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Conserved domains on  [gi|1304834872|gb|AUD52711|]
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titin, partial [Pseudis paradoxa]

Protein Classification

FN3 and Ig_Titin_like domain-containing protein( domain architecture ID 10046110)

FN3 and Ig_Titin_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 238-317 4.50e-30

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


:

Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 109.60  E-value: 4.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 238 TLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTEL--RTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTLVV 315
Cdd:cd05748     1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80


                  ..
gi 1304834872 316 KV 317
Cdd:cd05748    81 KV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 127-218 1.10e-19

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: 82.54  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 127 PSPPSKPKIIDSTKTSVTIGWVKPLFDGGsPVTGYTIDYRKSDETDWTTA-VTNVRGTEYTVIALTSGAEYVFRVRSVNK 205
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|...
gi 1304834872 206 VGQSDPSDSSEPQ 218
Cdd:cd00063    80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 26-113 1.88e-19

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: 81.77  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  26 PSPPRSLEITGVTKEAMTLCWARPESDGGsEIAGYIIERREKNSLRWMRVNKKPVYDLRVKSSGLREGCEYEYRVYAENA 105
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ....*...
gi 1304834872 106 AGLSAPSD 113
Cdd:cd00063    80 GGESPPSE 87
 
Name Accession Description Interval E-value
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 238-317 4.50e-30

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


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 109.60  E-value: 4.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 238 TLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTEL--RTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTLVV 315
Cdd:cd05748     1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80


                  ..
gi 1304834872 316 KV 317
Cdd:cd05748    81 KV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 127-218 1.10e-19

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: 82.54  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 127 PSPPSKPKIIDSTKTSVTIGWVKPLFDGGsPVTGYTIDYRKSDETDWTTA-VTNVRGTEYTVIALTSGAEYVFRVRSVNK 205
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|...
gi 1304834872 206 VGQSDPSDSSEPQ 218
Cdd:cd00063    80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 26-113 1.88e-19

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: 81.77  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  26 PSPPRSLEITGVTKEAMTLCWARPESDGGsEIAGYIIERREKNSLRWMRVNKKPVYDLRVKSSGLREGCEYEYRVYAENA 105
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ....*...
gi 1304834872 106 AGLSAPSD 113
Cdd:cd00063    80 GGESPPSE 87
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
7-317 6.01e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 84.67  E-value: 6.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872   7 GVGEPLESEAIKALNPYTVPSPPRSLEITGVTKEAMTLCWARPESDGgseIAGYIIERREKNSLRWMRVNKkpVYDLRVK 86
Cdd:COG3401   214 TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSYT 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  87 SSGLREGCEYEYRVYAENAAGLsaPSDCSPLIRAEDPVFLPSPPSKPKIIDSTKTSVTIGWVKPLfdgGSPVTGYTIDYR 166
Cdd:COG3401   289 DTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRS 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 167 KSDETDWTTAVTNVRGTEYTVIALTSGAEYVFRVRSVNKVG-QSDPSDSSEPQIVKEREEEPAFDIDSEMRKTLIVKAGG 245
Cdd:COG3401   364 TSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304834872 246 SFTMTVPYKGKPTPNVTWSKPDTELRTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTLVVKV 317
Cdd:COG3401   444 AASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGAS 515
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 127-209 7.37e-16

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.88  E-value: 7.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  127 PSPPSKPKIIDSTKTSVTIGWVKPLFDGG-SPVTGYTIDYRKSDEtDWTTAVTNVRGTEYTVIALTSGAEYVFRVRSVNK 205
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                   ....
gi 1304834872  206 VGQS 209
Cdd:smart00060  80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
128-212 5.07e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 5.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 128 SPPSKPKIIDSTKTSVTIGWvKPLFDGGSPVTGYTIDYRKSDETDWTTAVTNVRGT-EYTVIALTSGAEYVFRVRSVNKV 206
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79


                  ....*.
gi 1304834872 207 GQSDPS 212
Cdd:pfam00041  80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 26-109 9.65e-14

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: 65.71  E-value: 9.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872   26 PSPPRSLEITGVTKEAMTLCWARPESDGG-SEIAGYIIERREKNSlRWMRVNKKPVyDLRVKSSGLREGCEYEYRVYAEN 104
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPS-STSYTLTGLKPGTEYEFRVRAVN 78


                   ....*
gi 1304834872  105 AAGLS 109
Cdd:smart00060  79 GAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
92-216 1.37e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.41  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  92 EGCEYEYRVYAENAAGLSAPSdcsPLIRAEDPVFLPSPPSKPKIIDSTKTSVTIGWVKPLFDGgspVTGYTIdYRKSDET 171
Cdd:COG3401   201 PGTTYYYRVAATDTGGESAPS---NEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRV-YRSNSGD 273

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1304834872 172 DWTTAVTNVRGTEYTVIALTSGAEYVFRVRSVNKVG-QSDPSDSSE 216
Cdd:COG3401   274 GPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVS 319
I-set pfam07679
Immunoglobulin I-set domain;
237-317 1.56e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.96  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 237 KTLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTELRT--RATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTLV 314
Cdd:pfam07679   8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSsdRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87


                  ...
gi 1304834872 315 VKV 317
Cdd:pfam07679  88 LTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 237-317 2.53e-11

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.06  E-value: 2.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  237 KTLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTEL---RTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTL 313
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81


                   ....
gi 1304834872  314 VVKV 317
Cdd:smart00410  82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
27-112 3.03e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.97  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  27 SPPRSLEITGVTKEAMTLCWARPEsDGGSEIAGYIIERREKNSLRWMRVNKKPVYDLRVKSSGLREGCEYEYRVYAENAA 106
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                  ....*.
gi 1304834872 107 GLSAPS 112
Cdd:pfam00041  80 GEGPPS 85
 
Name Accession Description Interval E-value
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 238-317 4.50e-30

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


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 109.60  E-value: 4.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 238 TLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTEL--RTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTLVV 315
Cdd:cd05748     1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80


                  ..
gi 1304834872 316 KV 317
Cdd:cd05748    81 KV 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 127-218 1.10e-19

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: 82.54  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 127 PSPPSKPKIIDSTKTSVTIGWVKPLFDGGsPVTGYTIDYRKSDETDWTTA-VTNVRGTEYTVIALTSGAEYVFRVRSVNK 205
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|...
gi 1304834872 206 VGQSDPSDSSEPQ 218
Cdd:cd00063    80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 26-113 1.88e-19

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: 81.77  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  26 PSPPRSLEITGVTKEAMTLCWARPESDGGsEIAGYIIERREKNSLRWMRVNKKPVYDLRVKSSGLREGCEYEYRVYAENA 105
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ....*...
gi 1304834872 106 AGLSAPSD 113
Cdd:cd00063    80 GGESPPSE 87
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
7-317 6.01e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 84.67  E-value: 6.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872   7 GVGEPLESEAIKALNPYTVPSPPRSLEITGVTKEAMTLCWARPESDGgseIAGYIIERREKNSLRWMRVNKkpVYDLRVK 86
Cdd:COG3401   214 TGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT--VTTTSYT 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  87 SSGLREGCEYEYRVYAENAAGLsaPSDCSPLIRAEDPVFLPSPPSKPKIIDSTKTSVTIGWVKPLfdgGSPVTGYTIDYR 166
Cdd:COG3401   289 DTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASS---DADVTGYNVYRS 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 167 KSDETDWTTAVTNVRGTEYTVIALTSGAEYVFRVRSVNKVG-QSDPSDSSEPQIVKEREEEPAFDIDSEMRKTLIVKAGG 245
Cdd:COG3401   364 TSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304834872 246 SFTMTVPYKGKPTPNVTWSKPDTELRTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTLVVKV 317
Cdd:COG3401   444 AASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGAS 515
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 127-209 7.37e-16

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.88  E-value: 7.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  127 PSPPSKPKIIDSTKTSVTIGWVKPLFDGG-SPVTGYTIDYRKSDEtDWTTAVTNVRGTEYTVIALTSGAEYVFRVRSVNK 205
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                   ....
gi 1304834872  206 VGQS 209
Cdd:smart00060  80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
128-212 5.07e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 5.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 128 SPPSKPKIIDSTKTSVTIGWvKPLFDGGSPVTGYTIDYRKSDETDWTTAVTNVRGT-EYTVIALTSGAEYVFRVRSVNKV 206
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79


                  ....*.
gi 1304834872 207 GQSDPS 212
Cdd:pfam00041  80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 26-109 9.65e-14

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: 65.71  E-value: 9.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872   26 PSPPRSLEITGVTKEAMTLCWARPESDGG-SEIAGYIIERREKNSlRWMRVNKKPVyDLRVKSSGLREGCEYEYRVYAEN 104
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS-EWKEVNVTPS-STSYTLTGLKPGTEYEFRVRAVN 78


                   ....*
gi 1304834872  105 AAGLS 109
Cdd:smart00060  79 GAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
92-216 1.37e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.41  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  92 EGCEYEYRVYAENAAGLSAPSdcsPLIRAEDPVFLPSPPSKPKIIDSTKTSVTIGWVKPLFDGgspVTGYTIdYRKSDET 171
Cdd:COG3401   201 PGTTYYYRVAATDTGGESAPS---NEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD---ATGYRV-YRSNSGD 273

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1304834872 172 DWTTAVTNVRGTEYTVIALTSGAEYVFRVRSVNKVG-QSDPSDSSE 216
Cdd:COG3401   274 GPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVS 319
I-set pfam07679
Immunoglobulin I-set domain;
237-317 1.56e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.96  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 237 KTLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTELRT--RATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTLV 314
Cdd:pfam07679   8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSsdRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87


                  ...
gi 1304834872 315 VKV 317
Cdd:pfam07679  88 LTV 90
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
 238-317 1.91e-11

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 59.47  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 238 TLIVKAGGSFTMTVPYKGKPTPNVTWSKPD---TELRTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTLV 314
Cdd:cd05894     4 TIVVVAGNKLRLDVPISGEPAPTVTWSRGDkafTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLF 83


                  ...
gi 1304834872 315 VKV 317
Cdd:cd05894    84 VKV 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 237-317 2.53e-11

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.06  E-value: 2.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  237 KTLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTEL---RTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTL 313
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaeSGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81


                   ....
gi 1304834872  314 VVKV 317
Cdd:smart00410  82 TLTV 85
fn3 pfam00041
Fibronectin type III domain;
27-112 3.03e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.97  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  27 SPPRSLEITGVTKEAMTLCWARPEsDGGSEIAGYIIERREKNSLRWMRVNKKPVYDLRVKSSGLREGCEYEYRVYAENAA 106
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                  ....*.
gi 1304834872 107 GLSAPS 112
Cdd:pfam00041  80 GEGPPS 85
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 237-318 1.08e-09

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 54.67  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 237 KTLIVKAGGSFTMTVPYKGKPTPNVTWSKP----DTELRTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLT 312
Cdd:cd20974     8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRDgqviSTSTLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATST 87


                  ....*.
gi 1304834872 313 LVVKVL 318
Cdd:cd20974    88 AELLVL 93
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
13-320 8.87e-09

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 56.88  E-value: 8.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  13 ESEAIKALNPYTVPSPPRSLEIT-----GVTKEAMTLCWARPESDggseiAGYIIERReKNSLRWmrVNKKPVYDLRVKS 87
Cdd:COG4733   520 DAGAFDDVPPQWPPVNVTTSESLsvvaqGTAVTTLTVSWDAPAGA-----VAYEVEWR-RDDGNW--VSVPRTSGTSFEV 591

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872  88 SGLREGcEYEYRVYAENAAGLSAPSDCSPLIRAedpVFLPSPPSKPK--IIDSTKTSVTIGWVkplFDGGSPVTGYTIDY 165
Cdd:COG4733   592 PGIYAG-DYEVRVRAINALGVSSAWAASSETTV---TGKTAPPPAPTglTATGGLGGITLSWS---FPVDADTLRTEIRY 664

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 166 rkSDETDWTTAV---TNVRGTEYTVIALTSGAEYVFRVRSVNKVGQS-----------DPSDSSEPQIVKEREEEPAFDI 231
Cdd:COG4733   665 --STTGDWASATvaqALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVsawwvsgqasaDAAGILDAITGQILETELGQEL 742

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 232 DSEMRKTLIVKAGGSFTMTVPYK-------GKPTPNVTWSKPDTELRTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQN 304
Cdd:COG4733   743 DAIIQNATVAEVVAATVTDVTAQidtavlfAGVATAAAIGAEARVAATVAESATAAAATGTAADAAGDASGGVTAGTSGT 822

                         330
                  ....*....|....*.
gi 1304834872 305 ILNTATLTLVVKVLDS 320
Cdd:COG4733   823 TGAGDTAASTTRVAAA 838
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 227-317 8.60e-08

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 49.38  E-value: 8.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 227 PAFDIDsEMRKTLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTELRTRATIDTTDSKTsLSIEKATRNDSGKYTLTLQNIL 306
Cdd:cd04969     1 PDFELN-PVKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDGS-LKIKNVTKSDEGKYTCFAVNFF 78

                          90
                  ....*....|.
gi 1304834872 307 NTATLTLVVKV 317
Cdd:cd04969    79 GKANSTGSLSV 89
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 237-304 1.02e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 48.72  E-value: 1.02e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 237 KTLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTELRTRATIDTTDSKT--SLSIEKATRNDSGKYTLTLQN 304
Cdd:pfam13927   9 SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSnsTLTISNVTRSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 247-304 4.04e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 46.94  E-value: 4.04e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 247 FTMTVPYKGKPTPNVTWSKPDTELR--TRATIDTTDSKTSLSIEKATRNDSGKYTLTLQN 304
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPpsSRDSRRSELGNGTLTISNVTLEDSGTYTCVASN 60
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 236-317 4.77e-07

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


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 46.83  E-value: 4.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 236 RKTLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTELRTRATIDTTDSKTsLSIEKATRNDSGKYTLTLQNILNTATLTLVV 315
Cdd:cd05876     2 SSSLVALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQNHNKT-LQLLNVGESDDGEYVCLAENSLGSARHAYYV 80


                  ..
gi 1304834872 316 KV 317
Cdd:cd05876    81 TV 82
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 241-317 2.00e-06

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 45.18  E-value: 2.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1304834872 241 VKAGGSFTMTVPYKGKPTPNVTWSKPDTELRTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTLVVKV 317
Cdd:cd20952    11 VAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 227-317 4.91e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. 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, FGFR2, FGFR3, FGFR4). 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: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 44.52  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 227 PAFDIDSEMRKTLI-VKAGGSFTMTVPYKGKPTPNVTWSKPDTELRTRATIDTTDSKT---SLSIEKATRNDSGKYTLTL 302
Cdd:cd05729     1 PRFTDTEKMEEREHaLPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEkgwSLIIERAIPRDKGKYTCIV 80

                          90
                  ....*....|....*
gi 1304834872 303 QNILNTATLTLVVKV 317
Cdd:cd05729    81 ENEYGSINHTYDVDV 95
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 244-317 8.02e-06

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of 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: 43.74  E-value: 8.02e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1304834872 244 GGSFTMTVPYKGKPTPNVTWSKPD--TELRTRATIDTTDSK-TSLSIEKATRNDSGKYTLTLQNILNTATLTLVVKV 317
Cdd:cd05891    16 GKTLNLTCTVFGNPDPEVIWFKNDqdIELSEHYSVKLEQGKyASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 237-312 1.46e-05

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.95  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 237 KTLIVKAGGSFTMTVPYK-GKPTPNVTWSKPDTELRTRATI---DTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLT 312
Cdd:pfam00047   4 PTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVkhdNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLS 83
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 241-310 2.77e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 42.32  E-value: 2.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304834872 241 VKAGGSFTMTVPYKGKPTPNVTWSKPDTELRTRATIDT--TDSKTSLSIEKATRNDSGKYTLTLQNILNTAT 310
Cdd:cd20949    11 VKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSkyRILADGLLINKVTQDDTGEYTCRAYQVNSIAS 82
IgI_VEGFR-1 cd07702
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); ...
 246-315 2.86e-05

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1). VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-1 binds VEGF-A strongly; VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-1 may play an inhibitory role in the function of VEGFR-2 by binding VEGF-A and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis and may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409499  Cd Length: 92  Bit Score: 42.17  E-value: 2.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1304834872 246 SFTMTVPYKGKPTPNVTWSK---PDTELRTRATIDTTdsktSLSIEKATRNDSGKYTLTLQ----NILNTATLTLVV 315
Cdd:cd07702    20 SYRLSMKVKAFPSPEVIWLKdglPATEKCARYLTRGY----SLIIKDVTEEDAGNYTILLSikqsNLFKNLTATLIV 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 227-304 4.16e-05

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


Pssm-ID: 409442  Cd Length: 92  Bit Score: 41.77  E-value: 4.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1304834872 227 PAFDIDSEMRKTLIVK-AGGSFTMTVPYKGKPTPNVTWSKPDTELRTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQN 304
Cdd:cd05856     1 PRFTQPAKMRRRVIARpVGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKKWTLSLKNLKPEDSGKYTCHVSN 79
IgI_VEGFR-2 cd05864
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); ...
 231-315 4.93e-05

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-2 (KDR/Flk-1) is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A; VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGF-A also interacts with VEGFR-1, which it binds more strongly than VEGFR-2. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409450  Cd Length: 89  Bit Score: 41.45  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 231 IDSEMRKTLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTELRTRATIdttDSKTSLSIEKATRNDSGKYTLTLQNILNTA- 309
Cdd:cd05864     4 LGSGMESLVEAKVGERVRIPVKYLGYPPPEIKWYKNGIPIESNHTI---KAGHVLTIMEVTEKDAGNYTVVLTNPISKEk 80


                  ....*....
gi 1304834872 310 ---TLTLVV 315
Cdd:cd05864    81 qrhTFSLVV 89
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 227-317 1.12e-04

Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409438  Cd Length: 89  Bit Score: 40.37  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 227 PAFDIDSeMRKTLIVKAGGSFTMTVPYKGKPTPNVTWSKpDTELRTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNIL 306
Cdd:cd05852     1 PTFEFNP-MKKKILAAKGGRVIIECKPKAAPKPKFSWSK-GTELLVNNSRISIWDDGSLEILNITKLDEGSYTCFAENNR 78

                          90
                  ....*....|.
gi 1304834872 307 NTATLTLVVKV 317
Cdd:cd05852    79 GKANSTGVLSV 89
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 237-304 1.45e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. 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. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 40.42  E-value: 1.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 237 KTLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTELRT--RATIDTTDSKTSLSIEKATRNDSGKYTLTLQN 304
Cdd:cd05747    11 RSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSsqRHQITSTEYKSTFEISKVQMSDEGNYTVVVEN 80
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 233-317 1.66e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 39.93  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 233 SEMRKTLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTELRTRATIDTTDSKTS-LSIEKATRNDSGKYTLTLQNILNTATL 311
Cdd:cd20976     5 SSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGVGeLHIQDVLPEDHGTYTCLAKNAAGQVSC 84


                  ....*.
gi 1304834872 312 TLVVKV 317
Cdd:cd20976    85 SAWVTV 90
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 239-317 4.00e-04

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 38.71  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 239 LIVKAGGSFTMTVPYKGKPTPNVTWSK---PDTELRTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTLVV 315
Cdd:cd20973     7 KEVVEGSAARFDCKVEGYPDPEVKWMKddnPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86


                  ..
gi 1304834872 316 KV 317
Cdd:cd20973    87 TV 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 255-315 4.97e-04

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


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 38.53  E-value: 4.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304834872 255 GKPTPNVTWSKPDTEL-RTRATIdtTDSKtSLSIEKATRNDSGKYTLTLQNILN--TATLTLVV 315
Cdd:cd05725    23 GDPVPTVRWRKEDGELpKGRYEI--LDDH-SLKIRKVTAGDMGSYTCVAENMVGkiEASATLTV 83
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 252-308 8.49e-04

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 37.77  E-value: 8.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1304834872 252 PYKGKPTPNVTWSKPDTELRTRATIDTTDSKTSLSIEKATRNDSGKYTLTLQNILNT 308
Cdd:cd05724    21 PPRGHPEPTVSWRKDGQPLNLDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGE 77
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 238-317 8.61e-04

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 37.77  E-value: 8.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 238 TLIVKAGGSFTMTVPYKGKPTPNVTWSKPDTEL-RTRATIDttDSKTSLSIEKATRNDSGKYTLTLQNILNTATLTLVVK 316
Cdd:cd05731     4 STMVLRGGVLLLECIAEGLPTPDIRWIKLGGELpKGRTKFE--NFNKTLKIENVSEADSGEYQCTASNTMGSARHTISVT 81


                  .
gi 1304834872 317 V 317
Cdd:cd05731    82 V 82
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 255-309 8.76e-04

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 37.99  E-value: 8.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1304834872 255 GKPTPNVTWSKPDTELRTRATIDTTDSKtSLSIEKATRNDSGKYTLTLQNILNTA 309
Cdd:cd20968    25 GNPKPSVSWIKGDDLIKENNRIAVLESG-SLRIHNVQKEDAGQYRCVAKNSLGIA 78
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 244-304 2.16e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 36.60  E-value: 2.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304834872 244 GGSFTMTVPYKGKPTPNVTWSKPDTELRTRatidttdskTSLSIEKATRNDSGKYTLTLQN 304
Cdd:pfam13895  14 GEPVTLTCSAPGNPPPSYTWYKDGSAISSS---------PNFFTLSVSAEDSGTYTCVARN 65
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
 217-325 2.47e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (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: 409419  Cd Length: 99  Bit Score: 36.86  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 217 PQIVKereeepaFDIDSEMRKTLIVKAGGSFTMTVPYkgkptpNVTWSKPDTELRTRA--TIDTTDSKTSLSIEKATRND 294
Cdd:cd05762     2 PQIIQ-------FPEDMKVRAGESVELFCKVTGTQPI------TCTWMKFRKQIQEGEgiKIENTENSSKLTITEGQQEH 68

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1304834872 295 SGKYTLTLQNILNTATLTLVVKVLDSPGPPS 325
Cdd:cd05762    69 CGCYTLEVENKLGSRQAQVNLTVVDKPDPPA 99
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 241-317 5.63e-03

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 35.64  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304834872 241 VKAGGSFTMTVPYKGKPTPNVTWSKPDTELR--TRATIDTTDSKT-SLSIEKATRNDSGKYTLTLQNILNTATLTLVVKV 317
Cdd:cd05737    13 IMEGKTLNLTCNVWGDPPPEVSWLKNDQALAflDHCNLKVEAGRTvYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
IgI_VEGFR cd04976
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); member ...
 246-315 5.69e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic, and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409365  Cd Length: 90  Bit Score: 35.65  E-value: 5.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304834872 246 SFTMTVPYKGKPTPNVTWSKPDTELRTRATIDTtdsKTSLSIEKATRNDSGKYTLTLQN----ILNTATLTLVV 315
Cdd:cd04976    20 SVRLPMKVKAYPPPEVVWYKDGLPLTEKARYLT---RHSLIIKEVTEEDTGNYTILLSNkqsnVFKNLTATLVV 90
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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