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Conserved domains on  [gi|22474511|dbj|BAC10616|]
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projectin-like protein [Bombyx mori]

Protein Classification

Ig and FN3 domain-containing protein (domain architecture ID 11510743)

protein containing domains Ig, I-set, and FN3

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
I-set pfam07679
Immunoglobulin I-set domain;
164-251 1.44e-18

Immunoglobulin I-set domain;


:

Pssm-ID: 336764  Cd Length: 90  Bit Score: 81.14  E-value: 1.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511    164 PVFIKRLEDVTALENDKVEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATNRGG 243
Cdd:pfam07679    1 PKFTQKPKDVEVSEGESARFTCTVTGDPDPEVSWFKDGSPLRSSSRFRVTYEGGTYTLTISNVQIDDSGKYTCVATNSAG 80

                   ....*...
gi 22474511    244 HAVTKARL 251
Cdd:pfam07679   81 EAEASAEL 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
353-441 1.98e-17

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 78.31  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  353 PDPPRNVSVTRQVDKSVTLDWEPPADDGGcKVGNYIVEYYRTGWNVWLKAIT--SRKTNVTLFDLIEGSEYKFRIKAESP 430
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                         90
                 ....*....|.
gi 22474511  431 YGMSAPSSESS 441
Cdd:cd00063   80 GGESPPSESVT 90
I-set pfam07679
Immunoglobulin I-set domain;
275-349 4.26e-17

Immunoglobulin I-set domain;


:

Pssm-ID: 336764  Cd Length: 90  Bit Score: 76.90  E-value: 4.26e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22474511    275 ETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:pfam07679   16 ESARFTCTVTGDPDPEVSWFKDGSPLRSSSRFRVTYEGGTYTLTISNVQIDDSGKYTCVATNSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
56-153 3.23e-16

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 74.84  E-value: 3.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511   56 PAPPGKPQIipilSDDEPNAITLKWAPATHDGGaPLRGYQVECNRLGSTEWIRTAPPIVLRPELVLTGLEPPHKYQFRVA 135
Cdd:cd00063    1 PSPPTNLRV----TDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVR 75
                         90
                 ....*....|....*...
gi 22474511  136 ALNDVGHSNYSELSDVLT 153
Cdd:cd00063   76 AVNGGGESPPSESVTVTT 93
 
Name Accession Description Interval E-value
I-set pfam07679
Immunoglobulin I-set domain;
164-251 1.44e-18

Immunoglobulin I-set domain;


Pssm-ID: 336764  Cd Length: 90  Bit Score: 81.14  E-value: 1.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511    164 PVFIKRLEDVTALENDKVEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATNRGG 243
Cdd:pfam07679    1 PKFTQKPKDVEVSEGESARFTCTVTGDPDPEVSWFKDGSPLRSSSRFRVTYEGGTYTLTISNVQIDDSGKYTCVATNSAG 80

                   ....*...
gi 22474511    244 HAVTKARL 251
Cdd:pfam07679   81 EAEASAEL 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
353-441 1.98e-17

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 78.31  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  353 PDPPRNVSVTRQVDKSVTLDWEPPADDGGcKVGNYIVEYYRTGWNVWLKAIT--SRKTNVTLFDLIEGSEYKFRIKAESP 430
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                         90
                 ....*....|.
gi 22474511  431 YGMSAPSSESS 441
Cdd:cd00063   80 GGESPPSESVT 90
I-set pfam07679
Immunoglobulin I-set domain;
275-349 4.26e-17

Immunoglobulin I-set domain;


Pssm-ID: 336764  Cd Length: 90  Bit Score: 76.90  E-value: 4.26e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22474511    275 ETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:pfam07679   16 ESARFTCTVTGDPDPEVSWFKDGSPLRSSSRFRVTYEGGTYTLTISNVQIDDSGKYTCVATNSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
56-153 3.23e-16

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 74.84  E-value: 3.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511   56 PAPPGKPQIipilSDDEPNAITLKWAPATHDGGaPLRGYQVECNRLGSTEWIRTAPPIVLRPELVLTGLEPPHKYQFRVA 135
Cdd:cd00063    1 PSPPTNLRV----TDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVR 75
                         90
                 ....*....|....*...
gi 22474511  136 ALNDVGHSNYSELSDVLT 153
Cdd:cd00063   76 AVNGGGESPPSESVTVTT 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin ...
283-349 1.30e-15

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


Pssm-ID: 319305  Cd Length: 74  Bit Score: 72.25  E-value: 1.30e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22474511  283 IVGKPTPTIEWRHDGHPIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05748    8 ISGRPTPTVTWSKDGQPLKLSGRVQIETTATSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATVNVKV 74
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
353-434 2.32e-15

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.88  E-value: 2.32e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511     353 PDPPRNVSVTRQVDKSVTLDWEPPADDGGckvGNYIVEY---YRTGWNVWLKAITS-RKTNVTLFDLIEGSEYKFRIKAE 428
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI---TGYIVGYrveYREEGSEWKEVNVTpSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 22474511     429 SPYGMS 434
Cdd:smart00060   78 NGAGEG 83
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
181-250 1.12e-11

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: 61.10  E-value: 1.12e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  181 VEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATNRGGHAVTKAR 250
Cdd:cd00096    1 VTLTCSASGNPPPTITWLKNGKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
IG smart00409
Immunoglobulin;
171-251 1.62e-11

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 60.98  E-value: 1.62e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511     171 EDVTALENDKVEFHVTFSGIPSPTIAWFKDDYE-IFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATNRGGHAVTKA 249
Cdd:smart00409    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ..
gi 22474511     250 RL 251
Cdd:smart00409   82 TL 83
IG smart00409
Immunoglobulin;
275-349 1.48e-10

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 58.29  E-value: 1.48e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22474511     275 ETIFLKTTIVGKPTPTIEWRHDGH-PIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:smart00409   10 ESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
56-143 3.59e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 57.24  E-value: 3.59e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511      56 PAPPGKPQIIPIlsddEPNAITLKWAPATHDGG-APLRGYQVEcNRLGSTEWIRTaPPIVLRPELVLTGLEPPHKYQFRV 134
Cdd:smart00060    1 PSPPSNLRVTDV----TSTSVTLSWEPPPDDGItGYIVGYRVE-YREEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRV 74

                    ....*....
gi 22474511     135 AALNDVGHS 143
Cdd:smart00060   75 RAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
354-436 5.19e-10

Fibronectin type III domain;


Pssm-ID: 333790  Cd Length: 84  Bit Score: 56.65  E-value: 5.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511    354 DPPRNVSVTRQVDKSVTLDWEPPADDGGcKVGNYIVEYYRTGWNVWLKAIT--SRKTNVTLFDLIEGSEYKFRIKAESPY 431
Cdd:pfam00041    1 SAPTNLSVTDVTSTSLTVSWTPPPDGNG-PITGYRVEYRPVNGGEPWNEITvpGTTTSVTLTGLRPGTEYEVRVQAVNGG 79

                   ....*
gi 22474511    432 GMSAP 436
Cdd:pfam00041   80 GEGPP 84
fn3 pfam00041
Fibronectin type III domain;
58-143 8.25e-08

Fibronectin type III domain;


Pssm-ID: 333790  Cd Length: 84  Bit Score: 50.48  E-value: 8.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511     58 PPGKPQIIPIlsddEPNAITLKWAPAThDGGAPLRGYQVECNRLGSTE---WIRTAPPivlRPELVLTGLEPPHKYQFRV 134
Cdd:pfam00041    2 APTNLSVTDV----TSTSLTVSWTPPP-DGNGPITGYRVEYRPVNGGEpwnEITVPGT---TTSVTLTGLRPGTEYEVRV 73

                   ....*....
gi 22474511    135 AALNDVGHS 143
Cdd:pfam00041   74 QAVNGGGEG 82
 
Name Accession Description Interval E-value
I-set pfam07679
Immunoglobulin I-set domain;
164-251 1.44e-18

Immunoglobulin I-set domain;


Pssm-ID: 336764  Cd Length: 90  Bit Score: 81.14  E-value: 1.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511    164 PVFIKRLEDVTALENDKVEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATNRGG 243
Cdd:pfam07679    1 PKFTQKPKDVEVSEGESARFTCTVTGDPDPEVSWFKDGSPLRSSSRFRVTYEGGTYTLTISNVQIDDSGKYTCVATNSAG 80

                   ....*...
gi 22474511    244 HAVTKARL 251
Cdd:pfam07679   81 EAEASAEL 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
353-441 1.98e-17

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 78.31  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  353 PDPPRNVSVTRQVDKSVTLDWEPPADDGGcKVGNYIVEYYRTGWNVWLKAIT--SRKTNVTLFDLIEGSEYKFRIKAESP 430
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNG 79
                         90
                 ....*....|.
gi 22474511  431 YGMSAPSSESS 441
Cdd:cd00063   80 GGESPPSESVT 90
I-set pfam07679
Immunoglobulin I-set domain;
275-349 4.26e-17

Immunoglobulin I-set domain;


Pssm-ID: 336764  Cd Length: 90  Bit Score: 76.90  E-value: 4.26e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22474511    275 ETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:pfam07679   16 ESARFTCTVTGDPDPEVSWFKDGSPLRSSSRFRVTYEGGTYTLTISNVQIDDSGKYTCVATNSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
56-153 3.23e-16

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 74.84  E-value: 3.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511   56 PAPPGKPQIipilSDDEPNAITLKWAPATHDGGaPLRGYQVECNRLGSTEWIRTAPPIVLRPELVLTGLEPPHKYQFRVA 135
Cdd:cd00063    1 PSPPTNLRV----TDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVR 75
                         90
                 ....*....|....*...
gi 22474511  136 ALNDVGHSNYSELSDVLT 153
Cdd:cd00063   76 AVNGGGESPPSESVTVTT 93
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin ...
283-349 1.30e-15

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


Pssm-ID: 319305  Cd Length: 74  Bit Score: 72.25  E-value: 1.30e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22474511  283 IVGKPTPTIEWRHDGHPIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05748    8 ISGRPTPTVTWSKDGQPLKLSGRVQIETTATSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATVNVKV 74
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
353-434 2.32e-15

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.88  E-value: 2.32e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511     353 PDPPRNVSVTRQVDKSVTLDWEPPADDGGckvGNYIVEY---YRTGWNVWLKAITS-RKTNVTLFDLIEGSEYKFRIKAE 428
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI---TGYIVGYrveYREEGSEWKEVNVTpSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 22474511     429 SPYGMS 434
Cdd:smart00060   78 NGAGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
163-240 2.61e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 339005  Cd Length: 79  Bit Score: 62.93  E-value: 2.61e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22474511    163 PPVFIKRLEDVTALENDKVEFHVTFSGIPSPTIAWFKDDYEIFSSR-RTAITTDESTSVLLFHQILPSDEGEIKCTATN 240
Cdd:pfam13927    1 KPVITVSPSSVVVVEGESVTLTCEATGGPPPTITWYKNGEEISSGStSARISVSGSNSTLTISNVTREDSGTYTCVASN 79
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
181-250 1.12e-11

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: 61.10  E-value: 1.12e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  181 VEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATNRGGHAVTKAR 250
Cdd:cd00096    1 VTLTCSASGNPPPTITWLKNGKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
282-345 1.36e-11

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: 60.72  E-value: 1.36e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22474511  282 TIVGKPTPTIEWRHDGHPIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAF 345
Cdd:cd00096    6 SASGNPPPTITWLKNGKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASV 69
IG smart00409
Immunoglobulin;
171-251 1.62e-11

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 60.98  E-value: 1.62e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511     171 EDVTALENDKVEFHVTFSGIPSPTIAWFKDDYE-IFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATNRGGHAVTKA 249
Cdd:smart00409    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ..
gi 22474511     250 RL 251
Cdd:smart00409   82 TL 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
171-251 1.62e-11

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 60.98  E-value: 1.62e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511     171 EDVTALENDKVEFHVTFSGIPSPTIAWFKDDYE-IFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATNRGGHAVTKA 249
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ..
gi 22474511     250 RL 251
Cdd:smart00410   82 TL 83
IG smart00409
Immunoglobulin;
275-349 1.48e-10

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 58.29  E-value: 1.48e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22474511     275 ETIFLKTTIVGKPTPTIEWRHDGH-PIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:smart00409   10 ESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
275-349 1.48e-10

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 58.29  E-value: 1.48e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22474511     275 ETIFLKTTIVGKPTPTIEWRHDGH-PIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:smart00410   10 ESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
56-143 3.59e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 57.24  E-value: 3.59e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511      56 PAPPGKPQIIPIlsddEPNAITLKWAPATHDGG-APLRGYQVEcNRLGSTEWIRTaPPIVLRPELVLTGLEPPHKYQFRV 134
Cdd:smart00060    1 PSPPSNLRVTDV----TSTSVTLSWEPPPDDGItGYIVGYRVE-YREEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRV 74

                    ....*....
gi 22474511     135 AALNDVGHS 143
Cdd:smart00060   75 RAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
354-436 5.19e-10

Fibronectin type III domain;


Pssm-ID: 333790  Cd Length: 84  Bit Score: 56.65  E-value: 5.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511    354 DPPRNVSVTRQVDKSVTLDWEPPADDGGcKVGNYIVEYYRTGWNVWLKAIT--SRKTNVTLFDLIEGSEYKFRIKAESPY 431
Cdd:pfam00041    1 SAPTNLSVTDVTSTSLTVSWTPPPDGNG-PITGYRVEYRPVNGGEPWNEITvpGTTTSVTLTGLRPGTEYEVRVQAVNGG 79

                   ....*
gi 22474511    432 GMSAP 436
Cdd:pfam00041   80 GEGPP 84
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); Ig_C5_MyBP_C: the ...
279-349 2.94e-09

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


Pssm-ID: 143302  Cd Length: 86  Bit Score: 54.85  E-value: 2.94e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22474511  279 LKTTIVGKPTPTIEWRHDGHPII-TDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05894   15 LDVPISGEPAPTVTWSRGDKAFTeTEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
272-336 1.31e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 339005  Cd Length: 79  Bit Score: 52.53  E-value: 1.31e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22474511    272 EINETIFLKTTIVGKPTPTIEWRHDGHPIIT-DDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKN 336
Cdd:pfam13927   14 VEGESVTLTCEATGGPPPTITWYKNGEEISSgSTSARISVSGSNSTLTISNVTREDSGTYTCVASN 79
IGc2 smart00408
Immunoglobulin C-2 Type;
273-339 7.64e-08

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 49.71  E-value: 7.64e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22474511     273 INETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISItpkfSVLKIHSAKRSDRGEYQIQAKNIIG 339
Cdd:smart00408    1 EGQSVTLTCPAEGNPVPNITWLKDGKPLPESNRFVASG----STLTIKSVSLEDSGLYTCVAENSAG 63
fn3 pfam00041
Fibronectin type III domain;
58-143 8.25e-08

Fibronectin type III domain;


Pssm-ID: 333790  Cd Length: 84  Bit Score: 50.48  E-value: 8.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511     58 PPGKPQIIPIlsddEPNAITLKWAPAThDGGAPLRGYQVECNRLGSTE---WIRTAPPivlRPELVLTGLEPPHKYQFRV 134
Cdd:pfam00041    2 APTNLSVTDV----TSTSLTVSWTPPP-DGNGPITGYRVEYRPVNGGEpwnEITVPGT---TTSVTLTGLRPGTEYEVRV 73

                   ....*....
gi 22474511    135 AALNDVGHS 143
Cdd:pfam00041   74 QAVNGGGEG 82
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
275-348 1.94e-07

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: 49.66  E-value: 1.94e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22474511  275 ETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVT 348
Cdd:cd05747   19 ESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFTLT 92
Ig2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain ...
284-346 2.59e-07

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: 49.32  E-value: 2.59e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22474511  284 VGKPTPTIEWRHDGHPIITDD-RIEISITPKfsvLKIHSAKRSDRGEYQIQAKNIIG--EDTAAFL 346
Cdd:cd05724   22 RGHPEPTVSWRKDGQPLNLDNeRVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGerESAAARL 84
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
181-251 9.03e-07

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: 47.02  E-value: 9.03e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22474511  181 VEFHVTFSGIPSPTIAWFKDDYEIfSSRRTAITTDEStsvLLFHQILPSDEGEIKCTATNRGGHAVTKARL 251
Cdd:cd05725    1 VEFQCEVGGDPVPTVLWRKEDGEL-PKGRAEILDDKS---LKIRNVTAGDEGSYTCEAENMVGKIEASASL 67
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin ...
180-243 3.95e-06

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


Pssm-ID: 319305  Cd Length: 74  Bit Score: 45.29  E-value: 3.95e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22474511  180 KVEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATNRGG 243
Cdd:cd05748    1 SVRLEVPISGRPTPTVTWSKDGQPLKLSGRVQIETTATSTSLVIKNAKRSDSGKYTLTLKNSAG 64
Ig2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain ...
189-251 5.57e-06

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: 45.46  E-value: 5.57e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22474511  189 GIPSPTIAWFKDDYEI-FSSRRTAITTDEStsvLLFHQILPSDEGEIKCTATNRGGHAVTK-ARL 251
Cdd:cd05724   23 GHPEPTVSWRKDGQPLnLDNERVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGERESAaARL 84
Ig4_Neogenin cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth ...
277-344 8.27e-06

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


Pssm-ID: 212460  Cd Length: 71  Bit Score: 44.57  E-value: 8.27e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22474511  277 IFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISITPKFSVLKIhsaKRSDRGEYQIQAKNIIGEDTAA 344
Cdd:cd05723    2 IVFECEVTGKPTPTVKWVKNGDMVIPSDYFKIVKEHNLQVLGL---VKSDEGFYQCIAENDVGNVQAG 66
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
163-243 1.41e-05

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


Pssm-ID: 143224  Cd Length: 92  Bit Score: 44.27  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  163 PPVFIKRLEDVTALENDKVEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATNRG 242
Cdd:cd05747    3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSE 82

                 .
gi 22474511  243 G 243
Cdd:cd05747   83 G 83
Ig1_Robo cd07693
First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; ...
285-342 1.68e-05

First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; Ig1_Robo: domain similar to the first immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 143317  Cd Length: 100  Bit Score: 44.46  E-value: 1.68e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22474511  285 GKPTPTIEWRHDGHPIITDD------RIEISITPKFSVLKIHSAKR-SDRGEYQIQAKNIIGEDT 342
Cdd:cd07693   27 GRPTPTIQWLKNGQPLETDKddprshRIVLPSGSLFFLRVVHGRKGrSDEGVYVCVAHNSLGEAV 91
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
275-354 2.12e-05

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: 43.63  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  275 ETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGedtaaflvTVTAPPD 354
Cdd:cd05743    2 ETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRG--------MVFGIPD 73
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
273-342 4.36e-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: 43.09  E-value: 4.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  273 INETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISitpkFSVLKIHSAKRSDRGEYQIQAKNIIGEDT 342
Cdd:cd05851   15 KGQNVTLECFALGNPVPVIRWRKILEPMPATAEISMS----GAVLKIFNIQPEDEGTYECEAENIKGKDK 80
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7, also known as CCK4; ...
277-340 5.55e-05

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


Pssm-ID: 143237  Cd Length: 77  Bit Score: 42.21  E-value: 5.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22474511  277 IFLKTTIVGKPTPTIEWRHDGHPiITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGE 340
Cdd:cd05760    1 VTLRCHIDGHPRPTYQWFRDGTP-LSDGQGNYSVSSKERTLTLRSAGPDDSGLYYCCAHNAFGS 63
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig) ...
282-343 6.14e-05

Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules, which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG1, -2, -3, and -4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions; for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors; in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms, which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and -3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 143227  Cd Length: 75  Bit Score: 42.13  E-value: 6.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22474511  282 TIVGKPTPTIEWRHDGHPIITDDRIEISI---TPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTA 343
Cdd:cd05750    7 ATSEYPSLRFKWFKDGKELNRKNKPRNIKirnKKKNSELQINKAKLADSGEYTCVVENILGNDTV 71
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
255-349 6.40e-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: 42.66  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  255 AAPKLRYprqYEDGLLYEINETIFLKTTIVGKPTPTIEWRHDGHPIIT-----DDRIEISITPKFSVLKIHSAKRSDRGE 329
Cdd:cd05869    1 AKPKITY---VENQTAMELEEQITLTCEASGDPIPSITWRTSTRNISSeektlDGHIVVRSHARVSSLTLKYIQYTDAGE 77
                         90       100
                 ....*....|....*....|
gi 22474511  330 YQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05869   78 YLCTASNTIGQDSQSMYLEV 97
Ig4_Neogenin cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth ...
181-253 6.75e-05

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


Pssm-ID: 212460  Cd Length: 71  Bit Score: 41.87  E-value: 6.75e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22474511  181 VEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAITTDESTSVLlfhQILPSDEGEIKCTATNRGGHAVTKARLCL 253
Cdd:cd05723    2 IVFECEVTGKPTPTVKWVKNGDMVIPSDYFKIVKEHNLQVL---GLVKSDEGFYQCIAENDVGNVQAGAQLII 71
Ig1_Robo cd07693
First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; ...
163-255 7.02e-05

First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; Ig1_Robo: domain similar to the first immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 143317  Cd Length: 100  Bit Score: 42.53  E-value: 7.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  163 PPVFIKRLEDVTALENDKVEFHVTFSGIPSPTIAWFKDDYEI---FSSRRTAITTDESTSvLLFHQILP-----SDEGEI 234
Cdd:cd07693    1 PPRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLetdKDDPRSHRIVLPSGS-LFFLRVVHgrkgrSDEGVY 79
                         90       100
                 ....*....|....*....|.
gi 22474511  235 KCTATNRGGHAVTKARLCLEA 255
Cdd:cd07693   80 VCVAHNSLGEAVSRNASLEVA 100
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
263-351 7.02e-05

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: 42.61  E-value: 7.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  263 RQYEDGLLYEINETIFLKTTIVGKPTPTIEWRHDGHPIITDDRiEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDT 342
Cdd:cd05730    7 RQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQE 85

                 ....*....
gi 22474511  343 AAFLVTVTA 351
Cdd:cd05730   86 AEIHLKVFA 94
IGc2 smart00408
Immunoglobulin C-2 Type;
177-243 8.25e-05

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 41.24  E-value: 8.25e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22474511     177 ENDKVEFHVTFSGIPSPTIAWFKDDYEIFSSRRtaitTDESTSVLLFHQILPSDEGEIKCTATNRGG 243
Cdd:smart00408    1 EGQSVTLTCPAEGNPVPNITWLKDGKPLPESNR----FVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth ...
285-348 8.28e-05

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: 41.40  E-value: 8.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22474511  285 GKPTPTIEWRHDGhpiitddrIEISITPKFSV-----LKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVT 348
Cdd:cd05746    9 GDPEPTITWNKDG--------VQVTESGKFHIspegyLAIRDVGVADQGRYECVARNTIGYASVSMVLS 69
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; ...
272-336 1.39e-04

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: 41.43  E-value: 1.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22474511  272 EINETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISI-TPKFSVLKIhsakrSDRGEYQIQAKN 336
Cdd:cd05728   12 DIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAgDLRITKLSL-----SDSGMYQCVAEN 72
Ig2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar ...
274-349 1.56e-04

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


Pssm-ID: 319297  Cd Length: 85  Bit Score: 41.43  E-value: 1.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22474511  274 NETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEIS-ITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05729    9 NTKVRLECGARGNPTPNITWLKDGKQKWKINVIRPTrVEEKGWVLIIRRAIPRDTGKYTCIVSNQYGTINHTYDVKV 85
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
167-244 1.91e-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: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  167 IKRLEDVTALENDKVEFHVTFSGIPSPTIAWfKDDYEIFSSR------RTAITTDESTSVLLFHQILPSDEGEIKCTATN 240
Cdd:cd05732    5 ITYLENQTAVELEQITLTCEAEGDPIPEITW-RRATRNFSEGdksldgRIVVRGHARVSSLTLKDVQLTDAGRYDCEASN 83

                 ....*
gi 22474511  241 R-GGH 244
Cdd:cd05732   84 RiGGD 88
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
177-251 2.68e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death, and protection of the organism against non-self.


Pssm-ID: 143222  Cd Length: 74  Bit Score: 40.31  E-value: 2.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22474511  177 ENDKVEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAITtdeSTSVLLFHQILPSDEGEIKCTATNRGGHAVTKARL 251
Cdd:cd05745    1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVL---SSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQL 72
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
181-247 3.30e-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: 40.17  E-value: 3.30e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22474511  181 VEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATN-RGGHAVT 247
Cdd:cd05743    4 VEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINtRGMVFGI 71
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth Ig domain of ...
285-339 3.60e-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: 39.74  E-value: 3.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22474511  285 GKPTPTIEWRHDGHPIITDDRIeiSITPKFSvLKIHSAKRSDRGEYQIQAKNIIG 339
Cdd:cd04969   12 ASPKPTISWSKGTELLTNSSRI--CILPDGS-LKIKNVSKSDEGKYTCFAVNFFG 63
Ig_1 cd05763
Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: subgroup of the immunoglobulin (Ig) ...
189-251 3.62e-04

Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 143240  Cd Length: 75  Bit Score: 39.92  E-value: 3.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22474511  189 GIPSPTIAWFKD---DYEIFSSRRTAITTDEstSVLLFHQILPSDEGEIKCTATNRGGHAVTKARL 251
Cdd:cd05763    9 GHPTPQIAWQKDggtDFPAARERRMHVMPED--DVFFIVDVKIEDTGVYSCTAQNTAGSISANATL 72
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
274-349 3.97e-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: 40.59  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  274 NETIFLKTTIVGKPTPTIEWRHDGHPIIT-----DDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVT 348
Cdd:cd05732   16 LEQITLTCEAEGDPIPEITWRRATRNFSEgdkslDGRIVVRGHARVSSLTLKDVQLTDAGRYDCEASNRIGGDQQSMYLE 95

                 .
gi 22474511  349 V 349
Cdd:cd05732   96 V 96
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
173-251 4.63e-04

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


Pssm-ID: 333796  Cd Length: 86  Bit Score: 39.86  E-value: 4.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511    173 VTALENDKVEF--HVTFsGIPSPTIAWFKDD-YEIFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTATNRGGHAVTKA 249
Cdd:pfam00047    6 VTVLEGESATLtcSAST-GSPLPDVTWSKEGgTLIESLRVGHDNGRTTQSSLLISNVTLEDAGTYTCVVNNPGGPATLST 84

                   ..
gi 22474511    250 RL 251
Cdd:pfam00047   85 SL 86
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
163-254 5.28e-04

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: 40.00  E-value: 5.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  163 PPVFIKRLEDVTALENDKVEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAIttdeSTSVLLFHQILPSDEGEIKCTATNRG 242
Cdd:cd05851    1 PADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKILEPMPATAEISM----SGAVLKIFNIQPEDEGTYECEAENIK 76
                         90
                 ....*....|..
gi 22474511  243 GHAVTKARLCLE 254
Cdd:cd05851   77 GKDKHQARVYVQ 88
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
285-349 5.45e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: domain similar to the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 319298  Cd Length: 71  Bit Score: 39.34  E-value: 5.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22474511  285 GKPTPTIEWRHDGHPIITDdrieisiTPKF----SVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05731    9 GLPTPDIRWIKLGGELPKG-------RTKFenfnKTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 70
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: ...
279-356 5.62e-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: 39.63  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  279 LKTTIVGKPTPTIEWRHDGHpIITDDRIEISITPK------FSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTVTAP 352
Cdd:cd05735    6 MSCTAHGEKPIIVRWEKEDR-IINPEMSRYLVSTKevgdevISTLQILPTVREDSGFFSCHAINSYGEDRGIIQLTVQEP 84

                 ....
gi 22474511  353 PDPP 356
Cdd:cd05735   85 PDPP 88
Ig2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; ...
279-347 8.15e-04

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: 8.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22474511  279 LKTTIVGKPTPTIEWRHDGHPIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIG--EDTAAFLV 347
Cdd:cd05736    3 LRCHAEGIPLPRLTWLKNGMDITPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEAGvdEDISSLFV 73
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
285-349 8.78e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death, and protection of the organism against non-self.


Pssm-ID: 143222  Cd Length: 74  Bit Score: 38.77  E-value: 8.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22474511  285 GKPTPTIEWRHDGHPIITDDRIEISITpkfSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05745   13 GYPQPVIAWTKGGSQLSVDRRHLVLSS---GTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of ...
275-343 9.31e-04

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: 39.07  E-value: 9.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  275 ETIFLKTTIVGKPTPTIEWRH-DGHPIITDDRIEISitpkfSVLKIHSAKRSDRGEYQIQAKNIIGEDTA 343
Cdd:cd04968   17 QTVTLECFALGNPVPQIKWRKvDGSPSSQWTTSTSE-----PVLEIPNVQFEDEGTYECEAENSRGKDTV 81
Ig2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
273-349 1.12e-03

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: 38.66  E-value: 1.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22474511  273 INETIFLKTTIVGKPTPTIEWRHDGHPiITDDRIEISITPKFSvLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05856    8 VGSSVRLKCVASGNPRPDITWLKDNKP-LTPTEIGESRKKKWT-LSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 82
Ig_Myomesin_like_C cd05737
C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein; Ig_Myomesin_like_C: ...
275-349 1.33e-03

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 38.73  E-value: 1.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22474511  275 ETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISITP-KFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05737   17 KTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAgRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
Ig2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar ...
178-243 1.40e-03

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


Pssm-ID: 319297  Cd Length: 85  Bit Score: 38.74  E-value: 1.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22474511  178 NDKVEFHVTFSGIPSPTIAWFKDDYEIFSSRRTAITTDESTS-VLLFHQILPSDEGEIKCTATNRGG 243
Cdd:cd05729    9 NTKVRLECGARGNPTPNITWLKDGKQKWKINVIRPTRVEEKGwVLIIRRAIPRDTGKYTCIVSNQYG 75
Ig_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2); ...
275-349 1.68e-03

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 38.35  E-value: 1.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22474511  275 ETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISI-TPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05891   17 KTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLeQGKYASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth ...
188-251 1.85e-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: 37.55  E-value: 1.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22474511  188 SGIPSPTIAWFKDDYEIFSSRRTAITTDestSVLLFHQILPSDEGEIKCTATNRGGHAVTKARL 251
Cdd:cd05746    8 QGDPEPTITWNKDGVQVTESGKFHISPE---GYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
Ig_TrkB_d5 cd05855
Fifth domain (immunoglobulin-like) of Trk receptor TrkB; TrkB_d5: the fifth domain of Trk ...
282-341 2.12e-03

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


Pssm-ID: 143263  Cd Length: 79  Bit Score: 37.90  E-value: 2.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22474511  282 TIVGKPTPTIEWRHDGHPIITDDRI-----EISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGED 341
Cdd:cd05855    6 TVKGNPKPTLQWFHEGAILNESEYIctkihVINNTEYHGCLQLDNPTHLNNGIYTLVAKNEYGED 70
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
188-245 2.48e-03

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: 37.41  E-value: 2.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22474511  188 SGIPSPTIAWFKDDYEIFSSRrtaITTDESTSVLLFHQILPSDEGEIKCTATNRGGHA 245
Cdd:cd05731    8 EGLPTPDIRWIKLGGELPKGR---TKFENFNKTLKIENVSEADSGEYQCTASNTMGSA 62
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
285-349 3.00e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar to the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 143202  Cd Length: 69  Bit Score: 37.00  E-value: 3.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22474511  285 GKPTPTIEWRHDGH--PI----ITDDRieisitpkfsVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05725    9 GDPVPTVLWRKEDGelPKgraeILDDK----------SLKIRNVTAGDEGSYTCEAENMVGKIEASASLTV 69
Ig_1 cd05763
Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: subgroup of the immunoglobulin (Ig) ...
279-349 3.05e-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: 3.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22474511  279 LKTTIVGKPTPTIEWRHDG---HPIITDDRIEisITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTAAFLVTV 349
Cdd:cd05763    3 LECAATGHPTPQIAWQKDGgtdFPAARERRMH--VMPEDDVFFIVDVKIEDTGVYSCTAQNTAGSISANATLTV 74
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
163-245 3.25e-03

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


Pssm-ID: 143207  Cd Length: 95  Bit Score: 37.99  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  163 PPVFIKRLEDVTALENdkVEFHVTFS----GIPSPTIAWFKDDyEIFSSRRTAITTDESTSVLLFHQILPSDEGEIKCTA 238
Cdd:cd05730    1 PPTIRARQSEVNATAN--LGQSVTLAcdadGFPEPTMTWTKDG-EPIESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIA 77

                 ....*..
gi 22474511  239 TNRGGHA 245
Cdd:cd05730   78 ENKAGEQ 84
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth Ig domain of ...
189-251 3.59e-03

Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth Ig domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal act ivity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319278  Cd Length: 73  Bit Score: 37.04  E-value: 3.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22474511  189 GIPSPTIAWFKDDYEIFSSRRTAITTDEStsvLLFHQILPSDEGEIKCTATNRGGHAVTKARL 251
Cdd:cd04969   12 ASPKPTISWSKGTELLTNSSRICILPDGS---LKIKNVSKSDEGKYTCFAVNFFGKANSTGSL 71
Ig8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
264-356 4.35e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar domains; Ig8_hMLCK_like: the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar domains. MLCK is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+, which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 143239  Cd Length: 98  Bit Score: 37.63  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  264 QYEDGLLYEINETIFLKTTIVGKPTPTIEWRHDGHPIITDDRIEISITPKFSVLKIHSAKRSDRGEYQIQAKNIIGEDTA 343
Cdd:cd05762    5 QFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQA 84
                         90
                 ....*....|...
gi 22474511  344 AFLVTVTAPPDPP 356
Cdd:cd05762   85 QVNLTVVDKPDPP 97
Ig2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: ...
168-243 4.47e-03

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


Pssm-ID: 143265  Cd Length: 85  Bit Score: 37.15  E-value: 4.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22474511  168 KRLEDVTAleNDKVEFHVTFSGIPSPTIAWFKDDYEIFSSRRT-AITTDESTSVLLFHQILPSDEGEIKCTATNRGG 243
Cdd:cd05857    1 KKLHAVPA--ANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIgGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYG 75
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig) ...
186-251 5.66e-03

Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules, which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG1, -2, -3, and -4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions; for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors; in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms, which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and -3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 143227  Cd Length: 75  Bit Score: 36.35  E-value: 5.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22474511  186 TFSGIPSPTIAWFKDDYEIFSSRR---TAITTDESTSVLLFHQILPSDEGEIKCTATNRGGHAVTKARL 251
Cdd:cd05750    7 ATSEYPSLRFKWFKDGKELNRKNKprnIKIRNKKKNSELQINKAKLADSGEYTCVVENILGNDTVTANV 75
Ig_TrkABC_d4 cd04972
Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d4: the ...
172-251 5.96e-03

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


Pssm-ID: 143173  Cd Length: 90  Bit Score: 36.73  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511  172 DVTALENDKVEFHVTFSGIPSPTIAWFKD-DYEIFSSRRTAITTDESTSvLLFHQILPSDEGEIKCTATNRGGHAVTKAR 250
Cdd:cd04972    9 ATVVYEGGTATIRCTAEGSPLPKVEWIIAgLIVIQTRTDTLETTVDIYN-LQLSNITSETQTTVTCTAENPVGQANVSVQ 87

                 .
gi 22474511  251 L 251
Cdd:cd04972   88 V 88
Interfer-bind pfam09294
Interferon-alpha/beta receptor, fibronectin type III; Members of this family adopt a secondary ...
336-444 9.84e-03

Interferon-alpha/beta receptor, fibronectin type III; Members of this family adopt a secondary structure consisting of seven beta-strands arranged in an immunoglobulin-like beta-sandwich, in a Greek-key topology. They are required for binding to interferon-alpha.


Pssm-ID: 312706  Cd Length: 104  Bit Score: 36.56  E-value: 9.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22474511    336 NIIGEDTAAfLVTVTAPPDPP-RNVSVTRQVDKSVTldweppaddggckvgnYIVEYYRTGWNVWLKAITSRKTNVTLFD 414
Cdd:pfam09294    9 NLEVEGGSL-NVTVKDPRTPRnGKNLSLRDIYGSLS----------------YRVSYWKNSSNGEKKVTTGTNSFVVLED 71
                           90       100       110
                   ....*....|....*....|....*....|
gi 22474511    415 LIEGSEYKFRIKAESPYgmSAPSSESSPVR 444
Cdd:pfam09294   72 LEPGTTYCVSVQAFSPL--DNKKSQPSPPQ 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
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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