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Conserved domains on  [gi|4507875|ref|NP_001069.1|]
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vascular cell adhesion protein 1 isoform a precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ig_VCAM-1 cd07689
Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, ...
116-214 6.73e-47

Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and intercellular cell adhesion molecule-1 (ICAM-1, CD54) and similar domains; Ig_ VCAM-1_like: immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and similar domains. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. The interaction of VCAM-1 binding to the beta1 integrin very late antigen (VLA-4) expressed by lymphocytes and monocytes mediates the adhesion of leucocytes to blood vessel walls, and regulates migration across the endothelium. During metastasis, some circulating cancer cells extravasate to a secondary site by a similar process. VCAM-1 may be involved in organ targeted tumor metastasis and may also act as host receptors for viruses and parasites. VCAM-1 contains seven Ig domains.


:

Pssm-ID: 143313  Cd Length: 99  Bit Score: 162.75  E-value: 6.73e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  116 PKDPEIHLSGPLEAGKPITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIEDIGKVLVC 195
Cdd:cd07689   1 PKDPEILLSGPLEEGKPVTVKCEVPDVYPFDRLEIELLKGETLLPSKSFLEDMDKKSLETKSLEVTFTPTIEDIGKVLVC 80
                        90
                ....*....|....*....
gi 4507875  196 RAKLHIDEMDSVPTVRQAV 214
Cdd:cd07689  81 RAKLHIDEMEKEPKQRQSL 99
Ig_VCAM-1 cd07689
Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, ...
404-502 4.56e-41

Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and intercellular cell adhesion molecule-1 (ICAM-1, CD54) and similar domains; Ig_ VCAM-1_like: immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and similar domains. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. The interaction of VCAM-1 binding to the beta1 integrin very late antigen (VLA-4) expressed by lymphocytes and monocytes mediates the adhesion of leucocytes to blood vessel walls, and regulates migration across the endothelium. During metastasis, some circulating cancer cells extravasate to a secondary site by a similar process. VCAM-1 may be involved in organ targeted tumor metastasis and may also act as host receptors for viruses and parasites. VCAM-1 contains seven Ig domains.


:

Pssm-ID: 143313  Cd Length: 99  Bit Score: 146.96  E-value: 4.56e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  404 PRDPEIEMSGGLVNGSSVTVSCKVPSVYPLDRLEIELLKGETILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGKALVC 483
Cdd:cd07689   1 PKDPEILLSGPLEEGKPVTVKCEVPDVYPFDRLEIELLKGETLLPSKSFLEDMDKKSLETKSLEVTFTPTIEDIGKVLVC 80
                        90
                ....*....|....*....
gi 4507875  484 QAKLHIDDMEFEPKQRQST 502
Cdd:cd07689  81 RAKLHIDEMEKEPKQRQSL 99
IGc2 smart00408
Immunoglobulin C-2 Type;
238-298 5.98e-14

Immunoglobulin C-2 Type;


:

Pssm-ID: 197706  Cd Length: 63  Bit Score: 68.97  E-value: 5.98e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875     238 EGGSVTMTCSSEGLPAPEIFWSKKLD--NGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIG 298
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKDGKplPESNRFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
IG smart00409
Immunoglobulin;
33-112 2.16e-13

Immunoglobulin;


:

Pssm-ID: 214652  Cd Length: 85  Bit Score: 67.92  E-value: 2.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875      33 SRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPL----NGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGI 108
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 4507875     109 QVEI 112
Cdd:smart00409  82 TLTV 85
I-set super family cl28434
Immunoglobulin I-set domain;
313-399 3.82e-13

Immunoglobulin I-set domain;


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 333254  Cd Length: 90  Bit Score: 67.28  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    313 FTVEISPgprIAAQIGDSVMLTCSVMGCESPSFSWRTQiDSPLS----GKVRSEGTNSTLTLSPVSFENEHSYLCTVTCG 388
Cdd:pfam07679   3 FTQKPKD---VEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRssdrFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                          90
                  ....*....|.
gi 4507875    389 HKKLEKGIQVE 399
Cdd:pfam07679  79 AGEAEASAELT 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
519-596 1.77e-10

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


:

Pssm-ID: 214653  Cd Length: 85  Bit Score: 59.44  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     519 SPSSILEEGSSVNMTCLSQGFPAPKILWSRQLP-------NGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKE 591
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkllaesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 4507875     592 VELII 596
Cdd:smart00410  81 TTLTV 85
IG smart00409
Immunoglobulin;
609-685 1.39e-06

Immunoglobulin;


:

Pssm-ID: 214652  Cd Length: 85  Bit Score: 47.89  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     609 PSESVKEGDTVIISCTCGNVPETWIILKKKAET------GDTVLKSIDGAY-TIRKAQLKDAGVYECESKNKVGSQLRSL 681
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKllaesgRFSVSRSGSTSTlTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 4507875     682 TLDV 685
Cdd:smart00409  82 TLTV 85
 
Name Accession Description Interval E-value
Ig_VCAM-1 cd07689
Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, ...
116-214 6.73e-47

Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and intercellular cell adhesion molecule-1 (ICAM-1, CD54) and similar domains; Ig_ VCAM-1_like: immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and similar domains. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. The interaction of VCAM-1 binding to the beta1 integrin very late antigen (VLA-4) expressed by lymphocytes and monocytes mediates the adhesion of leucocytes to blood vessel walls, and regulates migration across the endothelium. During metastasis, some circulating cancer cells extravasate to a secondary site by a similar process. VCAM-1 may be involved in organ targeted tumor metastasis and may also act as host receptors for viruses and parasites. VCAM-1 contains seven Ig domains.


Pssm-ID: 143313  Cd Length: 99  Bit Score: 162.75  E-value: 6.73e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  116 PKDPEIHLSGPLEAGKPITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIEDIGKVLVC 195
Cdd:cd07689   1 PKDPEILLSGPLEEGKPVTVKCEVPDVYPFDRLEIELLKGETLLPSKSFLEDMDKKSLETKSLEVTFTPTIEDIGKVLVC 80
                        90
                ....*....|....*....
gi 4507875  196 RAKLHIDEMDSVPTVRQAV 214
Cdd:cd07689  81 RAKLHIDEMEKEPKQRQSL 99
Ig_VCAM-1 cd07689
Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, ...
404-502 4.56e-41

Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and intercellular cell adhesion molecule-1 (ICAM-1, CD54) and similar domains; Ig_ VCAM-1_like: immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and similar domains. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. The interaction of VCAM-1 binding to the beta1 integrin very late antigen (VLA-4) expressed by lymphocytes and monocytes mediates the adhesion of leucocytes to blood vessel walls, and regulates migration across the endothelium. During metastasis, some circulating cancer cells extravasate to a secondary site by a similar process. VCAM-1 may be involved in organ targeted tumor metastasis and may also act as host receptors for viruses and parasites. VCAM-1 contains seven Ig domains.


Pssm-ID: 143313  Cd Length: 99  Bit Score: 146.96  E-value: 4.56e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  404 PRDPEIEMSGGLVNGSSVTVSCKVPSVYPLDRLEIELLKGETILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGKALVC 483
Cdd:cd07689   1 PKDPEILLSGPLEEGKPVTVKCEVPDVYPFDRLEIELLKGETLLPSKSFLEDMDKKSLETKSLEVTFTPTIEDIGKVLVC 80
                        90
                ....*....|....*....
gi 4507875  484 QAKLHIDDMEFEPKQRQST 502
Cdd:cd07689  81 RAKLHIDEMEKEPKQRQSL 99
C2-set pfam05790
Immunoglobulin C2-set domain;
133-221 6.00e-18

Immunoglobulin C2-set domain;


Pssm-ID: 283453  Cd Length: 80  Bit Score: 80.85  E-value: 6.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    133 ITVKCSVaDVYPFDRLEIDLLKGdHLMKSQEFLEDADRKSLETKSLEVTFTPVIEDIGkVLVCRAKlhidemDSVPTVRQ 212
Cdd:pfam05790   1 VTVSCSN-NLLTCEVLELTLPKG-SKMDPSLKLKGQEAKSLETKKLESTFQPTTEDSG-TWVCLAS------DNDQKKLE 71

                  ....*....
gi 4507875    213 AVKELQVYI 221
Cdd:pfam05790  72 SVIEVLVLE 80
C2-set pfam05790
Immunoglobulin C2-set domain;
421-509 1.30e-14

Immunoglobulin C2-set domain;


Pssm-ID: 283453  Cd Length: 80  Bit Score: 71.61  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    421 VTVSCKVpSVYPLDRLEIELLKGeTILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGkALVCQAKlhiddmEFEPKQRQ 500
Cdd:pfam05790   1 VTVSCSN-NLLTCEVLELTLPKG-SKMDPSLKLKGQEAKSLETKKLESTFQPTTEDSG-TWVCLAS------DNDQKKLE 71

                  ....*....
gi 4507875    501 STQTLYVNV 509
Cdd:pfam05790  72 SVIEVLVLE 80
IGc2 smart00408
Immunoglobulin C-2 Type;
238-298 5.98e-14

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 68.97  E-value: 5.98e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875     238 EGGSVTMTCSSEGLPAPEIFWSKKLD--NGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIG 298
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKDGKplPESNRFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
IG smart00409
Immunoglobulin;
33-112 2.16e-13

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 67.92  E-value: 2.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875      33 SRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPL----NGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGI 108
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 4507875     109 QVEI 112
Cdd:smart00409  82 TLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
313-399 3.82e-13

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 67.28  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    313 FTVEISPgprIAAQIGDSVMLTCSVMGCESPSFSWRTQiDSPLS----GKVRSEGTNSTLTLSPVSFENEHSYLCTVTCG 388
Cdd:pfam07679   3 FTQKPKD---VEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRssdrFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                          90
                  ....*....|.
gi 4507875    389 HKKLEKGIQVE 399
Cdd:pfam07679  79 AGEAEASAELT 89
IG smart00409
Immunoglobulin;
321-399 4.10e-13

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 67.15  E-value: 4.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     321 PRIAAQIGDSVMLTCSVMGCESPSFSWRTQIDSPLSGK----VRSEGTNSTLTLSPVSFENEHSYLCTVTCGHKKLEKGI 396
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESgrfsVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ...
gi 4507875     397 QVE 399
Cdd:smart00409  82 TLT 84
I-set pfam07679
Immunoglobulin I-set domain;
29-112 9.56e-13

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 66.13  E-value: 9.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     29 TTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQiDSPLN----GKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKL 104
Cdd:pfam07679   4 TQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRssdrFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                  ....*...
gi 4507875    105 EKGIQVEI 112
Cdd:pfam07679  83 EASAELTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
227-295 2.75e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 61.75  E-value: 2.75e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507875    227 VISVNPS-TKLQEGGSVTMTCSSEGLPAPEIFWSKklDNGNLQHL------SGNATLTLIAMRMEDSGIYVCEGVN 295
Cdd:pfam13927   3 VITVSPSsVVVLEGESVTLTCEATGGPPPTITWYK--NGKPGPTSsrislsGSNSTLTISNVTREDSGTYTCVASN 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
519-596 1.77e-10

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 59.44  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     519 SPSSILEEGSSVNMTCLSQGFPAPKILWSRQLP-------NGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKE 591
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkllaesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 4507875     592 VELII 596
Cdd:smart00410  81 TTLTV 85
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
242-305 7.03e-10

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: 57.64  E-value: 7.03e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  242 VTMTCSSEGLPAPEIFWSKK------LDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVE 305
Cdd:cd00096   1 VTLTCSASGNPPPTITWLKNgkplpsSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
515-583 7.77e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 57.51  E-value: 7.77e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507875    515 TVLVSPSS-ILEEGSSVNMTCLSQGFPAPKILWSRqlpNGELQPLSE-------NATLTLISTKMEDSGVYLCEGIN 583
Cdd:pfam13927   3 VITVSPSSvVVLEGESVTLTCEATGGPPPTITWYK---NGKPGPTSSrislsgsNSTLTISNVTREDSGTYTCVASN 76
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
530-593 1.35e-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: 53.79  E-value: 1.35e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  530 VNMTCLSQGFPAPKILWSR---QLPNGEL---QPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVE 593
Cdd:cd00096   1 VTLTCSASGNPPPTITWLKngkPLPSSSRfrrRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
331-397 9.77e-07

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: 48.39  E-value: 9.77e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  331 VMLTCSVMGCESPSFSWR---TQIDSPLSGKVRSEGTNSTLTLSPVSFENEHSYLCTVTCGHKKLEKGIQ 397
Cdd:cd00096   1 VTLTCSASGNPPPTITWLkngKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
IG smart00409
Immunoglobulin;
609-685 1.39e-06

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 47.89  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     609 PSESVKEGDTVIISCTCGNVPETWIILKKKAET------GDTVLKSIDGAY-TIRKAQLKDAGVYECESKNKVGSQLRSL 681
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKllaesgRFSVSRSGSTSTlTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 4507875     682 TLDV 685
Cdd:smart00409  82 TLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
604-672 7.52e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 45.57  E-value: 7.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507875    604 KLTAFPSES-VKEGDTVIISCTCGNVPE---TWIILKKKAETGDTVLKSIDGAY-TIRKAQLKDAGVYECESKN 672
Cdd:pfam13927   3 VITVSPSSVvVLEGESVTLTCEATGGPPptiTWYKNGKPGPTSSRISLSGSNSTlTISNVTREDSGTYTCVASN 76
PHA02785 PHA02785
IL-beta-binding protein; Provisional
521-710 5.24e-05

IL-beta-binding protein; Provisional


Pssm-ID: 165149  Cd Length: 326  Bit Score: 45.78  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875   521 SSILE-EGSSVNMTC-----LSQGFPAPKILWS-RQLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVE 593
Cdd:PHA02785  34 ASFMElENEPVILPCpqintLSSGYNILDILWEkRGADNDRIIPIDNGSNMLILNPTQSDSGIYICITKNETYCDMMSLN 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875   594 L-IIQVTPKDIKLTAFPsESVKEGDTVIISC------TCGNVPETWIILKKKAETGDTVLKSIDGAYTIRKAQLKDAGVY 666
Cdd:PHA02785 114 LtIVSVSESNIDLISYP-QIVNERSTGEMVCpninafIASNVNADIIWSGHRRLRNKRLKQRTPGIITIEDVRKNDAGYY 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 4507875   667 ECESKNKVGSQLRSLT----LDVQGRENNKDYFSPELLVLYFASSLII 710
Cdd:PHA02785 193 TCVLKYIYGDKTYNVTrivkLEVRDRIIPPTMQLPEGVVTSIGSNLTI 240
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
43-109 1.19e-04

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: 42.23  E-value: 1.19e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875   43 VSLTCSTTGCESPFFSWR---TQIDSPLNGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGIQ 109
Cdd:cd00096   1 VTLTCSASGNPPPTITWLkngKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
604-685 1.39e-04

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: 42.13  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  604 KLTAFPSESVKEGDTVIISCTCGNVPETWIILKKKAETGDTVLKSIDG-----------AYTIRKAQLKDAGVYECESKN 672
Cdd:cd05732   4 KITYLENQTAVELEQITLTCEAEGDPIPEITWRRATRNFSEGDKSLDGrivvrgharvsSLTLKDVQLTDAGRYDCEASN 83
                        90
                ....*....|...
gi 4507875  673 KVGSQLRSLTLDV 685
Cdd:cd05732  84 RIGGDQQSMYLEV 96
 
Name Accession Description Interval E-value
Ig_VCAM-1 cd07689
Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, ...
116-214 6.73e-47

Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and intercellular cell adhesion molecule-1 (ICAM-1, CD54) and similar domains; Ig_ VCAM-1_like: immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and similar domains. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. The interaction of VCAM-1 binding to the beta1 integrin very late antigen (VLA-4) expressed by lymphocytes and monocytes mediates the adhesion of leucocytes to blood vessel walls, and regulates migration across the endothelium. During metastasis, some circulating cancer cells extravasate to a secondary site by a similar process. VCAM-1 may be involved in organ targeted tumor metastasis and may also act as host receptors for viruses and parasites. VCAM-1 contains seven Ig domains.


Pssm-ID: 143313  Cd Length: 99  Bit Score: 162.75  E-value: 6.73e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  116 PKDPEIHLSGPLEAGKPITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIEDIGKVLVC 195
Cdd:cd07689   1 PKDPEILLSGPLEEGKPVTVKCEVPDVYPFDRLEIELLKGETLLPSKSFLEDMDKKSLETKSLEVTFTPTIEDIGKVLVC 80
                        90
                ....*....|....*....
gi 4507875  196 RAKLHIDEMDSVPTVRQAV 214
Cdd:cd07689  81 RAKLHIDEMEKEPKQRQSL 99
Ig_VCAM-1 cd07689
Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, ...
404-502 4.56e-41

Immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and intercellular cell adhesion molecule-1 (ICAM-1, CD54) and similar domains; Ig_ VCAM-1_like: immunoglobulin (Ig)-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1, CD106) and similar domains. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. The interaction of VCAM-1 binding to the beta1 integrin very late antigen (VLA-4) expressed by lymphocytes and monocytes mediates the adhesion of leucocytes to blood vessel walls, and regulates migration across the endothelium. During metastasis, some circulating cancer cells extravasate to a secondary site by a similar process. VCAM-1 may be involved in organ targeted tumor metastasis and may also act as host receptors for viruses and parasites. VCAM-1 contains seven Ig domains.


Pssm-ID: 143313  Cd Length: 99  Bit Score: 146.96  E-value: 4.56e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  404 PRDPEIEMSGGLVNGSSVTVSCKVPSVYPLDRLEIELLKGETILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGKALVC 483
Cdd:cd07689   1 PKDPEILLSGPLEEGKPVTVKCEVPDVYPFDRLEIELLKGETLLPSKSFLEDMDKKSLETKSLEVTFTPTIEDIGKVLVC 80
                        90
                ....*....|....*....
gi 4507875  484 QAKLHIDDMEFEPKQRQST 502
Cdd:cd07689  81 RAKLHIDEMEKEPKQRQSL 99
C2-set pfam05790
Immunoglobulin C2-set domain;
133-221 6.00e-18

Immunoglobulin C2-set domain;


Pssm-ID: 283453  Cd Length: 80  Bit Score: 80.85  E-value: 6.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    133 ITVKCSVaDVYPFDRLEIDLLKGdHLMKSQEFLEDADRKSLETKSLEVTFTPVIEDIGkVLVCRAKlhidemDSVPTVRQ 212
Cdd:pfam05790   1 VTVSCSN-NLLTCEVLELTLPKG-SKMDPSLKLKGQEAKSLETKKLESTFQPTTEDSG-TWVCLAS------DNDQKKLE 71

                  ....*....
gi 4507875    213 AVKELQVYI 221
Cdd:pfam05790  72 SVIEVLVLE 80
C2-set pfam05790
Immunoglobulin C2-set domain;
421-509 1.30e-14

Immunoglobulin C2-set domain;


Pssm-ID: 283453  Cd Length: 80  Bit Score: 71.61  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    421 VTVSCKVpSVYPLDRLEIELLKGeTILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGkALVCQAKlhiddmEFEPKQRQ 500
Cdd:pfam05790   1 VTVSCSN-NLLTCEVLELTLPKG-SKMDPSLKLKGQEAKSLETKKLESTFQPTTEDSG-TWVCLAS------DNDQKKLE 71

                  ....*....
gi 4507875    501 STQTLYVNV 509
Cdd:pfam05790  72 SVIEVLVLE 80
IGc2 smart00408
Immunoglobulin C-2 Type;
238-298 5.98e-14

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 68.97  E-value: 5.98e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875     238 EGGSVTMTCSSEGLPAPEIFWSKKLD--NGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIG 298
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKDGKplPESNRFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
IG smart00409
Immunoglobulin;
33-112 2.16e-13

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 67.92  E-value: 2.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875      33 SRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPL----NGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGI 108
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 4507875     109 QVEI 112
Cdd:smart00409  82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
33-112 2.16e-13

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 67.92  E-value: 2.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875      33 SRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPL----NGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGI 108
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 4507875     109 QVEI 112
Cdd:smart00410  82 TLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
313-399 3.82e-13

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 67.28  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    313 FTVEISPgprIAAQIGDSVMLTCSVMGCESPSFSWRTQiDSPLS----GKVRSEGTNSTLTLSPVSFENEHSYLCTVTCG 388
Cdd:pfam07679   3 FTQKPKD---VEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRssdrFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78
                          90
                  ....*....|.
gi 4507875    389 HKKLEKGIQVE 399
Cdd:pfam07679  79 AGEAEASAELT 89
IG smart00409
Immunoglobulin;
321-399 4.10e-13

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 67.15  E-value: 4.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     321 PRIAAQIGDSVMLTCSVMGCESPSFSWRTQIDSPLSGK----VRSEGTNSTLTLSPVSFENEHSYLCTVTCGHKKLEKGI 396
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESgrfsVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ...
gi 4507875     397 QVE 399
Cdd:smart00409  82 TLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
321-399 4.10e-13

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 67.15  E-value: 4.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     321 PRIAAQIGDSVMLTCSVMGCESPSFSWRTQIDSPLSGK----VRSEGTNSTLTLSPVSFENEHSYLCTVTCGHKKLEKGI 396
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESgrfsVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ...
gi 4507875     397 QVE 399
Cdd:smart00410  82 TLT 84
I-set pfam07679
Immunoglobulin I-set domain;
29-112 9.56e-13

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 66.13  E-value: 9.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     29 TTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQiDSPLN----GKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKL 104
Cdd:pfam07679   4 TQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKD-GQPLRssdrFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEA 82

                  ....*...
gi 4507875    105 EKGIQVEI 112
Cdd:pfam07679  83 EASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
232-308 2.12e-12

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 65.22  E-value: 2.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     232 PSTKLQEGGSVTMTCSSEGLPAPEIFWSKKL-------DNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEV 304
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgkllaesGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 4507875     305 ELIV 308
Cdd:smart00410  82 TLTV 85
IG smart00409
Immunoglobulin;
232-308 2.12e-12

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 65.22  E-value: 2.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     232 PSTKLQEGGSVTMTCSSEGLPAPEIFWSKKL-------DNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEV 304
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGgkllaesGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 4507875     305 ELIV 308
Cdd:smart00409  82 TLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
227-295 2.75e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 61.75  E-value: 2.75e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507875    227 VISVNPS-TKLQEGGSVTMTCSSEGLPAPEIFWSKklDNGNLQHL------SGNATLTLIAMRMEDSGIYVCEGVN 295
Cdd:pfam13927   3 VITVSPSsVVVLEGESVTLTCEATGGPPPTITWYK--NGKPGPTSsrislsGSNSTLTISNVTREDSGTYTCVASN 76
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
229-306 3.42e-11

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: 61.83  E-value: 3.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    229 SVNPSTKLQEGGSVTMTCS-SEGLPAPEIFWSKKLDNGNLQHL-------SGNATLTLIAMRMEDSGIYVCEGVNLIGKN 300
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSaSTGSPGPDVTWSKEGGTLIESLKvkhdngrTTQSSLLISNVTKEDAGTYTCVVNNPGGPA 80

                  ....*.
gi 4507875    301 RKEVEL 306
Cdd:pfam00047  81 TLSTSL 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
519-596 1.77e-10

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 59.44  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     519 SPSSILEEGSSVNMTCLSQGFPAPKILWSRQLP-------NGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKE 591
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkllaesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 4507875     592 VELII 596
Cdd:smart00410  81 TTLTV 85
IG smart00409
Immunoglobulin;
519-596 1.77e-10

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 59.44  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     519 SPSSILEEGSSVNMTCLSQGFPAPKILWSRQLP-------NGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKE 591
Cdd:smart00409   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkllaesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 4507875     592 VELII 596
Cdd:smart00409  81 TTLTV 85
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
242-305 7.03e-10

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: 57.64  E-value: 7.03e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  242 VTMTCSSEGLPAPEIFWSKK------LDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVE 305
Cdd:cd00096   1 VTLTCSASGNPPPTITWLKNgkplpsSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
515-583 7.77e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 57.51  E-value: 7.77e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507875    515 TVLVSPSS-ILEEGSSVNMTCLSQGFPAPKILWSRqlpNGELQPLSE-------NATLTLISTKMEDSGVYLCEGIN 583
Cdd:pfam13927   3 VITVSPSSvVVLEGESVTLTCEATGGPPPTITWYK---NGKPGPTSSrislsgsNSTLTISNVTREDSGTYTCVASN 76
IGc2 smart00408
Immunoglobulin C-2 Type;
526-586 3.45e-09

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 55.49  E-value: 3.45e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875     526 EGSSVNMTCLSQGFPAPKILWSR--QLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAG 586
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKdgKPLPESNRFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
530-593 1.35e-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: 53.79  E-value: 1.35e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  530 VNMTCLSQGFPAPKILWSR---QLPNGEL---QPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVE 593
Cdd:cd00096   1 VTLTCSASGNPPPTITWLKngkPLPSSSRfrrRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
I-set pfam07679
Immunoglobulin I-set domain;
233-308 2.43e-08

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 53.42  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    233 STKLQEGGSVTMTCSSEGLPAPEIFWSKK------LDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVEL 306
Cdd:pfam07679   9 DVEVQEGESARFTCTVTGTPDPEVSWFKDgqplrsSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                  ..
gi 4507875    307 IV 308
Cdd:pfam07679  89 TV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
311-386 4.36e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 52.50  E-value: 4.36e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507875    311 KPfTVEISPGPrIAAQIGDSVMLTCSVMGCESPSFSW-RTQIDSPLSGKVRSEGTNSTLTLSPVSFENEHSYLCTVT 386
Cdd:pfam13927   1 KP-VITVSPSS-VVVLEGESVTLTCEATGGPPPTITWyKNGKPGPTSSRISLSGSNSTLTISNVTREDSGTYTCVAS 75
IGc2 smart00408
Immunoglobulin C-2 Type;
327-386 1.83e-07

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 50.48  E-value: 1.83e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     327 IGDSVMLTCSVMGCESPSFSWRTQiDSPLSGKVRSEGTNSTLTLSPVSFENEHSYLCTVT 386
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKD-GKPLPESNRFVASGSTLTIKSVSLEDSGLYTCVAE 59
Ig_NCAM-2 cd05870
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM ...
238-306 3.81e-07

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: 49.98  E-value: 3.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  238 EGGSVTMTCSSEGLPAPEIFWSKKLD-----------NGNL----QHlsGNATLTLIAMRMEDSGIYVCEGVNLIGKNRK 302
Cdd:cd05870  15 ENGAATLSCKAEGEPIPEITWKRASDghtfsegdkspDGRIevkgQH--GESSLHIKDVKLSDSGRYDCEAASRIGGHQK 92

                ....
gi 4507875  303 EVEL 306
Cdd:cd05870  93 SMYL 96
Ig2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
527-587 4.64e-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: 49.45  E-value: 4.64e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507875  527 GSSVNMTCLSQGFPAPKILW----SRQLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAGR 587
Cdd:cd05856   9 GSSVRLKCVASGNPRPDITWlkdnKPLTPTEIGESRKKKWTLSLKNLKPEDSGKYTCHVSNRAGE 73
I-set pfam07679
Immunoglobulin I-set domain;
511-596 4.83e-07

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 49.56  E-value: 4.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    511 PRDTTVLvspssileEGSSVNMTCLSQGFPAPKILWSRqlpNGelQPLSE-----------NATLTLISTKMEDSGVYLC 579
Cdd:pfam07679   7 PKDVEVQ--------EGESARFTCTVTGTPDPEVSWFK---DG--QPLRSsdrfkvtyeggTYTLTISNVQPDDSGKYTC 73
                          90
                  ....*....|....*..
gi 4507875    580 EGINQAGRSRKEVELII 596
Cdd:pfam07679  74 VATNSAGEAEASAELTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
29-98 4.99e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 49.42  E-value: 4.99e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507875     29 TTPESRYLAQIGDSVSLTCSTTGCESPFFSW-RTQIDSPLNGKVTNEGTTSTLTMNPVSFGNEHSYLCTAT 98
Cdd:pfam13927   5 TVSPSSVVVLEGESVTLTCEATGGPPPTITWyKNGKPGPTSSRISLSGSNSTLTISNVTREDSGTYTCVAS 75
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
239-309 6.27e-07

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: 49.25  E-value: 6.27e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875  239 GGSVTMTCSSEGLPAPEIFWSKKLDN--GNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIVQ 309
Cdd:cd05851  16 GQNVTLECFALGNPVPVIRWRKILEPmpATAEISMSGAVLKIFNIQPEDEGTYECEAENIKGKDKHQARVYVQ 88
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
238-308 6.90e-07

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: 49.06  E-value: 6.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  238 EGGSVTMTCSSEGLPAPEIFWS----------KKLDnGNLQHLS--GNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVE 305
Cdd:cd05732  15 ELEQITLTCEAEGDPIPEITWRratrnfsegdKSLD-GRIVVRGhaRVSSLTLKDVQLTDAGRYDCEASNRIGGDQQSMY 93

                ...
gi 4507875  306 LIV 308
Cdd:cd05732  94 LEV 96
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
331-397 9.77e-07

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: 48.39  E-value: 9.77e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  331 VMLTCSVMGCESPSFSWR---TQIDSPLSGKVRSEGTNSTLTLSPVSFENEHSYLCTVTCGHKKLEKGIQ 397
Cdd:cd00096   1 VTLTCSASGNPPPTITWLkngKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
Ig2_ICAM-1_like cd05755
Second immunoglobulin (Ig)-like domain of intercellular cell adhesion molecule-1 (ICAM-1, ...
418-487 1.29e-06

Second immunoglobulin (Ig)-like domain of intercellular cell adhesion molecule-1 (ICAM-1, CD54) and similar proteins; Ig2_ ICAM-1_like: domain similar to the second immunoglobulin (Ig)-like domain of intercellular cell adhesion molecule-1 (ICAM-1, CD54). During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. ICAM-1 may be involved in organ targeted tumor metastasis. The interaction of ICAM-1 with leukocyte function-associated antigen-1 (LFA-1) plays a part in leukocyte-endothelial cell recognition. This group also contains ICAM-2, which also interacts with LFA-1. Transmigration of immature dendritic cells across resting endothelium is dependent on the interaction of ICAM-2 with, yet unidentified, ligand(s) on the dendritic cells. ICAM-1 has five Ig-like domains and ICAM-2 has two. ICAM-1 may also act as host receptor for viruses and parasites.


Pssm-ID: 143232  Cd Length: 100  Bit Score: 48.26  E-value: 1.29e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  418 GSSVTVSCKVPSVYPLDRLEIELLKGETILENIEFLEDTdmKSLENKSLEMTFIPTIEDTGKALVCQAKL 487
Cdd:cd05755  16 GKNYTLQCDVPGVAPRQNLTVVLLRGNETLSRQPFGDNT--KSPVNAPATITITVDREDHGANFSCETEL 83
IG smart00409
Immunoglobulin;
609-685 1.39e-06

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 47.89  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     609 PSESVKEGDTVIISCTCGNVPETWIILKKKAET------GDTVLKSIDGAY-TIRKAQLKDAGVYECESKNKVGSQLRSL 681
Cdd:smart00409   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKllaesgRFSVSRSGSTSTlTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 4507875     682 TLDV 685
Cdd:smart00409  82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
609-685 1.39e-06

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 47.89  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875     609 PSESVKEGDTVIISCTCGNVPETWIILKKKAET------GDTVLKSIDGAY-TIRKAQLKDAGVYECESKNKVGSQLRSL 681
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKllaesgRFSVSRSGSTSTlTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 4507875     682 TLDV 685
Cdd:smart00410  82 TLTV 85
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
526-596 1.75e-06

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: 47.63  E-value: 1.75e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507875  526 EGSSVNMTCLSQGFPAPKILWSR---QLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVELII 596
Cdd:cd05745   1 EGQTVDFLCEAQGYPQPVIAWTKggsQLSVDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
515-596 2.69e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 316418  Cd Length: 78  Bit Score: 46.98  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    515 TVLVSPSSILEEGSSVNMTCLSQGFPAPKILWSRqlpNGElqPLSENATLTLISTKmEDSGVYLCEGINQAGR-SRKEVE 593
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCSAPGNPPANYTWYK---GGE--ALNSSPNFISSVSA-EDSGTYTCVARNGRGGkVSNPVE 75

                  ...
gi 4507875    594 LII 596
Cdd:pfam13895  76 LTV 78
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
238-308 3.48e-06

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: 46.86  E-value: 3.48e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507875  238 EGGSVTMTCSSEGLPAPEIFWSK-----KLDNGNLQHLSGnaTLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIV 308
Cdd:cd05745   1 EGQTVDFLCEAQGYPQPVIAWTKggsqlSVDRRHLVLSSG--TLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
517-581 4.57e-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: 46.42  E-value: 4.57e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875    517 LVSPSSILEEGSSVNMTC-LSQGFPAPKILWSR---QLPNGELQPLSEN----ATLTLISTKMEDSGVYLCEG 581
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCsASTGSPGPDVTWSKeggTLIESLKVKHDNGrttqSSLLISNVTKEDAGTYTCVV 73
Ig_2 cd05764
Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: subgroup of the immunoglobulin (Ig) ...
527-596 4.94e-06

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: 46.32  E-value: 4.94e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507875  527 GSSVNMTCLSQGFPAPKILW----SRQLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVELII 596
Cdd:cd05764   1 GQRATLRCKARGDPEPAIHWispdGKLISNSSRTLVYDNGTLDILITTVKDTGSFTCIASNAAGEATATVELHI 74
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
604-672 7.52e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 45.57  E-value: 7.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507875    604 KLTAFPSES-VKEGDTVIISCTCGNVPE---TWIILKKKAETGDTVLKSIDGAY-TIRKAQLKDAGVYECESKN 672
Cdd:pfam13927   3 VITVSPSSVvVLEGESVTLTCEATGGPPptiTWYKNGKPGPTSSRISLSGSNSTlTISNVTREDSGTYTCVASN 76
Ig_3 cd05765
Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: subgroup of the immunoglobulin (Ig) ...
239-308 8.11e-06

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: 45.61  E-value: 8.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  239 GGSVTMTCSSEGLPAPEIFWSKKLDNG-NL----QHLSGNATLTLIAM------RMEDSGIYVCEGVNLIGKNRKEVELI 307
Cdd:cd05765   1 GETASFHCDVTGRPPPEITWEKQVHGKeNLimrpNHVRGNVVVTNIGQlviynaQPQDAGLYTCTARNSGGLLRANFPLS 80

                .
gi 4507875  308 V 308
Cdd:cd05765  81 V 81
Ig3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of ...
527-597 1.04e-05

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: 45.61  E-value: 1.04e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875  527 GSSVNMTCLSQGFPAPKILWSRQL--PNGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVELIIQ 597
Cdd:cd04968  16 GQTVTLECFALGNPVPQIKWRKVDgsPSSQWTTSTSEPVLEIPNVQFEDEGTYECEAENSRGKDTVQGRIIVQ 88
Ig3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of ...
239-309 1.08e-05

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: 45.23  E-value: 1.08e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875  239 GGSVTMTCSSEGLPAPEIFWSKKLDNGNLQHLS--GNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIVQ 309
Cdd:cd04968  16 GQTVTLECFALGNPVPQIKWRKVDGSPSSQWTTstSEPVLEIPNVQFEDEGTYECEAENSRGKDTVQGRIIVQ 88
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
507-597 1.53e-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: 45.01  E-value: 1.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  507 VNVAPRDTTVLVspssileeGSSVNMTCLSQGFPAPKILWSRQLpngELQPLS-----ENATLTLISTKMEDSGVYLCEG 581
Cdd:cd05851   4 INVKFKDTYALK--------GQNVTLECFALGNPVPVIRWRKIL---EPMPATaeismSGAVLKIFNIQPEDEGTYECEA 72
                        90
                ....*....|....*.
gi 4507875  582 INQAGRSRKEVELIIQ 597
Cdd:cd05851  73 ENIKGKDKHQARVYVQ 88
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
534-596 2.24e-05

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: 44.32  E-value: 2.24e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507875  534 CLSQGFPAPKILWSR---QLPNGELQPLSENaTLTLISTKMEDSGVYLCEGINQAGRSRKEVELII 596
Cdd:cd05725   5 CEVGGDPVPTVLWRKedgELPKGRAEILDDK-SLKIRNVTAGDEGSYTCEAENMVGKIEASASLTV 69
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth Ig domain of ...
239-308 2.37e-05

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: 44.36  E-value: 2.37e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875  239 GGSVTMTCSSEGLPAPEIFWSKK---LDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIV 308
Cdd:cd04969   1 GGDVIIECKPKASPKPTISWSKGtelLTNSSRICILPDGSLKIKNVSKSDEGKYTCFAVNFFGKANSTGSLSV 73
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
223-308 2.45e-05

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: 44.59  E-value: 2.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  223 PKNTVISVNPSTKLQEggSVTMTCSSEGLPAPEIFWSKKLDN--GNLQHLSGN---------ATLTLIAMRMEDSGIYVC 291
Cdd:cd05869   3 PKITYVENQTAMELEE--QITLTCEASGDPIPSITWRTSTRNisSEEKTLDGHivvrsharvSSLTLKYIQYTDAGEYLC 80
                        90
                ....*....|....*..
gi 4507875  292 EGVNLIGKNRKEVELIV 308
Cdd:cd05869  81 TASNTIGQDSQSMYLEV 97
Ig4_Robo cd05726
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig4_Robo: domain similar ...
527-586 2.81e-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: 44.18  E-value: 2.81e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507875  527 GSSVNMTCLSQGFPAPKILWSRQ------LPNGELQP-----LSENATLTLISTKMEDSGVYLCEGINQAG 586
Cdd:cd05726   1 GRTVTFQCEATGNPQPAIFWQKEgsqnllFSYQPPQSssrfsVSQTGDLTITNVQRSDVGYYICQTLNVAG 71
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
237-308 4.26e-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: 43.62  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    237 QEGGSVTMTC---SSEGLPAPEIFWSKKLDNGNLQHL------------------------SGNATLTLIAMRMEDSGIY 289
Cdd:pfam07686   9 AEGGSVTLPCtysSSMSEASYYIYWYRQPPGGGPEELiayysngyeegkkkgrfslrgdpsRSDFSLTIQNLTPSDSGTY 88
                          90       100
                  ....*....|....*....|
gi 4507875    290 VCEGV-NLIGKNRKEVELIV 308
Cdd:pfam07686  89 FCAVIpSGEGVFGSGTRLTV 108
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
246-309 5.15e-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: 43.19  E-value: 5.15e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507875  246 CSSEGLPAPEIFWSKK---LDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIVQ 309
Cdd:cd05731   5 CIAEGLPTPDIRWIKLggeLPKGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTVE 71
PHA02785 PHA02785
IL-beta-binding protein; Provisional
521-710 5.24e-05

IL-beta-binding protein; Provisional


Pssm-ID: 165149  Cd Length: 326  Bit Score: 45.78  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875   521 SSILE-EGSSVNMTC-----LSQGFPAPKILWS-RQLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVE 593
Cdd:PHA02785  34 ASFMElENEPVILPCpqintLSSGYNILDILWEkRGADNDRIIPIDNGSNMLILNPTQSDSGIYICITKNETYCDMMSLN 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875   594 L-IIQVTPKDIKLTAFPsESVKEGDTVIISC------TCGNVPETWIILKKKAETGDTVLKSIDGAYTIRKAQLKDAGVY 666
Cdd:PHA02785 114 LtIVSVSESNIDLISYP-QIVNERSTGEMVCpninafIASNVNADIIWSGHRRLRNKRLKQRTPGIITIEDVRKNDAGYY 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 4507875   667 ECESKNKVGSQLRSLT----LDVQGRENNKDYFSPELLVLYFASSLII 710
Cdd:PHA02785 193 TCVLKYIYGDKTYNVTrivkLEVRDRIIPPTMQLPEGVVTSIGSNLTI 240
Ig_CEACAM cd05740
Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion ...
227-304 5.50e-05

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: 43.42  E-value: 5.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  227 VISVNPST---KLQEGGSVTMTCSSEGlPAPEIFWSKK---LDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKN 300
Cdd:cd05740   3 VINSNNSVgnqPPEDNQPVTLTCEAEG-QATYIWWVNNgslLVPPRLQLSNDNRTLTFNNVTRSDTGHYQCEASNEVSNM 81

                ....
gi 4507875  301 RKEV 304
Cdd:cd05740  82 TSDP 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
318-385 5.75e-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: 43.34  E-value: 5.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875    318 SPGPRIAAQIGDSVMLTCSVMGCES-PSFSWR----TQIDSPLSGKVRSEGTNSTLTLSPVSFENEHSYLCTV 385
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPgPDVTWSkeggTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVV 73
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
534-597 6.03e-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: 42.80  E-value: 6.03e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507875  534 CLSQGFPAPKILWSR---QLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEVELIIQ 597
Cdd:cd05731   5 CIAEGLPTPDIRWIKlggELPKGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTVE 71
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
35-97 7.54e-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: 42.95  E-value: 7.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507875     35 YLAQIGDSVSLTCSTTGCESPF-FSWRTQIDSPLNG----KVTNEGTTSTLTMNPVSFGNEHSYLCTA 97
Cdd:pfam00047   6 VTVLEGDSATLTCSASTGSPGPdVTWSKEGGTLIESlkvkHDNGRTTQSSLLISNVTKEDAGTYTCVV 73
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
242-308 8.15e-05

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: 42.39  E-value: 8.15e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507875  242 VTMTCSSEGLPAPEIFWSKklDNGNLQ----HLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIV 308
Cdd:cd05725   1 VEFQCEVGGDPVPTVLWRK--EDGELPkgraEILDDKSLKIRNVTAGDEGSYTCEAENMVGKIEASASLTV 69
I-set pfam07679
Immunoglobulin I-set domain;
596-685 8.59e-05

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 42.63  E-value: 8.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    596 IQVTPKDIKltafpsesVKEGDTVIISCTCGNVPE---TWIILKKKAETGDTVLKSIDGAY---TIRKAQLKDAGVYECE 669
Cdd:pfam07679   3 FTQKPKDVE--------VQEGESARFTCTVTGTPDpevSWFKDGQPLRSSDRFKVTYEGGTytlTISNVQPDDSGKYTCV 74
                          90
                  ....*....|....*.
gi 4507875    670 SKNKVGSQLRSLTLDV 685
Cdd:pfam07679  75 ATNSAGEAEASAELTV 90
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
527-587 1.05e-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: 42.48  E-value: 1.05e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4507875  527 GSSVNMTCLSQGFPAPKILWsrQLPNG------ELQPLSENA--TLTLISTKMEDSGVYLCEGINQAGR 587
Cdd:cd05743   1 GETVEFTCVATGVPTPIINW--RLNWGhvpdsaRVSITSEGGygTLTIRDVKESDQGAYTCEAINTRGM 67
Ig_3 cd05765
Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: subgroup of the immunoglobulin (Ig) ...
527-586 1.16e-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: 42.14  E-value: 1.16e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507875  527 GSSVNMTCLSQGFPAPKILWSRQLPNGELQPLSEN-----------ATLTLISTKMEDSGVYLCEGINQAG 586
Cdd:cd05765   1 GETASFHCDVTGRPPPEITWEKQVHGKENLIMRPNhvrgnvvvtniGQLVIYNAQPQDAGLYTCTARNSGG 71
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
43-109 1.19e-04

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: 42.23  E-value: 1.19e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875   43 VSLTCSTTGCESPFFSWR---TQIDSPLNGKVTNEGTTSTLTMNPVSFGNEHSYLCTATCESRKLEKGIQ 109
Cdd:cd00096   1 VTLTCSASGNPPPTITWLkngKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
Ig2_ICAM-1_like cd05755
Second immunoglobulin (Ig)-like domain of intercellular cell adhesion molecule-1 (ICAM-1, ...
130-199 1.23e-04

Second immunoglobulin (Ig)-like domain of intercellular cell adhesion molecule-1 (ICAM-1, CD54) and similar proteins; Ig2_ ICAM-1_like: domain similar to the second immunoglobulin (Ig)-like domain of intercellular cell adhesion molecule-1 (ICAM-1, CD54). During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. ICAM-1 may be involved in organ targeted tumor metastasis. The interaction of ICAM-1 with leukocyte function-associated antigen-1 (LFA-1) plays a part in leukocyte-endothelial cell recognition. This group also contains ICAM-2, which also interacts with LFA-1. Transmigration of immature dendritic cells across resting endothelium is dependent on the interaction of ICAM-2 with, yet unidentified, ligand(s) on the dendritic cells. ICAM-1 has five Ig-like domains and ICAM-2 has two. ICAM-1 may also act as host receptor for viruses and parasites.


Pssm-ID: 143232  Cd Length: 100  Bit Score: 42.09  E-value: 1.23e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  130 GKPITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDAdrKSLETKSLEVTFTPVIEDIGKVLVCRAKL 199
Cdd:cd05755  16 GKNYTLQCDVPGVAPRQNLTVVLLRGNETLSRQPFGDNT--KSPVNAPATITITVDREDHGANFSCETEL 83
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth Ig domain of ...
527-586 1.32e-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: 42.05  E-value: 1.32e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875  527 GSSVNMTCLSQGFPAPKILWSR---QLPNGELQPLSENATLTLISTKMEDSGVYLCEGINQAG 586
Cdd:cd04969   1 GGDVIIECKPKASPKPTISWSKgteLLTNSSRICILPDGSLKIKNVSKSDEGKYTCFAVNFFG 63
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
604-685 1.39e-04

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: 42.13  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  604 KLTAFPSESVKEGDTVIISCTCGNVPETWIILKKKAETGDTVLKSIDG-----------AYTIRKAQLKDAGVYECESKN 672
Cdd:cd05732   4 KITYLENQTAVELEQITLTCEAEGDPIPEITWRRATRNFSEGDKSLDGrivvrgharvsSLTLKDVQLTDAGRYDCEASN 83
                        90
                ....*....|...
gi 4507875  673 KVGSQLRSLTLDV 685
Cdd:cd05732  84 RIGGDQQSMYLEV 96
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
515-594 1.48e-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: 41.96  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  515 TVLVSPSSI-LEEGSSVNMTCLSQGFPAPKILWSRqlpngELQPLSENATLTLISTK-----------MEDSGVYLCEGI 582
Cdd:cd05747   5 TILTKPRSLtVSEGESARFSCDVDGEPAPTVTWMR-----EGQIIVSSQRHQITSTEykstfeiskvqMSDEGNYTVVVE 79
                        90
                ....*....|..
gi 4507875  583 NQAGRSRKEVEL 594
Cdd:cd05747  80 NSEGKQEAQFTL 91
Ig4_Robo cd05726
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig4_Robo: domain similar ...
239-312 1.58e-04

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: 41.86  E-value: 1.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  239 GGSVTMTCSSEGLPAPEIFWSKK------LDNGNLQ-----HLSGNATLTLIAMRMEDSGIYVCEGVNLIG----KNRKE 303
Cdd:cd05726   1 GRTVTFQCEATGNPQPAIFWQKEgsqnllFSYQPPQsssrfSVSQTGDLTITNVQRSDVGYYICQTLNVAGsiltKAYLE 80

                ....*....
gi 4507875  304 VELIVQEKP 312
Cdd:cd05726  81 VTDVIADRP 89
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
519-579 2.09e-04

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: 41.69  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    519 SPSSIL-EEGSSVNMTC---LSQGFPAPKILWSRQLPNGELQPL------------------------SENATLTLISTK 570
Cdd:pfam07686   2 TPRSVTvAEGGSVTLPCtysSSMSEASYYIYWYRQPPGGGPEELiayysngyeegkkkgrfslrgdpsRSDFSLTIQNLT 81

                  ....*....
gi 4507875    571 MEDSGVYLC 579
Cdd:pfam07686  82 PSDSGTYFC 90
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
526-596 2.25e-04

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: 41.36  E-value: 2.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  526 EGSSVNMTCLSQGFPAPKILWSR---------QLPNGELQPLSEN--ATLTLISTKMEDSGVYLCEGINQAGRSRKEVEL 594
Cdd:cd05732  15 ELEQITLTCEAEGDPIPEITWRRatrnfsegdKSLDGRIVVRGHArvSSLTLKDVQLTDAGRYDCEASNRIGGDQQSMYL 94

                ..
gi 4507875  595 II 596
Cdd:cd05732  95 EV 96
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: ...
242-304 2.44e-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: 2.44e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507875  242 VTMTCSSEGLPAPEIFWSKKLDNGNLQH-----------LSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEV 304
Cdd:cd05734   1 VTLNCSAEGYPPPTIVWKHSKGRGHPQHthtcclagriqLLSNGSLLIKHVLEEDSGYYLCKVSNDVGADASKS 74
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: ...
530-589 2.51e-04

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: 41.06  E-value: 2.51e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507875  530 VNMTCLSQGFPAPKILWSRqlPNGELQP-----LSENATLTLISTKMEDSGVYLCEGINQAGRSR 589
Cdd:cd05876   1 LVLECIAEGLPTPEVHWDR--IDGPLSPnrtkkLNNNKTLQLDNVLESDDGEYVCTAENSEGSAR 63
Ig_NCAM-2 cd05870
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM ...
526-596 2.52e-04

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: 41.12  E-value: 2.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  526 EGSSVNMTCLSQGFPAPKILWSR-----------QLPNG--ELQPLSENATLTLISTKMEDSGVYLCEGINQAGRSRKEV 592
Cdd:cd05870  15 ENGAATLSCKAEGEPIPEITWKRasdghtfsegdKSPDGriEVKGQHGESSLHIKDVKLSDSGRYDCEAASRIGGHQKSM 94

                ....
gi 4507875  593 ELII 596
Cdd:cd05870  95 YLDI 98
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
322-384 2.93e-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: 41.12  E-value: 2.93e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507875  322 RIAAQIGDSVMLTCSVMGCESPSFSWRTQI------DSPLSGK--VRSEGTNSTLTLSPVSFENEHSYLCT 384
Cdd:cd05869  11 QTAMELEEQITLTCEASGDPIPSITWRTSTrnisseEKTLDGHivVRSHARVSSLTLKYIQYTDAGEYLCT 81
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
239-298 2.96e-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: 40.94  E-value: 2.96e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507875  239 GGSVTMTCSSEGLPAPEIFWskKLDNGNL--------QHLSGNATLTLIAMRMEDSGIYVCEGVNLIG 298
Cdd:cd05743   1 GETVEFTCVATGVPTPIINW--RLNWGHVpdsarvsiTSEGGYGTLTIRDVKESDQGAYTCEAINTRG 66
IGc2 smart00408
Immunoglobulin C-2 Type;
39-98 3.07e-04

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 40.85  E-value: 3.07e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875      39 IGDSVSLTCSTTGCESPFFSWRTQiDSPLNGKVTNEGTTSTLTMNPVSFGNEHSYLCTAT 98
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKD-GKPLPESNRFVASGSTLTIKSVSLEDSGLYTCVAE 59
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
225-308 3.52e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 316418  Cd Length: 78  Bit Score: 40.82  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    225 NTVISVNPSTkLQEGGSVTMTCSSEGLPAPEIFWSKkldNGnlQHLSGNATLTLiAMRMEDSGIYVCEGVN-LIGKNRKE 303
Cdd:pfam13895   1 KPVLTPSPTV-VTEGEPVTLTCSAPGNPPANYTWYK---GG--EALNSSPNFIS-SVSAEDSGTYTCVARNgRGGKVSNP 73

                  ....*
gi 4507875    304 VELIV 308
Cdd:pfam13895  74 VELTV 78
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
527-594 3.69e-04

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: 40.69  E-value: 3.69e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875  527 GSSVNMTCLSQGFPAPKILWSRQ---LPNGELQ-PLSENAT-LTLISTKMEDSGVYLCEGINQAGRSRKEVEL 594
Cdd:cd05730  18 GQSVTLACDADGFPEPTMTWTKDgepIESGEEKySFNEDGSeMTILDVDKLDEAEYTCIAENKAGEQEAEIHL 90
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
40-97 4.03e-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: 40.55  E-value: 4.03e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507875   40 GDSVSLTCSTTGCESPFFSWRTQ---IDSPLNGKVTNEGTTSTLTMNPVSFGNEHSYLCTA 97
Cdd:cd05743   1 GETVEFTCVATGVPTPIINWRLNwghVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEA 61
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: ...
527-600 5.15e-04

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: immunoglobulin (Ig) 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: 143212  Cd Length: 88  Bit Score: 40.40  E-value: 5.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  527 GSSVNMTCLSQGFPAPKILWSRQ--LPNGEL-------QPLSEN--ATLTLISTKMEDSGVYLCEGINQAGRSRKEVELI 595
Cdd:cd05735   1 GQKKEMSCTAHGEKPIIVRWEKEdrIINPEMsrylvstKEVGDEviSTLQILPTVREDSGFFSCHAINSYGEDRGIIQLT 80

                ....*
gi 4507875  596 IQVTP 600
Cdd:cd05735  81 VQEPP 85
Ig2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
239-299 5.21e-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: 40.20  E-value: 5.21e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507875  239 GGSVTMTCSSEGLPAPEIFWSKklDNGNL------QHLSGNATLTLIAMRMEDSGIYVCEGVNLIGK 299
Cdd:cd05856   9 GSSVRLKCVASGNPRPDITWLK--DNKPLtpteigESRKKKWTLSLKNLKPEDSGKYTCHVSNRAGE 73
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
228-308 5.41e-04

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: 40.30  E-value: 5.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  228 ISVNPSTKLqeGGSVTMTCSSEGLPAPEIFWSKK---LDNGNLQHL--SGNATLTLIAMRMEDSGIYVCEGVNLIGKNRK 302
Cdd:cd05730   9 SEVNATANL--GQSVTLACDADGFPEPTMTWTKDgepIESGEEKYSfnEDGSEMTILDVDKLDEAEYTCIAENKAGEQEA 86

                ....*.
gi 4507875  303 EVELIV 308
Cdd:cd05730  87 EIHLKV 92
Ig_Perlecan_like cd05754
Igmmunoglobulin (Ig)-like domain found in Perlecan and similar proteins; Ig_Perlecan_like: ...
515-584 5.89e-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: 5.89e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507875  515 TVLVSPSSILE--EGSSVNMTCLSQG-FPAPKILWSRQ---LPNgelQPLSENATLTLISTKMEDSGVYLCEGINQ 584
Cdd:cd05754   2 QVTVEEPRSQEvrPGADVSFICRAKSkSPAYTLVWTRVgggLPS---RAMDFNGILTIRNVQLSDAGTYVCTGSNM 74
IGc2 smart00408
Immunoglobulin C-2 Type;
615-675 7.23e-04

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 39.70  E-value: 7.23e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507875     615 EGDTVIISCTCGNVPE---TWiiLKKKAETGDTVLKSIDGAY-TIRKAQLKDAGVYECESKNKVG 675
Cdd:smart00408   1 EGQSVTLTCPAEGNPVpniTW--LKDGKPLPESNRFVASGSTlTIKSVSLEDSGLYTCVAENSAG 63
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
519-579 7.93e-04

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; IgV_TCR_alpha: immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens; they recognize proteins antigens directly and without antigen processing, and MHC independently of the bound peptide.


Pssm-ID: 319287  Cd Length: 109  Bit Score: 39.94  E-value: 7.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  519 SPSSI-LEEGSSVNMTCLSQGFPAPKILWSRQLPNGELQPLSENA----------------------TLTLISTKMEDSG 575
Cdd:cd04983   4 SPQSLsVQEGENVTLNCNYSTSTFPYLFWYRQYPGQGPEFLLYISsngeekekgrfsatldksrkssSLHITAAQLSDSA 83

                ....
gi 4507875  576 VYLC 579
Cdd:cd04983  84 VYYC 87
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) bet a chain; IgV_TCR_beta: ...
519-579 8.43e-04

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) bet a chain; IgV_TCR_beta: immunoglobulin (Ig) variable domain of the beta chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. This group includes the variable domain of the alpha chain of alpha/beta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens; they recognize proteins antigens directly and without antigen processing, and MHC independently of the bound peptide.


Pssm-ID: 143307  Cd Length: 110  Bit Score: 39.58  E-value: 8.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  519 SPSSIL-EEGSSVNMTClSQGFPAPKILWSRQLPNGELQ-------------------------PLSENATLTLISTKME 572
Cdd:cd05899   4 SPRYLIkGRGQSVTLRC-SQTSGHDNMYWYRQDPGKGLQllfysnggslneeegdpkdrfsasrPSLTRSSLTIKSAEPE 82

                ....*..
gi 4507875  573 DSGVYLC 579
Cdd:cd05899  83 DSAVYLC 89
IgV cd00099
Immunoglobulin variable domain (IgV); IgV: Immunoglobulin variable domain (IgV). Members of ...
525-579 9.14e-04

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: 39.69  E-value: 9.14e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507875  525 EEGSSVNMTC-LSQGFPAPKILWSRQLPNGELQPLSE----------------------NATLTLISTKMEDSGVYLC 579
Cdd:cd00099   4 STGESVTLNCvLSGSFSLYSISWYRQKPGKQPQFLISgsstgkpgipgrfsgtrnggssSFSLTISNLRPEDSGTYYC 81
Ig2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; ...
243-310 1.02e-03

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: 39.13  E-value: 1.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  243 TMTCSSEGLPAPEIFW-----------SKKLDngnlqhLSGNATLTLIA-MRMEDSGIYVCEGVNLIGKNRKEVELIVQE 310
Cdd:cd05736   2 SLRCHAEGIPLPRLTWlkngmditpklSKQLT------LIANGSELHISnVRYEDTGAYTCIAKNEAGVDEDISSLFVED 75
Ig_NCAM-2 cd05870
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM ...
598-685 1.03e-03

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: 39.19  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  598 VTPKDIKLTafpSESVKEGDTVIISCTCGN--VPE-TWiilkKKAETGDTVL---KSIDG-----------AYTIRKAQL 660
Cdd:cd05870   1 VQPHIIQLK---NETTVENGAATLSCKAEGepIPEiTW----KRASDGHTFSegdKSPDGrievkgqhgesSLHIKDVKL 73
                        90       100
                ....*....|....*....|....*
gi 4507875  661 KDAGVYECESKNKVGSQLRSLTLDV 685
Cdd:cd05870  74 SDSGRYDCEAASRIGGHQKSMYLDI 98
Ig2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain ...
230-308 1.11e-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: 39.30  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  230 VNPS-TKLQEGGSVTMTCSS-EGLPAPEIFWSKK----LDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKE 303
Cdd:cd05724   1 VEPSdTQVAVGEMAVLECSPpRGHPEPTVSWRKDgqplNLDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGERESA 80

                ....*.
gi 4507875  304 V-ELIV 308
Cdd:cd05724  81 AaRLSV 86
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: ...
274-312 1.13e-03

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: immunoglobulin (Ig) 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: 143212  Cd Length: 88  Bit Score: 39.24  E-value: 1.13e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 4507875  274 ATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIVQEKP 312
Cdd:cd05735  47 STLQILPTVREDSGFFSCHAINSYGEDRGIIQLTVQEPP 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
609-683 1.19e-03

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: 39.10  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875    609 PSESVKEGDTVIISCTC-GNVPETWIILKKKAETGDTVLKSIDGAY-------TIRKAQLKDAGVYECESKNKVGSQLRS 680
Cdd:pfam00047   4 PTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGrttqsslLISNVTKEDAGTYTCVVNNPGGPATLS 83

                  ...
gi 4507875    681 LTL 683
Cdd:pfam00047  84 TSL 86
Ig_1 cd05763
Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: subgroup of the immunoglobulin (Ig) ...
532-586 1.26e-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: 39.15  E-value: 1.26e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4507875  532 MTCLSQGFPAPKILWSR----QLPNGE---LQPLSENATLTLISTKMEDSGVYLCEGINQAG 586
Cdd:cd05763   3 LECAATGHPTPQIAWQKdggtDFPAARerrMHVMPEDDVFFIVDVKIEDTGVYSCTAQNTAG 64
Ig_2 cd05764
Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: subgroup of the immunoglobulin (Ig) ...
239-308 1.36e-03

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: 39.01  E-value: 1.36e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507875  239 GGSVTMTCSSEGLPAPEIFW----SKKLDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIV 308
Cdd:cd05764   1 GQRATLRCKARGDPEPAIHWispdGKLISNSSRTLVYDNGTLDILITTVKDTGSFTCIASNAAGEATATVELHI 74
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth ...
242-306 1.50e-03

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: 38.70  E-value: 1.50e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4507875  242 VTMTCSSEGLPAPEIFWSKK----LDNGNLqHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVEL 306
Cdd:cd05746   1 VQIPCSAQGDPEPTITWNKDgvqvTESGKF-HISPEGYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; ...
527-594 1.86e-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: 38.35  E-value: 1.86e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507875  527 GSSVNMTCLSQGFPAPKILWsrqLPNGelQPLS-------ENATLTLISTKMEDSGVYLCEGINQAGRSRKEVEL 594
Cdd:cd05728  14 GSSLRWECKASGNPRPAYRW---LKNG--QPLAsenrievEAGDLRITKLSLSDSGMYQCVAENKHGTIYASAEL 83
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
29-98 1.91e-03

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: 38.42  E-value: 1.91e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507875   29 TTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQI------DSPLNGK--VTNEGTTSTLTMNPVSFGNEHSYLCTAT 98
Cdd:cd05869   6 TYVENQTAMELEEQITLTCEASGDPIPSITWRTSTrnisseEKTLDGHivVRSHARVSSLTLKYIQYTDAGEYLCTAS 83
Ig_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar domains; ...
237-309 1.91e-03

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar domains; Ig_pIgR: Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar domains. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their c-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620 residue extracellular region, a 23 residue transmembrane region, and a 103 residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK Cell Receptor Nkp44 and myeloid receptors, among others.


Pssm-ID: 143193  Cd Length: 98  Bit Score: 38.58  E-value: 1.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  237 QEGGSVTMTCS-SEGLPAPEIFWSKKLDNGNLQHL---------------------SGNATLTLIAMRMEDSGIYVCeGV 294
Cdd:cd05716   5 ELGGSVTIPCPyPPKNRSYEKYWCKWGSAGCCLIIvsegsvqsqyegrvsltddpdNGVFTVTLNQLRKEDAGWYWC-GV 83
                        90
                ....*....|....*
gi 4507875  295 NLIGKNRKEVELIVQ 309
Cdd:cd05716  84 GDDGDQGLTLSVTLV 98
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: ...
242-301 2.85e-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: 37.98  E-value: 2.85e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875  242 VTMTCSSEGLPAPEIFW---SKKLDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNR 301
Cdd:cd05876   1 LVLECIAEGLPTPEVHWdriDGPLSPNRTKKLNNNKTLQLDNVLESDDGEYVCTAENSEGSAR 63
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: ...
239-295 2.91e-03

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: 37.94  E-value: 2.91e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875  239 GGSVTMTCSSEGLPAPEIFWS------KKLDNGNLQHLSGNAtLTLIAMRMEDSGIYVCEGVN 295
Cdd:cd05867   1 GETARLDCQVEGIPTPNITWSingapiEGTDPDPRRHVSSGA-LILTDVQPSDTAVYQCEARN 62
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; Ig5_Contactin-1: fifth Ig domain of the ...
239-299 3.96e-03

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: 37.31  E-value: 3.96e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507875  239 GGSVTMTCSSEGLPAPEIFWSKK---LDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGK 299
Cdd:cd05852   1 GGRVIIECKPKAAPKPKFSWSKGtelLVNNSRISIWDDGSLEILNITKLDEGSYTCFAENNRGK 64
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
227-291 4.20e-03

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; IgV_TCR_alpha: immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens; they recognize proteins antigens directly and without antigen processing, and MHC independently of the bound peptide.


Pssm-ID: 319287  Cd Length: 109  Bit Score: 37.63  E-value: 4.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  227 VISVNPSTKLQEGGSVTMTCSSEGLPAPEIFWSKKLDNGNLQHL----------------------SGNATLTLIAMRME 284
Cdd:cd04983   1 VTQSPQSLSVQEGENVTLNCNYSTSTFPYLFWYRQYPGQGPEFLlyissngeekekgrfsatldksRKSSSLHITAAQLS 80

                ....*..
gi 4507875  285 DSGIYVC 291
Cdd:cd04983  81 DSAVYYC 87
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; IgV_TCR_delta: ...
227-291 4.31e-03

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; IgV_TCR_delta: immunoglobulin (Ig) variable (V) domain of the delta chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor.


Pssm-ID: 319330  Cd Length: 112  Bit Score: 37.48  E-value: 4.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507875  227 VISVNPSTKLQEGGSVTMTCSSE-GLPAPEIFWSKKLDNGNLQHL------SGNAT----------------LTLIAMRM 283
Cdd:cd07706   2 VTQAQPDVSVQVGEEVTLNCRYEtSWTNYYLFWYKQLPSGEMTFLirqdssRSNATsgrysvnfqkaqksisLTISALQL 81

                ....*...
gi 4507875  284 EDSGIYVC 291
Cdd:cd07706  82 EDSAKYFC 89
Ig2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; ...
531-597 4.33e-03

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: 37.21  E-value: 4.33e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507875  531 NMTCLSQGFPAPKILWsrqLPNGELQPLSENATLTLI---------STKMEDSGVYLCEGINQAGRSRKEVELIIQ 597
Cdd:cd05736   2 SLRCHAEGIPLPRLTW---LKNGMDITPKLSKQLTLIangselhisNVRYEDTGAYTCIAKNEAGVDEDISSLFVE 74
Ig4_PDGFR cd05859
Fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR); ...
537-598 4.40e-03

Fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR); IG4_PDGFR: The fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR) alpha and beta. PDGF is a potent mitogen for connective tissue cells. PDGF-stimulated processes are mediated by three different PDGFs (PDGF-A,-B, and C). PDGFR alpha binds to all three PDGFs, whereas the PDGFR beta binds only to PDGF-B. PDGF alpha is organized as an extracellular component having five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. In mice, PDGFR alpha and PDGFR beta are essential for normal development.


Pssm-ID: 143267  Cd Length: 101  Bit Score: 37.54  E-value: 4.40e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4507875  537 QGFPAPKILWsrqLPNGelQPLSENAT-----------------LTLISTKMEDSGVYLCEGINQAGRSRKEVELIIQV 598
Cdd:cd05859  28 EAYPPPQIRW---LKDN--RTLIENLTeittsehnvqetryvskLKLIRAKEEDSGLYTALAQNEDAVKSYTFALQIQV 101
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
328-384 4.68e-03

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: 37.12  E-value: 4.68e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507875  328 GDSVMLTCSVMGCESPSFSWRTQI------DSPLSGK--VRSEGTNSTLTLSPVSFENEHSYLCT 384
Cdd:cd05732  16 LEQITLTCEAEGDPIPEITWRRATrnfsegDKSLDGRivVRGHARVSSLTLKDVQLTDAGRYDCE 80
Ig_1 cd05763
Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: subgroup of the immunoglobulin (Ig) ...
244-298 4.93e-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: 4.93e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507875  244 MTCSSEGLPAPEIFWSKklDNGN---------LQHLSGNATLTLIAMRMEDSGIYVCEGVNLIG 298
Cdd:cd05763   3 LECAATGHPTPQIAWQK--DGGTdfpaarerrMHVMPEDDVFFIVDVKIEDTGVYSCTAQNTAG 64
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
327-389 5.16e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 316418  Cd Length: 78  Bit Score: 36.96  E-value: 5.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875    327 IGDSVMLTCSVMGCESPSFSWRTQidsplsGKVRSEGTNSTLTLSPvsfENEHSYLCTVTCGH 389
Cdd:pfam13895  13 EGEPVTLTCSAPGNPPANYTWYKG------GEALNSSPNFISSVSA---EDSGTYTCVARNGR 66
IgC_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; IgC_Tapasin_R: Immunoglobulin-like domain on Tapasin-R. ...
368-434 5.77e-03

Tapasin-R immunoglobulin-like domain; IgC_Tapasin_R: Immunoglobulin-like domain on Tapasin-R. Tapasin is a V-C1 (variable-constant) immunoglobulin superfamily molecule present in the endoplasmic reticulum (ER), where it links MHC class I molecules to the transporter associated with antigen processing (TAP). Tapasin-R is a tapasin-related protein that contains similar structural motifs to Tapasin, with some marked differences, especially in the V domain, transmembrane and cytoplasmic regions. The majority of Tapasin-R is located within the ER; however, there may be some expression of Tapasin-R at the cell surface. Tapasin-R lacks an obvious ER retention signal.


Pssm-ID: 319313  Cd Length: 138  Bit Score: 37.50  E-value: 5.77e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507875  368 LTLSPVSFENEHSYLCTVTCGHKKLEKGIQVELYSFPRDpEIEMSGGLVNGSSVTVSCKVPSVYPLD 434
Cdd:cd05771   3 LTLPGLTVLDEGTYICSVSTPPFQAQQIIQLSVSEPPRV-RLSLEKTVSIEEPQTLICHIAGYYPLD 68
Ig_Perlecan_like cd05754
Igmmunoglobulin (Ig)-like domain found in Perlecan and similar proteins; Ig_Perlecan_like: ...
228-295 5.96e-03

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: 36.76  E-value: 5.96e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875  228 ISVNPSTK--LQEGGSVTMTCSSEG-LPAPEIFWSKKldNGNL--QHLSGNATLTLIAMRMEDSGIYVCEGVN 295
Cdd:cd05754   3 VTVEEPRSqeVRPGADVSFICRAKSkSPAYTLVWTRV--GGGLpsRAMDFNGILTIRNVQLSDAGTYVCTGSN 73
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: ...
530-586 8.02e-03

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: 36.45  E-value: 8.02e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4507875  530 VNMTCLSQGFPAPKILWS--------RQLP----NGELQPLSeNATLTLISTKMEDSGVYLCEGINQAG 586
Cdd:cd05734   1 VTLNCSAEGYPPPTIVWKhskgrghpQHTHtcclAGRIQLLS-NGSLLIKHVLEEDSGYYLCKVSNDVG 68
Ig_Perlecan_like cd05754
Igmmunoglobulin (Ig)-like domain found in Perlecan and similar proteins; Ig_Perlecan_like: ...
603-672 8.28e-03

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: 36.37  E-value: 8.28e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507875  603 IKLTAFPSES--VKEGDTVIISCTC-GNVPETWIILKKKAETGDTVLKSIDGAYTIRKAQLKDAGVYECESKN 672
Cdd:cd05754   1 IQVTVEEPRSqeVRPGADVSFICRAkSKSPAYTLVWTRVGGGLPSRAMDFNGILTIRNVQLSDAGTYVCTGSN 73
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; Ig6_Contactin_like: Sixth Ig domain of ...
651-687 8.70e-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: 36.38  E-value: 8.70e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 4507875  651 GAYTIRKAQLKDAGVYECESKNKVGSQLRSLTLDVQG 687
Cdd:cd04970  47 GDLEIVNAQLKHAGRYTCTAQTVVDSDSASATLVVRG 83
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
234-309 9.32e-03

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan; Ig_Aggrecan: immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggrecan has a wide distribution in connective tissue and extracellular matrices. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 143308  Cd Length: 112  Bit Score: 36.46  E-value: 9.32e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507875  234 TKLQEGGSVTMTCSSEGLPAPEIFWSKKLDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEVELIVQ 309
Cdd:cd05900  34 SFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAIPSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVK 109
 
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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