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Conserved domains on  [gi|568938739|ref|XP_006504775|]
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protein sidekick-1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1436-1858 9.18e-22

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.39  E-value: 9.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1436 LPGGEWQTYSSSISHEATACAVERLRPFTSYKLRLKATNDIGDSDFSAETEAVTTLqdVPGEPPGSVSATPHTTSSVLIQ 1515
Cdd:COG3401   175 SATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPT--TPPSAPTGLTATADTPGSVTLS 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1516 WQPPRDESlnglLQGYRIYYRElesetgmspepktlkspsalraelTAQSSFKTVNSSSSlTTYELTHLKKYRRYEVIMT 1595
Cdd:COG3401   253 WDPVTESD----ATGYRVYRSN------------------------SGDGPFTKVATVTT-TSYTDTGLTNGTTYYYRVT 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1596 AYNIIG-ESPASVPVEVFVGEAAPAmAPQNVQVTPLTASQLEVTWDPpppeSQNGNIQGYKVYYWEADSrNETEKMKVLf 1674
Cdd:COG3401   304 AVDAAGnESAPSNVVSVTTDLTPPA-APSGLTATAVGSSSITLSWTA----SSDADVTGYNVYRSTSGG-GTYTKIAET- 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1675 LPEPVVKIKDLTSHTKYLISISAFNAAGD-GPKSDPCQGrTHQAAPGPPSFLAFSEITSTTLNVSWGEPSAAngilqgyR 1753
Cdd:COG3401   377 VTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSA-TTASAASGESLTASVDAVPLTDVAGATAAASA-------A 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1754 VVYEPLAPVQGVSKVVTVDVKGNWQRWLKVRDLTKGVTYFFRVQARTIAYGPELQANVTAGPAEGSPGSPRNVLVTKSAS 1833
Cdd:COG3401   449 SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTP 528
                         410       420
                  ....*....|....*....|....*
gi 568938739 1834 ELTLQWTEGNAGTTPTTGYVIEARP 1858
Cdd:COG3401   529 NVTGASPVTVGASTGDVLITDLVSL 553
I-set pfam07679
Immunoglobulin I-set domain;
397-487 6.08e-20

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 86.16  E-value: 6.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvripRFMLLESGG---LRIAPVFIQDAGNYTCYAA 473
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD----RFKVTYEGGtytLTISNVQPDDSGKYTCVAT 76
                           90
                   ....*....|....
gi 568938739   474 NTEASVNASAMLTV 487
Cdd:pfam07679   77 NSAGEAEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
587-672 1.56e-17

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 79.38  E-value: 1.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   587 PPQNLlaSLSPARSHSVTLSWVRPFDGNSPVLYYIVQVSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVNQV 666
Cdd:pfam00041    2 APSNL--TVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 568938739   667 GKGQYS 672
Cdd:pfam00041   80 GEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1295-1388 1.50e-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: 73.68  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1295 PGPPVRLVFPEVRLTAVRIVWQPPEEPNGVILGYQIAYRLASGSPHTFTTVEVGaTVRQFTATELAPESAYIFRLSAKTR 1374
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|....
gi 568938739 1375 QGWGEPLEATVITT 1388
Cdd:cd00063    80 GGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
688-774 2.17e-15

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 2.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   688 PPKNIVASGRTNQSIMVQWQPPPEteHNGVLRGYILRYRLAGLPGEHQQRNISSPEvNYCLVTDLIIWTQYEIQVAAYNG 767
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNSGEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 568938739   768 AGLGVFS 774
Cdd:pfam00041   79 GGEGPPS 85
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
489-878 9.60e-15

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: 80.05  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  489 NRTSIVHPPEDRVVIKGTTATLCCGATHDPRTSLRYVWKKDNVVITASSSSRIVVEKDGSLVISQTWSGDIGD------- 561
Cdd:COG3401   126 TTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDiepgtty 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  562 -YTCEIISEGGSDSRTARLEVI---ELPHPPQNLLASlsPARSHSVTLSWVRPfdGNSPVLYYIVQVSENNSPWKVHLSN 637
Cdd:COG3401   206 yYRVAATDTGGESAPSNEVSVTtptTPPSAPTGLTAT--ADTPGSVTLSWDPV--TESDATGYRVYRSNSGDGPFTKVAT 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  638 VgpEMTGVTVSGLTPARTYQFRVCAVNQVG-KGQYSTETSrlMLPEEPPSAPPKNIVASGRTNQSIMVQWQPPPetehNG 716
Cdd:COG3401   282 V--TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVS--VTTDLTPPAAPSGLTATAVGSSSITLSWTASS----DA 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  717 VLRGYILrYRLAGLPGEHQQRNISSPEVNYcLVTDLIIWTQYEIQVAAYNGAGL-GVFSRAVTEYTLQGVPTAPPQNVQA 795
Cdd:COG3401   354 DVTGYNV-YRSTSGGGTYTKIAETVTTTSY-TDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVD 431
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  796 EAVNSTTVHFLW-----NPPPQQFINGINQGYKLLAWPADAPETVTVVTIAPDFHGIHHGYITNLKKFTAYFTSVLCFTT 870
Cdd:COG3401   432 AVPLTDVAGATAaasaaSNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV 511

                  ....*...
gi 568938739  871 PGDGPPSS 878
Cdd:COG3401   512 IGASAAAA 519
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1820-1913 1.87e-14

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: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1820 PGSPRNVLVTK-SASELTLQWTEGNAGTTPTTGYVIEARPSDEGLWDMFAKDIPrSATSYTVDldKLRQGVTYEFRVVAV 1898
Cdd:cd00063     1 PSPPTNLRVTDvTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG-SETSYTLT--GLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*
gi 568938739 1899 NKAGFGEPSRPSIAV 1913
Cdd:cd00063    78 NGGGESPPSESVTVT 92
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
957-1358 2.06e-13

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: 75.81  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  957 TYTIDVAALTAAGVGVTTSSTISSGVPPDLPGAPSNLVISNISPRSATLQFRPGYDGKTAICRWIVEGQVGAIGDEEEWV 1036
Cdd:COG3401    90 TATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVV 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1037 T-----------LYEEENEPDAQMLEIPNLTPYTHYRFRMRQVNIVGPSPFSQSSRVIQTLQAPpdVAPTSLTVRTASET 1105
Cdd:COG3401   170 VspdtsataavaTTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPP--SAPTGLTATADTPG 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1106 SLRLRWVPlpdsqyNGNPESVGYRVKywRSDQPSSALAQVVSDRlERELTIEELEEWTEYELRMQAFNAIG-AGPWSELV 1184
Cdd:COG3401   248 SVTLSWDP------VTESDATGYRVY--RSNSGDGPFTKVATVT-TTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVV 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1185 RGRTRESVPsAAPENVSAEAVSSTQILLTWASVPEQDqnglILGYKVLYcaKDLDPEPRSHVVRGNHTQSALLAGLRKFV 1264
Cdd:COG3401   319 SVTTDLTPP-AAPSGLTATAVGSSSITLSWTASSDAD----VTGYNVYR--STSGGGTYTKIAETVTTTSYTDTGLTPGT 391
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1265 VYELQVLAFTRIGNGVPSSPLILERTKDDTPG-----PPVRLVFPEVRLTAVRIVWQPPeePNGVILGYQIAYRLASGSP 1339
Cdd:COG3401   392 TYYYKVTAVDAAGNESAPSEEVSATTASAASGesltaSVDAVPLTDVAGATAAASAASN--PGVSAAVLADGGDTGNAVP 469
                         410
                  ....*....|....*....
gi 568938739 1340 HTFTTVEVGATVRQFTATE 1358
Cdd:COG3401   470 FTTTSSTVTATTTDTTTAN 488
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
889-971 3.11e-12

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: 64.44  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  889 PGAVGHLSFTEILDTSLKVSWQEPLERNGIIMGYQISWEVYGRNDSRLTHTLNSTMHEYKIQGLSSLTTYTIDVAALTAA 968
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                  ...
gi 568938739  969 GVG 971
Cdd:cd00063    81 GES 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
275-347 9.31e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.80  E-value: 9.31e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739   275 PIIVVAPGNRSVVAGSSeTTLECIANARPVEElsVHWKRNGVRLTSGLHS------YGRRLTITNPTSADTGMYVCEAT 347
Cdd:pfam13927    2 PVITVSPSSVTVREGET-VTLTCEATGSPPPT--ITWYKNGEPISSGSTRsrslsgSNSTLTISNVTRSDAGTYTCVAS 77
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
86-155 1.25e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 53.72  E-value: 1.25e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938739    86 PYFKTEPGlPQIHLEGNRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYKY--------IIPSLQKLDAGFYRCVVRN 155
Cdd:pfam13927    2 PVITVSPS-SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSlsgsnstlTISNVTRSDAGTYTCVASN 78
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
180-248 4.97e-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.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 49.56  E-value: 4.97e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568938739   180 QRKTVSQGHAALLNLlPIVSCPQPQVTWFREGHKIIPSSRIAITLENQ---LVILATTASDAGAYYVQAVNE 248
Cdd:pfam07679    8 KDVEVQEGESARFTC-TVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGtytLTISNVQPDDSGKYTCVATNS 78
 
Name Accession Description Interval E-value
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1436-1858 9.18e-22

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.39  E-value: 9.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1436 LPGGEWQTYSSSISHEATACAVERLRPFTSYKLRLKATNDIGDSDFSAETEAVTTLqdVPGEPPGSVSATPHTTSSVLIQ 1515
Cdd:COG3401   175 SATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPT--TPPSAPTGLTATADTPGSVTLS 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1516 WQPPRDESlnglLQGYRIYYRElesetgmspepktlkspsalraelTAQSSFKTVNSSSSlTTYELTHLKKYRRYEVIMT 1595
Cdd:COG3401   253 WDPVTESD----ATGYRVYRSN------------------------SGDGPFTKVATVTT-TSYTDTGLTNGTTYYYRVT 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1596 AYNIIG-ESPASVPVEVFVGEAAPAmAPQNVQVTPLTASQLEVTWDPpppeSQNGNIQGYKVYYWEADSrNETEKMKVLf 1674
Cdd:COG3401   304 AVDAAGnESAPSNVVSVTTDLTPPA-APSGLTATAVGSSSITLSWTA----SSDADVTGYNVYRSTSGG-GTYTKIAET- 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1675 LPEPVVKIKDLTSHTKYLISISAFNAAGD-GPKSDPCQGrTHQAAPGPPSFLAFSEITSTTLNVSWGEPSAAngilqgyR 1753
Cdd:COG3401   377 VTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSA-TTASAASGESLTASVDAVPLTDVAGATAAASA-------A 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1754 VVYEPLAPVQGVSKVVTVDVKGNWQRWLKVRDLTKGVTYFFRVQARTIAYGPELQANVTAGPAEGSPGSPRNVLVTKSAS 1833
Cdd:COG3401   449 SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTP 528
                         410       420
                  ....*....|....*....|....*
gi 568938739 1834 ELTLQWTEGNAGTTPTTGYVIEARP 1858
Cdd:COG3401   529 NVTGASPVTVGASTGDVLITDLVSL 553
I-set pfam07679
Immunoglobulin I-set domain;
397-487 6.08e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 86.16  E-value: 6.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvripRFMLLESGG---LRIAPVFIQDAGNYTCYAA 473
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD----RFKVTYEGGtytLTISNVQPDDSGKYTCVAT 76
                           90
                   ....*....|....
gi 568938739   474 NTEASVNASAMLTV 487
Cdd:pfam07679   77 NSAGEAEASAELTV 90
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
399-487 3.84e-18

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: 81.00  E-value: 3.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  399 FTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILAsgsVRIPRFMLLESGGLRIAPVFIQDAGNYTCYAANTEAS 478
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLL---GKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78

                  ....*....
gi 568938739  479 VNASAMLTV 487
Cdd:cd20952    79 ATWSAVLDV 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1621-1714 1.13e-17

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1621 APQNVQVTPLTASQLEVTWDPPPPEsqNGNIQGYKVYYWEADSrNETEKMKVLFLPEPVVKIKDLTSHTKYLISISAFNA 1700
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGS-GDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|....
gi 568938739 1701 AGDGPKSDPCQGRT 1714
Cdd:cd00063    80 GGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
587-672 1.56e-17

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 79.38  E-value: 1.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   587 PPQNLlaSLSPARSHSVTLSWVRPFDGNSPVLYYIVQVSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVNQV 666
Cdd:pfam00041    2 APSNL--TVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 568938739   667 GKGQYS 672
Cdd:pfam00041   80 GEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
585-676 1.93e-17

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  585 PHPPQNLlaSLSPARSHSVTLSWVRPFDGNSPVLYYIVQVSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVN 664
Cdd:cd00063     1 PSPPTNL--RVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|..
gi 568938739  665 QVGKGQYSTETS 676
Cdd:cd00063    79 GGGESPPSESVT 90
fn3 pfam00041
Fibronectin type III domain;
1621-1707 3.13e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.53  E-value: 3.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1621 APQNVQVTPLTASQLEVTWDPPPPesQNGNIQGYKVYYWEADSrNETEKMKVLFLPEPVVKIKDLTSHTKYLISISAFNA 1700
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNS-GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 568938739  1701 AGDGPKS 1707
Cdd:pfam00041   79 GGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1295-1388 1.50e-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: 73.68  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1295 PGPPVRLVFPEVRLTAVRIVWQPPEEPNGVILGYQIAYRLASGSPHTFTTVEVGaTVRQFTATELAPESAYIFRLSAKTR 1374
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|....
gi 568938739 1375 QGWGEPLEATVITT 1388
Cdd:cd00063    80 GGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
688-774 2.17e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 2.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   688 PPKNIVASGRTNQSIMVQWQPPPEteHNGVLRGYILRYRLAGLPGEHQQRNISSPEvNYCLVTDLIIWTQYEIQVAAYNG 767
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNSGEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 568938739   768 AGLGVFS 774
Cdd:pfam00041   79 GGEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
489-878 9.60e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.05  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  489 NRTSIVHPPEDRVVIKGTTATLCCGATHDPRTSLRYVWKKDNVVITASSSSRIVVEKDGSLVISQTWSGDIGD------- 561
Cdd:COG3401   126 TTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDiepgtty 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  562 -YTCEIISEGGSDSRTARLEVI---ELPHPPQNLLASlsPARSHSVTLSWVRPfdGNSPVLYYIVQVSENNSPWKVHLSN 637
Cdd:COG3401   206 yYRVAATDTGGESAPSNEVSVTtptTPPSAPTGLTAT--ADTPGSVTLSWDPV--TESDATGYRVYRSNSGDGPFTKVAT 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  638 VgpEMTGVTVSGLTPARTYQFRVCAVNQVG-KGQYSTETSrlMLPEEPPSAPPKNIVASGRTNQSIMVQWQPPPetehNG 716
Cdd:COG3401   282 V--TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVS--VTTDLTPPAAPSGLTATAVGSSSITLSWTASS----DA 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  717 VLRGYILrYRLAGLPGEHQQRNISSPEVNYcLVTDLIIWTQYEIQVAAYNGAGL-GVFSRAVTEYTLQGVPTAPPQNVQA 795
Cdd:COG3401   354 DVTGYNV-YRSTSGGGTYTKIAETVTTTSY-TDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVD 431
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  796 EAVNSTTVHFLW-----NPPPQQFINGINQGYKLLAWPADAPETVTVVTIAPDFHGIHHGYITNLKKFTAYFTSVLCFTT 870
Cdd:COG3401   432 AVPLTDVAGATAaasaaSNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV 511

                  ....*...
gi 568938739  871 PGDGPPSS 878
Cdd:COG3401   512 IGASAAAA 519
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1820-1913 1.87e-14

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: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1820 PGSPRNVLVTK-SASELTLQWTEGNAGTTPTTGYVIEARPSDEGLWDMFAKDIPrSATSYTVDldKLRQGVTYEFRVVAV 1898
Cdd:cd00063     1 PSPPTNLRVTDvTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG-SETSYTLT--GLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*
gi 568938739 1899 NKAGFGEPSRPSIAV 1913
Cdd:cd00063    78 NGGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
585-669 2.19e-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: 70.34  E-value: 2.19e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    585 PHPPQNLlaSLSPARSHSVTLSWVRPFDGN--SPVLYYIVQVSENNSPWKVHlsNVGPEMTGVTVSGLTPARTYQFRVCA 662
Cdd:smart00060    1 PSPPSNL--RVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREEGSEWKEV--NVTPSSTSYTLTGLKPGTEYEFRVRA 76

                    ....*..
gi 568938739    663 VNQVGKG 669
Cdd:smart00060   77 VNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1621-1704 6.40e-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: 68.80  E-value: 6.40e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1621 APQNVQVTPLTASQLEVTWDPPPPESQNGNIQGYKVYYWEADSRNETEKMKVlflPEPVVKIKDLTSHTKYLISISAFNA 1700
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTP---SSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 568938739   1701 AGDG 1704
Cdd:smart00060   80 AGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
403-487 6.43e-14

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: 69.07  E-value: 6.43e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    403 PVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvriPRFMLLESGG---LRIAPVFIQDAGNYTCYAANTEASV 479
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES---GRFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSA 77

                    ....*...
gi 568938739    480 NASAMLTV 487
Cdd:smart00410   78 SSGTTLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
957-1358 2.06e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.81  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  957 TYTIDVAALTAAGVGVTTSSTISSGVPPDLPGAPSNLVISNISPRSATLQFRPGYDGKTAICRWIVEGQVGAIGDEEEWV 1036
Cdd:COG3401    90 TATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVV 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1037 T-----------LYEEENEPDAQMLEIPNLTPYTHYRFRMRQVNIVGPSPFSQSSRVIQTLQAPpdVAPTSLTVRTASET 1105
Cdd:COG3401   170 VspdtsataavaTTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPP--SAPTGLTATADTPG 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1106 SLRLRWVPlpdsqyNGNPESVGYRVKywRSDQPSSALAQVVSDRlERELTIEELEEWTEYELRMQAFNAIG-AGPWSELV 1184
Cdd:COG3401   248 SVTLSWDP------VTESDATGYRVY--RSNSGDGPFTKVATVT-TTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVV 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1185 RGRTRESVPsAAPENVSAEAVSSTQILLTWASVPEQDqnglILGYKVLYcaKDLDPEPRSHVVRGNHTQSALLAGLRKFV 1264
Cdd:COG3401   319 SVTTDLTPP-AAPSGLTATAVGSSSITLSWTASSDAD----VTGYNVYR--STSGGGTYTKIAETVTTTSYTDTGLTPGT 391
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1265 VYELQVLAFTRIGNGVPSSPLILERTKDDTPG-----PPVRLVFPEVRLTAVRIVWQPPeePNGVILGYQIAYRLASGSP 1339
Cdd:COG3401   392 TYYYKVTAVDAAGNESAPSEEVSATTASAASGesltaSVDAVPLTDVAGATAAASAASN--PGVSAAVLADGGDTGNAVP 469
                         410
                  ....*....|....*....
gi 568938739 1340 HTFTTVEVGATVRQFTATE 1358
Cdd:COG3401   470 FTTTSSTVTATTTDTTTAN 488
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
688-781 3.50e-13

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: 67.14  E-value: 3.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  688 PPKNIVASGRTNQSIMVQWQPPPETehNGVLRGYILRYRLAGlPGEHQQRNISSPEVNYCLVTDLIIWTQYEIQVAAYNG 767
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKG-SGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|....
gi 568938739  768 AGLGVFSRAVTEYT 781
Cdd:cd00063    80 GGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
1821-1907 5.85e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.28  E-value: 5.85e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1821 GSPRNVLVT-KSASELTLQWTEGNAGTTPTTGYVIEARPSDEGlWDMFAKDIPRSATSYTVDldKLRQGVTYEFRVVAVN 1899
Cdd:pfam00041    1 SAPSNLTVTdVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLT--GLKPGTEYEVRVQAVN 77

                   ....*...
gi 568938739  1900 KAGFGEPS 1907
Cdd:pfam00041   78 GGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
889-971 3.11e-12

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: 64.44  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  889 PGAVGHLSFTEILDTSLKVSWQEPLERNGIIMGYQISWEVYGRNDSRLTHTLNSTMHEYKIQGLSSLTTYTIDVAALTAA 968
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                  ...
gi 568938739  969 GVG 971
Cdd:cd00063    81 GES 83
fn3 pfam00041
Fibronectin type III domain;
890-971 4.54e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 4.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   890 GAVGHLSFTEILDTSLKVSWQEPLERNGIIMGYQISWEVYGRNDSRLTHTLNSTMHEYKIQGLSSLTTYTIDVAALTAAG 969
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ..
gi 568938739   970 VG 971
Cdd:pfam00041   81 EG 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
688-771 5.91e-12

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: 63.40  E-value: 5.91e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    688 PPKNIVASGRTNQSIMVQWQPPPETEHNgvlrGYILRYRLAGLPGEHQQRNIS-SPEVNYCLVTDLIIWTQYEIQVAAYN 766
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGIT----GYIVGYRVEYREEGSEWKEVNvTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 568938739    767 GAGLG 771
Cdd:smart00060   79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
1196-1282 7.98e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 7.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1196 APENVSAEAVSSTQILLTWAsvPEQDQNGLILGYKVLYCAKDlDPEPRSHVVRGNHTQSALLAGLRKFVVYELQVLAFTR 1275
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWT--PPPDGNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 568938739  1276 IGNGVPS 1282
Cdd:pfam00041   79 GGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1196-1284 9.69e-11

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: 60.20  E-value: 9.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1196 APENVSAEAVSSTQILLTWasVPEQDQNGLILGYKVLYCAKDlDPEPRSHVVRGNHTQSALLAGLRKFVVYELQVLAFTR 1275
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSW--TPPEDDGGPITGYVVEYREKG-SGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*....
gi 568938739 1276 IGNGVPSSP 1284
Cdd:cd00063    80 GGESPPSES 88
fn3 pfam00041
Fibronectin type III domain;
1296-1380 1.03e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1296 GPPVRLVFPEVRLTAVRIVWQPPEEPNGVILGYQIAYRlASGSPHTFTTVEVGATVRQFTATELAPESAYIFRLSAKTRQ 1375
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR-PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*
gi 568938739  1376 GWGEP 1380
Cdd:pfam00041   80 GEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1295-1378 2.71e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.39  E-value: 2.71e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1295 PGPPVRLVFPEVRLTAVRIVWQPPEEPNGV--ILGYQIAYRlasGSPHTFTTVEVGATVRQFTATELAPESAYIFRLSAK 1372
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYR---EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 568938739   1373 TRQGWG 1378
Cdd:smart00060   78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
889-971 2.90e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.39  E-value: 2.90e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    889 PGAVGHLSFTEILDTSLKVSWQEPLERNGIimGYQISWEVYGRNDSRLTHTLNST--MHEYKIQGLSSLTTYTIDVAALT 966
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGSEWKEVNVTpsSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 568938739    967 AAGVG 971
Cdd:smart00060   79 GAGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
275-347 9.31e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.80  E-value: 9.31e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739   275 PIIVVAPGNRSVVAGSSeTTLECIANARPVEElsVHWKRNGVRLTSGLHS------YGRRLTITNPTSADTGMYVCEAT 347
Cdd:pfam13927    2 PVITVSPSSVTVREGET-VTLTCEATGSPPPT--ITWYKNGEPISSGSTRsrslsgSNSTLTISNVTRSDAGTYTCVAS 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1820-1904 1.30e-09

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: 56.47  E-value: 1.30e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1820 PGSPRNVLVTK-SASELTLQWT--EGNAGTTPTTGYVIEARPSDEGlWdmfaKDIPRSATSYTVDLDKLRQGVTYEFRVV 1896
Cdd:smart00060    1 PSPPSNLRVTDvTSTSVTLSWEppPDDGITGYIVGYRVEYREEGSE-W----KEVNVTPSSTSYTLTGLKPGTEYEFRVR 75

                    ....*...
gi 568938739   1897 AVNKAGFG 1904
Cdd:smart00060   76 AVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
789-884 4.56e-09

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: 55.58  E-value: 4.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  789 PPQNVQAEAVNSTTVHFLWNPPPqqFINGINQGYKLLAWPADAPETVTVVTIAPDFHGIHhgyITNLKKFTAYFTSVLCF 868
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT---LTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*.
gi 568938739  869 TTPGDGPPSSPQLVWT 884
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
492-581 7.05e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.57  E-value: 7.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   492 SIVHPPEDRVVIKGTTATLCCGATHDPRTSLryVWKKDNVVItaSSSSRIVVEKDG---SLVISQTWSGDIGDYTCEIIS 568
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEV--SWFKDGQPL--RSSDRFKVTYEGgtyTLTISNVQPDDSGKYTCVATN 77
                           90
                   ....*....|...
gi 568938739   569 EGGSDSRTARLEV 581
Cdd:pfam07679   78 SAGEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1196-1279 9.85e-09

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: 54.16  E-value: 9.85e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1196 APENVSAEAVSSTQILLTWASVPEQDQNGLILGYKVLYCAKDldpEPRSHVVRGNHTQSALLAGLRKFVVYELQVLAFTR 1275
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEG---SEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 568938739   1276 IGNG 1279
Cdd:smart00060   80 AGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
86-155 1.25e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 53.72  E-value: 1.25e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938739    86 PYFKTEPGlPQIHLEGNRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYKY--------IIPSLQKLDAGFYRCVVRN 155
Cdd:pfam13927    2 PVITVSPS-SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSlsgsnstlTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
100-169 1.19e-07

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: 50.97  E-value: 1.19e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739    100 EGNRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYK---------YIIPSLQKLDAGFYRCVVRNRMGallQRKSEIQV 169
Cdd:smart00410    8 EGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSvsrsgststLTISNVTPEDSGTYTCAATNSSG---SASSGTTL 83
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
86-171 3.92e-07

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first 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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 49.93  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   86 PYFKTEPG---LPQIHLEGnRLVLTCLAEGSWPLEFKWIRNDSELT-TYSSEYKYII-------PSLQKlDAGFYRCVVR 154
Cdd:cd04967     2 PVFEEQPDdtiFPEDSDEK-KVALNCRARANPVPSYRWLMNGTEIDlESDYRYSLVDgtlvisnPSKAK-DAGHYQCLAT 79
                          90
                  ....*....|....*..
gi 568938739  155 NRMGALLQRKSEIQVAY 171
Cdd:cd04967    80 NTVGSVLSREATLQFGY 96
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
497-581 4.00e-07

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: 49.81  E-value: 4.00e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    497 PEDRVVIKGTTATLCCGATHDPRTSLRYVWKKDNVVItasSSSRIVVEKDG---SLVISQTWSGDIGDYTCEIISEGGSD 573
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLA---ESGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSA 77

                    ....*...
gi 568938739    574 SRTARLEV 581
Cdd:smart00410   78 SSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
180-248 4.97e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 49.56  E-value: 4.97e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568938739   180 QRKTVSQGHAALLNLlPIVSCPQPQVTWFREGHKIIPSSRIAITLENQ---LVILATTASDAGAYYVQAVNE 248
Cdd:pfam07679    8 KDVEVQEGESARFTC-TVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGtytLTISNVQPDDSGKYTCVATNS 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
294-347 1.37e-06

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: 47.71  E-value: 1.37e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  294 TLECIANARPveELSVHWKRNGVRLTSGLHSYGRR------LTITNPTSADTGMYVCEAT 347
Cdd:cd00096     2 TLTCSASGNP--PPTITWYKNGKPLPPSSRDSRRSelgngtLTISNVTLEDSGTYTCVAS 59
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
175-256 1.73e-06

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: 47.88  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  175 FMDTDQRKTVSQGHAALLNLlPIVSCPQPQVTWFREGHKIIPSSRIAITLEN----QLVILATTASDAGAYYVQAVNEKn 250
Cdd:cd05744     3 FLQAPGDLEVQEGRLCRFDC-KVSGLPTPDLFWQLNGKPVRPDSAHKMLVREngrhSLIIEPVTKRDAGIYTCIARNRA- 80

                  ....*.
gi 568938739  251 GENKTS 256
Cdd:cd05744    81 GENSFN 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
281-357 4.94e-06

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: 46.73  E-value: 4.94e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    281 PGNRSVVAGSSeTTLECIANARPveELSVHWKRNGVRL------TSGLHSYGR-RLTITNPTSADTGMYVCEATL-RGST 352
Cdd:smart00410    1 PPSVTVKEGES-VTLSCEASGSP--PPEVTWYKQGGKLlaesgrFSVSRSGSTsTLTISNVTPEDSGTYTCAATNsSGSA 77

                    ....*
gi 568938739    353 FEPAR 357
Cdd:smart00410   78 SSGTT 82
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
183-263 3.51e-04

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: 41.34  E-value: 3.51e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    183 TVSQGHAALLnllpivSC-----PQPQVTWFREGHK-IIPSSRIAITLENQ---LVILATTASDAGAYYVQAVNEKNGEN 253
Cdd:smart00410    5 TVKEGESVTL------SCeasgsPPPEVTWYKQGGKlLAESGRFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSAS 78
                            90
                    ....*....|
gi 568938739    254 KTspfIHLSV 263
Cdd:smart00410   79 SG---TTLTV 85
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
585-729 6.48e-03

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 41.85  E-value: 6.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  585 PHPPQNLLASLSPARSHSV----------TLSWVRPfdgnSPVLYYIVQVSENNSPWkVHLSNVGPemTGVTVSGLtPAR 654
Cdd:COG4733   526 DVPPQWPPVNVTTSESLSVvaqgtavttlTVSWDAP----AGAVAYEVEWRRDDGNW-VSVPRTSG--TSFEVPGI-YAG 597
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938739  655 TYQFRVCAVN---QVGKGQYSTETSrLMLPEEPPSAPPkNIVASGRTNQsIMVQWQPPPETEhngvLRGYILRYRLAG 729
Cdd:COG4733   598 DYEVRVRAINalgVSSAWAASSETT-VTGKTAPPPAPT-GLTATGGLGG-ITLSWSFPVDAD----TLRTEIRYSTTG 668
 
Name Accession Description Interval E-value
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1436-1858 9.18e-22

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.39  E-value: 9.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1436 LPGGEWQTYSSSISHEATACAVERLRPFTSYKLRLKATNDIGDSDFSAETEAVTTLqdVPGEPPGSVSATPHTTSSVLIQ 1515
Cdd:COG3401   175 SATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPT--TPPSAPTGLTATADTPGSVTLS 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1516 WQPPRDESlnglLQGYRIYYRElesetgmspepktlkspsalraelTAQSSFKTVNSSSSlTTYELTHLKKYRRYEVIMT 1595
Cdd:COG3401   253 WDPVTESD----ATGYRVYRSN------------------------SGDGPFTKVATVTT-TSYTDTGLTNGTTYYYRVT 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1596 AYNIIG-ESPASVPVEVFVGEAAPAmAPQNVQVTPLTASQLEVTWDPpppeSQNGNIQGYKVYYWEADSrNETEKMKVLf 1674
Cdd:COG3401   304 AVDAAGnESAPSNVVSVTTDLTPPA-APSGLTATAVGSSSITLSWTA----SSDADVTGYNVYRSTSGG-GTYTKIAET- 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1675 LPEPVVKIKDLTSHTKYLISISAFNAAGD-GPKSDPCQGrTHQAAPGPPSFLAFSEITSTTLNVSWGEPSAAngilqgyR 1753
Cdd:COG3401   377 VTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSA-TTASAASGESLTASVDAVPLTDVAGATAAASA-------A 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1754 VVYEPLAPVQGVSKVVTVDVKGNWQRWLKVRDLTKGVTYFFRVQARTIAYGPELQANVTAGPAEGSPGSPRNVLVTKSAS 1833
Cdd:COG3401   449 SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTP 528
                         410       420
                  ....*....|....*....|....*
gi 568938739 1834 ELTLQWTEGNAGTTPTTGYVIEARP 1858
Cdd:COG3401   529 NVTGASPVTVGASTGDVLITDLVSL 553
I-set pfam07679
Immunoglobulin I-set domain;
397-487 6.08e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 86.16  E-value: 6.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvripRFMLLESGG---LRIAPVFIQDAGNYTCYAA 473
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD----RFKVTYEGGtytLTISNVQPDDSGKYTCVAT 76
                           90
                   ....*....|....
gi 568938739   474 NTEASVNASAMLTV 487
Cdd:pfam07679   77 NSAGEAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1531-1920 3.18e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 91.22  E-value: 3.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1531 YRIYYRELESETGMSPEPKTLKSPSALRAELTAQSSFKTVNSSSSLTTYELTHLKKYRRYEVIMTAYNIIGESPAS-VPV 1609
Cdd:COG3401    39 YLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSdEVP 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1610 EVFVGEAAPAMAPQNVQVTPLTASQLEVTWDP-PPPESQNGNIQGYKVYYWEADSRNETEKMKVLFLPEPVVKIKD---- 1684
Cdd:COG3401   119 SPAVGTATTATAVAGGAATAGTYALGAGLYGVdGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDgggd 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1685 LTSHTKYLISISAFNAAGDGPKSDPCQGRTHQAAPGPPSFLAFSEITSTTLNVSWgEPSAANGiLQGYRV--------VY 1756
Cdd:COG3401   199 IEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW-DPVTESD-ATGYRVyrsnsgdgPF 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1757 EPLAPVQGVSKVVTvdvkgnwqrwlkvrDLTKGVTYFFRVQARTIAYGPELQAN-VTAGPAEGSPGSPRNVLVT-KSASE 1834
Cdd:COG3401   277 TKVATVTTTSYTDT--------------GLTNGTTYYYRVTAVDAAGNESAPSNvVSVTTDLTPPAAPSGLTATaVGSSS 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1835 LTLQWTEgnAGTTPTTGYVIEARPSDEGLWDMFAKDIprSATSYTVdlDKLRQGVTYEFRVVAVNKAGFGepSRPSIAVS 1914
Cdd:COG3401   343 ITLSWTA--SSDADVTGYNVYRSTSGGGTYTKIAETV--TTTSYTD--TGLTPGTTYYYKVTAVDAAGNE--SAPSEEVS 414

                  ....*.
gi 568938739 1915 AQAEAP 1920
Cdd:COG3401   415 ATTASA 420
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
399-487 3.84e-18

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: 81.00  E-value: 3.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  399 FTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILAsgsVRIPRFMLLESGGLRIAPVFIQDAGNYTCYAANTEAS 478
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLL---GKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78

                  ....*....
gi 568938739  479 VNASAMLTV 487
Cdd:cd20952    79 ATWSAVLDV 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1621-1714 1.13e-17

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.85  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1621 APQNVQVTPLTASQLEVTWDPPPPEsqNGNIQGYKVYYWEADSrNETEKMKVLFLPEPVVKIKDLTSHTKYLISISAFNA 1700
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGS-GDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|....
gi 568938739 1701 AGDGPKSDPCQGRT 1714
Cdd:cd00063    80 GGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
587-672 1.56e-17

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 79.38  E-value: 1.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   587 PPQNLlaSLSPARSHSVTLSWVRPFDGNSPVLYYIVQVSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVNQV 666
Cdd:pfam00041    2 APSNL--TVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 568938739   667 GKGQYS 672
Cdd:pfam00041   80 GEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
585-676 1.93e-17

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 79.08  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  585 PHPPQNLlaSLSPARSHSVTLSWVRPFDGNSPVLYYIVQVSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVN 664
Cdd:cd00063     1 PSPPTNL--RVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                          90
                  ....*....|..
gi 568938739  665 QVGKGQYSTETS 676
Cdd:cd00063    79 GGGESPPSESVT 90
fn3 pfam00041
Fibronectin type III domain;
1621-1707 3.13e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.53  E-value: 3.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1621 APQNVQVTPLTASQLEVTWDPPPPesQNGNIQGYKVYYWEADSrNETEKMKVLFLPEPVVKIKDLTSHTKYLISISAFNA 1700
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNS-GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 568938739  1701 AGDGPKS 1707
Cdd:pfam00041   79 GGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1295-1388 1.50e-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: 73.68  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1295 PGPPVRLVFPEVRLTAVRIVWQPPEEPNGVILGYQIAYRLASGSPHTFTTVEVGaTVRQFTATELAPESAYIFRLSAKTR 1374
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|....
gi 568938739 1375 QGWGEPLEATVITT 1388
Cdd:cd00063    80 GGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
688-774 2.17e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 2.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   688 PPKNIVASGRTNQSIMVQWQPPPEteHNGVLRGYILRYRLAGLPGEHQQRNISSPEvNYCLVTDLIIWTQYEIQVAAYNG 767
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNSGEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 568938739   768 AGLGVFS 774
Cdd:pfam00041   79 GGEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1266-1516 7.87e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.05  E-value: 7.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1266 YELQVLAFTRIGNGVPSSPlILERTKDDTPGPPVRLVFPEVRLTAVRIVWQPPEEPNgvILGYQIaYRlASGSPHTFTTV 1345
Cdd:COG3401   205 YYYRVAATDTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRV-YR-SNSGDGPFTKV 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1346 EVGATVRqFTATELAPESAYIFRLSAKTRQGWGEPLEATVITTEKRERPAPPRELLVpqAEVTARSLRLQWVPGSDgaSP 1425
Cdd:COG3401   280 ATVTTTS-YTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAAPSGLTA--TAVGSSSITLSWTASSD--AD 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1426 IRYFTVQVRELPGGEWQTYSSSISheATACAVERLRPFTSYKLRLKATNDIGDSDFSAETEAVTTLQDVPGEPPGSVSAT 1505
Cdd:COG3401   355 VTGYNVYRSTSGGGTYTKIAETVT--TTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDA 432
                         250
                  ....*....|.
gi 568938739 1506 PHTTSSVLIQW 1516
Cdd:COG3401   433 VPLTDVAGATA 443
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
489-878 9.60e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.05  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  489 NRTSIVHPPEDRVVIKGTTATLCCGATHDPRTSLRYVWKKDNVVITASSSSRIVVEKDGSLVISQTWSGDIGD------- 561
Cdd:COG3401   126 TTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDiepgtty 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  562 -YTCEIISEGGSDSRTARLEVI---ELPHPPQNLLASlsPARSHSVTLSWVRPfdGNSPVLYYIVQVSENNSPWKVHLSN 637
Cdd:COG3401   206 yYRVAATDTGGESAPSNEVSVTtptTPPSAPTGLTAT--ADTPGSVTLSWDPV--TESDATGYRVYRSNSGDGPFTKVAT 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  638 VgpEMTGVTVSGLTPARTYQFRVCAVNQVG-KGQYSTETSrlMLPEEPPSAPPKNIVASGRTNQSIMVQWQPPPetehNG 716
Cdd:COG3401   282 V--TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVS--VTTDLTPPAAPSGLTATAVGSSSITLSWTASS----DA 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  717 VLRGYILrYRLAGLPGEHQQRNISSPEVNYcLVTDLIIWTQYEIQVAAYNGAGL-GVFSRAVTEYTLQGVPTAPPQNVQA 795
Cdd:COG3401   354 DVTGYNV-YRSTSGGGTYTKIAETVTTTSY-TDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVD 431
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  796 EAVNSTTVHFLW-----NPPPQQFINGINQGYKLLAWPADAPETVTVVTIAPDFHGIHHGYITNLKKFTAYFTSVLCFTT 870
Cdd:COG3401   432 AVPLTDVAGATAaasaaSNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV 511

                  ....*...
gi 568938739  871 PGDGPPSS 878
Cdd:COG3401   512 IGASAAAA 519
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1394-1489 9.72e-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: 71.37  E-value: 9.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1394 PAPPRELLVpqAEVTARSLRLQWVPGSDGASPIRYFTVQVRELPGGEWQTYSSSISHEaTACAVERLRPFTSYKLRLKAT 1473
Cdd:cd00063     1 PSPPTNLRV--TDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*.
gi 568938739 1474 NDIGDSDFSAETEAVT 1489
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
402-487 1.18e-14

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: 70.89  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  402 RPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNhilasGSVRIPRFMLLESGGLRIAPVFIQDAGNYTCYAANTEASVNA 481
Cdd:cd05725     3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKED-----GELPKGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEA 77

                  ....*.
gi 568938739  482 SAMLTV 487
Cdd:cd05725    78 SATLTV 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1820-1913 1.87e-14

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: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1820 PGSPRNVLVTK-SASELTLQWTEGNAGTTPTTGYVIEARPSDEGLWDMFAKDIPrSATSYTVDldKLRQGVTYEFRVVAV 1898
Cdd:cd00063     1 PSPPTNLRVTDvTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG-SETSYTLT--GLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*
gi 568938739 1899 NKAGFGEPSRPSIAV 1913
Cdd:cd00063    78 NGGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
585-669 2.19e-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: 70.34  E-value: 2.19e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    585 PHPPQNLlaSLSPARSHSVTLSWVRPFDGN--SPVLYYIVQVSENNSPWKVHlsNVGPEMTGVTVSGLTPARTYQFRVCA 662
Cdd:smart00060    1 PSPPSNL--RVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREEGSEWKEV--NVTPSSTSYTLTGLKPGTEYEFRVRA 76

                    ....*..
gi 568938739    663 VNQVGKG 669
Cdd:smart00060   77 VNGAGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
397-474 2.90e-14

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 69.52  E-value: 2.90e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938739   397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRiPRFMLLESGGLRIAPVFIQDAGNYTCYAAN 474
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTR-SRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1621-1704 6.40e-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: 68.80  E-value: 6.40e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1621 APQNVQVTPLTASQLEVTWDPPPPESQNGNIQGYKVYYWEADSRNETEKMKVlflPEPVVKIKDLTSHTKYLISISAFNA 1700
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTP---SSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 568938739   1701 AGDG 1704
Cdd:smart00060   80 AGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
403-487 6.43e-14

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: 69.07  E-value: 6.43e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    403 PVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvriPRFMLLESGG---LRIAPVFIQDAGNYTCYAANTEASV 479
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES---GRFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSA 77

                    ....*...
gi 568938739    480 NASAMLTV 487
Cdd:smart00410   78 SSGTTLTV 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
397-487 6.97e-14

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: 69.06  E-value: 6.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRIprfMLLESGG---LRIAPVFIQDAGNYTCYAA 473
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHK---MLVRENGrhsLIIEPVTKRDAGIYTCIAR 77
                          90
                  ....*....|....
gi 568938739  474 NTEASVNASAMLTV 487
Cdd:cd05744    78 NRAGENSFNAELVV 91
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
397-487 7.01e-14

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: 69.03  E-value: 7.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVD--TTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvripRFMLLESGGLRIAPVFIQDAGNYTCYAAN 474
Cdd:cd04969     1 PDFELNPVKkkILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSS----RICILPDGSLKIKNVTKSDEGKYTCFAVN 76
                          90
                  ....*....|...
gi 568938739  475 TEASVNASAMLTV 487
Cdd:cd04969    77 FFGKANSTGSLSV 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
957-1358 2.06e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.81  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  957 TYTIDVAALTAAGVGVTTSSTISSGVPPDLPGAPSNLVISNISPRSATLQFRPGYDGKTAICRWIVEGQVGAIGDEEEWV 1036
Cdd:COG3401    90 TATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVV 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1037 T-----------LYEEENEPDAQMLEIPNLTPYTHYRFRMRQVNIVGPSPFSQSSRVIQTLQAPpdVAPTSLTVRTASET 1105
Cdd:COG3401   170 VspdtsataavaTTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPP--SAPTGLTATADTPG 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1106 SLRLRWVPlpdsqyNGNPESVGYRVKywRSDQPSSALAQVVSDRlERELTIEELEEWTEYELRMQAFNAIG-AGPWSELV 1184
Cdd:COG3401   248 SVTLSWDP------VTESDATGYRVY--RSNSGDGPFTKVATVT-TTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVV 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1185 RGRTRESVPsAAPENVSAEAVSSTQILLTWASVPEQDqnglILGYKVLYcaKDLDPEPRSHVVRGNHTQSALLAGLRKFV 1264
Cdd:COG3401   319 SVTTDLTPP-AAPSGLTATAVGSSSITLSWTASSDAD----VTGYNVYR--STSGGGTYTKIAETVTTTSYTDTGLTPGT 391
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1265 VYELQVLAFTRIGNGVPSSPLILERTKDDTPG-----PPVRLVFPEVRLTAVRIVWQPPeePNGVILGYQIAYRLASGSP 1339
Cdd:COG3401   392 TYYYKVTAVDAAGNESAPSEEVSATTASAASGesltaSVDAVPLTDVAGATAAASAASN--PGVSAAVLADGGDTGNAVP 469
                         410
                  ....*....|....*....
gi 568938739 1340 HTFTTVEVGATVRQFTATE 1358
Cdd:COG3401   470 FTTTSSTVTATTTDTTTAN 488
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
688-781 3.50e-13

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: 67.14  E-value: 3.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  688 PPKNIVASGRTNQSIMVQWQPPPETehNGVLRGYILRYRLAGlPGEHQQRNISSPEVNYCLVTDLIIWTQYEIQVAAYNG 767
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKG-SGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                          90
                  ....*....|....
gi 568938739  768 AGLGVFSRAVTEYT 781
Cdd:cd00063    80 GGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
1821-1907 5.85e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.28  E-value: 5.85e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1821 GSPRNVLVT-KSASELTLQWTEGNAGTTPTTGYVIEARPSDEGlWDMFAKDIPRSATSYTVDldKLRQGVTYEFRVVAVN 1899
Cdd:pfam00041    1 SAPSNLTVTdVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLT--GLKPGTEYEVRVQAVN 77

                   ....*...
gi 568938739  1900 KAGFGEPS 1907
Cdd:pfam00041   78 GGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1719-1800 2.34e-12

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: 64.83  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1719 PGPPSFLAFSEITSTTLNVSWGEPSAANGILQGYRVVYEPLapvqGVSKVVTVDVKGNWQRWLKVRDLTKGVTYFFRVQA 1798
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREK----GSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                  ..
gi 568938739 1799 RT 1800
Cdd:cd00063    77 VN 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
889-971 3.11e-12

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: 64.44  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  889 PGAVGHLSFTEILDTSLKVSWQEPLERNGIIMGYQISWEVYGRNDSRLTHTLNSTMHEYKIQGLSSLTTYTIDVAALTAA 968
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                  ...
gi 568938739  969 GVG 971
Cdd:cd00063    81 GES 83
fn3 pfam00041
Fibronectin type III domain;
890-971 4.54e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 4.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   890 GAVGHLSFTEILDTSLKVSWQEPLERNGIIMGYQISWEVYGRNDSRLTHTLNSTMHEYKIQGLSSLTTYTIDVAALTAAG 969
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ..
gi 568938739   970 VG 971
Cdd:pfam00041   81 EG 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
850-1137 4.88e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 71.19  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  850 GYITNLKKFTAYFTSVLCFTTPGDGPPSSPQLVWTHEDKPGAVGHLSFTEILDTSLKVSWQEPLERNgiIMGYQISWEVY 929
Cdd:COG3401   194 DGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNS 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  930 GRNDSRLTHTLNSTmhEYKIQGLSSLTTYTIDVAALTAAGVGVTTSSTISSGVPPDLPGAPSNLVISNISPRSATLQFRP 1009
Cdd:COG3401   272 GDGPFTKVATVTTT--SYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTA 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1010 GYDGKTAicRWIVEGQVGAIGdeeEWVTLYEEENEPdaqMLEIPNLTPYTHYRFRMRQVNIVGPSPFSQSSRVIQTLQAP 1089
Cdd:COG3401   350 SSDADVT--GYNVYRSTSGGG---TYTKIAETVTTT---SYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAA 421
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568938739 1090 PDVAPTSLTVRTASET------SLRLRWVPLPDSQYNGNPESVGYRVKYWRSDQ 1137
Cdd:COG3401   422 SGESLTASVDAVPLTDvagataAASAASNPGVSAAVLADGGDTGNAVPFTTTSS 475
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
688-771 5.91e-12

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: 63.40  E-value: 5.91e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    688 PPKNIVASGRTNQSIMVQWQPPPETEHNgvlrGYILRYRLAGLPGEHQQRNIS-SPEVNYCLVTDLIIWTQYEIQVAAYN 766
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGIT----GYIVGYRVEYREEGSEWKEVNvTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 568938739    767 GAGLG 771
Cdd:smart00060   79 GAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1497-1611 6.45e-12

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: 63.67  E-value: 6.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1497 EPPGSVSATPHTTSSVLIQWQPPRDEslNGLLQGYRIYYRELESETGMSPEPKTLKSpsalraeltaqssfktvnssssl 1576
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGSGDWKEVEVTPGSE----------------------- 56
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568938739 1577 TTYELTHLKKYRRYEVIMTAYNIIGESPASVPVEV 1611
Cdd:cd00063    57 TSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVTV 91
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
400-475 7.42e-12

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: 63.03  E-value: 7.42e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568938739  400 TQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvripRFMLLESGGLRIAPVFIQDAGNYTCYAANT 475
Cdd:cd20968     3 TRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENN----RIAVLESGSLRIHNVQKEDAGQYRCVAKNS 74
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
398-487 9.03e-12

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: 63.02  E-value: 9.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  398 AFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKR--GNHILASGSVRIprFMLLESGGLRIAPVFIQDAGNYTCYAANT 475
Cdd:cd05763     1 SFTKTPHDITIRAGSTARLECAATGHPTPQIAWQKdgGTDFPAARERRM--HVMPEDDVFFIVDVKIEDTGVYSCTAQNS 78
                          90
                  ....*....|..
gi 568938739  476 EASVNASAMLTV 487
Cdd:cd05763    79 AGSISANATLTV 90
fn3 pfam00041
Fibronectin type III domain;
1720-1806 1.11e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 1.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1720 GPPSFLAFSEITSTTLNVSWGEPSAANGILQGYRVVYEplaPVQGVSKVVTVDVKGNwQRWLKVRDLTKGVTYFFRVQAR 1799
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR---PKNSGEPWNEITVPGT-TTSVTLTGLKPGTEYEVRVQAV 76

                   ....*...
gi 568938739  1800 T-IAYGPE 1806
Cdd:pfam00041   77 NgGGEGPP 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
414-474 1.51e-11

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: 61.58  E-value: 1.51e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938739  414 AVLRCEVSGAPKPAITWKRGNHILASgSVRIPRFMLLESGGLRIAPVFIQDAGNYTCYAAN 474
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPP-SSRDSRRSELGNGTLTISNVTLEDSGTYTCVASN 60
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
397-487 4.28e-11

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: 60.87  E-value: 4.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRP-VDTTVTDGMTAVLRCEVSGAPKPAITW-KRGNHIlasgSVRIPRFmLLESGGLRIAPVFIQDAGNYTCYAAN 474
Cdd:cd20978     1 PKFIQKPeKNVVVKGGQDVTLPCQVTGVPQPKITWlHNGKPL----QGPMERA-TVEDGTLTIINVQPEDTGYYGCVATN 75
                          90
                  ....*....|...
gi 568938739  475 TEASVNASAMLTV 487
Cdd:cd20978    76 EIGDIYTETLLHV 88
fn3 pfam00041
Fibronectin type III domain;
1196-1282 7.98e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 7.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1196 APENVSAEAVSSTQILLTWAsvPEQDQNGLILGYKVLYCAKDlDPEPRSHVVRGNHTQSALLAGLRKFVVYELQVLAFTR 1275
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWT--PPPDGNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 568938739  1276 IGNGVPS 1282
Cdd:pfam00041   79 GGEGPPS 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
396-487 8.18e-11

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: 60.34  E-value: 8.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  396 APAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRIPRFMLLesGGLRIAPVFIQDAGNYTCYAANT 475
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGV--GELHIQDVLPEDHGTYTCLAKNA 78
                          90
                  ....*....|..
gi 568938739  476 EASVNASAMLTV 487
Cdd:cd20976    79 AGQVSCSAWVTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1196-1284 9.69e-11

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: 60.20  E-value: 9.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1196 APENVSAEAVSSTQILLTWasVPEQDQNGLILGYKVLYCAKDlDPEPRSHVVRGNHTQSALLAGLRKFVVYELQVLAFTR 1275
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSW--TPPEDDGGPITGYVVEYREKG-SGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                  ....*....
gi 568938739 1276 IGNGVPSSP 1284
Cdd:cd00063    80 GGESPPSES 88
fn3 pfam00041
Fibronectin type III domain;
1296-1380 1.03e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1296 GPPVRLVFPEVRLTAVRIVWQPPEEPNGVILGYQIAYRlASGSPHTFTTVEVGATVRQFTATELAPESAYIFRLSAKTRQ 1375
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR-PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*
gi 568938739  1376 GWGEP 1380
Cdd:pfam00041   80 GEGPP 84
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
410-487 1.86e-10

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


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 58.80  E-value: 1.86e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938739  410 DGMTAVLRCEVSGAPKPAITWKRGNHILASGSvripRFMLLESGGLRIAPVFIQDAGNYTCYAANTEASVNASAMLTV 487
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDR----RHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
399-487 2.02e-10

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth 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: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 59.58  E-value: 2.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  399 FTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKR--GNHILASGSVRIP--RFMLLESGGLRIAPVFIQDAGNYTCYAAN 474
Cdd:cd05726     2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKegSQNLLFPYQPPQPssRFSVSPTGDLTITNVQRSDVGYYICQALN 81
                          90
                  ....*....|...
gi 568938739  475 TEASVNASAMLTV 487
Cdd:cd05726    82 VAGSILAKAQLEV 94
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1295-1378 2.71e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.39  E-value: 2.71e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1295 PGPPVRLVFPEVRLTAVRIVWQPPEEPNGV--ILGYQIAYRlasGSPHTFTTVEVGATVRQFTATELAPESAYIFRLSAK 1372
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYR---EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 568938739   1373 TRQGWG 1378
Cdd:smart00060   78 NGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
1498-1606 2.81e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 2.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1498 PPGSVSATPHTTSSVLIQWQPPRDesLNGLLQGYRIYYRELESETGMspepktlkspsalraeltaqssfKTVNSSSSLT 1577
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNSGEPW-----------------------NEITVPGTTT 56
                           90       100
                   ....*....|....*....|....*....
gi 568938739  1578 TYELTHLKKYRRYEVIMTAYNIIGESPAS 1606
Cdd:pfam00041   57 SVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
889-971 2.90e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.39  E-value: 2.90e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    889 PGAVGHLSFTEILDTSLKVSWQEPLERNGIimGYQISWEVYGRNDSRLTHTLNST--MHEYKIQGLSSLTTYTIDVAALT 966
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGSEWKEVNVTpsSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 568938739    967 AAGVG 971
Cdd:smart00060   79 GAGEG 83
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
397-487 3.00e-10

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: 58.86  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTV--TDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvripRFMLLESGGLRIAPVFIQDAGNYTCYAAN 474
Cdd:cd05852     1 PTFEFNPMKKKIlaAKGGRVIIECKPKAAPKPKFSWSKGTELLVNNS----RISIWDDGSLEILNITKLDEGSYTCFAEN 76
                          90
                  ....*....|...
gi 568938739  475 TEASVNASAMLTV 487
Cdd:cd05852    77 NRGKANSTGVLSV 89
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
401-487 5.19e-10

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 58.00  E-value: 5.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  401 QRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvRIPrfmlLESGGLRIAPVFIQDAGNYTCYAANTEASVN 480
Cdd:cd05728     4 KVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASEN-RIE----VEAGDLRITKLSLSDSGMYQCVAENKHGTIY 78

                  ....*..
gi 568938739  481 ASAMLTV 487
Cdd:cd05728    79 ASAELAV 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
987-1083 6.48e-10

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: 57.89  E-value: 6.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  987 PGAPSNLVISNISPRSATLQFRPGYDGKTAICRWIVEGQVGaigDEEEWVTLyeEENEPDAQMLEIPNLTPYTHYRFRMR 1066
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREK---GSGDWKEV--EVTPGSETSYTLTGLKPGTEYEFRVR 75
                          90
                  ....*....|....*..
gi 568938739 1067 QVNIVGPSPFSQSSRVI 1083
Cdd:cd00063    76 AVNGGGESPPSESVTVT 92
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
397-487 9.27e-10

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. 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: 409473  Cd Length: 92  Bit Score: 57.47  E-value: 9.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRIPrfMLLESGG---LRIAPVFIQDAGNYTCYAA 473
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRIS--LYQDNCGricLLIQNANKKDAGWYTVSAV 78
                          90
                  ....*....|....
gi 568938739  474 NTEASVNASAMLTV 487
Cdd:cd05892    79 NEAGVVSCNARLDV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
275-347 9.31e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.80  E-value: 9.31e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739   275 PIIVVAPGNRSVVAGSSeTTLECIANARPVEElsVHWKRNGVRLTSGLHS------YGRRLTITNPTSADTGMYVCEAT 347
Cdd:pfam13927    2 PVITVSPSSVTVREGET-VTLTCEATGSPPPT--ITWYKNGEPISSGSTRsrslsgSNSTLTISNVTRSDAGTYTCVAS 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1498-1603 9.83e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 56.85  E-value: 9.83e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1498 PPGSVSATPHTTSSVLIQWQPPRDESLNGLLQGYRIYYRELESEtgmspepktlkspsalraeltaqssFKTVNSSSSLT 1577
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSE-------------------------WKEVNVTPSST 57
                            90       100
                    ....*....|....*....|....*.
gi 568938739   1578 TYELTHLKKYRRYEVIMTAYNIIGES 1603
Cdd:smart00060   58 SYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1820-1904 1.30e-09

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: 56.47  E-value: 1.30e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1820 PGSPRNVLVTK-SASELTLQWT--EGNAGTTPTTGYVIEARPSDEGlWdmfaKDIPRSATSYTVDLDKLRQGVTYEFRVV 1896
Cdd:smart00060    1 PSPPSNLRVTDvTSTSVTLSWEppPDDGITGYIVGYRVEYREEGSE-W----KEVNVTPSSTSYTLTGLKPGTEYEFRVR 75

                    ....*...
gi 568938739   1897 AVNKAGFG 1904
Cdd:smart00060   76 AVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1719-1802 1.41e-09

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: 56.47  E-value: 1.41e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1719 PGPPSFLAFSEITSTTLNVSWGEPSAANGIlqGYRVVYEpLAPVQGVSKVVTVDVKGNwQRWLKVRDLTKGVTYFFRVQA 1798
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYR-VEYREEGSEWKEVNVTPS-STSYTLTGLKPGTEYEFRVRA 76

                    ....
gi 568938739   1799 RTIA 1802
Cdd:smart00060   77 VNGA 80
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
396-487 1.85e-09

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: 56.44  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  396 APAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKR-GNHILASgsvriPRFMLLESGGLR---IAPVFIQDAGNYTCY 471
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCeGKELQNS-----PDIQIHQEGDLHsliIAEAFEEDTGRYSCL 75
                          90
                  ....*....|....*.
gi 568938739  472 AANTEASVNASAMLTV 487
Cdd:cd20972    76 ATNSVGSDTTSAEIFV 91
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
399-487 2.16e-09

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: 56.19  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  399 FTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRIPRFMLLESgGLRIAPVFIQDAGNYTCYAANTEAS 478
Cdd:cd20949     2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILAD-GLLINKVTQDDTGEYTCRAYQVNSI 80

                  ....*....
gi 568938739  479 VNASAMLTV 487
Cdd:cd20949    81 ASDMQERTV 89
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
397-487 2.37e-09

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: 56.27  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRgNHILASGSVRIPRFMLLESGG---LRIAPVFIQDAGNYTCYAA 473
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYK-NGVPIDPSSIPGKYKIESEYGvhvLHIRRVTVEDSAVYSAVAK 79
                          90
                  ....*....|....
gi 568938739  474 NTEASVNASAMLTV 487
Cdd:cd20951    80 NIHGEASSSASVVV 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
789-884 4.56e-09

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: 55.58  E-value: 4.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  789 PPQNVQAEAVNSTTVHFLWNPPPqqFINGINQGYKLLAWPADAPETVTVVTIAPDFHGIHhgyITNLKKFTAYFTSVLCF 868
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT---LTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*.
gi 568938739  869 TTPGDGPPSSPQLVWT 884
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
988-1077 6.21e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.73  E-value: 6.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   988 GAPSNLVISNISPRSATLQFRPGYDGKTAICRWIVegQVGAIGDEEEWVtlyEEENEPDAQMLEIPNLTPYTHYRFRMRQ 1067
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEV--EYRPKNSGEPWN---EITVPGTTTSVTLTGLKPGTEYEVRVQA 75
                           90
                   ....*....|
gi 568938739  1068 VNIVGPSPFS 1077
Cdd:pfam00041   76 VNGGGEGPPS 85
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
497-581 6.24e-09

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. 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: 409387  Cd Length: 97  Bit Score: 55.18  E-value: 6.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  497 PEDRVVIKGTTATLCCGATHDPRTSLRyvWKKDNVVITASSSSRIVVEKDGSLVI-----SQTWSGDIGDYTCE--IISE 569
Cdd:cd05722     8 PSDIVAMRGGPVVLNCSAESDPPPKIE--WKKDGVLLNLVSDERRQQLPNGSLLItsvvhSKHNKPDEGFYQCVaqNESL 85
                          90
                  ....*....|..
gi 568938739  570 GGSDSRTARLEV 581
Cdd:cd05722    86 GSIVSRTARVTV 97
I-set pfam07679
Immunoglobulin I-set domain;
492-581 7.05e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.57  E-value: 7.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   492 SIVHPPEDRVVIKGTTATLCCGATHDPRTSLryVWKKDNVVItaSSSSRIVVEKDG---SLVISQTWSGDIGDYTCEIIS 568
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEV--SWFKDGQPL--RSSDRFKVTYEGgtyTLTISNVQPDDSGKYTCVATN 77
                           90
                   ....*....|...
gi 568938739   569 EGGSDSRTARLEV 581
Cdd:pfam07679   78 SAGEAEASAELTV 90
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
401-487 7.30e-09

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: 54.71  E-value: 7.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  401 QRPVDTTVTDGMTAVLRCEVS-GAPKPAITWKRGNHILASGSVRIprfMLLESGGLRIAPVFIQDAGNYTCYAANTE-AS 478
Cdd:cd05724     2 VEPSDTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLDNERV---RIVDDGNLLIAEARKSDEGTYKCVATNMVgER 78

                  ....*....
gi 568938739  479 VNASAMLTV 487
Cdd:cd05724    79 ESRAARLSV 87
fn3 pfam00041
Fibronectin type III domain;
1396-1482 7.55e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 7.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1396 PPRELLVpqAEVTARSLRLQWVPGSDGASPIRYFTVQVRELPGGE-WQTYssSISHEATACAVERLRPFTSYKLRLKATN 1474
Cdd:pfam00041    2 APSNLTV--TDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEpWNEI--TVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*...
gi 568938739  1475 DIGDSDFS 1482
Cdd:pfam00041   78 GGGEGPPS 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
492-565 9.43e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.11  E-value: 9.43e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568938739   492 SIVHPPEDRVVIKGTTATLCCGATHDPRTSlrYVWKKDNVVI-TASSSSRIVVEKDGSLVISQTWSGDIGDYTCE 565
Cdd:pfam13927    3 VITVSPSSVTVREGETVTLTCEATGSPPPT--ITWYKNGEPIsSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1196-1279 9.85e-09

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: 54.16  E-value: 9.85e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1196 APENVSAEAVSSTQILLTWASVPEQDQNGLILGYKVLYCAKDldpEPRSHVVRGNHTQSALLAGLRKFVVYELQVLAFTR 1275
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEG---SEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 568938739   1276 IGNG 1279
Cdd:smart00060   80 AGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
86-155 1.25e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 53.72  E-value: 1.25e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938739    86 PYFKTEPGlPQIHLEGNRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYKY--------IIPSLQKLDAGFYRCVVRN 155
Cdd:pfam13927    2 PVITVSPS-SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSlsgsnstlTISNVTRSDAGTYTCVASN 78
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
397-487 1.36e-08

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: 54.09  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWK-----RGNHILASGSVRiPRFMLLESGGLRIAPVFIQDAGNYTCY 471
Cdd:cd05765     1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEkqvpgKENLIMRPNHVR-GNVVVTNIGQLVIYNAQPQDAGLYTCT 79
                          90
                  ....*....|....*.
gi 568938739  472 AANTEASVNASAMLTV 487
Cdd:cd05765    80 ARNSGGLLRANFPLSV 95
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
397-487 2.49e-08

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


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 53.27  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWK----RGNHILASGSVRIPRFMLLESGGLRIAPVFIQDAGNYTCYA 472
Cdd:cd05734     2 PRFVVQPNDQDGIYGKAVVLNCSADGYPPPTIVWKhskgSGVPQFQHIVPLNGRIQLLSNGSLLIKHVLEEDSGYYLCKV 81
                          90
                  ....*....|....*.
gi 568938739  473 AN-TEASVNASAMLTV 487
Cdd:cd05734    82 SNdVGADISKSMYLTV 97
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
402-486 2.61e-08

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: 53.13  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  402 RPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvripRFMLLES---GGLRIAPVFIQDAGNYTCYAANTEAS 478
Cdd:cd05747     9 KPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQ----RHQITSTeykSTFEISKVQMSDEGNYTVVVENSEGK 84

                  ....*...
gi 568938739  479 VNASAMLT 486
Cdd:cd05747    85 QEAQFTLT 92
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
402-487 2.62e-08

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. 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: 409388  Cd Length: 84  Bit Score: 52.97  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  402 RPVDTTVTDGMTAVLRCEVSGAPKPAITWkrgnhiLASGSVRIPR--FMLLESGGLRIAPVFIQDAGNYTCYAANTEASV 479
Cdd:cd05723     3 KPSNIYAHESMDIVFECEVTGKPTPTVKW------VKNGDVVIPSdyFKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNA 76

                  ....*...
gi 568938739  480 NASAMLTV 487
Cdd:cd05723    77 QASAQLII 84
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
497-581 2.70e-08

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: 53.17  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  497 PEDRVVIKGTTATLCCGATH---DPRTSlryvWKKDNVVItASSSSRIVVEKDGSLVISQTWSGDIGDYTCEII-SEGGS 572
Cdd:cd05724     4 PSDTQVAVGEMAVLECSPPRghpEPTVS----WRKDGQPL-NLDNERVRIVDDGNLLIAEARKSDEGTYKCVATnMVGER 78

                  ....*....
gi 568938739  573 DSRTARLEV 581
Cdd:cd05724    79 ESRAARLSV 87
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
397-487 3.34e-08

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group 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.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 53.09  E-value: 3.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRgnhilASGSV--------RIPRFMLLESGGLRIAPVFIQDAGNY 468
Cdd:cd20954     2 PRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKK-----ATGSTpgeykdllYDPNVRILPNGTLVFGHVQKENEGHY 76
                          90       100
                  ....*....|....*....|
gi 568938739  469 TCYAANTEAS-VNASAMLTV 487
Cdd:cd20954    77 LCEAKNGIGSgLSKVIFLKV 96
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
403-485 4.05e-08

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 52.53  E-value: 4.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  403 PVDTTVTDGMTAVLRCEVSGAPKPAITW-KRGNHILASGSVRIprfmlLESGGLRIAPVFIQDAGNYTCYAANTEASVNA 481
Cdd:cd20957     8 PPVQTVDFGRTAVFNCSVTGNPIHTVLWmKDGKPLGHSSRVQI-----LSEDVLVIPSVKREDKGMYQCFVRNDGDSAQA 82

                  ....
gi 568938739  482 SAML 485
Cdd:cd20957    83 TAEL 86
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
397-487 4.95e-08

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. 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: 409582  Cd Length: 91  Bit Score: 52.41  E-value: 4.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRipRFMLLESG--GLRIAPVFIQDAGNYTCYAAN 474
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAH--KMLVRENGvhSLIIEPVTSRDAGIYTCIATN 78
                          90
                  ....*....|...
gi 568938739  475 TEASVNASAMLTV 487
Cdd:cd20990    79 RAGQNSFNLELVV 91
fn3 pfam00041
Fibronectin type III domain;
789-877 7.06e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 51.65  E-value: 7.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   789 PPQNVQAEAVNSTTVHFLWNPPPQQfiNGINQGYKLLAWPADAPETVTVVTIAPDfhgiHHGY-ITNLKKFTAYFTSVLC 867
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDG--NGPITGYEVEYRPKNSGEPWNEITVPGT----TTSVtLTGLKPGTEYEVRVQA 75
                           90
                   ....*....|
gi 568938739   868 FTTPGDGPPS 877
Cdd:pfam00041   76 VNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1394-1479 9.23e-08

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: 51.46  E-value: 9.23e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1394 PAPPRELLVpqAEVTARSLRLQWVPGSD--GASPIRYFTVQVRElPGGEWQTYSSSISHeaTACAVERLRPFTSYKLRLK 1471
Cdd:smart00060    1 PSPPSNLRV--TDVTSTSVTLSWEPPPDdgITGYIVGYRVEYRE-EGSEWKEVNVTPSS--TSYTLTGLKPGTEYEFRVR 75

                    ....*...
gi 568938739   1472 ATNDIGDS 1479
Cdd:smart00060   76 AVNGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
100-169 1.19e-07

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: 50.97  E-value: 1.19e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739    100 EGNRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYK---------YIIPSLQKLDAGFYRCVVRNRMGallQRKSEIQV 169
Cdd:smart00410    8 EGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSvsrsgststLTISNVTPEDSGTYTCAATNSSG---SASSGTTL 83
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
86-171 3.92e-07

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first 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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 49.93  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   86 PYFKTEPG---LPQIHLEGnRLVLTCLAEGSWPLEFKWIRNDSELT-TYSSEYKYII-------PSLQKlDAGFYRCVVR 154
Cdd:cd04967     2 PVFEEQPDdtiFPEDSDEK-KVALNCRARANPVPSYRWLMNGTEIDlESDYRYSLVDgtlvisnPSKAK-DAGHYQCLAT 79
                          90
                  ....*....|....*..
gi 568938739  155 NRMGALLQRKSEIQVAY 171
Cdd:cd04967    80 NTVGSVLSREATLQFGY 96
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
497-581 4.00e-07

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: 49.81  E-value: 4.00e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    497 PEDRVVIKGTTATLCCGATHDPRTSLRYVWKKDNVVItasSSSRIVVEKDG---SLVISQTWSGDIGDYTCEIISEGGSD 573
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLA---ESGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSA 77

                    ....*...
gi 568938739    574 SRTARLEV 581
Cdd:smart00410   78 SSGTTLTV 85
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
397-487 4.43e-07

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (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: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 49.78  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRIprfMLLESGGLRIAPVFIQDAGNYTCYAANTE 476
Cdd:cd05764     1 PLITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNSSRT---LVYDNGTLDILITTVKDTGAFTCIASNPA 77
                          90
                  ....*....|.
gi 568938739  477 ASVNASAMLTV 487
Cdd:cd05764    78 GEATARVELHI 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
987-1074 4.68e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.54  E-value: 4.68e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    987 PGAPSNLVISNISPRSATLQFRPGYDGKTA--ICRWIVEGQvgaiGDEEEWVTLyeeENEPDAQMLEIPNLTPYTHYRFR 1064
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYR----EEGSEWKEV---NVTPSSTSYTLTGLKPGTEYEFR 73
                            90
                    ....*....|
gi 568938739   1065 MRQVNIVGPS 1074
Cdd:smart00060   74 VRAVNGAGEG 83
I-set pfam07679
Immunoglobulin I-set domain;
180-248 4.97e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 49.56  E-value: 4.97e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568938739   180 QRKTVSQGHAALLNLlPIVSCPQPQVTWFREGHKIIPSSRIAITLENQ---LVILATTASDAGAYYVQAVNE 248
Cdd:pfam07679    8 KDVEVQEGESARFTC-TVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGtytLTISNVQPDDSGKYTCVATNS 78
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
401-474 5.90e-07

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). 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: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 49.43  E-value: 5.90e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568938739  401 QRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvriPRFMLLESGG-LRIAPVFIQDAGNYTCYAAN 474
Cdd:cd20970     7 QPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFN---TRYIVRENGTtLTIRNIRRSDMGIYLCIASN 78
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
403-487 7.72e-07

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. 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: 409444  Cd Length: 105  Bit Score: 49.57  E-value: 7.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  403 PVDTTVTDGMTAVLRCEVSGAPKPAITWKRgnHILASGSVR----IPRFMLLESGG----------LRIAPVFIQDAGNY 468
Cdd:cd05858     8 PANTSVVVGTDAEFVCKVYSDAQPHIQWLK--HVEKNGSKYgpdgLPYVEVLKTAGvnttdkeievLYLRNVTFEDAGEY 85
                          90
                  ....*....|....*....
gi 568938739  469 TCYAANTEASVNASAMLTV 487
Cdd:cd05858    86 TCLAGNSIGISHHSAWLTV 104
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
416-486 8.51e-07

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


Pssm-ID: 143223  Cd Length: 69  Bit Score: 48.33  E-value: 8.51e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568938739  416 LRCEVSGAPKPAITW-KRGNHILASGsvripRFMLLESGGLRIAPVFIQDAGNYTCYAANTEASVNASAMLT 486
Cdd:cd05746     3 IPCSAQGDPEPTITWnKDGVQVTESG-----KFHISPEGYLAIRDVGVADQGRYECVARNTIGYASVSMVLS 69
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
294-347 1.37e-06

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: 47.71  E-value: 1.37e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  294 TLECIANARPveELSVHWKRNGVRLTSGLHSYGRR------LTITNPTSADTGMYVCEAT 347
Cdd:cd00096     2 TLTCSASGNP--PPTITWYKNGKPLPPSSRDSRRSelgngtLTISNVTLEDSGTYTCVAS 59
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
104-158 1.38e-06

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: 47.71  E-value: 1.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568938739  104 LVLTCLAEGSWPLEFKWIRNDSELTTYSSEYKY--------IIPSLQKLDAGFYRCVVRNRMG 158
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRselgngtlTISNVTLEDSGTYTCVASNSAG 63
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
175-256 1.73e-06

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: 47.88  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  175 FMDTDQRKTVSQGHAALLNLlPIVSCPQPQVTWFREGHKIIPSSRIAITLEN----QLVILATTASDAGAYYVQAVNEKn 250
Cdd:cd05744     3 FLQAPGDLEVQEGRLCRFDC-KVSGLPTPDLFWQLNGKPVRPDSAHKMLVREngrhSLIIEPVTKRDAGIYTCIARNRA- 80

                  ....*.
gi 568938739  251 GENKTS 256
Cdd:cd05744    81 GENSFN 86
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
397-482 1.89e-06

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) 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, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), 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 Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 48.32  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITW-KRGNHILASGSVRIPRFMLLESGGLRIAPVF-----IQDAGNYTC 470
Cdd:cd07693     1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWlKNGQPLETDKDDPRSHRIVLPSGSLFFLRVVhgrkgRSDEGVYVC 80
                          90
                  ....*....|....*
gi 568938739  471 YAAN---TEASVNAS 482
Cdd:cd07693    81 VAHNslgEAVSRNAS 95
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
491-581 2.10e-06

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth 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: 409359  Cd Length: 102  Bit Score: 48.32  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  491 TSIVHPPEDRVVIKGTTATLCCGATHDPRTSLRYVWKKDNVVITASSSS-----RIVVEKDGSLVISQTWSGDIGDYTCE 565
Cdd:cd04970     3 TRITLAPSNADITVGENATLQCHASHDPTLDLTFTWSFNGVPIDLEKIEghyrrRYGKDSNGDLEIVNAQLKHAGRYTCT 82
                          90
                  ....*....|....*.
gi 568938739  566 IISEGGSDSRTARLEV 581
Cdd:cd04970    83 AQTVVDSDSASATLVV 98
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
588-675 2.52e-06

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


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 47.79  E-value: 2.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   588 PQNLLASLSpARSHSVTLSWVRPFDGNSPVLYYIVQVSENNSPWKVHLSNVGPEMTG------VTVSGLTPARTYQFRVC 661
Cdd:pfam16656    1 PEQVHLSLT-GDSTSMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGtgyihrATLTGLEPGTTYYYRVG 79
                           90
                   ....*....|....
gi 568938739   662 AVNQVGKGQYSTET 675
Cdd:pfam16656   80 DDNGGWSEVYSFTT 93
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
497-581 2.75e-06

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth 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: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 47.64  E-value: 2.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  497 PEDRVVIKGTTATLCCGATHDPRTSLryVWKKD---NVVITAS---SSSRIVVEKDGSLVISQTWSGDIGDYTCEIISEG 570
Cdd:cd05726     6 PRDQVVALGRTVTFQCETKGNPQPAI--FWQKEgsqNLLFPYQppqPSSRFSVSPTGDLTITNVQRSDVGYYICQALNVA 83
                          90
                  ....*....|.
gi 568938739  571 GSDSRTARLEV 581
Cdd:cd05726    84 GSILAKAQLEV 94
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
407-481 3.81e-06

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. 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 Lingo-1 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: 409561  Cd Length: 92  Bit Score: 47.00  E-value: 3.81e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938739  407 TVTDGMTAVLRCEVSGAPKPAITW-KRGNHILASGSVriPRFMLLESGGLRIAPVFIQDAGNYTCYAAN--TEASVNA 481
Cdd:cd20969    13 FVDEGHTVQFVCRADGDPPPAILWlSPRKHLVSAKSN--GRLTVFPDGTLEVRYAQVQDNGTYLCIAANagGNDSMPA 88
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
86-171 3.86e-06

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


Pssm-ID: 409435  Cd Length: 96  Bit Score: 47.24  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   86 PYFKTEPG--LPQIHLEGNRLVLTCLAEGSWPLEFKWIRNDSELTTySSEYKY-------II--PSLQKlDAGFYRCVVR 154
Cdd:cd05848     2 PVFVQEPDdaIFPTDSDEKKVILNCEARGNPVPTYRWLRNGTEIDT-ESDYRYslidgnlIIsnPSEVK-DSGRYQCLAT 79
                          90
                  ....*....|....*..
gi 568938739  155 NRMGALLQRKSEIQVAY 171
Cdd:cd05848    80 NSIGSILSREALLQFAY 96
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
789-874 4.75e-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: 46.45  E-value: 4.75e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    789 PPQNVQAEAVNSTTVHFLWNPPPQQFINGINQGYKLLAWPADAPETVTVVTIAPDFHgihhgYITNLKKFTAYFTSVLCF 868
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSY-----TLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 568938739    869 TTPGDG 874
Cdd:smart00060   78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
281-357 4.94e-06

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: 46.73  E-value: 4.94e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    281 PGNRSVVAGSSeTTLECIANARPveELSVHWKRNGVRL------TSGLHSYGR-RLTITNPTSADTGMYVCEATL-RGST 352
Cdd:smart00410    1 PPSVTVKEGES-VTLSCEASGSP--PPEVTWYKQGGKLlaesgrFSVSRSGSTsTLTISNVTPEDSGTYTCAATNsSGSA 77

                    ....*
gi 568938739    353 FEPAR 357
Cdd:smart00410   78 SSGTT 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1093-1188 5.48e-06

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: 46.72  E-value: 5.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739 1093 APTSLTVRTASETSLRLRWVPLPDSqyngNPESVGYRVKYWRSDQPSSALAQVVSDRlERELTIEELEEWTEYELRMQAF 1172
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDD----GGPITGYVVEYREKGSGDWKEVEVTPGS-ETSYTLTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*.
gi 568938739 1173 NAIGAGPWSELVRGRT 1188
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
1093-1181 6.21e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 6.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  1093 APTSLTVRTASETSLRLRWVPLPDsqynGNPESVGYRVKYWRSDQPSSALAQVVSdRLERELTIEELEEWTEYELRMQAF 1172
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD----GNGPITGYEVEYRPKNSGEPWNEITVP-GTTTSVTLTGLKPGTEYEVRVQAV 76

                   ....*....
gi 568938739  1173 NAIGAGPWS 1181
Cdd:pfam00041   77 NGGGEGPPS 85
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
100-158 7.89e-06

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 46.35  E-value: 7.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  100 EGNRLVLTCLAEGSWP-LEFKWIRNDSELTTYSSEYKYI----------IPSLQKLDAGFYRCVVRNRMG 158
Cdd:cd05750    13 EGSKLVLKCEATSENPsPRYRWFKDGKELNRKRPKNIKIrnkkknselqINKAKLEDSGEYTCVVENILG 82
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
508-577 8.05e-06

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: 45.40  E-value: 8.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568938739  508 ATLCCGATHDPRTSlrYVWKKDNVVITASSSSRIVVEK-DGSLVISQTWSGDIGDYTCEII-SEGGSDSRTA 577
Cdd:cd00096     1 VTLTCSASGNPPPT--ITWYKNGKPLPPSSRDSRRSELgNGTLTISNVTLEDSGTYTCVASnSAGGSASASV 70
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
501-581 9.70e-06

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (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: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 45.93  E-value: 9.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  501 VVIKGTTATLCCGATHDPRTSLRYVWKKDNVVitaSSSSRIVVEKDGSLVISQTWSGDIGDYTCeiISEGGSDSRTARLE 580
Cdd:cd05764    11 RVLEGQRATLRCKARGDPEPAIHWISPEGKLI---SNSSRTLVYDNGTLDILITTVKDTGAFTC--IASNPAGEATARVE 85

                  .
gi 568938739  581 V 581
Cdd:cd05764    86 L 86
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
281-347 9.71e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). 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: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.96  E-value: 9.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568938739  281 PGNRSVVAGSsETTLECIANARPVEELSvhWKRNGVRLTSGLHSY-----GRRLTITNPTSADTGMYVCEAT 347
Cdd:cd20970     9 SFTVTAREGE-NATFMCRAEGSPEPEIS--WTRNGNLIIEFNTRYivrenGTTLTIRNIRRSDMGIYLCIAS 77
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
407-487 1.07e-05

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 45.97  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  407 TVTDGMTAVLRCE-VSGAPKPAITW-KRGNHILASGSVRIPRFMLLESGGLRIAPVFIQDAGNYTCYAANTEASVNASAM 484
Cdd:cd05750    10 TVQEGSKLVLKCEaTSENPSPRYRWfKDGKELNRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGN 89

                  ...
gi 568938739  485 LTV 487
Cdd:cd05750    90 VTV 92
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
400-487 1.08e-05

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: 45.64  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  400 TQRPVDTTVTDGMTAVLRCEVSGAPKPAITW-KRGNHILASGSVRIPRfmlLESG--GLRIAPVFIQDAGNYTCYAANTE 476
Cdd:cd20973     1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWmKDDNPIVESRRFQIDQ---DEDGlcSLIISDVCGDDSGKYTCKAVNSL 77
                          90
                  ....*....|.
gi 568938739  477 ASVNASAMLTV 487
Cdd:cd20973    78 GEATCSAELTV 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
494-581 1.17e-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: 45.46  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  494 VHPPEDRVVIKGTTATLCCGATHDPRTSLRyvWKKDNVVItasSSSRIVVEKDGSLVISQTWSGDIGDYTCEIISEGGSD 573
Cdd:cd05725     1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVR--WRKEDGEL---PKGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGKI 75

                  ....*...
gi 568938739  574 SRTARLEV 581
Cdd:cd05725    76 EASATLTV 83
I-set pfam07679
Immunoglobulin I-set domain;
86-158 1.18e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 45.71  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    86 PYFKTEPGlPQIHLEGNRLVLTCLAEGSWPLEFKWIRNDSELTTySSEYKY---------IIPSLQKLDAGFYRCVVRNR 156
Cdd:pfam07679    1 PKFTQKPK-DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS-SDRFKVtyeggtytlTISNVQPDDSGKYTCVATNS 78

                   ..
gi 568938739   157 MG 158
Cdd:pfam07679   79 AG 80
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
402-487 1.19e-05

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


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 45.52  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  402 RPVDTTVTDGMTAVLRCEVSGAPKPAITWK-RGNHILASGSVRIprfMLLESGGLRIAPVFIQDAGNYTCYAANTEASVN 480
Cdd:cd04978     5 EPPSLVLSPGETGELICEAEGNPQPTITWRlNGVPIEPAPEDMR---RTVDGRTLIFSNLQPNDTAVYQCNASNVHGYLL 81

                  ....*..
gi 568938739  481 ASAMLTV 487
Cdd:cd04978    82 ANAFLHV 88
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
94-169 1.31e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 45.08  E-value: 1.31e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938739    94 LPQIHL-EGNRLVLTCLAEGSWPLEFKWIRNDSELttySSEYKYIIPSLQKLDAGFYRCVVRNRMGALLQRKSEIQV 169
Cdd:pfam13895    6 PSPTVVtEGEPVTLTCSAPGNPPPSYTWYKDGSAI---SSSPNFFTLSVSAEDSGTYTCVARNGRGGKVSNPVELTV 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
201-256 1.60e-05

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: 44.63  E-value: 1.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739  201 PQPQVTWFREGHKIIPSSRIAITLEN---QLVILATTASDAGAYYVQAVNEKNGENKTS 256
Cdd:cd00096    11 PPPTITWYKNGKPLPPSSRDSRRSELgngTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
401-487 2.00e-05

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third 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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 44.85  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  401 QRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRgnhilASGSVrIPRFMLLESGG-LRIAPVFIQDAGNYTCYAANTEASV 479
Cdd:cd04968     6 RFPADTYALKGQTVTLECFALGNPVPQIKWRK-----VDGSP-SSQWEITTSEPvLEIPNVQFEDEGTYECEAENSRGKD 79

                  ....*...
gi 568938739  480 NASAMLTV 487
Cdd:cd04968    80 TVQGRIIV 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
493-581 2.12e-05

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: 44.79  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  493 IVHPPEDRVVIKGTTATLCCGATHDPRTSLRyvWKKDNVVItASSSSRIVVEKDGSLVISQTWSGDIGDYTCEIISEGGS 572
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTIS--WLKDGVPL-LGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78

                  ....*....
gi 568938739  573 DSRTARLEV 581
Cdd:cd20952    79 ATWSAVLDV 87
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
403-483 2.21e-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: 44.88  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   403 PVDTTVTDGMTAVLRCEVSGAPKPA-ITWKRGNHILASGSVRIPRFMLLESGGLRIAPVFIQDAGNYTCYAANTEASVNA 481
Cdd:pfam00047    3 PPTVTVLEGDSATLTCSASTGSPGPdVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82

                   ..
gi 568938739   482 SA 483
Cdd:pfam00047   83 ST 84
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
399-474 2.29e-05

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. 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: 409387  Cd Length: 97  Bit Score: 45.16  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  399 FTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRipRFMLLESGGLRIAPVFIQ-----DAGNYTCYAA 473
Cdd:cd05722     4 FLSEPSDIVAMRGGPVVLNCSAESDPPPKIEWKKDGVLLNLVSDE--RRQQLPNGSLLITSVVHSkhnkpDEGFYQCVAQ 81

                  .
gi 568938739  474 N 474
Cdd:cd05722    82 N 82
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
396-487 2.34e-05

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group 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.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 44.86  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  396 APAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKR-GNHILASGSVRIPRFMLLES---GGLRIAPVFIQDAGNYTCY 471
Cdd:cd20956     1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLdGFPIPESPRFRVGDYVTSDGdvvSYVNISSVRVEDGGEYTCT 80
                          90
                  ....*....|....*.
gi 568938739  472 AANTEASVNASAMLTV 487
Cdd:cd20956    81 ATNDVGSVSHSARINV 96
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
87-169 2.36e-05

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. 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: 409387  Cd Length: 97  Bit Score: 45.16  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   87 YFKTEPGlPQIHLEGNRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYKYIIP--SL----------QKLDAGFYRCVVR 154
Cdd:cd05722     3 YFLSEPS-DIVAMRGGPVVLNCSAESDPPPKIEWKKDGVLLNLVSDERRQQLPngSLlitsvvhskhNKPDEGFYQCVAQ 81
                          90
                  ....*....|....*.
gi 568938739  155 N-RMGALLQRKSEIQV 169
Cdd:cd05722    82 NeSLGSIVSRTARVTV 97
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
397-487 2.92e-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: 44.52  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQ----------RPVDTTVTdgmtavLRCEVSGAPKPAITWKRGN------HILASGSVRIPRFMLLesgglrIAPV 460
Cdd:cd05729     1 PRFTDtekmeerehaLPAANKVR------LECGAGGNPMPNITWLKDGkefkkeHRIGGTKVEEKGWSLI------IERA 68
                          90       100
                  ....*....|....*....|....*..
gi 568938739  461 FIQDAGNYTCYAANTEASVNASAMLTV 487
Cdd:cd05729    69 IPRDKGKYTCIVENEYGSINHTYDVDV 95
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
402-487 2.93e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 44.31  E-value: 2.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   402 RPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGsvriPRFMLLEsgglriapVFIQDAGNYTCYAANTEAS-VN 480
Cdd:pfam13895    5 TPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSS----PNFFTLS--------VSAEDSGTYTCVARNGRGGkVS 72

                   ....*..
gi 568938739   481 ASAMLTV 487
Cdd:pfam13895   73 NPVELTV 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
201-247 4.39e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 43.71  E-value: 4.39e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568938739   201 PQPQVTWFREGHKIIPSSRIAITLEN---QLVILATTASDAGAYYVQAVN 247
Cdd:pfam13927   29 PPPTITWYKNGEPISSGSTRSRSLSGsnsTLTISNVTRSDAGTYTCVASN 78
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
496-581 4.68e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). 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: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 44.04  E-value: 4.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  496 PPEDRVVIKGTTATLCCGATHDPRTSLRyvWKKDNVVITASSSSRIVVEKDGSLVISQTWSGDIGDYTCEIISE-GGSDS 574
Cdd:cd20970     8 PSFTVTAREGENATFMCRAEGSPEPEIS--WTRNGNLIIEFNTRYIVRENGTTLTIRNIRRSDMGIYLCIASNGvPGSVE 85

                  ....*..
gi 568938739  575 RTARLEV 581
Cdd:cd20970    86 KRITLQV 92
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
492-572 4.75e-05

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


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 43.85  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  492 SIVHPPEDRVVIKGTTATLCCGATHDPRTSLryVWKKDNVVI-TASSSSRIVVEKDGSLVISQTWSGDIGDYTCEIISEG 570
Cdd:cd05738     1 IIDMGPQLKVVEKARTATMLCAASGNPDPEI--SWFKDFLPVdTATSNGRIKQLRSGALQIENSEESDQGKYECVATNSA 78

                  ..
gi 568938739  571 GS 572
Cdd:cd05738    79 GT 80
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
99-156 5.18e-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: 43.72  E-value: 5.18e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739    99 LEGNRLVLTCLA-EGSWPLEFKWIRNDSELTTySSEYK----------YIIPSLQKLDAGFYRCVVRNR 156
Cdd:pfam00047    9 LEGDSATLTCSAsTGSPGPDVTWSKEGGTLIE-SLKVKhdngrttqssLLISNVTKEDAGTYTCVVNNP 76
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
406-478 5.19e-05

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: 43.55  E-value: 5.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568938739  406 TTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRIPRFmlleSGGLRIAPVFIQDAGNYTCYAANTEAS 478
Cdd:cd05731     5 TMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGRTKFENF----NKTLKIENVSEADSGEYQCTASNTMGS 73
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
407-476 5.71e-05

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group 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.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 43.71  E-value: 5.71e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938739  407 TVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvripRFMLLESGGLRIAPVF-IQDAGNYTCYAANTE 476
Cdd:cd20958    11 TAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNH----RQRVFPNGTLVIENVQrSSDEGEYTCTARNQQ 77
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
397-479 5.72e-05

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first 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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 43.77  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDT---TVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRipRFMLLeSGGLRIA-PVFIQDAGNYTCYA 472
Cdd:cd04967     2 PVFEEQPDDTifpEDSDEKKVALNCRARANPVPSYRWLMNGTEIDLESDY--RYSLV-DGTLVISnPSKAKDAGHYQCLA 78

                  ....*..
gi 568938739  473 ANTEASV 479
Cdd:cd04967    79 TNTVGSV 85
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
501-581 7.31e-05

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 43.27  E-value: 7.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  501 VVIKGTTATLCCGATHDpRTSLRYVWKKDNVVITASSSSRIVV---EKDGSLVISQTWSGDIGDYTCEIISEGGSDSRTA 577
Cdd:cd05750    10 TVQEGSKLVLKCEATSE-NPSPRYRWFKDGKELNRKRPKNIKIrnkKKNSELQINKAKLEDSGEYTCVVENILGKDTVTG 88

                  ....
gi 568938739  578 RLEV 581
Cdd:cd05750    89 NVTV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
275-347 7.42e-05

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: 43.25  E-value: 7.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  275 PIIVVAPGNRSVVAGSSeTTLECIANARPVEELSvhWKRNGVRLT-----------SGLHSygrrLTITNPTSADTGMYV 343
Cdd:cd05744     1 PHFLQAPGDLEVQEGRL-CRFDCKVSGLPTPDLF--WQLNGKPVRpdsahkmlvreNGRHS----LIIEPVTKRDAGIYT 73

                  ....
gi 568938739  344 CEAT 347
Cdd:cd05744    74 CIAR 77
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
397-487 7.47e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. 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: 409474  Cd Length: 92  Bit Score: 43.55  E-value: 7.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITW-KRGNHILASGSVRIPRFMLLESGGLRIAPVFIQDAGNYTCYAANT 475
Cdd:cd05893     1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWfKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                          90
                  ....*....|..
gi 568938739  476 EASVNASAMLTV 487
Cdd:cd05893    81 QGRISCTGRLMV 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
494-581 8.85e-05

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: 43.25  E-value: 8.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  494 VHPPEDRVVIKGTTATLCCGATHDPRTSLryVWKKDNVVITASSSSRIVVEKDG--SLVISQTWSGDIGDYTCEIISEGG 571
Cdd:cd05744     4 LQAPGDLEVQEGRLCRFDCKVSGLPTPDL--FWQLNGKPVRPDSAHKMLVRENGrhSLIIEPVTKRDAGIYTCIARNRAG 81
                          90
                  ....*....|
gi 568938739  572 SDSRTARLEV 581
Cdd:cd05744    82 ENSFNAELVV 91
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
99-169 9.03e-05

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: 43.00  E-value: 9.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568938739   99 LEGNRLVLTCLAEGSWPLEFKWIRNDSELTTYS-----SEYKYIIPSLQKLDAGFYRCVVRNRMGALLQRKSEIQV 169
Cdd:cd20968    12 IEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNriavlESGSLRIHNVQKEDAGQYRCVAKNSLGIAYSKPVTIEV 87
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
99-169 9.17e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). 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: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 43.27  E-value: 9.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938739   99 LEGNRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYKY-------IIPSLQKLDAGFYRCVVRNRMGALLQRKSEIQV 169
Cdd:cd20970    15 REGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVrengttlTIRNIRRSDMGIYLCIASNGVPGSVEKRITLQV 92
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
408-487 1.14e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; 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.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 42.92  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  408 VTDGMTAVLRCEVSGAPKPAITWK------RGNHILASGSVRIPRFML-LESgglriapVFIQDAGNYTCYAANTEASVN 480
Cdd:cd05857    16 VPAANTVKFRCPAAGNPTPTMRWLkngkefKQEHRIGGYKVRNQHWSLiMES-------VVPSDKGNYTCVVENEYGSIN 88

                  ....*..
gi 568938739  481 ASAMLTV 487
Cdd:cd05857    89 HTYHLDV 95
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
499-581 1.20e-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: 42.56  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  499 DRVVIKGTTATLCCGATHDPRTSLryVWKKDNVVITASSSSRIVVEKDG--SLVISQTWSGDIGDYTCEIISEGGSDSRT 576
Cdd:cd20973     6 DKEVVEGSAARFDCKVEGYPDPEV--KWMKDDNPIVESRRFQIDQDEDGlcSLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                  ....*
gi 568938739  577 ARLEV 581
Cdd:cd20973    84 AELTV 88
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
397-487 1.20e-04

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: 42.73  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHilASGSVRIPRFMLLESGG---LRIAPVFIQDAGNYTCYAA 473
Cdd:cd20974     1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQ--VISTSTLPGVQISFSDGrakLSIPAVTKANSGRYSLTAT 78
                          90
                  ....*....|....
gi 568938739  474 NTEASVNASAMLTV 487
Cdd:cd20974    79 NGSGQATSTAELLV 92
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
411-474 1.38e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 42.63  E-value: 1.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938739  411 GMTAVLRCEVSGAPKPAITW-KRGNHIlasgSVRIPRFMLLESGG--LRIAPVFIQDAGNYTCYAAN 474
Cdd:cd05736    15 GVEASLRCHAEGIPLPRVQWlKNGMDI----NPKLSKQLTLIANGseLHISNVRYEDTGAYTCIAKN 77
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
399-487 1.49e-04

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and 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: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 42.57  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  399 FTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWkRGNHILASGSVRIPRFMlLESGGLRIAPVFIQDAGNYTCYAANTEAS 478
Cdd:cd05867     2 WTRRPQSHLYGPGETARLDCQVEGIPTPNITW-SINGAPIEGTDPDPRRH-VSSGALILTDVQPSDTAVYQCEARNRHGN 79

                  ....*....
gi 568938739  479 VNASAMLTV 487
Cdd:cd05867    80 LLANAHVHV 88
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
397-479 1.51e-04

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


Pssm-ID: 409435  Cd Length: 96  Bit Score: 42.62  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVD---TTVTDGMTAVLRCEVSGAPKPAITWKR-GNHILASGSVripRFMLLEsGGLRIA-PVFIQDAGNYTCY 471
Cdd:cd05848     2 PVFVQEPDDaifPTDSDEKKVILNCEARGNPVPTYRWLRnGTEIDTESDY---RYSLID-GNLIISnPSEVKDSGRYQCL 77

                  ....*...
gi 568938739  472 AANTEASV 479
Cdd:cd05848    78 ATNSIGSI 85
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
86-158 1.51e-04

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: 42.48  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   86 PYFKTEPGLPQIhLEGNRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYKY---------IIPSLQKLDAGFYRCVVRNR 156
Cdd:cd05744     1 PHFLQAPGDLEV-QEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLvrengrhslIIEPVTKRDAGIYTCIARNR 79

                  ..
gi 568938739  157 MG 158
Cdd:cd05744    80 AG 81
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
97-159 1.57e-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: 42.21  E-value: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938739   97 IHLEGNRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYKYIIPSLQKL-----DAGFYRCVVRNRMGA 159
Cdd:cd05876     6 VALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQNHNKTLQLLnvgesDDGEYVCLAENSLGS 73
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
401-488 1.80e-04

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: 42.61  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  401 QRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSvriPRFMLLESGG-LRIAPVFIQDAGNYTCYAANTEASV 479
Cdd:cd05730     8 QSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGE---EKYSFNEDGSeMTILDVDKLDEAEYTCIAENKAGEQ 84

                  ....*....
gi 568938739  480 NASAMLTVW 488
Cdd:cd05730    85 EAEIHLKVF 93
I-set pfam07679
Immunoglobulin I-set domain;
275-347 1.87e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 42.24  E-value: 1.87e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739   275 PIIVVAPGNRSVVAGSSeTTLECIANARPveELSVHWKRNGVRLTSGLH------SYGRRLTITNPTSADTGMYVCEAT 347
Cdd:pfam07679    1 PKFTQKPKDVEVQEGES-ARFTCTVTGTP--DPEVSWFKDGQPLRSSDRfkvtyeGGTYTLTISNVQPDDSGKYTCVAT 76
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
397-482 2.06e-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: 42.15  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQ----------RPVDTTVTdgmtavLRCEVSGAPKPAITWKRGNHILAS---GSVRIPRFMLLESgglRIAPvfiQ 463
Cdd:cd05856     1 PRFTQpakmrrrviaRPVGSSVR------LKCVASGNPRPDITWLKDNKPLTPpeiGENKKKKWTLSLK---NLKP---E 68
                          90
                  ....*....|....*....
gi 568938739  464 DAGNYTCYAANTEASVNAS 482
Cdd:cd05856    69 DSGKYTCHVSNRAGEINAT 87
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
201-247 2.12e-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: 42.06  E-value: 2.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568938739  201 PQPQVTWFREGHKIIPSSRIAITLENQLVILATTASDAGAYYVQAVN 247
Cdd:cd04969    30 PKPTISWSKGTELLTNSSRICILPDGSLKIKNVTKSDEGKYTCFAVN 76
Ig6_Contactin-2 cd05854
Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth ...
491-581 2.40e-04

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


Pssm-ID: 409440  Cd Length: 102  Bit Score: 42.34  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  491 TSIVHPPEDRVVIKGTTATLCCGATHDPRTSLRYVWKKDNVVITASSSS----RI-VVEKDGSLVISQTWSGDIGDYTCE 565
Cdd:cd05854     3 TKITLAPSSADINQGENLTLQCHASHDPTMDLTFTWSLDDFPIDLDKPNghyrRMeVKETIGDLVIVNAQLSHAGTYTCT 82
                          90
                  ....*....|....*.
gi 568938739  566 IISEGGSDSRTARLEV 581
Cdd:cd05854    83 AQTVVDSASASATLVV 98
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
397-487 2.48e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). 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 human APEG-1 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: 409567  Cd Length: 91  Bit Score: 42.07  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRIPRFMLLESGGLRIAPVFIQDAGNYTCYAANTE 476
Cdd:cd20975     1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEY 80
                          90
                  ....*....|.
gi 568938739  477 ASVNASAMLTV 487
Cdd:cd20975    81 GARQCEARLEV 91
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
397-475 2.55e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth 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. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 42.13  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  397 PAFTQRPVDTTVtDGMTAVLRCEVSGAPKPAITWKRG--NHILASGSV--RIPRFMLLESGGLRIAPVFIQDAGNYTCYA 472
Cdd:cd05732     3 PKITYLENQTAV-ELEQITLTCEAEGDPIPEITWRRAtrGISFEEGDLdgRIVVRGHARVSSLTLKDVQLTDAGRYDCEA 81

                  ...
gi 568938739  473 ANT 475
Cdd:cd05732    82 SNR 84
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
100-158 2.79e-04

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 41.90  E-value: 2.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938739  100 EGNRLVLTCLAEGSWP-LEFKWIRNDSELTTYSSEYKYIIPSLQK-----------LDAGFYRCVVRNRMG 158
Cdd:cd05895    13 AGSKLVLRCETSSEYPsLRFKWFKNGKEINRKNKPENIKIQKKKKkselrinkaslADSGEYMCKVSSKLG 83
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
411-487 3.06e-04

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


Pssm-ID: 143220  Cd Length: 78  Bit Score: 41.32  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  411 GMTAVLRCEVSGAPKPAITWKrgnhiLASGSVRIPRFMLLES----GGLRIAPVFIQDAGNYTCYAANTEASV--NASAM 484
Cdd:cd05743     1 GETVEFTCVATGVPTPIINWR-----LNWGHVPDSARVSITSeggyGTLTIRDVKESDQGAYTCEAINTRGMVfgIPDGI 75

                  ...
gi 568938739  485 LTV 487
Cdd:cd05743    76 LTV 78
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
182-256 3.12e-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: 41.41  E-value: 3.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739  182 KTVSQGHAALLNLLpIVSCPQPQVTWFREGHKIIPSSRIAITLENQ----LVILATTASDAGAYYVQAVNeKNGENKTS 256
Cdd:cd20973     7 KEVVEGSAARFDCK-VEGYPDPEVKWMKDDNPIVESRRFQIDQDEDglcsLIISDVCGDDSGKYTCKAVN-SLGEATCS 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
183-263 3.51e-04

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: 41.34  E-value: 3.51e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739    183 TVSQGHAALLnllpivSC-----PQPQVTWFREGHK-IIPSSRIAITLENQ---LVILATTASDAGAYYVQAVNEKNGEN 253
Cdd:smart00410    5 TVKEGESVTL------SCeasgsPPPEVTWYKQGGKlLAESGRFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSAS 78
                            90
                    ....*....|
gi 568938739    254 KTspfIHLSV 263
Cdd:smart00410   79 SG---TTLTV 85
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
416-475 4.71e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(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. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 41.50  E-value: 4.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568938739  416 LRCEVSGAPKPAITWKRGNHILASGSVRIPRFMLLES----GGLRIAPVFIQDAGNYTCYAANT 475
Cdd:cd05869    22 LTCEASGDPIPSITWRTSTRNISSEEKTLDGHIVVRSharvSSLTLKYIQYTDAGEYLCTASNT 85
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
400-487 5.82e-04

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth 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: 409359  Cd Length: 102  Bit Score: 41.00  E-value: 5.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  400 TQRPVDTTVTDGMTAVLRCEVSGAPKPAIT--WKRGNHIL---ASGSVRIPRFMLLESGGLRIAPVFIQDAGNYTCYAAN 474
Cdd:cd04970     6 TLAPSNADITVGENATLQCHASHDPTLDLTftWSFNGVPIdleKIEGHYRRRYGKDSNGDLEIVNAQLKHAGRYTCTAQT 85
                          90
                  ....*....|...
gi 568938739  475 TEASVNASAMLTV 487
Cdd:cd04970    86 VVDSDSASATLVV 98
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
526-581 6.04e-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: 40.91  E-value: 6.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568938739  526 WKKDNVVITASSssRIVVEKDGSLVISQTWSGDIGDYTCEIISEGGSDSRTARLEV 581
Cdd:cd04969    36 WSKGTELLTNSS--RICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
406-487 6.51e-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: 40.66  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  406 TTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRIPRFmlleSGGLRIAPVFIQDAGNYTCYAANTEASVNASAML 485
Cdd:cd05876     5 LVALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQNH----NKTLQLLNVGESDDGEYVCLAENSLGSARHAYYV 80

                  ..
gi 568938739  486 TV 487
Cdd:cd05876    81 TV 82
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
493-581 8.39e-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: 40.30  E-value: 8.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  493 IVHPPEDRVVIKGTTATLCCGATHDPRTSLRYVwKKDNVVitaSSSSRIVVEKDGSLVISQTWSGDIGDYTCEII-SEGG 571
Cdd:cd20968     2 ITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWI-KGDDLI---KENNRIAVLESGSLRIHNVQKEDAGQYRCVAKnSLGI 77
                          90
                  ....*....|
gi 568938739  572 SDSRTARLEV 581
Cdd:cd20968    78 AYSKPVTIEV 87
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
201-252 8.84e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). 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: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 40.18  E-value: 8.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568938739  201 PQPQVTWFREGHKIIPSSRIAITLEN--QLVILATTASDAGAYYVQAVNEKNGE 252
Cdd:cd20970    30 PEPEISWTRNGNLIIEFNTRYIVRENgtTLTIRNIRRSDMGIYLCIASNGVPGS 83
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
180-256 8.96e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 40.21  E-value: 8.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938739  180 QRKTVSQGHAALLNLLpIVSCPQPQVTWFREGHKIIPSSRIAITLENQLVILATTASDAGAYYVQAVNEKNGENKTS 256
Cdd:cd20957     9 PVQTVDFGRTAVFNCS-VTGNPIHTVLWMKDGKPLGHSSRVQILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQATA 84
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
276-363 1.03e-03

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. 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: 409412  Cd Length: 85  Bit Score: 39.85  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  276 IIVVAPGNRSVVAGSsETTLECIANARPVEeLSVHWKRNGVRLTSGLHSYGRRLTITNPTSADTGMYVCEATLRGSTFEp 355
Cdd:cd05754     3 VTVEEPRSQEVRPGA-DVSFICRAKSKSPA-YTLVWTRVNGTLPSRAMDFNGILTIRNVQLSDAGTYVCTGSNMLDTDE- 79

                  ....*...
gi 568938739  356 arARAFLS 363
Cdd:cd05754    80 --ATATLY 85
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
184-247 1.07e-03

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: 40.08  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568938739  184 VSQGHAALLNLLPIVSCPQPQVTWFREGHKII-PSSRIAITLENQLVILATTASDAGAYYVQAVN 247
Cdd:cd05724     9 VAVGEMAVLECSPPRGHPEPTVSWRKDGQPLNlDNERVRIVDDGNLLIAEARKSDEGTYKCVATN 73
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
497-582 1.11e-03

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: 39.91  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  497 PEDRVVIKGTTATLCCGATHDPrtSLRYVWKKD-NVVITASSSSRI-VVEKDGSLVISQTWSGDIGDYTCEIISEGGSDS 574
Cdd:cd05763     6 PHDITIRAGSTARLECAATGHP--TPQIAWQKDgGTDFPAARERRMhVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSIS 83

                  ....*...
gi 568938739  575 RTARLEVI 582
Cdd:cd05763    84 ANATLTVL 91
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
492-581 1.39e-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: 39.68  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  492 SIVHPPEDRVVIKGT-TATLCCGATHDPRTSLRyvWKKDNVVITASSSSRIVveKDGSLVISQTWSGDIGDYTCEIISEG 570
Cdd:cd20978     2 KFIQKPEKNVVVKGGqDVTLPCQVTGVPQPKIT--WLHNGKPLQGPMERATV--EDGTLTIINVQPEDTGYYGCVATNEI 77
                          90
                  ....*....|.
gi 568938739  571 GSDSRTARLEV 581
Cdd:cd20978    78 GDIYTETLLHV 88
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
395-474 1.59e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143278 [Multi-domain]  Cd Length: 98  Bit Score: 39.96  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  395 IAPAFTQRPVDTTVTDGmTAVLRCEVSGAPKPAITWKRGN--HILASGSV----RIPRFMLLESGGLRIAPVFIQDAGNY 468
Cdd:cd05870     1 VQPHIIQLKNETTVENG-AATLSCKAEGEPIPEITWKRASdgHTFSEGDKspdgRIEVKGQHGESSLHIKDVKLSDSGRY 79

                  ....*.
gi 568938739  469 TCYAAN 474
Cdd:cd05870    80 DCEAAS 85
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
403-485 1.76e-03

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. 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: 409412  Cd Length: 85  Bit Score: 39.46  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  403 PVDTTVTDGMTAVLRCE-VSGAPKPAITWKRGNHILASgsvRIPRFMllesGGLRIAPVFIQDAGNYTCYAANTEASVNA 481
Cdd:cd05754     8 PRSQEVRPGADVSFICRaKSKSPAYTLVWTRVNGTLPS---RAMDFN----GILTIRNVQLSDAGTYVCTGSNMLDTDEA 80

                  ....
gi 568938739  482 SAML 485
Cdd:cd05754    81 TATL 84
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
175-259 1.93e-03

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: 39.33  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  175 FMDTDQRKTVSQGHAALLNLLpIVSCPQPQVTWFREGHKIIPSSRIAI-TLENQ-----LVILATTASDAGAYYVQAVNE 248
Cdd:cd20951     3 FIIRLQSHTVWEKSDAKLRVE-VQGKPDPEVKWYKNGVPIDPSSIPGKyKIESEygvhvLHIRRVTVEDSAVYSAVAKNI 81
                          90
                  ....*....|.
gi 568938739  249 KnGENKTSPFI 259
Cdd:cd20951    82 H-GEASSSASV 91
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
396-484 2.00e-03

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. 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 structures of the titin-A168169 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: 409563  Cd Length: 93  Bit Score: 39.38  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  396 APAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKR--------GNHILASGSVRIPRFMLLesgGLRIApvfiQDAGN 467
Cdd:cd20971     1 APHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRqgkeiiadGLKYRIQEFKGGYHQLII---ASVTD----DDATV 73
                          90
                  ....*....|....*..
gi 568938739  468 YTCYAANTEAsvNASAM 484
Cdd:cd20971    74 YQVRATNQGG--SVSGT 88
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
175-248 2.20e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. 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: 409473  Cd Length: 92  Bit Score: 39.37  E-value: 2.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739  175 FMDTDQRKTVSQGHAALLNLLpIVSCPQPQVTWFREGHKI-IPSSRIAITLENQ----LVILATTASDAGAYYVQAVNE 248
Cdd:cd05892     3 FIQKPQNKKVLEGDPVRLECQ-ISAIPPPQIFWKKNNEMLqYNTDRISLYQDNCgricLLIQNANKKDAGWYTVSAVNE 80
IgI_1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; ...
86-171 2.27e-03

First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; The members here are composed of the first 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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409436 [Multi-domain]  Cd Length: 95  Bit Score: 39.17  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   86 PYFKTEPG---LPQIHLEGnRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYKYI-------IPSLQKlDAGFYRCVVRN 155
Cdd:cd05849     2 PVFEEQPIdtiYPEESTEG-KVSVNCRARANPFPIYKWRKNNLDIDLTNDRYSMVggnlvinNPDKYK-DAGRYVCIVSN 79
                          90
                  ....*....|....*.
gi 568938739  156 RMGALLQRKSEIQVAY 171
Cdd:cd05849    80 IYGKVRSREATLSFGY 95
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
201-247 2.40e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth 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: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 39.17  E-value: 2.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568938739  201 PQPQVTWFREGHKII--------PSSRIAITLENQLVILATTASDAGAYYVQAVN 247
Cdd:cd05726    27 PQPAIFWQKEGSQNLlfpyqppqPSSRFSVSPTGDLTITNVQRSDVGYYICQALN 81
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
274-368 2.48e-03

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth 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: 409359  Cd Length: 102  Bit Score: 39.46  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  274 APIIVVAPGNRSVVAGSSeTTLECIANARPVEELSVHWKRNGVRL---TSGLHsYGRR--------LTITNPTSADTGMY 342
Cdd:cd04970     2 ATRITLAPSNADITVGEN-ATLQCHASHDPTLDLTFTWSFNGVPIdleKIEGH-YRRRygkdsngdLEIVNAQLKHAGRY 79
                          90       100
                  ....*....|....*....|....*.
gi 568938739  343 VCEATlrgSTFEPARARAFLSIIEPP 368
Cdd:cd04970    80 TCTAQ---TVVDSDSASATLVVRGPP 102
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
505-581 2.50e-03

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: 39.13  E-value: 2.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739  505 GTTATLCCGATHDPRTSLRyvWKKDNVVITASSSSRI--VVEKDGSLVISQTWSGDIGDYTCEIISEGGSDSRTARLEV 581
Cdd:cd05729    19 ANKVRLECGAGGNPMPNIT--WLKDGKEFKKEHRIGGtkVEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
279-351 2.54e-03

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 38.72  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   279 VAPGNRSVVAGSSeTTLECIANARPVEeLSVHWKRNGVRLTSGL---HSYGRR----LTITNPTSADTGMYVCEATLRGS 351
Cdd:pfam00047    1 SAPPTVTVLEGDS-ATLTCSASTGSPG-PDVTWSKEGGTLIESLkvkHDNGRTtqssLLISNVTKEDAGTYTCVVNNPGG 78
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
201-248 2.59e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. 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: 409388  Cd Length: 84  Bit Score: 38.72  E-value: 2.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568938739  201 PQPQVTWFREGHKIIPSSRIAITLENQLVILATTASDAGAYYVQAVNE 248
Cdd:cd05723    25 PTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVKSDEGFYQCIAEND 72
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
86-169 2.78e-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: 38.91  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   86 PYFKTEPGLPQIHLEGNRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYKY-----IIPSLQKLDAGFYRCVVRNRMGAl 160
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVedgtlTIINVQPEDTGYYGCVATNEIGD- 79

                  ....*....
gi 568938739  161 LQRKSEIQV 169
Cdd:cd20978    80 IYTETLLHV 88
IgI_1_Axl_like cd20966
First immunoglobulin (Ig)-like domain of Axl receptor tyrosine kinase (RTK), and similar ...
399-470 2.92e-03

First immunoglobulin (Ig)-like domain of Axl receptor tyrosine kinase (RTK), and similar domains; member of the I-set Ig domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Axl receptor tyrosine kinase (RTK). Axl together with Tyro3 and Mer form the Axl/Tyro3 family of receptor tyrosine kinases (RTKs). This family includes Axl (also known as Ark, Ufo, and Tyro7), Tyro3 (also known as Sky, Rse, Brt, Dtk, and Tif), and Mer (also known as Nyk, c-Eyk, and Tyro12). Axl/Tyro3 family receptors have an extracellular portion with two Ig-like domains followed by two fibronectin-types III (FNIII) domains, a membrane-spanning single helix, and a cytoplasmic tyrosine kinase domain. Axl, Tyro3 and Mer are widely expressed in adult tissues, though they show higher expression in the brain, in the lymphatic and vascular systems, and in the testis. Axl, Tyro3, and Mer bind the vitamin K dependent protein Gas6 with high affinity, and in doing so activate their tyrosine kinase activity. Axl/Gas6 signaling may play a part in cell adhesion processes, prevention of apoptosis, and cell proliferation. Ig superfamily 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 Axl 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.


Pssm-ID: 409558  Cd Length: 101  Bit Score: 39.29  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  399 FTQRPVDTTVTDGMTAVLRCE--VSGAPkPAITWKRGNHILASGSVRIPRFMLLESGG--------LRIAPVFIQDAGNY 468
Cdd:cd20966     3 FVGNPGNITGARGLTGTLRCQlqVQGEP-PEVHWLRDGQILELADSTQTQVPLGEDEQddwivvsqLRITSLQLSDTGQY 81

                  ..
gi 568938739  469 TC 470
Cdd:cd20966    82 QC 83
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
96-158 2.96e-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: 38.54  E-value: 2.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938739   96 QIHLEGNRLVLTCLAEGSWPLEFKWIRNDSEL-----TTYSSEYKYIIPSLQKLDAGFYRCVVRNRMG 158
Cdd:cd05731     5 TMVLRGGVLLLECIAEGLPTPDIRWIKLGGELpkgrtKFENFNKTLKIENVSEADSGEYQCTASNTMG 72
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
182-260 2.98e-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: 38.91  E-value: 2.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938739  182 KTVSQGHAALLNLlPIVSCPQPQVTWFREGHKIIPSSRIAITLENQLVILATTASDAGAYYVQAVNEkNGENKTSPFIH 260
Cdd:cd20978    11 VVVKGGQDVTLPC-QVTGVPQPKITWLHNGKPLQGPMERATVEDGTLTIINVQPEDTGYYGCVATNE-IGDIYTETLLH 87
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
493-581 3.35e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) 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, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), 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 Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 39.07  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  493 IVHPPEDRVVIKGTTATLCCGATHDPRTSLRyvWKKDN---VVITASSSSRIVVEKDGSLVISQTWSG-----DIGDYTC 564
Cdd:cd07693     3 IVEHPSDLIVSKGDPATLNCKAEGRPTPTIQ--WLKNGqplETDKDDPRSHRIVLPSGSLFFLRVVHGrkgrsDEGVYVC 80
                          90
                  ....*....|....*...
gi 568938739  565 EIISE-GGSDSRTARLEV 581
Cdd:cd07693    81 VAHNSlGEAVSRNASLEV 98
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
403-486 4.50e-03

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. 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: 409363  Cd Length: 102  Bit Score: 38.56  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  403 PVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILAS--GSVRIPRFMLLESGG---------LRIAPVFIQDAGNYTCY 471
Cdd:cd04974     8 PANQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSkyGPDGLPYVTVLKVAGvnttgeentLTISNVTFDDAGEYICL 87
                          90
                  ....*....|....*
gi 568938739  472 AANTEASVNASAMLT 486
Cdd:cd04974    88 AGNSIGLSFHSAWLT 102
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
201-252 4.76e-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: 38.35  E-value: 4.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568938739  201 PQPQVTWFREGHKIIPSSRIAITLEN----QLVILATTASDAGAYYVQAVNEKNGE 252
Cdd:cd05891    29 PDPEVIWFKNDQDIELSEHYSVKLEQgkyaSLTIKGVTSEDSGKYSINVKNKYGGE 84
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
407-487 5.43e-03

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.


Pssm-ID: 409368  Cd Length: 88  Bit Score: 37.82  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  407 TVTDGMTAVLRCEVSGAPKPAiTWKRGNHILasGSVRIPRFMLLESGGLRIAPVFIQDAGNYTCYAAN-TEASVNASAML 485
Cdd:cd04979     7 SVKEGDTVILSCSVKSNNAPV-TWIHNGKKV--PRYRSPRLVLKTERGLLIRSAQEADAGVYECHSGErVLGSTLRSVTL 83

                  ..
gi 568938739  486 TV 487
Cdd:cd04979    84 HV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1093-1178 5.57e-03

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: 37.98  E-value: 5.57e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739   1093 APTSLTVRTASETSLRLRWVPLPDSQYNGnpESVGYRVKYWRSDQPSSalaQVVSDRLERELTIEELEEWTEYELRMQAF 1172
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITG--YIVGYRVEYREEGSEWK---EVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*.
gi 568938739   1173 NAIGAG 1178
Cdd:smart00060   78 NGAGEG 83
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
494-581 6.07e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. 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: 409473  Cd Length: 92  Bit Score: 37.83  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  494 VHPPEDRVVIKGTTATLCCGATHDPrtSLRYVWKKDNVVITaSSSSRIVVEKDGS----LVISQTWSGDIGDYTCEIISE 569
Cdd:cd05892     4 IQKPQNKKVLEGDPVRLECQISAIP--PPQIFWKKNNEMLQ-YNTDRISLYQDNCgricLLIQNANKKDAGWYTVSAVNE 80
                          90
                  ....*....|..
gi 568938739  570 GGSDSRTARLEV 581
Cdd:cd05892    81 AGVVSCNARLDV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
196-263 6.12e-03

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: 37.57  E-value: 6.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938739  196 PIVSCPQPQVTWFREGHKIIPSSRIAITLEN---QLVILATTASDAGAYYVQAvneKNGENKTSPFIHLSV 263
Cdd:cd05748    15 PIKGRPTPTVTWSKDGQPLKETGRVQIETTAsstSLVIKNAKRSDSGKYTLTL---KNSAGEKSATINVKV 82
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
498-581 6.25e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth 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. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 37.89  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  498 EDRVVIKGTTATLCCGATHDPRTSLryVWKKDNVVITASSSS---RIVVEKD---GSLVISQTWSGDIGDYTCEIISEGG 571
Cdd:cd05732     9 ENQTAVELEQITLTCEAEGDPIPEI--TWRRATRGISFEEGDldgRIVVRGHarvSSLTLKDVQLTDAGRYDCEASNRIG 86
                          90
                  ....*....|
gi 568938739  572 SDSRTARLEV 581
Cdd:cd05732    87 GDQQSMYLEV 96
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
585-729 6.48e-03

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 41.85  E-value: 6.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  585 PHPPQNLLASLSPARSHSV----------TLSWVRPfdgnSPVLYYIVQVSENNSPWkVHLSNVGPemTGVTVSGLtPAR 654
Cdd:COG4733   526 DVPPQWPPVNVTTSESLSVvaqgtavttlTVSWDAP----AGAVAYEVEWRRDDGNW-VSVPRTSG--TSFEVPGI-YAG 597
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938739  655 TYQFRVCAVN---QVGKGQYSTETSrLMLPEEPPSAPPkNIVASGRTNQsIMVQWQPPPETEhngvLRGYILRYRLAG 729
Cdd:COG4733   598 DYEVRVRAINalgVSSAWAASSETT-VTGKTAPPPAPT-GLTATGGLGG-ITLSWSFPVDAD----TLRTEIRYSTTG 668
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
174-271 6.70e-03

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: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938739  174 NFMDTDQRKTVSQGHAALLNLLpIVSCPQPQVTWFREGHKIIPSSRIAITLENQ---LVILATTASDAGAYYVQAVNekn 250
Cdd:cd20972     3 QFIQKLRSQEVAEGSKVRLECR-VTGNPTPVVRWFCEGKELQNSPDIQIHQEGDlhsLIIAEAFEEDTGRYSCLATN--- 78
                          90       100
                  ....*....|....*....|.
gi 568938739  251 genktspfihlSVARDTGTHE 271
Cdd:cd20972    79 -----------SVGSDTTSAE 88
 
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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