NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|430728128|gb|AGA54254|]
View 

titin, partial [Saimiri oerstedii]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 10046111)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 108-186 1.36e-33

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: 118.85  E-value: 1.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 108 IVVRAGGSARIHIPFKGRPTPEITWSREEGEF--TDKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVK 185
Cdd:cd05748    2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81


                 .
gi 430728128 186 V 186
Cdd:cd05748   82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 190-281 3.70e-18

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: 3.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 190 PGPPQNLAVKEVRKDSVLLVWEPPIIDGGaKVKNYVIDKRESTRKAYANVSSKCSK-TSFKVENLTEGAIYYFRVMAENE 268
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79

                         90
                 ....*....|...
gi 430728128 269 FGVGVPVETVDAV 281
Cdd:cd00063   80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1-88 2.48e-15

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: 70.60  E-value: 2.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128   1 HIAATTKNSITLAWGKPIYDGGsEILGYVVEICKADEEEWQIVTPQTGlRVTRFEISKLTEHQEYKIRVCALNKVGLGEA 80
Cdd:cd00063    8 RVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85


                 ....*...
gi 430728128  81 tSVPGTVK 88
Cdd:cd00063   86 -SESVTVT 92
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
250-324 8.99e-08

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 53.47  E-value: 8.99e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 430728128 250 VENLTEGAIYYFRVMAENEFGVGVPVETVDAVKAAEPPSPPGKVTLTDVSQTSASLMWEKPEhdgGSRVVGYVVE 324
Cdd:COG3401  196 GGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVT---ESDATGYRVY 267
 
Name Accession Description Interval E-value
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 108-186 1.36e-33

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: 118.85  E-value: 1.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 108 IVVRAGGSARIHIPFKGRPTPEITWSREEGEF--TDKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVK 185
Cdd:cd05748    2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81


                 .
gi 430728128 186 V 186
Cdd:cd05748   82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 190-281 3.70e-18

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: 3.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 190 PGPPQNLAVKEVRKDSVLLVWEPPIIDGGaKVKNYVIDKRESTRKAYANVSSKCSK-TSFKVENLTEGAIYYFRVMAENE 268
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79

                         90
                 ....*....|...
gi 430728128 269 FGVGVPVETVDAV 281
Cdd:cd00063   80 GGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 190-272 6.61e-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: 6.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128   190 PGPPQNLAVKEVRKDSVLLVWEPPIIDGGAKVKNYVIDKRESTRKAYANVSSKCSKTSFKVENLTEGAIYYFRVMAENEF 269
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   ...
gi 430728128   270 GVG 272
Cdd:smart00060  81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1-88 2.48e-15

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: 70.60  E-value: 2.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128   1 HIAATTKNSITLAWGKPIYDGGsEILGYVVEICKADEEEWQIVTPQTGlRVTRFEISKLTEHQEYKIRVCALNKVGLGEA 80
Cdd:cd00063    8 RVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85


                 ....*...
gi 430728128  81 tSVPGTVK 88
Cdd:cd00063   86 -SESVTVT 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 106-186 7.65e-12

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: 60.60  E-value: 7.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128   106 KGIVVRAGGSARIHIPFKGRPTPEITWSREEGE---FTDKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFV 182
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKllaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81


                   ....
gi 430728128   183 TVKV 186
Cdd:smart00410  82 TLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
65-310 1.62e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.02  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128  65 YKIRVCALNKVGLGEATSVPGTVKPEDKLEAPEldldselrkGIVVRAGGSARIHIPFKGRPTPEITWSR------EEGE 138
Cdd:COG3401  205 YYYRVAATDTGGESAPSNEVSVTTPTTPPSAPT---------GLTATADTPGSVTLSWDPVTESDATGYRvyrsnsGDGP 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 139 FTdKVQIEKGVNYTqlsidncDRN-DAGK---YILKLENSSGSKSAF---VTVKVLDT-PGPPQNLAVKEVRKDSVLLVW 210
Cdd:COG3401  276 FT-KVATVTTTSYT-------DTGlTNGTtyyYRVTAVDAAGNESAPsnvVSVTTDLTpPAAPSGLTATAVGSSSITLSW 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 211 EPPiidGGAKVKNYVIDKRESTRKAYANVSSKCSKTSFKVENLTEGAIYYFRVMAENEFGVG------VPVETVDAVKAA 284
Cdd:COG3401  348 TAS---SDADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNEsapseeVSATTASAASGE 424

                        250       260
                 ....*....|....*....|....*.
gi 430728128 285 EPPSPPGKVTLTDVSQTSASLMWEKP 310
Cdd:COG3401  425 SLTASVDAVPLTDVAGATAAASAASN 450
I-set pfam07679
Immunoglobulin I-set domain;
106-186 2.13e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128  106 KGIVVRAGGSARIHIPFKGRPTPEITWSREEGEFT--DKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVT 183
Cdd:pfam07679   8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRssDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87


                  ...
gi 430728128  184 VKV 186
Cdd:pfam07679  88 LTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1-78 8.67e-11

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: 57.62  E-value: 8.67e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 430728128     1 HIAATTKNSITLAWGKPIYDGG-SEILGYVVEICKADEEeWQIVTPQTglRVTRFEISKLTEHQEYKIRVCALNKVGLG 78
Cdd:smart00060   8 RVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
1-81 1.10e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.42  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128    1 HIAATTKNSITLAWgKPIYDGGSEILGYVVEICKADEEE---WQIVTPQTglrvTRFEISKLTEHQEYKIRVCALNKVGL 77
Cdd:pfam00041   7 TVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSGEpwnEITVPGTT----TSVTLTGLKPGTEYEVRVQAVNGGGE 81


                  ....
gi 430728128   78 GEAT 81
Cdd:pfam00041  82 GPPS 85
fn3 pfam00041
Fibronectin type III domain;
191-274 3.74e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128  191 GPPQNLAVKEVRKDSVLLVWEPPIiDGGAKVKNYVI---DKRESTRKAYANVSSkcSKTSFKVENLTEGAIYYFRVMAEN 267
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVeyrPKNSGEPWNEITVPG--TTTSVTLTGLKPGTEYEVRVQAVN 77


                  ....*..
gi 430728128  268 EFGVGVP 274
Cdd:pfam00041  78 GGGEGPP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
250-324 8.99e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 53.47  E-value: 8.99e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 430728128 250 VENLTEGAIYYFRVMAENEFGVGVPVETVDAVKAAEPPSPPGKVTLTDVSQTSASLMWEKPEhdgGSRVVGYVVE 324
Cdd:COG3401  196 GGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVT---ESDATGYRVY 267
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 287-330 1.94e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 48.26  E-value: 1.94e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 430728128 287 PSPPGKVTLTDVSQTSASLMWEKPEHDGGsRVVGYVVEMQPKGT 330
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGS 43
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 287-330 2.37e-06

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: 44.91  E-value: 2.37e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 430728128   287 PSPPGKVTLTDVSQTSASLMWEKPEHDGG-SRVVGYVVEMQPKGT 330
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS 45
fn3 pfam00041
Fibronectin type III domain;
288-330 3.20e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.63  E-value: 3.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 430728128  288 SPPGKVTLTDVSQTSASLMWEKPEhDGGSRVVGYVVEMQPKGT 330
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNS 42
 
Name Accession Description Interval E-value
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 108-186 1.36e-33

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: 118.85  E-value: 1.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 108 IVVRAGGSARIHIPFKGRPTPEITWSREEGEF--TDKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVK 185
Cdd:cd05748    2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLkeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVK 81


                 .
gi 430728128 186 V 186
Cdd:cd05748   82 V 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 190-281 3.70e-18

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: 3.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 190 PGPPQNLAVKEVRKDSVLLVWEPPIIDGGaKVKNYVIDKRESTRKAYANVSSKCSK-TSFKVENLTEGAIYYFRVMAENE 268
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNG 79

                         90
                 ....*....|...
gi 430728128 269 FGVGVPVETVDAV 281
Cdd:cd00063   80 GGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 190-272 6.61e-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: 6.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128   190 PGPPQNLAVKEVRKDSVLLVWEPPIIDGGAKVKNYVIDKRESTRKAYANVSSKCSKTSFKVENLTEGAIYYFRVMAENEF 269
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   ...
gi 430728128   270 GVG 272
Cdd:smart00060  81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1-88 2.48e-15

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: 70.60  E-value: 2.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128   1 HIAATTKNSITLAWGKPIYDGGsEILGYVVEICKADEEEWQIVTPQTGlRVTRFEISKLTEHQEYKIRVCALNKVGLGEA 80
Cdd:cd00063    8 RVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85


                 ....*...
gi 430728128  81 tSVPGTVK 88
Cdd:cd00063   86 -SESVTVT 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 106-186 7.65e-12

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: 60.60  E-value: 7.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128   106 KGIVVRAGGSARIHIPFKGRPTPEITWSREEGE---FTDKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFV 182
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKllaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81


                   ....
gi 430728128   183 TVKV 186
Cdd:smart00410  82 TLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
65-310 1.62e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.02  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128  65 YKIRVCALNKVGLGEATSVPGTVKPEDKLEAPEldldselrkGIVVRAGGSARIHIPFKGRPTPEITWSR------EEGE 138
Cdd:COG3401  205 YYYRVAATDTGGESAPSNEVSVTTPTTPPSAPT---------GLTATADTPGSVTLSWDPVTESDATGYRvyrsnsGDGP 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 139 FTdKVQIEKGVNYTqlsidncDRN-DAGK---YILKLENSSGSKSAF---VTVKVLDT-PGPPQNLAVKEVRKDSVLLVW 210
Cdd:COG3401  276 FT-KVATVTTTSYT-------DTGlTNGTtyyYRVTAVDAAGNESAPsnvVSVTTDLTpPAAPSGLTATAVGSSSITLSW 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 211 EPPiidGGAKVKNYVIDKRESTRKAYANVSSKCSKTSFKVENLTEGAIYYFRVMAENEFGVG------VPVETVDAVKAA 284
Cdd:COG3401  348 TAS---SDADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNEsapseeVSATTASAASGE 424

                        250       260
                 ....*....|....*....|....*.
gi 430728128 285 EPPSPPGKVTLTDVSQTSASLMWEKP 310
Cdd:COG3401  425 SLTASVDAVPLTDVAGATAAASAASN 450
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
 108-186 2.10e-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: 2.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 108 IVVRAGGSARIHIPFKGRPTPEITWSREEGEFTD---KVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTV 184
Cdd:cd05894    5 IVVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTAtegRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84


                 ..
gi 430728128 185 KV 186
Cdd:cd05894   85 KV 86
I-set pfam07679
Immunoglobulin I-set domain;
106-186 2.13e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128  106 KGIVVRAGGSARIHIPFKGRPTPEITWSREEGEFT--DKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVT 183
Cdd:pfam07679   8 KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRssDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAE 87


                  ...
gi 430728128  184 VKV 186
Cdd:pfam07679  88 LTV 90
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 106-187 7.83e-11

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: 58.13  E-value: 7.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 106 KGIVVRAGGSARIHIPFKGRPTPEITWSREeGEFTD-----KVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSA 180
Cdd:cd20974    8 QSVVVLEGSTATFEAHVSGKPVPEVSWFRD-GQVIStstlpGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATS 86


                 ....*..
gi 430728128 181 FVTVKVL 187
Cdd:cd20974   87 TAELLVL 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1-78 8.67e-11

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: 57.62  E-value: 8.67e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 430728128     1 HIAATTKNSITLAWGKPIYDGG-SEILGYVVEICKADEEeWQIVTPQTglRVTRFEISKLTEHQEYKIRVCALNKVGLG 78
Cdd:smart00060   8 RVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGSE-WKEVNVTP--SSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
1-81 1.10e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.42  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128    1 HIAATTKNSITLAWgKPIYDGGSEILGYVVEICKADEEE---WQIVTPQTglrvTRFEISKLTEHQEYKIRVCALNKVGL 77
Cdd:pfam00041   7 TVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSGEpwnEITVPGTT----TSVTLTGLKPGTEYEVRVQAVNGGGE 81


                  ....
gi 430728128   78 GEAT 81
Cdd:pfam00041  82 GPPS 85
fn3 pfam00041
Fibronectin type III domain;
191-274 3.74e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128  191 GPPQNLAVKEVRKDSVLLVWEPPIiDGGAKVKNYVI---DKRESTRKAYANVSSkcSKTSFKVENLTEGAIYYFRVMAEN 267
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVeyrPKNSGEPWNEITVPG--TTTSVTLTGLKPGTEYEVRVQAVN 77


                  ....*..
gi 430728128  268 EFGVGVP 274
Cdd:pfam00041  78 GGGEGPP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
250-324 8.99e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 53.47  E-value: 8.99e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 430728128 250 VENLTEGAIYYFRVMAENEFGVGVPVETVDAVKAAEPPSPPGKVTLTDVSQTSASLMWEKPEhdgGSRVVGYVVE 324
Cdd:COG3401  196 GGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVT---ESDATGYRVY 267
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 287-330 1.94e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 48.26  E-value: 1.94e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 430728128 287 PSPPGKVTLTDVSQTSASLMWEKPEHDGGsRVVGYVVEMQPKGT 330
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGS 43
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 108-187 2.57e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 48.00  E-value: 2.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 108 IVVRAGGSARIHIPFKGRPTPEITWSREEGefTD---------KVQIEKGVNYtqlsIDNCDRNDAGKYILKLENSSGSK 178
Cdd:cd05763    9 ITIRAGSTARLECAATGHPTPQIAWQKDGG--TDfpaarerrmHVMPEDDVFF----IVDVKIEDTGVYSCTAQNSAGSI 82


                 ....*....
gi 430728128 179 SAFVTVKVL 187
Cdd:cd05763   83 SANATLTVL 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 287-330 2.37e-06

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: 44.91  E-value: 2.37e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 430728128   287 PSPPGKVTLTDVSQTSASLMWEKPEHDGG-SRVVGYVVEMQPKGT 330
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEGS 45
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
 110-193 4.14e-06

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: 44.94  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 110 VRAGGSARIHIPFKGRPTPEITWSR-----EEGEFtdkVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTV 184
Cdd:cd05762   13 VRAGESVELFCKVTGTQPITCTWMKfrkqiQEGEG---IKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNL 89


                 ....*....
gi 430728128 185 KVLDTPGPP 193
Cdd:cd05762   90 TVVDKPDPP 98
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 110-185 6.04e-06

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 43.95  E-value: 6.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 110 VRAGGSARIHIPFKGRPTPEITWSRE----EGEFTD-KVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSG--SKSAFV 182
Cdd:cd20951   12 VWEKSDAKLRVEVQGKPDPEVKWYKNgvpiDPSSIPgKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGeaSSSASV 91


                 ...
gi 430728128 183 TVK 185
Cdd:cd20951   92 VVE 94
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 109-186 1.20e-05

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: 43.15  E-value: 1.20e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 430728128 109 VVRAGGSARIHIPFKGRPTPEITWSREEGEFTD-KVQIekgVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVKV 186
Cdd:cd05725    8 VVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKgRYEI---LDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 108-173 1.25e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.94  E-value: 1.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 430728128  108 IVVRAGGSARIHIPFKGRPTPEITWSREEGEFTDKVQIEKGV--NYTQLSIDNCDRNDAGKYILKLEN 173
Cdd:pfam13927  11 VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLsgSNSTLTISNVTRSDAGTYTCVASN 78
fn3 pfam00041
Fibronectin type III domain;
288-330 3.20e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.63  E-value: 3.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 430728128  288 SPPGKVTLTDVSQTSASLMWEKPEhDGGSRVVGYVVEMQPKGT 330
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNS 42
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 106-184 3.59e-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: 41.80  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128  106 KGIVVRAGGSARIH-IPFKGRPTPEITWSREEGEFTDKVQIEKGVNYT---QLSIDNCDRNDAGKYILKLENSSGSKSAF 181
Cdd:pfam00047   4 PTVTVLEGDSATLTcSASTGSPGPDVTWSKEGGTLIESLKVKHDNGRTtqsSLLISNVTKEDAGTYTCVVNNPGGSATLS 83


                  ...
gi 430728128  182 VTV 184
Cdd:pfam00047  84 TSL 86
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 121-184 5.85e-05

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 41.23  E-value: 5.85e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 121 PFKGRPTPEITWSREEGEFTDK---VQIEKGVNytqLSIDNCDRNDAGKYILKLENSSG---SKSAFVTV 184
Cdd:cd05724   21 PPRGHPEPTVSWRKDGQPLNLDnerVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGereSRAARLSV 87
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 105-186 9.40e-05

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: 40.67  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 105 RKGIVVRAGGSARIHIPFKGRPTPEITWSREEGEFTDKVQIEKGVNYTQ---LSIDNCDRNDAGKYILKLENSSGSKSAF 181
Cdd:cd05729   11 EREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKgwsLIIERAIPRDKGKYTCIVENEYGSINHT 90


                 ....*
gi 430728128 182 VTVKV 186
Cdd:cd05729   91 YDVDV 95
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 110-180 1.01e-04

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. 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. 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: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 40.61  E-value: 1.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 430728128 110 VRAGGSARIHIPFKGRPTPEITWSR----EEGEFTDKVQIEKGV---NYTQLSIDNCDRNDAGKYILKLENSSGSKSA 180
Cdd:cd05765   12 VKVGETASFHCDVTGRPQPEITWEKqvpgKENLIMRPNHVRGNVvvtNIGQLVIYNAQPQDAGLYTCTARNSGGLLRA 89
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 106-184 2.61e-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: 39.65  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 106 KGIVVRAGGSARIHIPFKGRPTPEITWSReEGEF---TDKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFV 182
Cdd:cd05747   11 RSLTVSEGESARFSCDVDGEPAPTVTWMR-EGQIivsSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQF 89


                 ..
gi 430728128 183 TV 184
Cdd:cd05747   90 TL 91
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 124-186 2.82e-04

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: 39.50  E-value: 2.82e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 430728128 124 GRPTPEITWSREEG--EFTD--KVQIEKGvNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVKV 186
Cdd:cd05737   27 GDPPPEVSWLKNDQalAFLDhcNLKVEAG-RTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 121-180 3.19e-04

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: 38.46  E-value: 3.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 430728128 121 PFKGRPTPEITWSREEGEFTDKVQIEKGVNYT--QLSIDNCDRNDAGKYILKLENSSGSKSA 180
Cdd:cd00096    6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELGngTLTISNVTLEDSGTYTCVASNSAGGSAS 67
Ig0_BSG1 cd20940
Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are ...
 113-211 3.79e-04

Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of the collagenase stimulatory factor, basigin-1 (BSG1; also known as Cluster of Differentiation 147 (CD147) and Extracellular Matrix Metalloproteinase Inducer (EMMPRIN)) and similar proteins. CD147 is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It is expressed in nearly all cells including platelets and fibroblasts and is involved in inflammatory diseases, and cancer progression. CD147 is highly expressed in several cancers and used as a prognostic marker. The two primary isoforms of CD147 that are related to cancer progression have been identified: CD147 Ig1-Ig2 (also called Basigin-2) that is ubiquitously expressed in most tissues and CD147 Ig0-Ig1-Ig2 (also called Basigin-1) that is retinal specific and implicated in retinoblastoma. Studies showed that CD147 Ig0 domain is a potent stimulator of interleukin-6 and suggest that the CD147 Ig0 dimer is the functional unit required for activity.


Pssm-ID: 409534  Cd Length: 116  Bit Score: 39.56  E-value: 3.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 113 GGSARIHIPFKGRPTPEITWSREEGE------------FTDKVQIEKGVN---YTQLSIDNCDRNDAGKYILKLENSSGS 177
Cdd:cd20940   15 GDSVELHCEAVGSPIPEIQWWFEGQEpneicsqlwdgaRLDRVHINATYHqhaTSTISIDNLTEEDTGTYECRASNDPDR 94

                         90       100       110
                 ....*....|....*....|....*....|....
gi 430728128 178 KsafvtvkvlDTPGPPQnlaVKEVRKDSVLLVWE 211
Cdd:cd20940   95 N---------HLTRAPK---VKWIRSQANVLVLE 116
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 107-186 4.10e-04

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: 38.85  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 107 GIVVRAGGSARIHIPFKGRPTPEITWSREEGEFTDKVQIEK--GVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTV 184
Cdd:cd20949    8 VTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSkyRILADGLLINKVTQDDTGEYTCRAYQVNSIASDMQER 87


                 ..
gi 430728128 185 KV 186
Cdd:cd20949   88 TV 89
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 109-186 4.11e-04

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 38.63  E-value: 4.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 430728128 109 VVRAGGSARIHIPFKGRPTPEITWSREEGEFTDKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVKV 186
Cdd:cd20952   10 TVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 96-186 5.00e-04

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: 38.69  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128  96 PELDLDSELRKGIVVR-AGGSARIHIPFKGRPTPEITWSREEGEFTDKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENS 174
Cdd:cd05856    1 PRFTQPAKMRRRVIARpVGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKKWTLSLKNLKPEDSGKYTCHVSNR 80

                         90
                 ....*....|..
gi 430728128 175 SGSKSAFVTVKV 186
Cdd:cd05856   81 AGEINATYKVDV 92
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 105-186 6.47e-04

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: 37.97  E-value: 6.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 105 RKGIVVRAGGSARIHIPFKGRPTPEITWSREEGEF-TDKVQieKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVT 183
Cdd:cd05876    2 SSSLVALRGQSLVLECIAEGLPTPTVKWLRPSGPLpPDRVK--YQNHNKTLQLLNVGESDDGEYVCLAENSLGSARHAYY 79


                 ...
gi 430728128 184 VKV 186
Cdd:cd05876   80 VTV 82
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 96-179 7.91e-04

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: 37.82  E-value: 7.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128  96 PELDLDsELRKGIVVRAGGSARIHIPFKGRPTPEITWSREEGEFTDKVQIEKGVNYTqLSIDNCDRNDAGKYILKLENSS 175
Cdd:cd04969    1 PDFELN-PVKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDGS-LKIKNVTKSDEGKYTCFAVNFF 78


                 ....
gi 430728128 176 GSKS 179
Cdd:cd04969   79 GKAN 82
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 110-179 9.14e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second 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: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 37.95  E-value: 9.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 430728128 110 VRAGGSARIHIPFKGRPTPEITWSREEGEF--TDKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKS 179
Cdd:cd20972   13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELqnSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDT 84
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 124-186 1.37e-03

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: 37.58  E-value: 1.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 430728128 124 GRPTPEITWSR--EEGEFTDK--VQIEKGvNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVKV 186
Cdd:cd05891   27 GNPDPEVIWFKndQDIELSEHysVKLEQG-KYASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 123-186 1.42e-03

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


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 37.23  E-value: 1.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 430728128 123 KGRPTPEITWSREEGEFT---DKVQIEKGVnyTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVKV 186
Cdd:cd20976   26 RGKPVPRITWIRNAQPLQyaaDRSTCEAGV--GELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 102-186 1.49e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 36.99  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 102 SELRKGIVVRAGGSARIHIPFKGRPTPEITWSREEGEFTD---KVQIEKGVnytqLSIDNCDRNDAGKYILKLENSSGSK 178
Cdd:cd20978    5 QKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGpmeRATVEDGT----LTIINVQPEDTGYYGCVATNEIGDI 80


                 ....*...
gi 430728128 179 SAFVTVKV 186
Cdd:cd20978   81 YTETLLHV 88
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 124-186 2.80e-03

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). 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 [Multi-domain]  Cd Length: 95  Bit Score: 36.45  E-value: 2.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 430728128 124 GRPTPEITWSREeGEFTDKVQIEKGVNY--TQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVKV 186
Cdd:cd05730   29 GFPEPTMTWTKD-GEPIESGEEKYSFNEdgSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 110-176 5.58e-03

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


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 35.55  E-value: 5.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 430728128 110 VRAGGSARIHIPFKGRPTPEITWSREEGEFTDKVQIEKGVNYT---QLSIDNCDRNDAGKYILKLENSSG 176
Cdd:cd05744   12 VQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENgrhSLIIEPVTKRDAGIYTCIARNRAG 81
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 124-186 9.65e-03

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: 34.69  E-value: 9.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 430728128 124 GRPTPEITWSREEGEF-TDKVQIEkgvNYTQ-LSIDNCDRNDAGKYILKLENSSGSKSAFVTVKV 186
Cdd:cd05731   21 GLPTPDIRWIKLGGELpKGRTKFE---NFNKtLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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