSQHSLQIKDVTEASAGTYTLVLWNSAAGLEKRISLELIV 67
Ig_CEACAM_like cd05741
Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion ...
78-111 6.58e-03

Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and similar proteins; Ig_CEACAM_like: immunoglobulin (Ig)-like domain in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and related domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions, it is a cell adhesion molecule, and a signaling molecule that regulates the growth of tumor cells, it is an angiogenic factor, and is a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface. This family corresponds to the D1 Ig-like domain. Also belonging to this group is the N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family, CD84-like family. The SLAM family is a group of immune-cell specific receptors that can regulate both adaptive and innate immune responses. SLAM family proteins are organized as an extracellular domain with having two or four Ig-like domains, a single transmembrane segment, and a cytoplasmic region having tyr-based motifs. The extracellular domain is organized as a membrane-distal Ig variable (IgV) domain that is responsible for ligand recognition and a membrane-proximal truncated Ig constant-2 (IgC2) domain.


Pssm-ID: 319302  Cd Length: 93  Bit Score: 36.90  E-value: 6.58e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 42821116  78 LTIYNANIEDAGIYRCQATDAKGQTQEATVVLEI 111
Cdd:cd05741  60 LLIQNVTQEDSGFYTLQIISTNGKVEQATFHLEV 93
Ig1_Necl_like cd05717
First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; Ig1_Necl_like: ...
219-281 7.21e-03

First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; Ig1_Necl_like: N-terminal immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 (CADM3)), Necl-2 (CADM1), Necl-3 (CADM2), and similar proteins. At least five nectin-like molecules have been identified (Necl-1 to Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1, Necl-2, and Necl-3 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue, and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 accumulates in central and peripheral nervous system tissue, and has been shown to selectively interact with oligodendrocytes. This group also contains Class-I MHC-restricted T-cell-associated molecule (CRTAM), whose expression pattern is consistent with its expression in Class-I MHC-restricted T-cells.


Pssm-ID: 319294  Cd Length: 95  Bit Score: 36.72  E-value: 7.21e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42821116 219 NATAERGEEMTLTCKASGSPDPAISWFR-NGKLIEENEKYILKGSNTEL----------TVRNIINKDGGSYVC 281
Cdd:cd05717   6 DVTVVEGETLTLKCQVRNADNSSLQWLNpNGQTIYFNDKKALRDSRYQLlnlseselsiSVSNVTLSDEGLYTC 79
Ig_VEGFR cd05862
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); ...
35-110 7.69e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); Ig_VEGFR: immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4). VEGF_A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF, VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-2 and -1 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth.


Pssm-ID: 143270  Cd Length: 86  Bit Score: 36.72  E-value: 7.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42821116  35 GESKFFTCTAIGEPES---IDWYNP----QGEKIISTQRVMLQ--KEgVRSRLTIYNANIEDAGIYRCQATDAKGQTQEA 105
Cdd:cd05862   1 GEKLVLNCTARTELNVgidFQWDYPgkkeQRAKSVSENRRSLQehTE-LSSTLTIENVTLSDLGRYTCTASSGQMIAKNS 79

                ....*
gi 42821116 106 TVVLE 110
Cdd:cd05862  80 TIVIV 84
Ig2_IL1R_like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R) and similar proteins; ...
239-284 8.53e-03

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R) and similar proteins; Ig2_IL1R_like: domain similar to the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with an accessory protein, IL1RAP. IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 319309  Cd Length: 92  Bit Score: 36.55  E-value: 8.53e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 42821116 239 DPAISWFRNGKLIEENEKYILKGSntELTVRNIINKDGGSYVCKAT 284
Cdd:cd05757  29 LPPVQWYKDCKPLEGERFRFPKGS--KLLIQNVTEEDAGNYTCKFT 72
Ig_3 cd05765
Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: subgroup of the immunoglobulin (Ig) ...
415-482 9.01e-03

Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: 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. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 143242  Cd Length: 81  Bit Score: 36.37  E-value: 9.01e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42821116 415 GNPINISCDVKANPPASIHWrrEKLVLPAENTTHLKTHSVGRKMILEIAR-----TSDNDFGRYNCTATNRLG 482
Cdd:cd05765   1 GETASFHCDVTGRPPPEITW--EKQVHGKENLIMRPNHVRGNVVVTNIGQlviynAQPQDAGLYTCTARNSGG 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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