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Conserved domains on  [gi|1370509662|ref|XP_024302452|]
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protein sidekick-1 isoform X2 [Homo sapiens]

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];
1271-1635 8.34e-22

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.39  E-value: 8.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1271 GEWQTYSSSISHEATACVVDRLRPFTSYKLRLKATNDIGDSDFSSETEAVTTLqdVPGEPPGSVSATPHTTSSVLIQWQP 1350
Cdd:COG3401    178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPT--TPPSAPTGLTATADTPGSVTLSWDP 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1351 PRDESlnglLQGYRIYYRelEYEAGSGTEAKTLKNPIALHAELTDLKKYrRYEVimTAYNIIG-ESPASAPVEVFVGEAA 1429
Cdd:COG3401    256 VTESD----ATGYRVYRS--NSGDGPFTKVATVTTTSYTDTGLTNGTTY-YYRV--TAVDAAGnESAPSNVVSVTTDLTP 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1430 PAmAPQNVQVTPLTASQLEVTWDPpppeSQNGNIQGYKIYYWEADSQNETEKMKVlfLPEPVVRLKNLTSHTKYLVSISA 1509
Cdd:COG3401    327 PA-APSGLTATAVGSSSITLSWTA----SSDADVTGYNVYRSTSGGGTYTKIAET--VTTTSYTDTGLTPGTTYYYKVTA 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1510 FNAAGDGPKSDPQQGRTHQAAPGAPSFLAFSEITSTTLNVSWGEPAAANGILQGYRVVYEPLAPVQGVSKVVTVEVRGNW 1589
Cdd:COG3401    400 VDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTA 479

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1370509662 1590 QRWLKVRDLTKGVTYFFRVQARTITYGPELQANITAGPAEGSPGSP 1635
Cdd:COG3401    480 TTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPD 525
I-set pfam07679
Immunoglobulin I-set domain;
229-319 1.67e-20

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.70  E-value: 1.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSvripRFMLLESGG---LQIAPVFIQDAGNYTCYAA 305
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD----RFKVTYEGGtytLTISNVQPDDSGKYTCVAT 76

                           90
                   ....*....|....
gi 1370509662  306 NTEGSLNASATLTV 319
Cdd:pfam07679   77 NSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 417-508 5.44e-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: 77.92  E-value: 5.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  417 PHSPQNLLVSPNSSHShaVVLSWVRPFDGNSPILYYIVELSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVN 496
Cdd:cd00063      1 PSPPTNLRVTDVTSTS--VTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                           90
                   ....*....|..
gi 1370509662  497 EVGRGQYSAETS 508
Cdd:cd00063     79 GGGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1127-1220 6.87e-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: 77.54  E-value: 6.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1127 PGPPVRLVFPEVRLTSVRIVWQPPEEPNGIILGYQIAYRLASSSPHTFTTVEVGaTVRQFTATDLAPESAYIFRLSAKTR 1206
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1370509662 1207 QGWGEPLEATVITT 1220
Cdd:cd00063     80 GGESPPSESVTVTT 93
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 135-224 9.26e-17

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 cd20978:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 88  Bit Score: 77.05  E-value: 9.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISRlQNPRYKVlASGGLRIQKLRPEDSGIFQCFASNEGG 214
Cdd:cd20978      1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG-PMERATV-EDGTLTIINVQPEDTGYYGCVATNEIG 78

                           90
                   ....*....|
gi 1370509662  215 EIQTHTYLDV 224
Cdd:cd20978     79 DIYTETLLHV 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1632-1725 4.39e-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: 72.53  E-value: 4.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1632 PGSPRDVLVTK-SASELTLQWTEGHSGDTPTTGYVIEARPSDEGLWdMFVKDIPRSATSYTLslDKLRQGVTYEFRVVAV 1710
Cdd:cd00063      1 PSPPTNLRVTDvTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDW-KEVEVTPGSETSYTL--TGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....*
gi 1370509662 1711 NEAGYGEPSNPSTAV 1725
Cdd:cd00063     78 NGGGESPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
722-803 3.76e-14

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 3.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  722 GAVGHLSFTEILDTSLKVSWQEPLEKNGIITGYQISWEVYGRNDSRLTHTLNSTTHEYKIQGLSSLTTYTIDVAAVTAVG 801
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ..
gi 1370509662  802 TG 803
Cdd:pfam00041   81 EG 82
fn3 pfam00041
Fibronectin type III domain;
520-606 4.27e-14

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 4.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  520 PPKNIVASGRTNQSIMVQWQPPPEteHNGVLRGYILRYRLAGLPGEYQQRNITSPEvNYCLVTDLIIWTQYEIQVAAYNG 599
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNSGEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 1370509662  600 AGLGVFS 606
Cdd:pfam00041   79 GGEGPPS 85
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
686-953 5.48e-12

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: 70.80  E-value: 5.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  686 NLKKFTAYFTSVLCFTTPGDGPPSTPQLVWTQEDKPGAVGHLSFTEILDTSLKVSWQEPLEKNgiITGYQISWEVYGRND 765
Cdd:COG3401    198 DIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNSGDGP 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  766 SRLTHTLNSTTheYKIQGLSSLTTYTIDVAAVTAVGTGLVTSSTISSGVPPDLPGAPSNLVISNISPRSATLQFRPGYDG 845
Cdd:COG3401    276 FTKVATVTTTS--YTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDA 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  846 KtsISRWIVEGQVGAIGdeeEWVTLYEEENEPdaqMLEIPNLTPYTHYRFRMKQVNIVGPSPYSPSSRVIQTLQAPPDVA 925
Cdd:COG3401    354 D--VTGYNVYRSTSGGG---TYTKIAETVTTT---SYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGES 425

                          250       260
                   ....*....|....*....|....*...
gi 1370509662  926 PTSVTVRTASETSLRLRWVPLPDSQYNG 953
Cdd:COG3401    426 LTASVDAVPLTDVAGATAAASAASNPGV 453
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
1000-1344 8.35e-12

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: 70.42  E-value: 8.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1000 QMQAFNAVGAGPWSEVVRGRTRESVPSAaPENVSAEAVSSTQILLTWTSVPEQDqnglILGYKIlFRAKDlDPEPRSHIV 1079
Cdd:COG3401    208 RVAATDTGGESAPSNEVSVTTPTTPPSA-PTGLTATADTPGSVTLSWDPVTESD----ATGYRV-YRSNS-GDGPFTKVA 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1080 RGNHTqSALLAGLRKFVLYELQVLAFTRIGN-GVPSTPLILErTKDDAPGPPVRLVFPEVRLTSVRIVWQPPEEPNgiIL 1158
Cdd:COG3401    281 TVTTT-SYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVT-TDLTPPAAPSGLTATAVGSSSITLSWTASSDAD--VT 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1159 GYQIaYRlASSSPHTFTTVEVGATVRQFTATDLAPESAYIFRLSAKTRQG----WGEPLEATVITTEKRERP-APPRELL 1233
Cdd:COG3401    357 GYNV-YR-STSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSATTASAASGESLtASVDAVP 434

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1234 VPQAEVTARSLRLQWVPGSDGASPIRYFTMQVRELPRGEWQTYSSSISheatacvvdrlrPFTSYKLRLKATNDIGDSDF 1313
Cdd:COG3401    435 LTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTT------------DTTTANLSVTTGSLVGGSGA 502

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1370509662 1314 SSETEAVTTLQDVPGEPPGSVSATPHTTSSV 1344
Cdd:COG3401    503 SSVTNSVSVIGASAAAAVGGAPDGTPNVTGA 533
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 42-113 6.07e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 60.27  E-value: 6.07e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662   42 PTIVVPPGNRSVVAGSSeTTLECIASARPVEdlSVTWKRNGVRITSGLHSF------GRRLTISNPTSADTGPYVCEA 113
Cdd:pfam13927    2 PVITVSPSSVTVREGET-VTLTCEATGSPPP--TITWYKNGEPISSGSTRSrslsgsNSTLTISNVTRSDAGTYTCVA 76
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 329-413 6.22e-10

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 cd05722:

Pssm-ID: 472250  Cd Length: 97  Bit Score: 57.87  E-value: 6.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  329 PEDHVVIKGTTATLHCGATHDPRVSLRyvWKKDNVALTPSSTSRIVVEKDGSLLI-----SQTWSGDIGDYSCE--IVSE 401
Cdd:cd05722      8 PSDIVAMRGGPVVLNCSAESDPPPKIE--WKKDGVLLNLVSDERRQQLPNGSLLItsvvhSKHNKPDEGFYQCVaqNESL 85

                           90
                   ....*....|..
gi 1370509662  402 GGNDSRMARLEV 413
Cdd:cd05722     86 GSIVSRTARVTV 97
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 621-716 8.71e-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: 54.42  E-value: 8.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  621 PPQNVQTEAVNSTTIQFLWNPPPqqFINGINQGYKLLAWPADAPEAVTVVTIAPDfhgVHHGHITNLKKFTAYFTSVLCF 700
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGYVVEYREKGSGDWKEVEVTPGS---ETSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....*.
gi 1370509662  701 TTPGDGPPSTPQLVWT 716
Cdd:cd00063     78 NGGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
925-1013 1.63e-05

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.10  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  925 APTSVTVRTASETSLRLRWVPLPDsqynGNPESVGYRIKYWRSDLQSSAVAQVVSdRLEREFTIEELEEWMEYELQMQAF 1004
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD----GNGPITGYEVEYRPKNSGEPWNEITVP-GTTTSVTLTGLKPGTEYEVRVQAV 76


                   ....*....
gi 1370509662 1005 NAVGAGPWS 1013
Cdd:pfam00041   77 NGGGEGPPS 85
 
Name Accession Description Interval E-value
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1271-1635 8.34e-22

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.39  E-value: 8.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1271 GEWQTYSSSISHEATACVVDRLRPFTSYKLRLKATNDIGDSDFSSETEAVTTLqdVPGEPPGSVSATPHTTSSVLIQWQP 1350
Cdd:COG3401    178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPT--TPPSAPTGLTATADTPGSVTLSWDP 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1351 PRDESlnglLQGYRIYYRelEYEAGSGTEAKTLKNPIALHAELTDLKKYrRYEVimTAYNIIG-ESPASAPVEVFVGEAA 1429
Cdd:COG3401    256 VTESD----ATGYRVYRS--NSGDGPFTKVATVTTTSYTDTGLTNGTTY-YYRV--TAVDAAGnESAPSNVVSVTTDLTP 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1430 PAmAPQNVQVTPLTASQLEVTWDPpppeSQNGNIQGYKIYYWEADSQNETEKMKVlfLPEPVVRLKNLTSHTKYLVSISA 1509
Cdd:COG3401    327 PA-APSGLTATAVGSSSITLSWTA----SSDADVTGYNVYRSTSGGGTYTKIAET--VTTTSYTDTGLTPGTTYYYKVTA 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1510 FNAAGDGPKSDPQQGRTHQAAPGAPSFLAFSEITSTTLNVSWGEPAAANGILQGYRVVYEPLAPVQGVSKVVTVEVRGNW 1589
Cdd:COG3401    400 VDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTA 479

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1370509662 1590 QRWLKVRDLTKGVTYFFRVQARTITYGPELQANITAGPAEGSPGSP 1635
Cdd:COG3401    480 TTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPD 525
I-set pfam07679
Immunoglobulin I-set domain;
229-319 1.67e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.70  E-value: 1.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSvripRFMLLESGG---LQIAPVFIQDAGNYTCYAA 305
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD----RFKVTYEGGtytLTISNVQPDDSGKYTCVAT 76

                           90
                   ....*....|....
gi 1370509662  306 NTEGSLNASATLTV 319
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 ...
 230-319 9.73e-20

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: 85.63  E-value: 9.73e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  230 VFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILAsgsVRIPRFMLLESGGLQIAPVFIQDAGNYTCYAANTEG 309
Cdd:cd20952      1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLL---GKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSG 77

                           90
                   ....*....|
gi 1370509662  310 SLNASATLTV 319
Cdd:cd20952     78 EATWSAVLDV 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1433-1526 1.94e-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: 1.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1433 APQNVQVTPLTASQLEVTWDPPPPEsqNGNIQGYKIYYWEADSqNETEKMKVLFLPEPVVRLKNLTSHTKYLVSISAFNA 1512
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGS-GDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1370509662 1513 AGDGPKSDPQQGRT 1526
Cdd:cd00063     80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 417-508 5.44e-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: 77.92  E-value: 5.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  417 PHSPQNLLVSPNSSHShaVVLSWVRPFDGNSPILYYIVELSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVN 496
Cdd:cd00063      1 PSPPTNLRVTDVTSTS--VTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                           90
                   ....*....|..
gi 1370509662  497 EVGRGQYSAETS 508
Cdd:cd00063     79 GGGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1127-1220 6.87e-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: 77.54  E-value: 6.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1127 PGPPVRLVFPEVRLTSVRIVWQPPEEPNGIILGYQIAYRLASSSPHTFTTVEVGaTVRQFTATDLAPESAYIFRLSAKTR 1206
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1370509662 1207 QGWGEPLEATVITT 1220
Cdd:cd00063     80 GGESPPSESVTVTT 93
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 135-224 9.26e-17

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: 77.05  E-value: 9.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISRlQNPRYKVlASGGLRIQKLRPEDSGIFQCFASNEGG 214
Cdd:cd20978      1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG-PMERATV-EDGTLTIINVQPEDTGYYGCVATNEIG 78

                           90
                   ....*....|
gi 1370509662  215 EIQTHTYLDV 224
Cdd:cd20978     79 DIYTETLLHV 88
fn3 pfam00041
Fibronectin type III domain;
419-504 1.75e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.91  E-value: 1.75e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  419 SPQNLLVSPNSSHShaVVLSWVRPFDGNSPILYYIVELSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVNEV 498
Cdd:pfam00041    2 APSNLTVTDVTSTS--LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 1370509662  499 GRGQYS 504
Cdd:pfam00041   80 GEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
1433-1519 4.64e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 74.76  E-value: 4.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1433 APQNVQVTPLTASQLEVTWDPPPPesQNGNIQGYKIYYWEADSqNETEKMKVLFLPEPVVRLKNLTSHTKYLVSISAFNA 1512
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNS-GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 1370509662 1513 AGDGPKS 1519
Cdd:pfam00041   79 GGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1632-1725 4.39e-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: 72.53  E-value: 4.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1632 PGSPRDVLVTK-SASELTLQWTEGHSGDTPTTGYVIEARPSDEGLWdMFVKDIPRSATSYTLslDKLRQGVTYEFRVVAV 1710
Cdd:cd00063      1 PSPPTNLRVTDvTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDW-KEVEVTPGSETSYTL--TGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....*
gi 1370509662 1711 NEAGYGEPSNPSTAV 1725
Cdd:cd00063     78 NGGGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
135-224 5.19e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 71.90  E-value: 5.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPeSRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISrlQNPRYKVLASGG---LRIQKLRPEDSGIFQCFASN 211
Cdd:pfam07679    1 PKFTQKP-KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR--SSDRFKVTYEGGtytLTISNVQPDDSGKYTCVATN 77

                           90
                   ....*....|...
gi 1370509662  212 EGGEIQTHTYLDV 224
Cdd:pfam07679   78 SAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 235-319 1.19e-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: 71.00  E-value: 1.19e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   235 PVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIPRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGSLNAS 314
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 1370509662   315 ATLTV 319
Cdd:smart00410   81 TTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 417-501 1.32e-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: 70.72  E-value: 1.32e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   417 PHSPQNLLVSPNSSHShaVVLSWVRPFDGN--SPILYYIVELSENNSPWKVHlsNVGPEMTGVTVSGLTPARTYQFRVCA 494
Cdd:smart00060    1 PSPPSNLRVTDVTSTS--VTLSWEPPPDDGitGYIVGYRVEYREEGSEWKEV--NVTPSSTSYTLTGLKPGTEYEFRVRA 76


                    ....*..
gi 1370509662   495 VNEVGRG 501
Cdd:smart00060   77 VNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
722-803 3.76e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 3.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  722 GAVGHLSFTEILDTSLKVSWQEPLEKNGIITGYQISWEVYGRNDSRLTHTLNSTTHEYKIQGLSSLTTYTIDVAAVTAVG 801
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ..
gi 1370509662  802 TG 803
Cdd:pfam00041   81 EG 82
fn3 pfam00041
Fibronectin type III domain;
520-606 4.27e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 4.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  520 PPKNIVASGRTNQSIMVQWQPPPEteHNGVLRGYILRYRLAGLPGEYQQRNITSPEvNYCLVTDLIIWTQYEIQVAAYNG 599
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNSGEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 1370509662  600 AGLGVFS 606
Cdd:pfam00041   79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1433-1516 6.55e-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: 6.55e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  1433 APQNVQVTPLTASQLEVTWDPPPPESQNGNIQGYKIYYWEADSQNETEKMKVlflPEPVVRLKNLTSHTKYLVSISAFNA 1512
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTP---SSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1370509662  1513 AGDG 1516
Cdd:smart00060   80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
1633-1719 9.13e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.21  E-value: 9.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1633 GSPRDVLVT-KSASELTLQWTEGHSGDTPTTGYVIEARPSDEGlWDMFVKDIPRSATSYTLSldKLRQGVTYEFRVVAVN 1711
Cdd:pfam00041    1 SAPSNLTVTdVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLT--GLKPGTEYEVRVQAVN 77


                   ....*...
gi 1370509662 1712 EAGYGEPS 1719
Cdd:pfam00041   78 GGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 721-803 1.25e-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: 68.29  E-value: 1.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  721 PGAVGHLSFTEILDTSLKVSWQEPLEKNGIITGYQISWEVYGRNDSRLTHTLNSTTHEYKIQGLSSLTTYTIDVAAVTAV 800
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ...
gi 1370509662  801 GTG 803
Cdd:cd00063     81 GES 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 520-613 4.27e-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: 66.75  E-value: 4.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  520 PPKNIVASGRTNQSIMVQWQPPPETehNGVLRGYILRYRLAGlPGEYQQRNITSPEVNYCLVTDLIIWTQYEIQVAAYNG 599
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKG-SGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1370509662  600 AGLGVFSRAVTEYT 613
Cdd:cd00063     80 GGESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
686-953 5.48e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 70.80  E-value: 5.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  686 NLKKFTAYFTSVLCFTTPGDGPPSTPQLVWTQEDKPGAVGHLSFTEILDTSLKVSWQEPLEKNgiITGYQISWEVYGRND 765
Cdd:COG3401    198 DIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNSGDGP 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  766 SRLTHTLNSTTheYKIQGLSSLTTYTIDVAAVTAVGTGLVTSSTISSGVPPDLPGAPSNLVISNISPRSATLQFRPGYDG 845
Cdd:COG3401    276 FTKVATVTTTS--YTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDA 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  846 KtsISRWIVEGQVGAIGdeeEWVTLYEEENEPdaqMLEIPNLTPYTHYRFRMKQVNIVGPSPYSPSSRVIQTLQAPPDVA 925
Cdd:COG3401    354 D--VTGYNVYRSTSGGG---TYTKIAETVTTT---SYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGES 425

                          250       260
                   ....*....|....*....|....*...
gi 1370509662  926 PTSVTVRTASETSLRLRWVPLPDSQYNG 953
Cdd:COG3401    426 LTASVDAVPLTDVAGATAAASAASNPGV 453
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1000-1344 8.35e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 70.42  E-value: 8.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1000 QMQAFNAVGAGPWSEVVRGRTRESVPSAaPENVSAEAVSSTQILLTWTSVPEQDqnglILGYKIlFRAKDlDPEPRSHIV 1079
Cdd:COG3401    208 RVAATDTGGESAPSNEVSVTTPTTPPSA-PTGLTATADTPGSVTLSWDPVTESD----ATGYRV-YRSNS-GDGPFTKVA 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1080 RGNHTqSALLAGLRKFVLYELQVLAFTRIGN-GVPSTPLILErTKDDAPGPPVRLVFPEVRLTSVRIVWQPPEEPNgiIL 1158
Cdd:COG3401    281 TVTTT-SYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVT-TDLTPPAAPSGLTATAVGSSSITLSWTASSDAD--VT 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1159 GYQIaYRlASSSPHTFTTVEVGATVRQFTATDLAPESAYIFRLSAKTRQG----WGEPLEATVITTEKRERP-APPRELL 1233
Cdd:COG3401    357 GYNV-YR-STSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSATTASAASGESLtASVDAVP 434

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1234 VPQAEVTARSLRLQWVPGSDGASPIRYFTMQVRELPRGEWQTYSSSISheatacvvdrlrPFTSYKLRLKATNDIGDSDF 1313
Cdd:COG3401    435 LTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTT------------DTTTANLSVTTGSLVGGSGA 502

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1370509662 1314 SSETEAVTTLQDVPGEPPGSVSATPHTTSSV 1344
Cdd:COG3401    503 SSVTNSVSVIGASAAAAVGGAPDGTPNVTGA 533
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 520-603 1.00e-11

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 62.63  E-value: 1.00e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   520 PPKNIVASGRTNQSIMVQWQPPPETEHNGVLRGYILRYRLAGLPgeyQQRNITSPEVNYCLVTDLIIWTQYEIQVAAYNG 599
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSE---WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1370509662   600 AGLG 603
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1127-1210 1.36e-11

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 62.25  E-value: 1.36e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  1127 PGPPVRLVFPEVRLTSVRIVWQPPEEPNGI--ILGYQIAYRlasSSPHTFTTVEVGATVRQFTATDLAPESAYIFRLSAK 1204
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYR---EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 1370509662  1205 TRQGWG 1210
Cdd:smart00060   78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 143-224 1.52e-11

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.14  E-value: 1.52e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   143 SRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISrLQNPRYKVLASGG---LRIQKLRPEDSGIFQCFASNEGGEIQTH 219
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLL-AESGRFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 1370509662   220 TYLDV 224
Cdd:smart00410   81 TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
1028-1114 1.93e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 1.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1028 APENVSAEAVSSTQILLTWTsvPEQDQNGLILGYKILFRAKDlDPEPRSHIVRGNHTQSALLAGLRKFVLYELQVLAFTR 1107
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWT--PPPDGNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 1370509662 1108 IGNGVPS 1114
Cdd:pfam00041   79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 721-803 3.30e-11

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 61.09  E-value: 3.30e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   721 PGAVGHLSFTEILDTSLKVSWQEPLEKNGiiTGYQISWEVYGRNDSRLTHTLNST--THEYKIQGLSSLTTYTIDVAAVT 798
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTpsSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1370509662   799 AVGTG 803
Cdd:smart00060   79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
1128-1212 3.60e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 3.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1128 GPPVRLVFPEVRLTSVRIVWQPPEEPNGIILGYQIAYRlASSSPHTFTTVEVGATVRQFTATDLAPESAYIFRLSAKTRQ 1207
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR-PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*
gi 1370509662 1208 GWGEP 1212
Cdd:pfam00041   80 GEGPP 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 42-113 6.07e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 60.27  E-value: 6.07e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662   42 PTIVVPPGNRSVVAGSSeTTLECIASARPVEdlSVTWKRNGVRITSGLHSF------GRRLTISNPTSADTGPYVCEA 113
Cdd:pfam13927    2 PVITVSPSSVTVREGET-VTLTCEATGSPPP--TITWYKNGEPISSGSTRSrslsgsNSTLTISNVTRSDAGTYTCVA 76
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1028-1116 1.57e-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: 59.43  E-value: 1.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1028 APENVSAEAVSSTQILLTWTsvPEQDQNGLILGYKILFRAKDlDPEPRSHIVRGNHTQSALLAGLRKFVLYELQVLAFTR 1107
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWT--PPEDDGGPITGYVVEYREKG-SGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                   ....*....
gi 1370509662 1108 IGNGVPSTP 1116
Cdd:cd00063     80 GGESPPSES 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 819-915 4.91e-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: 4.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  819 PGAPSNLVISNISPRSATLQFRPGYDGKTSISRWIVEGQVGaigDEEEWVTLyeEENEPDAQMLEIPNLTPYTHYRFRMK 898
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREK---GSGDWKEV--EVTPGSETSYTLTGLKPGTEYEFRVR 75

                           90
                   ....*....|....*..
gi 1370509662  899 QVNIVGPSPYSPSSRVI 915
Cdd:cd00063     76 AVNGGGESPPSESVTVT 92
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 329-413 6.22e-10

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: 57.87  E-value: 6.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  329 PEDHVVIKGTTATLHCGATHDPRVSLRyvWKKDNVALTPSSTSRIVVEKDGSLLI-----SQTWSGDIGDYSCE--IVSE 401
Cdd:cd05722      8 PSDIVAMRGGPVVLNCSAESDPPPKIE--WKKDGVLLNLVSDERRQQLPNGSLLItsvvhSKHNKPDEGFYQCVaqNESL 85

                           90
                   ....*....|..
gi 1370509662  402 GGNDSRMARLEV 413
Cdd:cd05722     86 GSIVSRTARVTV 97
fn3 pfam00041
Fibronectin type III domain;
820-909 6.87e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 6.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  820 GAPSNLVISNISPRSATLQFRPGYDGKTSISRWIVegQVGAIGDEEEWVtlyEEENEPDAQMLEIPNLTPYTHYRFRMKQ 899
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEV--EYRPKNSGEPWN---EITVPGTTTSVTLTGLKPGTEYEVRVQA 75

                           90
                   ....*....|
gi 1370509662  900 VNIVGPSPYS 909
Cdd:pfam00041   76 VNGGGEGPPS 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 324-397 7.95e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.11  E-value: 7.95e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370509662  324 SIVHPPEDHVVIKGTTATLHCGATHDPRVSlrYVWKKDNVALTPSSTS-RIVVEKDGSLLISQTWSGDIGDYSCE 397
Cdd:pfam13927    3 VITVSPSSVTVREGETVTLTCEATGSPPPT--ITWYKNGEPISSGSTRsRSLSGSNSTLTISNVTRSDAGTYTCV 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 621-716 8.71e-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: 54.42  E-value: 8.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  621 PPQNVQTEAVNSTTIQFLWNPPPqqFINGINQGYKLLAWPADAPEAVTVVTIAPDfhgVHHGHITNLKKFTAYFTSVLCF 700
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGYVVEYREKGSGDWKEVEVTPGS---ETSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....*.
gi 1370509662  701 TTPGDGPPSTPQLVWT 716
Cdd:cd00063     78 NGGGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1632-1716 8.89e-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: 8.89e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  1632 PGSPRDVLVTK-SASELTLQWT--EGHSGDTPTTGYVIEARPSDEGlwdmfVKDIPRSATSYTLSLDKLRQGVTYEFRVV 1708
Cdd:smart00060    1 PSPPSNLRVTDvTSTSVTLSWEppPDDGITGYIVGYRVEYREEGSE-----WKEVNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ....*...
gi 1370509662  1709 AVNEAGYG 1716
Cdd:smart00060   76 AVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1028-1111 1.46e-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: 53.39  E-value: 1.46e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  1028 APENVSAEAVSSTQILLTWTSVPEQDQNGLILGYKILFRAKDldpEPRSHIVRGNHTQSALLAGLRKFVLYELQVLAFTR 1107
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEG---SEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1370509662  1108 IGNG 1111
Cdd:smart00060   80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
621-709 1.58e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.49  E-value: 1.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  621 PPQNVQTEAVNSTTIQFLWNPPPQQfiNGINQGYKLLAWPADAPEAVTVVTIAPDFHGVhhgHITNLKKFTAYFTSVLCF 700
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDG--NGPITGYEVEYRPKNSGEPWNEITVPGTTTSV---TLTGLKPGTEYEVRVQAV 76


                   ....*....
gi 1370509662  701 TTPGDGPPS 709
Cdd:pfam00041   77 NGGGEGPPS 85
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 47-119 3.97e-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: 49.81  E-value: 3.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   47 PPGNRSVVAGSsETTLECIASARPVEDlsVTWKRNGVRITSG-----LHSFGRRLTISNPTSADTGPYVCEAA--LPGSA 119
Cdd:cd20970      8 PSFTVTAREGE-NATFMCRAEGSPEPE--ISWTRNGNLIIEFntryiVRENGTTLTIRNIRRSDMGIYLCIASngVPGSV 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 819-906 1.86e-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: 47.61  E-value: 1.86e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   819 PGAPSNLVISNISPRSATLQF-RPGYDGKTS-ISRWIVEGQvgaiGDEEEWVTLyeeENEPDAQMLEIPNLTPYTHYRFR 896
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWePPPDDGITGyIVGYRVEYR----EEGSEWKEV---NVTPSSTSYTLTGLKPGTEYEFR 73

                            90
                    ....*....|
gi 1370509662   897 MKQVNIVGPS 906
Cdd:smart00060   74 VRAVNGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 48-113 5.11e-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: 46.34  E-value: 5.11e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370509662    48 PGNRSVVAGSSeTTLECIASARPveDLSVTWKRNGV-------RITSGLHSFGRRLTISNPTSADTGPYVCEA 113
Cdd:smart00410    1 PPSVTVKEGES-VTLSCEASGSP--PPEVTWYKQGGkllaesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAA 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 329-413 6.52e-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: 45.96  E-value: 6.52e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   329 PEDHVVIKGTTATLHCGATHDPRVSLRYVWKKDNVALTPSSTSRIVVEKDGSLLISQTWSGDIGDYSCEIVSEGGNDSRM 408
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 1370509662   409 ARLEV 413
Cdd:smart00410   81 TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
925-1013 1.63e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.10  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  925 APTSVTVRTASETSLRLRWVPLPDsqynGNPESVGYRIKYWRSDLQSSAVAQVVSdRLEREFTIEELEEWMEYELQMQAF 1004
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD----GNGPITGYEVEYRPKNSGEPWNEITVP-GTTTSVTLTGLKPGTEYEVRVQAV 76


                   ....*....
gi 1370509662 1005 NAVGAGPWS 1013
Cdd:pfam00041   77 NGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 621-706 2.44e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.53  E-value: 2.44e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   621 PPQNVQTEAVNSTTIQFLWNPPPQQFINGINQGYKLLAWPADAPEAVTVVTiapdfHGVHHGHITNLKKFTAYFTSVLCF 700
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVT-----PSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 1370509662   701 TTPGDG 706
Cdd:smart00060   78 NGAGEG 83
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
471-643 7.04e-04

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.55  E-value: 7.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  471 GPEMTGVTVSGLTPARTYQFRVCAVNEVGRGQYS-----------AETSRLMLPEEPPSAPPKNIVAS--------GRTN 531
Cdd:COG4733    472 TPEAGAVWAFGPDELETQLFRVVSIEENEDGTYTitavqhapekyAAIDAGAFDDVPPQWPPVNVTTSeslsvvaqGTAV 551

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  532 QSIMVQWQPPPETEHngvlrgYILRYRLAGlpGEYQQRNITSpevNYCLVTDLIIWTQYEIQVAAYNGAGLGVFSRAVTE 611
Cdd:COG4733    552 TTLTVSWDAPAGAVA------YEVEWRRDD--GNWVSVPRTS---GTSFEVPGIYAGDYEVRVRAINALGVSSAWAASSE 620

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1370509662  612 YTLQGVPTAPPQNVQTEAVNSTT-IQFLWNPPP 643
Cdd:COG4733    621 TTVTGKTAPPPAPTGLTATGGLGgITLSWSFPV 653
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 925-1010 4.65e-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: 4.65e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   925 APTSVTVRTASETSLRLRWVPLPDSQYNGnpESVGYRIKYWRSDLQSSAVAQVVSdrlEREFTIEELEEWMEYELQMQAF 1004
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITG--YIVGYRVEYREEGSEWKEVNVTPS---STSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 1370509662  1005 NAVGAG 1010
Cdd:smart00060   78 NGAGEG 83
 
Name Accession Description Interval E-value
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1271-1635 8.34e-22

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 102.39  E-value: 8.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1271 GEWQTYSSSISHEATACVVDRLRPFTSYKLRLKATNDIGDSDFSSETEAVTTLqdVPGEPPGSVSATPHTTSSVLIQWQP 1350
Cdd:COG3401    178 AAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPT--TPPSAPTGLTATADTPGSVTLSWDP 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1351 PRDESlnglLQGYRIYYRelEYEAGSGTEAKTLKNPIALHAELTDLKKYrRYEVimTAYNIIG-ESPASAPVEVFVGEAA 1429
Cdd:COG3401    256 VTESD----ATGYRVYRS--NSGDGPFTKVATVTTTSYTDTGLTNGTTY-YYRV--TAVDAAGnESAPSNVVSVTTDLTP 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1430 PAmAPQNVQVTPLTASQLEVTWDPpppeSQNGNIQGYKIYYWEADSQNETEKMKVlfLPEPVVRLKNLTSHTKYLVSISA 1509
Cdd:COG3401    327 PA-APSGLTATAVGSSSITLSWTA----SSDADVTGYNVYRSTSGGGTYTKIAET--VTTTSYTDTGLTPGTTYYYKVTA 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1510 FNAAGDGPKSDPQQGRTHQAAPGAPSFLAFSEITSTTLNVSWGEPAAANGILQGYRVVYEPLAPVQGVSKVVTVEVRGNW 1589
Cdd:COG3401    400 VDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTA 479

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1370509662 1590 QRWLKVRDLTKGVTYFFRVQARTITYGPELQANITAGPAEGSPGSP 1635
Cdd:COG3401    480 TTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPD 525
I-set pfam07679
Immunoglobulin I-set domain;
229-319 1.67e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.70  E-value: 1.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSvripRFMLLESGG---LQIAPVFIQDAGNYTCYAA 305
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD----RFKVTYEGGtytLTISNVQPDDSGKYTCVAT 76

                           90
                   ....*....|....
gi 1370509662  306 NTEGSLNASATLTV 319
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 ...
 230-319 9.73e-20

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: 85.63  E-value: 9.73e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  230 VFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILAsgsVRIPRFMLLESGGLQIAPVFIQDAGNYTCYAANTEG 309
Cdd:cd20952      1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLL---GKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSG 77

                           90
                   ....*....|
gi 1370509662  310 SLNASATLTV 319
Cdd:cd20952     78 EATWSAVLDV 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1433-1526 1.94e-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: 1.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1433 APQNVQVTPLTASQLEVTWDPPPPEsqNGNIQGYKIYYWEADSqNETEKMKVLFLPEPVVRLKNLTSHTKYLVSISAFNA 1512
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGS-GDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1370509662 1513 AGDGPKSDPQQGRT 1526
Cdd:cd00063     80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 417-508 5.44e-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: 77.92  E-value: 5.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  417 PHSPQNLLVSPNSSHShaVVLSWVRPFDGNSPILYYIVELSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVN 496
Cdd:cd00063      1 PSPPTNLRVTDVTSTS--VTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                           90
                   ....*....|..
gi 1370509662  497 EVGRGQYSAETS 508
Cdd:cd00063     79 GGGESPPSESVT 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1501-1729 6.34e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 86.59  E-value: 6.34e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1501 TKYLVSISAFNAAGDGPKSDPQQGRTHQAAPGAPSFLAFSEITSTTLNVSWgEPAAANGiLQGYRV--------VYEPLA 1572
Cdd:COG3401    203 TTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW-DPVTESD-ATGYRVyrsnsgdgPFTKVA 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1573 PVQGVSKVVTvevrgnwqrwlkvrDLTKGVTYFFRVQARTITYGPELQANI-TAGPAEGSPGSPRDVLVT-KSASELTLQ 1650
Cdd:COG3401    281 TVTTTSYTDT--------------GLTNGTTYYYRVTAVDAAGNESAPSNVvSVTTDLTPPAAPSGLTATaVGSSSITLS 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1651 WTEghSGDTPTTGYVIEARPSDEGLWDmfvkDIPRSATSYTLSLDKLRQGVTYEFRVVAVNEAG-YGEPSNPSTAVSAQV 1729
Cdd:COG3401    347 WTA--SSDADVTGYNVYRSTSGGGTYT----KIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTASA 420
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1127-1220 6.87e-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: 77.54  E-value: 6.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1127 PGPPVRLVFPEVRLTSVRIVWQPPEEPNGIILGYQIAYRLASSSPHTFTTVEVGaTVRQFTATDLAPESAYIFRLSAKTR 1206
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPG-SETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1370509662 1207 QGWGEPLEATVITT 1220
Cdd:cd00063     80 GGESPPSESVTVTT 93
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 135-224 9.26e-17

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: 77.05  E-value: 9.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISRlQNPRYKVlASGGLRIQKLRPEDSGIFQCFASNEGG 214
Cdd:cd20978      1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG-PMERATV-EDGTLTIINVQPEDTGYYGCVATNEIG 78

                           90
                   ....*....|
gi 1370509662  215 EIQTHTYLDV 224
Cdd:cd20978     79 DIYTETLLHV 88
fn3 pfam00041
Fibronectin type III domain;
419-504 1.75e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.91  E-value: 1.75e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  419 SPQNLLVSPNSSHShaVVLSWVRPFDGNSPILYYIVELSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVNEV 498
Cdd:pfam00041    2 APSNLTVTDVTSTS--LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 1370509662  499 GRGQYS 504
Cdd:pfam00041   80 GEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1098-1475 1.90e-16

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 85.44  E-value: 1.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1098 YELQVLAFTRIGNGVPSTPlILERTKDDAPGPPVRLVFPEVRLTSVRIVWQPPEEPNgiILGYQIaYRlASSSPHTFTTV 1177
Cdd:COG3401    205 YYYRVAATDTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRV-YR-SNSGDGPFTKV 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1178 EVGATVRqFTATDLAPESAYIFRLSAKTRQGWGEPLEATVITTEKRERPAPPRELLVpqAEVTARSLRLQWVPGSDgaSP 1257
Cdd:COG3401    280 ATVTTTS-YTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAAPSGLTA--TAVGSSSITLSWTASSD--AD 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1258 IRYFTMQVRELPRGEWQTYSSSISheATACVVDRLRPFTSYKLRLKATNDIGDSDFSSETEAVTTLQDVPGEPPGSVSAT 1337
Cdd:COG3401    355 VTGYNVYRSTSGGGTYTKIAETVT--TTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDA 432

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1338 PHTTSSVLIQWQPprdeSLNGLLQGYRIYYRELEYEAGSGTEAKTLKNPIALHAELTDLKKYRRYEVimTAYNIIGESPA 1417
Cdd:COG3401    433 VPLTDVAGATAAA----SAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGS--LVGGSGASSVT 506

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662 1418 SAPVEVFVGEAAPAMAPQNVQVTPLTASQLEVTWDPPPPESQNGNIQGYKIYYWEADS 1475
Cdd:COG3401    507 NSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGA 564
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 234-319 2.55e-16

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: 75.51  E-value: 2.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  234 RPVDTTVTDGMTAILRCEVSGAPKPAITWKRENhilasGSVRIPRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGSLNA 313
Cdd:cd05725      3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKED-----GELPKGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEA 77


                   ....*.
gi 1370509662  314 SATLTV 319
Cdd:cd05725     78 SATLTV 83
fn3 pfam00041
Fibronectin type III domain;
1433-1519 4.64e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 74.76  E-value: 4.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1433 APQNVQVTPLTASQLEVTWDPPPPesQNGNIQGYKIYYWEADSqNETEKMKVLFLPEPVVRLKNLTSHTKYLVSISAFNA 1512
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNS-GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 1370509662 1513 AGDGPKS 1519
Cdd:pfam00041   79 GGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1632-1725 4.39e-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: 72.53  E-value: 4.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1632 PGSPRDVLVTK-SASELTLQWTEGHSGDTPTTGYVIEARPSDEGLWdMFVKDIPRSATSYTLslDKLRQGVTYEFRVVAV 1710
Cdd:cd00063      1 PSPPTNLRVTDvTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDW-KEVEVTPGSETSYTL--TGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....*
gi 1370509662 1711 NEAGYGEPSNPSTAV 1725
Cdd:cd00063     78 NGGGESPPSESVTVT 92
I-set pfam07679
Immunoglobulin I-set domain;
135-224 5.19e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 71.90  E-value: 5.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPeSRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISrlQNPRYKVLASGG---LRIQKLRPEDSGIFQCFASN 211
Cdd:pfam07679    1 PKFTQKP-KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR--SSDRFKVTYEGGtytLTISNVQPDDSGKYTCVATN 77

                           90
                   ....*....|...
gi 1370509662  212 EGGEIQTHTYLDV 224
Cdd:pfam07679   78 SAGEAEASAELTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 229-306 6.63e-15

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 71.44  E-value: 6.63e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRiPRFMLLESGGLQIAPVFIQDAGNYTCYAAN 306
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTR-SRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 149-224 1.03e-14

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: 70.99  E-value: 1.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  149 VEETVDIG------CQAMGVPLPTLQWYKDAISIsRLQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGEIQTHTYL 222
Cdd:cd20952      7 QNQTVAVGgtvvlnCQATGEPVPTISWLKDGVPL-LGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVL 85


                   ..
gi 1370509662  223 DV 224
Cdd:cd20952     86 DV 87
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 235-319 1.19e-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: 71.00  E-value: 1.19e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   235 PVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIPRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGSLNAS 314
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 1370509662   315 ATLTV 319
Cdd:smart00410   81 TTLTV 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1226-1321 1.28e-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: 70.99  E-value: 1.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1226 PAPPRELLVpqAEVTARSLRLQWVPGSDGASPIRYFTMQVRELPRGEWQTYSSSISHEaTACVVDRLRPFTSYKLRLKAT 1305
Cdd:cd00063      1 PSPPTNLRV--TDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....*.
gi 1370509662 1306 NDIGDSDFSSETEAVT 1321
Cdd:cd00063     78 NGGGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 417-501 1.32e-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: 70.72  E-value: 1.32e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   417 PHSPQNLLVSPNSSHShaVVLSWVRPFDGN--SPILYYIVELSENNSPWKVHlsNVGPEMTGVTVSGLTPARTYQFRVCA 494
Cdd:smart00060    1 PSPPSNLRVTDVTSTS--VTLSWEPPPDDGitGYIVGYRVEYREEGSEWKEV--NVTPSSTSYTLTGLKPGTEYEFRVRA 76


                    ....*..
gi 1370509662   495 VNEVGRG 501
Cdd:smart00060   77 VNGAGEG 83
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 229-319 3.24e-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: 69.83  E-value: 3.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIprfMLLESGG---LQIAPVFIQDAGNYTCYAA 305
Cdd:cd05744      1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHK---MLVRENGrhsLIIEPVTKRDAGIYTCIAR 77

                           90
                   ....*....|....
gi 1370509662  306 NTEGSLNASATLTV 319
Cdd:cd05744     78 NRAGENSFNAELVV 91
fn3 pfam00041
Fibronectin type III domain;
722-803 3.76e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 3.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  722 GAVGHLSFTEILDTSLKVSWQEPLEKNGIITGYQISWEVYGRNDSRLTHTLNSTTHEYKIQGLSSLTTYTIDVAAVTAVG 801
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ..
gi 1370509662  802 TG 803
Cdd:pfam00041   81 EG 82
fn3 pfam00041
Fibronectin type III domain;
520-606 4.27e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 4.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  520 PPKNIVASGRTNQSIMVQWQPPPEteHNGVLRGYILRYRLAGLPGEYQQRNITSPEvNYCLVTDLIIWTQYEIQVAAYNG 599
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNSGEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 1370509662  600 AGLGVFS 606
Cdd:pfam00041   79 GGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1433-1516 6.55e-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: 6.55e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  1433 APQNVQVTPLTASQLEVTWDPPPPESQNGNIQGYKIYYWEADSQNETEKMKVlflPEPVVRLKNLTSHTKYLVSISAFNA 1512
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTP---SSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1370509662  1513 AGDG 1516
Cdd:smart00060   80 AGEG 83
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 229-319 8.00e-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: 68.64  E-value: 8.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVD--TTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSvripRFMLLESGGLQIAPVFIQDAGNYTCYAAN 306
Cdd:cd04969      1 PDFELNPVKkkILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSS----RICILPDGSLKIKNVTKSDEGKYTCFAVN 76

                           90
                   ....*....|...
gi 1370509662  307 TEGSLNASATLTV 319
Cdd:cd04969     77 FFGKANSTGSLSV 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
356-802 8.33e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.58  E-value: 8.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  356 YVWKKDNVALTPSSTSRIVVEKDGSLLISQTWSGDIGD--------YSCEIVSEGGNDSRMARLEVI---ELPHSPQNLL 424
Cdd:COG3401    161 SSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDiepgttyyYRVAATDTGGESAPSNEVSVTtptTPPSAPTGLT 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  425 VSPNSSHShaVVLSWVRPfdGNSPILYYIVELSENNSPWKVHLSNVgpEMTGVTVSGLTPARTYQFRVCAVNEVG-RGQY 503
Cdd:COG3401    241 ATADTPGS--VTLSWDPV--TESDATGYRVYRSNSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAP 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  504 SAETSrlMLPEEPPSAPPKNIVASGRTNQSIMVQWQPPPetehNGVLRGYILrYRLAGLPGEYQQRNITSPEVNYcLVTD 583
Cdd:COG3401    315 SNVVS--VTTDLTPPAAPSGLTATAVGSSSITLSWTASS----DADVTGYNV-YRSTSGGGTYTKIAETVTTTSY-TDTG 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  584 LIIWTQYEIQVAAYNGAGL-GVFSRAVTEYTLQGVPTAPPQNVQTEAVNSTTIQFLWNPppqqfinginqgykLLAWPAD 662
Cdd:COG3401    387 LTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAA--------------SAASNPG 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  663 APEAVTVVTIAPDFHGVHHGHITNLKKFTAYFTSVLCFTTPGDGPPSTPQLVWTQEDKPGAVGHLSFTEILDTSLKVSWQ 742
Cdd:COG3401    453 VSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTG 532

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662  743 EPLEKNGIITG--------YQISWEVYGRNDSRLTHTLNSTTHEYKIQGLSSLTTYTIDVAAVTAVGT 802
Cdd:COG3401    533 ASPVTVGASTGdvlitdlvSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTL 600
fn3 pfam00041
Fibronectin type III domain;
1633-1719 9.13e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.21  E-value: 9.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1633 GSPRDVLVT-KSASELTLQWTEGHSGDTPTTGYVIEARPSDEGlWDMFVKDIPRSATSYTLSldKLRQGVTYEFRVVAVN 1711
Cdd:pfam00041    1 SAPSNLTVTdVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLT--GLKPGTEYEVRVQAVN 77


                   ....*...
gi 1370509662 1712 EAGYGEPS 1719
Cdd:pfam00041   78 GGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 721-803 1.25e-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: 68.29  E-value: 1.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  721 PGAVGHLSFTEILDTSLKVSWQEPLEKNGIITGYQISWEVYGRNDSRLTHTLNSTTHEYKIQGLSSLTTYTIDVAAVTAV 800
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ...
gi 1370509662  801 GTG 803
Cdd:cd00063     81 GES 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 520-613 4.27e-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: 66.75  E-value: 4.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  520 PPKNIVASGRTNQSIMVQWQPPPETehNGVLRGYILRYRLAGlPGEYQQRNITSPEVNYCLVTDLIIWTQYEIQVAAYNG 599
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKG-SGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1370509662  600 AGLGVFSRAVTEYT 613
Cdd:cd00063     80 GGESPPSESVTVTT 93
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 231-319 1.38e-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: 65.33  E-value: 1.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  231 FTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRE--NHILASGSVRIprFMLLESGGLQIAPVFIQDAGNYTCYAANTE 308
Cdd:cd05763      2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDggTDFPAARERRM--HVMPEDDVFFIVDVKIEDTGVYSCTAQNSA 79

                           90
                   ....*....|.
gi 1370509662  309 GSLNASATLTV 319
Cdd:cd05763     80 GSISANATLTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1329-1423 3.21e-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: 3.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1329 EPPGSVSATPHTTSSVLIQWQPPRDEslNGLLQGYRIYYRELEyeAGSGTEAKTlKNPIALHAELTDLKKYRRYEVIMTA 1408
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKG--SGDWKEVEV-TPGSETSYTLTGLKPGTEYEFRVRA 76

                           90
                   ....*....|....*
gi 1370509662 1409 YNIIGESPASAPVEV 1423
Cdd:cd00063     77 VNGGGESPPSESVTV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1531-1612 5.18e-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: 5.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1531 PGAPSFLAFSEITSTTLNVSWGEPAAANGILQGYRVVYEPLapvqGVSKVVTVEVRGNWQRWLKVRDLTKGVTYFFRVQA 1610
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREK----GSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76


                   ..
gi 1370509662 1611 RT 1612
Cdd:cd00063     77 VN 78
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
686-953 5.48e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 70.80  E-value: 5.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  686 NLKKFTAYFTSVLCFTTPGDGPPSTPQLVWTQEDKPGAVGHLSFTEILDTSLKVSWQEPLEKNgiITGYQISWEVYGRND 765
Cdd:COG3401    198 DIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNSGDGP 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  766 SRLTHTLNSTTheYKIQGLSSLTTYTIDVAAVTAVGTGLVTSSTISSGVPPDLPGAPSNLVISNISPRSATLQFRPGYDG 845
Cdd:COG3401    276 FTKVATVTTTS--YTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDA 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  846 KtsISRWIVEGQVGAIGdeeEWVTLYEEENEPdaqMLEIPNLTPYTHYRFRMKQVNIVGPSPYSPSSRVIQTLQAPPDVA 925
Cdd:COG3401    354 D--VTGYNVYRSTSGGG---TYTKIAETVTTT---SYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGES 425

                          250       260
                   ....*....|....*....|....*...
gi 1370509662  926 PTSVTVRTASETSLRLRWVPLPDSQYNG 953
Cdd:COG3401    426 LTASVDAVPLTDVAGATAAASAASNPGV 453
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1000-1344 8.35e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 70.42  E-value: 8.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1000 QMQAFNAVGAGPWSEVVRGRTRESVPSAaPENVSAEAVSSTQILLTWTSVPEQDqnglILGYKIlFRAKDlDPEPRSHIV 1079
Cdd:COG3401    208 RVAATDTGGESAPSNEVSVTTPTTPPSA-PTGLTATADTPGSVTLSWDPVTESD----ATGYRV-YRSNS-GDGPFTKVA 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1080 RGNHTqSALLAGLRKFVLYELQVLAFTRIGN-GVPSTPLILErTKDDAPGPPVRLVFPEVRLTSVRIVWQPPEEPNgiIL 1158
Cdd:COG3401    281 TVTTT-SYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVT-TDLTPPAAPSGLTATAVGSSSITLSWTASSDAD--VT 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1159 GYQIaYRlASSSPHTFTTVEVGATVRQFTATDLAPESAYIFRLSAKTRQG----WGEPLEATVITTEKRERP-APPRELL 1233
Cdd:COG3401    357 GYNV-YR-STSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSATTASAASGESLtASVDAVP 434

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1234 VPQAEVTARSLRLQWVPGSDGASPIRYFTMQVRELPRGEWQTYSSSISheatacvvdrlrPFTSYKLRLKATNDIGDSDF 1313
Cdd:COG3401    435 LTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTT------------DTTTANLSVTTGSLVGGSGA 502

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1370509662 1314 SSETEAVTTLQDVPGEPPGSVSATPHTTSSV 1344
Cdd:COG3401    503 SSVTNSVSVIGASAAAAVGGAPDGTPNVTGA 533
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 231-319 9.78e-12

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: 63.05  E-value: 9.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  231 FTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRE--NHILASGSVRIP--RFMLLESGGLQIAPVFIQDAGNYTCYAAN 306
Cdd:cd05726      2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEgsQNLLFPYQPPQPssRFSVSPTGDLTITNVQRSDVGYYICQALN 81

                           90
                   ....*....|...
gi 1370509662  307 TEGSLNASATLTV 319
Cdd:cd05726     82 VAGSILAKAQLEV 94
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 520-603 1.00e-11

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 62.63  E-value: 1.00e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   520 PPKNIVASGRTNQSIMVQWQPPPETEHNGVLRGYILRYRLAGLPgeyQQRNITSPEVNYCLVTDLIIWTQYEIQVAAYNG 599
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSE---WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1370509662   600 AGLG 603
Cdd:smart00060   80 AGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 134-211 1.12e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.20  E-value: 1.12e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370509662  134 PPYFTAEPESrISAEVEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPRYKVLASGG-LRIQKLRPEDSGIFQCFASN 211
Cdd:pfam13927    1 KPVITVSPSS-VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNStLTISNVTRSDAGTYTCVASN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1127-1210 1.36e-11

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 62.25  E-value: 1.36e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  1127 PGPPVRLVFPEVRLTSVRIVWQPPEEPNGI--ILGYQIAYRlasSSPHTFTTVEVGATVRQFTATDLAPESAYIFRLSAK 1204
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYR---EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 1370509662  1205 TRQGWG 1210
Cdd:smart00060   78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 143-224 1.52e-11

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.14  E-value: 1.52e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   143 SRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISrLQNPRYKVLASGG---LRIQKLRPEDSGIFQCFASNEGGEIQTH 219
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLL-AESGRFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 1370509662   220 TYLDV 224
Cdd:smart00410   81 TTLTV 85
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 229-319 1.92e-11

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: 62.09  E-value: 1.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIPrfMLLESGG---LQIAPVFIQDAGNYTCYAA 305
Cdd:cd05892      1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRIS--LYQDNCGricLLIQNANKKDAGWYTVSAV 78

                           90
                   ....*....|....
gi 1370509662  306 NTEGSLNASATLTV 319
Cdd:cd05892     79 NEAGVVSCNARLDV 92
fn3 pfam00041
Fibronectin type III domain;
1028-1114 1.93e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 1.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1028 APENVSAEAVSSTQILLTWTsvPEQDQNGLILGYKILFRAKDlDPEPRSHIVRGNHTQSALLAGLRKFVLYELQVLAFTR 1107
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWT--PPPDGNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 1370509662 1108 IGNGVPS 1114
Cdd:pfam00041   79 GGEGPPS 85
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 232-310 2.10e-11

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: 61.87  E-value: 2.10e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370509662  232 TQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSvripRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGS 310
Cdd:cd20968      3 TRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENN----RIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGI 77
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 228-319 2.59e-11

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: 61.44  E-value: 2.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  228 APVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGsvriPRFMLLESGGLQ---IAPVFIQDAGNYTCYA 304
Cdd:cd20972      1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNS----PDIQIHQEGDLHsliIAEAFEEDTGRYSCLA 76

                           90
                   ....*....|....*
gi 1370509662  305 ANTEGSLNASATLTV 319
Cdd:cd20972     77 TNSVGSDTTSAEIFV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 229-319 2.67e-11

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: 61.67  E-value: 2.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKReNHILASGSVRIPRFMLLESGG---LQIAPVFIQDAGNYTCYAA 305
Cdd:cd20951      1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYK-NGVPIDPSSIPGKYKIESEYGvhvLHIRRVTVEDSAVYSAVAK 79

                           90
                   ....*....|....
gi 1370509662  306 NTEGSLNASATLTV 319
Cdd:cd20951     80 NIHGEASSSASVVV 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 721-803 3.30e-11

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 61.09  E-value: 3.30e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   721 PGAVGHLSFTEILDTSLKVSWQEPLEKNGiiTGYQISWEVYGRNDSRLTHTLNST--THEYKIQGLSSLTTYTIDVAAVT 798
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTpsSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1370509662   799 AVGTG 803
Cdd:smart00060   79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
1128-1212 3.60e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 3.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1128 GPPVRLVFPEVRLTSVRIVWQPPEEPNGIILGYQIAYRlASSSPHTFTTVEVGATVRQFTATDLAPESAYIFRLSAKTRQ 1207
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR-PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*
gi 1370509662 1208 GWGEP 1212
Cdd:pfam00041   80 GEGPP 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 246-306 3.87e-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: 60.42  E-value: 3.87e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370509662  246 AILRCEVSGAPKPAITWKRENHILASgSVRIPRFMLLESGGLQIAPVFIQDAGNYTCYAAN 306
Cdd:cd00096      1 VTLTCSASGNPPPTITWYKNGKPLPP-SSRDSRRSELGNGTLTISNVTLEDSGTYTCVASN 60
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 153-220 5.71e-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: 60.04  E-value: 5.71e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370509662  153 VDIGCQAMGVPLPTLQWYKDAISISR-LQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGEIQTHT 220
Cdd:cd00096      1 VTLTCSASGNPPPTITWYKNGKPLPPsSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASAS 69
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 42-113 6.07e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 60.27  E-value: 6.07e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662   42 PTIVVPPGNRSVVAGSSeTTLECIASARPVEdlSVTWKRNGVRITSGLHSF------GRRLTISNPTSADTGPYVCEA 113
Cdd:pfam13927    2 PVITVSPSSVTVREGET-VTLTCEATGSPPP--TITWYKNGEPISSGSTRSrslsgsNSTLTISNVTRSDAGTYTCVA 76
fn3 pfam00041
Fibronectin type III domain;
1532-1618 6.47e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 6.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1532 GAPSFLAFSEITSTTLNVSWGEPAAANGILQGYRVVYEplaPVQGVSKVVTVEVRGNwQRWLKVRDLTKGVTYFFRVQAR 1611
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR---PKNSGEPWNEITVPGT-TTSVTLTGLKPGTEYEVRVQAV 76


                   ....*...
gi 1370509662 1612 T-ITYGPE 1618
Cdd:pfam00041   77 NgGGEGPP 84
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 234-318 6.57e-11

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: 60.45  E-value: 6.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  234 RPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSvripRFMLLES---GGLQIAPVFIQDAGNYTCYAANTEGS 310
Cdd:cd05747      9 KPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQ----RHQITSTeykSTFEISKVQMSDEGNYTVVVENSEGK 84


                   ....*...
gi 1370509662  311 LNASATLT 318
Cdd:cd05747     85 QEAQFTLT 92
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 229-319 7.18e-11

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: 60.40  E-value: 7.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTV--TDGMTAILRCEVSGAPKPAITWKRENHILASGSvripRFMLLESGGLQIAPVFIQDAGNYTCYAAN 306
Cdd:cd05852      1 PTFEFNPMKKKIlaAKGGRVIIECKPKAAPKPKFSWSKGTELLVNNS----RISIWDDGSLEILNITKLDEGSYTCFAEN 76

                           90
                   ....*....|...
gi 1370509662  307 TEGSLNASATLTV 319
Cdd:cd05852     77 NRGKANSTGVLSV 89
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 229-319 1.01e-10

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: 59.71  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRP-VDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIprfmLLESGGLQIAPVFIQDAGNYTCYAANT 307
Cdd:cd20978      1 PKFIQKPeKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERA----TVEDGTLTIINVQPEDTGYYGCVATNE 76

                           90
                   ....*....|..
gi 1370509662  308 EGSLNASATLTV 319
Cdd:cd20978     77 IGDIYTETLLHV 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1028-1116 1.57e-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: 59.43  E-value: 1.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1028 APENVSAEAVSSTQILLTWTsvPEQDQNGLILGYKILFRAKDlDPEPRSHIVRGNHTQSALLAGLRKFVLYELQVLAFTR 1107
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWT--PPEDDGGPITGYVVEYREKG-SGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                   ....*....
gi 1370509662 1108 IGNGVPSTP 1116
Cdd:cd00063     80 GGESPPSES 88
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 135-214 1.68e-10

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: 59.58  E-value: 1.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRiSAEVEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPRYKVLASGG-LRIQKLRPEDSGIFQCFASNEG 213
Cdd:cd05736      1 PVIRVYPEFQ-AKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSeLHISNVRYEDTGAYTCIAKNEG 79


                   .
gi 1370509662  214 G 214
Cdd:cd05736     80 G 80
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 229-319 2.60e-10

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: 59.10  E-value: 2.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWK-----RENHILASGSVRiPRFMLLESGGLQIAPVFIQDAGNYTCY 303
Cdd:cd05765      1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEkqvpgKENLIMRPNHVR-GNVVVTNIGQLVIYNAQPQDAGLYTCT 79

                           90
                   ....*....|....*.
gi 1370509662  304 AANTEGSLNASATLTV 319
Cdd:cd05765     80 ARNSGGLLRANFPLSV 95
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 228-319 2.83e-10

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: 58.80  E-value: 2.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  228 APVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIPRFMLLesGGLQIAPVFIQDAGNYTCYAANT 307
Cdd:cd20976      1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGV--GELHIQDVLPEDHGTYTCLAKNA 78

                           90
                   ....*....|..
gi 1370509662  308 EGSLNASATLTV 319
Cdd:cd20976     79 AGQVSCSAWVTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
605-1063 3.77e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.02  E-value: 3.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  605 FSRAVTEYTLQGVPTAPPQNVQTEAVNSTTIQFLWNPPP-QQFINGINQGYKLLAWPADAPEAVTVVTIAPDFHGVHHGH 683
Cdd:COG3401     19 ANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVaAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLT 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  684 ITNLKKFTAYFTSVLCFTTPGDGPPSTPQLVWTQEDKPGAVGHLSFTEILDTSLKVSWQEPLEKNGIITGYQISWEVYGR 763
Cdd:COG3401     99 GSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  764 NDSRLTHTLNSTTHEYKIQGLSSLTTYTIDVAAVTAVGTGlVTSSTISSGVPPDLPGAPSNLVISNISPRSATLQFRPGY 843
Cdd:COG3401    179 AVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGES-APSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVT 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  844 DgkTSISRWIVEgqvGAIGDEEEWVTLYEEENEP--DaqmleiPNLTPYTHYRFRMKQVNIVG-PSPYSPSSRViQTLQA 920
Cdd:COG3401    258 E--SDATGYRVY---RSNSGDGPFTKVATVTTTSytD------TGLTNGTTYYYRVTAVDAAGnESAPSNVVSV-TTDLT 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  921 PPDvAPTSVTVRTASETSLRLRWvplpdsQYNGNPESVGYRIkyWRSDLQSSAVAQVVSDRLEREFTIEELEEWMEYELQ 1000
Cdd:COG3401    326 PPA-APSGLTATAVGSSSITLSW------TASSDADVTGYNV--YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYK 396

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662 1001 MQAFNAVG-AGPWSEVVRGRT----RESVPSAAPENVSAEAVSSTQILLTWTSVPEQDQNGLILGYKI 1063
Cdd:COG3401    397 VTAVDAAGnESAPSEEVSATTasaaSGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDT 464
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 233-319 4.46e-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: 4.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  233 QRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSvRIPrfmlLESGGLQIAPVFIQDAGNYTCYAANTEGSLN 312
Cdd:cd05728      4 KVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASEN-RIE----VEAGDLRITKLSLSDSGMYQCVAENKHGTIY 78


                   ....*..
gi 1370509662  313 ASATLTV 319
Cdd:cd05728     79 ASAELAV 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 819-915 4.91e-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: 4.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  819 PGAPSNLVISNISPRSATLQFRPGYDGKTSISRWIVEGQVGaigDEEEWVTLyeEENEPDAQMLEIPNLTPYTHYRFRMK 898
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREK---GSGDWKEV--EVTPGSETSYTLTGLKPGTEYEFRVR 75

                           90
                   ....*....|....*..
gi 1370509662  899 QVNIVGPSPYSPSSRVI 915
Cdd:cd00063     76 AVNGGGESPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
1330-1418 5.54e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.81  E-value: 5.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1330 PPGSVSATPHTTSSVLIQWQPPRDesLNGLLQGYRIYYRELeyeaGSGTEAKTLKNPIALH-AELTDLKKYRRYEVIMTA 1408
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPK----NSGEPWNEITVPGTTTsVTLTGLKPGTEYEVRVQA 75

                           90
                   ....*....|
gi 1370509662 1409 YNIIGESPAS 1418
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 ...
 329-413 6.22e-10

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: 57.87  E-value: 6.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  329 PEDHVVIKGTTATLHCGATHDPRVSLRyvWKKDNVALTPSSTSRIVVEKDGSLLI-----SQTWSGDIGDYSCE--IVSE 401
Cdd:cd05722      8 PSDIVAMRGGPVVLNCSAESDPPPKIE--WKKDGVLLNLVSDERRQQLPNGSLLItsvvhSKHNKPDEGFYQCVaqNESL 85

                           90
                   ....*....|..
gi 1370509662  402 GGNDSRMARLEV 413
Cdd:cd05722     86 GSIVSRTARVTV 97
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1330-1415 6.75e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 57.24  E-value: 6.75e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  1330 PPGSVSATPHTTSSVLIQWQPPRDESLNgllqGYRIYYReLEYEAGSGTEAKTLKNPIALHAELTDLKKYRRYEVIMTAY 1409
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGIT----GYIVGYR-VEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 1370509662  1410 NIIGES 1415
Cdd:smart00060   78 NGAGEG 83
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 231-319 7.55e-10

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: 57.34  E-value: 7.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  231 FTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIPRFMLLESgGLQIAPVFIQDAGNYTCYAANTEGS 310
Cdd:cd20949      2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILAD-GLLINKVTQDDTGEYTCRAYQVNSI 80


                   ....*....
gi 1370509662  311 LNASATLTV 319
Cdd:cd20949     81 ASDMQERTV 89
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 136-224 1.77e-09

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: 56.44  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  136 YFTAEPESRISAEvEETVDIGCQAMGVPLPTLQWYKDAISISRL-QNPRYKVlASGGLRIQKLRPEDSGIFQCFASNEGG 214
Cdd:cd05867      1 YWTRRPQSHLYGP-GETARLDCQVEGIPTPNITWSINGAPIEGTdPDPRRHV-SSGALILTDVQPSDTAVYQCEARNRHG 78

                           90
                   ....*....|
gi 1370509662  215 EIQTHTYLDV 224
Cdd:cd05867     79 NLLANAHVHV 88
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 329-413 1.89e-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: 56.25  E-value: 1.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  329 PEDHVVIKGTTATLHCGATH---DPRVSlryvWKKDNVALTpSSTSRIVVEKDGSLLISQTWSGDIGDYSCEIV-SEGGN 404
Cdd:cd05724      4 PSDTQVAVGEMAVLECSPPRghpEPTVS----WRKDGQPLN-LDNERVRIVDDGNLLIAEARKSDEGTYKCVATnMVGER 78


                   ....*....
gi 1370509662  405 DSRMARLEV 413
Cdd:cd05724     79 ESRAARLSV 87
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 151-215 2.10e-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: 55.87  E-value: 2.10e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370509662  151 ETVDIGCQA-MGVPLPTLQWYKDAISIsRLQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGE 215
Cdd:cd05724     13 EMAVLECSPpRGHPEPTVSWRKDGQPL-NLDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGE 77
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 233-319 2.36e-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: 55.87  E-value: 2.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  233 QRPVDTTVTDGMTAILRCEVS-GAPKPAITWKRENHILASGSVRIprfMLLESGGLQIAPVFIQDAGNYTCYAANTEGS- 310
Cdd:cd05724      2 VEPSDTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLDNERV---RIVDDGNLLIAEARKSDEGTYKCVATNMVGEr 78


                   ....*....
gi 1370509662  311 LNASATLTV 319
Cdd:cd05724     79 ESRAARLSV 87
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 136-224 2.56e-09

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: 55.92  E-value: 2.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  136 YFTAEPESRISAEvEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGE 215
Cdd:cd04978      1 YWIIEPPSLVLSP-GETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHGY 79


                   ....*....
gi 1370509662  216 IQTHTYLDV 224
Cdd:cd04978     80 LLANAFLHV 88
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 229-319 3.02e-09

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: 55.88  E-value: 3.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRipRFMLLESG--GLQIAPVFIQDAGNYTCYAAN 306
Cdd:cd20990      1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAH--KMLVRENGvhSLIIEPVTSRDAGIYTCIATN 78

                           90
                   ....*....|...
gi 1370509662  307 TEGSLNASATLTV 319
Cdd:cd20990     79 RAGQNSFNLELVV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1531-1612 4.66e-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: 54.93  E-value: 4.66e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  1531 PGAPSFLAFSEITSTTLNVSWGEPAAANGIlqGYRVVYEpLAPVQGVSKVVTVEVRGNwQRWLKVRDLTKGVTYFFRVQA 1610
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYR-VEYREEGSEWKEVNVTPS-STSYTLTGLKPGTEYEFRVRA 76


                    ..
gi 1370509662  1611 RT 1612
Cdd:smart00060   77 VN 78
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 242-319 6.43e-09

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: 54.17  E-value: 6.43e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662  242 DGMTAILRCEVSGAPKPAITWKRENHILASGSvripRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGSLNASATLTV 319
Cdd:cd05745      1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDR----RHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 229-319 6.81e-09

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: 54.79  E-value: 6.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIprfMLLESGGLQIAPVFIQDAGNYTCYAANTE 308
Cdd:cd05764      1 PLITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNSSRT---LVYDNGTLDILITTVKDTGAFTCIASNPA 77

                           90
                   ....*....|.
gi 1370509662  309 GSLNASATLTV 319
Cdd:cd05764     78 GEATARVELHI 88
fn3 pfam00041
Fibronectin type III domain;
820-909 6.87e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 6.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  820 GAPSNLVISNISPRSATLQFRPGYDGKTSISRWIVegQVGAIGDEEEWVtlyEEENEPDAQMLEIPNLTPYTHYRFRMKQ 899
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEV--EYRPKNSGEPWN---EITVPGTTTSVTLTGLKPGTEYEVRVQA 75

                           90
                   ....*....|
gi 1370509662  900 VNIVGPSPYS 909
Cdd:pfam00041   76 VNGGGEGPPS 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 324-397 7.95e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.11  E-value: 7.95e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370509662  324 SIVHPPEDHVVIKGTTATLHCGATHDPRVSlrYVWKKDNVALTPSSTS-RIVVEKDGSLLISQTWSGDIGDYSCE 397
Cdd:pfam13927    3 VITVSPSSVTVREGETVTLTCEATGSPPPT--ITWYKNGEPISSGSTRsRSLSGSNSTLTISNVTRSDAGTYTCV 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 621-716 8.71e-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: 54.42  E-value: 8.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  621 PPQNVQTEAVNSTTIQFLWNPPPqqFINGINQGYKLLAWPADAPEAVTVVTIAPDfhgVHHGHITNLKKFTAYFTSVLCF 700
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGYVVEYREKGSGDWKEVEVTPGS---ETSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....*.
gi 1370509662  701 TTPGDGPPSTPQLVWT 716
Cdd:cd00063     78 NGGGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1632-1716 8.89e-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: 8.89e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  1632 PGSPRDVLVTK-SASELTLQWT--EGHSGDTPTTGYVIEARPSDEGlwdmfVKDIPRSATSYTLSLDKLRQGVTYEFRVV 1708
Cdd:smart00060    1 PSPPSNLRVTDvTSTSVTLSWEppPDDGITGYIVGYRVEYREEGSE-----WKEVNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ....*...
gi 1370509662  1709 AVNEAGYG 1716
Cdd:smart00060   76 AVNGAGEG 83
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 234-319 9.62e-09

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: 54.12  E-value: 9.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  234 RPVDTTVTDGMTAILRCEVSGAPKPAITWkrenhiLASGSVRIPR--FMLLESGGLQIAPVFIQDAGNYTCYAANTEGSL 311
Cdd:cd05723      3 KPSNIYAHESMDIVFECEVTGKPTPTVKW------VKNGDVVIPSdyFKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNA 76


                   ....*...
gi 1370509662  312 NASATLTV 319
Cdd:cd05723     77 QASAQLII 84
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 229-319 9.72e-09

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: 54.63  E-value: 9.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKR-------ENHILASGsvriPRFMLLESGGLQIAPVFIQDAGNYT 301
Cdd:cd20954      2 PRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKatgstpgEYKDLLYD----PNVRILPNGTLVFGHVQKENEGHYL 77

                           90
                   ....*....|....*....
gi 1370509662  302 CYAANTEGS-LNASATLTV 319
Cdd:cd20954     78 CEAKNGIGSgLSKVIFLKV 96
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 156-224 1.01e-08

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: 54.14  E-value: 1.01e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370509662  156 GCQAMGVPLPTLQWYKDAISISRlQNpRYKVLAsGGLRIQKLRPEDSGIFQCFASNEGGEIQTHTYLDV 224
Cdd:cd05728     20 ECKASGNPRPAYRWLKNGQPLAS-EN-RIEVEA-GDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1028-1111 1.46e-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: 53.39  E-value: 1.46e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  1028 APENVSAEAVSSTQILLTWTSVPEQDQNGLILGYKILFRAKDldpEPRSHIVRGNHTQSALLAGLRKFVLYELQVLAFTR 1107
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEG---SEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1370509662  1108 IGNG 1111
Cdd:smart00060   80 AGEG 83
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 134-212 1.49e-08

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: 54.02  E-value: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  134 PPYFTAEPeSRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPRYKVLASGGLRIQ-----KLRPEDSGIFQCF 208
Cdd:cd05722      1 ELYFLSEP-SDIVAMRGGPVVLNCSAESDPPPKIEWKKDGVLLNLVSDERRQQLPNGSLLITsvvhsKHNKPDEGFYQCV 79


                   ....
gi 1370509662  209 ASNE 212
Cdd:cd05722     80 AQNE 83
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 135-224 1.56e-08

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: 53.70  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEP--ESRISAE-VEETVDIGCQAMGVPLPTLQWYKDAISISrlQNPR---YKV-LASGGLRIQKLRPEDSGIFQC 207
Cdd:cd05857      1 PYWTNPEkmEKKLHAVpAANTVKFRCPAAGNPTPTMRWLKNGKEFK--QEHRiggYKVrNQHWSLIMESVVPSDKGNYTC 78

                           90
                   ....*....|....*...
gi 1370509662  208 FASNEGGEIQtHTY-LDV 224
Cdd:cd05857     79 VVENEYGSIN-HTYhLDV 95
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 135-221 2.86e-08

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: 52.99  E-value: 2.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTaEPESR----ISAEVEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPR-YKVLASG-GLRIQKLRPEDSGIFQCF 208
Cdd:cd05729      1 PRFT-DTEKMeereHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGgTKVEEKGwSLIIERAIPRDKGKYTCI 79

                           90
                   ....*....|...
gi 1370509662  209 ASNEGGEIQtHTY 221
Cdd:cd05729     80 VENEYGSIN-HTY 91
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 229-319 4.46e-08

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: 52.51  E-value: 4.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFT--QRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSvriPRFMLLESGG-LQIAPVFIQDAGNYTCYAA 305
Cdd:cd20970      1 PVIStpQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFN---TRYIVRENGTtLTIRNIRRSDMGIYLCIAS 77

                           90
                   ....*....|....*
gi 1370509662  306 N-TEGSLNASATLTV 319
Cdd:cd20970     78 NgVPGSVEKRITLQV 92
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 151-224 4.68e-08

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: 51.86  E-value: 4.68e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370509662  151 ETVDIGCQAMGVPLPTLQWYK--DAISISRlqnpRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGEIQTHTYLDV 224
Cdd:cd05745      3 QTVDFLCEAQGYPQPVIAWTKggSQLSVDR----RHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 145-217 4.70e-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: 52.15  E-value: 4.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  145 ISAEVE---ETVDIG------CQAMGVPLPTLQWYKDAISISRlqNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGE 215
Cdd:cd20957      2 LSATIDppvQTVDFGrtavfnCSVTGNPIHTVLWMKDGKPLGH--SSRVQILSEDVLVIPSVKREDKGMYQCFVRNDGDS 79


                   ..
gi 1370509662  216 IQ 217
Cdd:cd20957     80 AQ 81
fn3 pfam00041
Fibronectin type III domain;
1228-1314 6.82e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 51.65  E-value: 6.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1228 PPRELLVpqAEVTARSLRLQWVPGSDGASPIRYFTMQVRELPRGE-WQTYssSISHEATACVVDRLRPFTSYKLRLKATN 1306
Cdd:pfam00041    2 APSNLTV--TDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEpWNEI--TVPGTTTSVTLTGLKPGTEYEVRVQAVN 77


                   ....*...
gi 1370509662 1307 DIGDSDFS 1314
Cdd:pfam00041   78 GGGEGPPS 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 157-224 8.97e-08

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: 51.65  E-value: 8.97e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370509662  157 CQAMGVPLPTLQWYKDAISISRLQNPR-YKVLASGG---LRIQKLRPEDSGIFQCFASNEGGEIQTHTYLDV 224
Cdd:cd20951     22 VEVQGKPDPEVKWYKNGVPIDPSSIPGkYKIESEYGvhvLHIRRVTVEDSAVYSAVAKNIHGEASSSASVVV 93
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 134-224 1.18e-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: 51.35  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  134 PPYFTAEPESRISAEVEETVDIGCQAMGVPLPTLQWYKDAISIsRLQNPRYKVLASGG-LRIQKLRPEDSGIFQCFASNE 212
Cdd:cd20970      1 PVISTPQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLI-IEFNTRYIVRENGTtLTIRNIRRSDMGIYLCIASNG 79

                           90
                   ....*....|...
gi 1370509662  213 -GGEIQTHTYLDV 224
Cdd:cd20970     80 vPGSVEKRITLQV 92
fn3 pfam00041
Fibronectin type III domain;
621-709 1.58e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.49  E-value: 1.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  621 PPQNVQTEAVNSTTIQFLWNPPPQQfiNGINQGYKLLAWPADAPEAVTVVTIAPDFHGVhhgHITNLKKFTAYFTSVLCF 700
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDG--NGPITGYEVEYRPKNSGEPWNEITVPGTTTSV---TLTGLKPGTEYEVRVQAV 76


                   ....*....
gi 1370509662  701 TTPGDGPPS 709
Cdd:pfam00041   77 NGGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
42-113 1.86e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 50.72  E-value: 1.86e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662   42 PTIVVPPGNRSVVAGSSeTTLECIASARPveDLSVTWKRNGVRITSGLH------SFGRRLTISNPTSADTGPYVCEA 113
Cdd:pfam07679    1 PKFTQKPKDVEVQEGES-ARFTCTVTGTP--DPEVSWFKDGQPLRSSDRfkvtyeGGTYTLTISNVQPDDSGKYTCVA 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1226-1311 1.95e-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: 50.31  E-value: 1.95e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  1226 PAPPRELLVpqAEVTARSLRLQWVPGSD--GASPIRYFTMQVRElPRGEWQTYSSSISHeaTACVVDRLRPFTSYKLRLK 1303
Cdd:smart00060    1 PSPPSNLRV--TDVTSTSVTLSWEPPPDdgITGYIVGYRVEYRE-EGSEWKEVNVTPSS--TSYTLTGLKPGTEYEFRVR 75


                    ....*...
gi 1370509662  1304 ATNDIGDS 1311
Cdd:smart00060   76 AVNGAGEG 83
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 235-319 2.17e-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: 51.11  E-value: 2.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  235 PVDTTVTDGMTAILRCEVSGAPKPAITWKRenHILASGSVR----IPRFMLLESGG----------LQIAPVFIQDAGNY 300
Cdd:cd05858      8 PANTSVVVGTDAEFVCKVYSDAQPHIQWLK--HVEKNGSKYgpdgLPYVEVLKTAGvnttdkeievLYLRNVTFEDAGEY 85

                           90
                   ....*....|....*....
gi 1370509662  301 TCYAANTEGSLNASATLTV 319
Cdd:cd05858     86 TCLAGNSIGISHHSAWLTV 104
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 134-218 2.77e-07

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: 50.27  E-value: 2.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  134 PPYFTAEPESRISAEVEEtVDIGCQAMGVPLPTLQWYKDAisiSRLQN-PRYKVLASGGLR---IQKLRPEDSGIFQCFA 209
Cdd:cd20972      1 PPQFIQKLRSQEVAEGSK-VRLECRVTGNPTPVVRWFCEG---KELQNsPDIQIHQEGDLHsliIAEAFEEDTGRYSCLA 76


                   ....*....
gi 1370509662  210 SNEGGEIQT 218
Cdd:cd20972     77 TNSVGSDTT 85
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 239-319 2.87e-07

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: 50.20  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  239 TVTDGMTAILRCE-VSGAPKPAITW-KRENHILASGSVRIPRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGSLNASAT 316
Cdd:cd05750     10 TVQEGSKLVLKCEaTSENPSPRYRWfKDGKELNRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGN 89


                   ...
gi 1370509662  317 LTV 319
Cdd:cd05750     90 VTV 92
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 229-319 2.97e-07

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: 50.18  E-value: 2.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWK--------RENHILASGSvripRFMLLESGGLQIAPVFIQDAGNY 300
Cdd:cd05734      2 PRFVVQPNDQDGIYGKAVVLNCSADGYPPPTIVWKhskgsgvpQFQHIVPLNG----RIQLLSNGSLLIKHVLEEDSGYY 77

                           90       100
                   ....*....|....*....|
gi 1370509662  301 TCYAANTEGS-LNASATLTV 319
Cdd:cd05734     78 LCKVSNDVGAdISKSMYLTV 97
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 140-224 3.23e-07

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: 49.70  E-value: 3.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  140 EPESRISAeVEETVDIGCQAMGVPLPTLQWYKDaisISRLQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGEIQTH 219
Cdd:cd05725      3 RPQNQVVL-VDDSAEFQCEVGGDPVPTVRWRKE---DGELPKGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEAS 78


                   ....*
gi 1370509662  220 TYLDV 224
Cdd:cd05725     79 ATLTV 83
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 229-319 3.58e-07

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: 50.04  E-value: 3.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHilASGSVRIPRFMLLESGG---LQIAPVFIQDAGNYTCYAA 305
Cdd:cd20974      1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQ--VISTSTLPGVQISFSDGrakLSIPAVTKANSGRYSLTAT 78

                           90
                   ....*....|....
gi 1370509662  306 NTEGSLNASATLTV 319
Cdd:cd20974     79 NGSGQATSTAELLV 92
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 234-319 3.70e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 49.32  E-value: 3.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  234 RPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASgsvriprfmlleSGGLQIAPVFIQDAGNYTCYAANTEGS-LN 312
Cdd:pfam13895    5 TPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISS------------SPNFFTLSVSAEDSGTYTCVARNGRGGkVS 72


                   ....*..
gi 1370509662  313 ASATLTV 319
Cdd:pfam13895   73 NPVELTV 79
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 235-317 3.85e-07

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: 49.50  E-value: 3.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  235 PVDTTVTDGMTAILRCEVSGAPKPA-ITWKRENHILASGSVRIPRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGSLNA 313
Cdd:pfam00047    3 PPTVTVLEGDSATLTCSASTGSPGPdVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82


                   ....
gi 1370509662  314 SATL 317
Cdd:pfam00047   83 STSL 86
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 47-119 3.97e-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: 49.81  E-value: 3.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   47 PPGNRSVVAGSsETTLECIASARPVEDlsVTWKRNGVRITSG-----LHSFGRRLTISNPTSADTGPYVCEAA--LPGSA 119
Cdd:cd20970      8 PSFTVTAREGE-NATFMCRAEGSPEPE--ISWTRNGNLIIEFntryiVRENGTTLTIRNIRRSDMGIYLCIASngVPGSV 84
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 248-318 4.99e-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: 48.72  E-value: 4.99e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370509662  248 LRCEVSGAPKPAITWKREN-HILASGsvripRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGSLNASATLT 318
Cdd:cd05746      3 IPCSAQGDPEPTITWNKDGvQVTESG-----KFHISPEGYLAIRDVGVADQGRYECVARNTIGYASVSMVLS 69
I-set pfam07679
Immunoglobulin I-set domain;
324-413 6.07e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 49.18  E-value: 6.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  324 SIVHPPEDHVVIKGTTATLHCGAT--HDPRVSlryvWKKDNVALTPSSTSRIVVE-KDGSLLISQTWSGDIGDYSCEIVS 400
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTVTgtPDPEVS----WFKDGQPLRSSDRFKVTYEgGTYTLTISNVQPDDSGKYTCVATN 77

                           90
                   ....*....|...
gi 1370509662  401 EGGNDSRMARLEV 413
Cdd:pfam07679   78 SAGEAEASAELTV 90
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 235-317 6.32e-07

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: 49.07  E-value: 6.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  235 PVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSvripRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGSLNAS 314
Cdd:cd20957      8 PPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSS----RVQILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQAT 83


                   ...
gi 1370509662  315 ATL 317
Cdd:cd20957     84 AEL 86
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 151-224 7.79e-07

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: 48.93  E-value: 7.79e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370509662  151 ETVDIGCQAMGVPLPTLQW-YKDAISISRLQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGEIQTHTYLDV 224
Cdd:cd20969     18 HTVQFVCRADGDPPPAILWlSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 233-319 8.71e-07

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: 48.70  E-value: 8.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  233 QRPVDTTVTDGMTAILRCEVSGAPKPAITWKRenhilASGSVrIPRFMLLESGG-LQIAPVFIQDAGNYTCYAANTEGSL 311
Cdd:cd04968      6 RFPADTYALKGQTVTLECFALGNPVPQIKWRK-----VDGSP-SSQWEITTSEPvLEIPNVQFEDEGTYECEAENSRGKD 79


                   ....*...
gi 1370509662  312 NASATLTV 319
Cdd:cd04968     80 TVQGRIIV 87
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 232-319 1.11e-06

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: 48.34  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  232 TQRPVDTTVTDGMTAILRCEVSGAPKPAITW-KRENHILASGSVRIPRfmlLESG--GLQIAPVFIQDAGNYTCYAANTE 308
Cdd:cd20973      1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWmKDDNPIVESRRFQIDQ---DEDGlcSLIISDVCGDDSGKYTCKAVNSL 77

                           90
                   ....*....|.
gi 1370509662  309 GSLNASATLTV 319
Cdd:cd20973     78 GEATCSAELTV 88
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 157-214 1.13e-06

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: 48.39  E-value: 1.13e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662  157 CQAMGVPLPTLQWYKDAISISrlQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGG 214
Cdd:cd20968     21 CTTMGNPKPSVSWIKGDDLIK--ENNRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLG 76
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 229-319 1.38e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 48.37  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQ----------RPVDTTVTdgmtaiLRCEVSGAPKPAITWKREN------HILASGSVRIPRFMLLesgglqIAPV 292
Cdd:cd05729      1 PRFTDtekmeerehaLPAANKVR------LECGAGGNPMPNITWLKDGkefkkeHRIGGTKVEEKGWSLI------IERA 68

                           90       100
                   ....*....|....*....|....*..
gi 1370509662  293 FIQDAGNYTCYAANTEGSLNASATLTV 319
Cdd:cd05729     69 IPRDKGKYTCIVENEYGSINHTYDVDV 95
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 61-113 1.70e-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: 47.32  E-value: 1.70e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370509662   61 TLECIASARPveDLSVTWKRNGVRITSGLHSFGRR------LTISNPTSADTGPYVCEA 113
Cdd:cd00096      2 TLTCSASGNP--PPTITWYKNGKPLPPSSRDSRRSelgngtLTISNVTLEDSGTYTCVA 58
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 229-317 1.78e-06

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: 48.01  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDT---TVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRipRFMLLeSGGLQIA-PVFIQDAGNYTCYA 304
Cdd:cd04967      2 PVFEEQPDDTifpEDSDEKKVALNCRARANPVPSYRWLMNGTEIDLESDY--RYSLV-DGTLVISnPSKAKDAGHYQCLA 78

                           90
                   ....*....|....
gi 1370509662  305 ANTEGS-LNASATL 317
Cdd:cd04967     79 TNTVGSvLSREATL 92
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
 135-214 1.85e-06

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin. 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 lacks a C" strand.


Pssm-ID: 409396 [Multi-domain]  Cd Length: 94  Bit Score: 47.79  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPRYKVL-ASGGLRIQ--KLRPED-SGIFQCFAS 210
Cdd:cd05733      1 PTITEQSPKDYIVDPRDNITIKCEAKGNPQPTFRWTKDGKFFDPAKDPRVSMRrRSGTLVIDnhNGGPEDyQGEYQCYAS 80


                   ....
gi 1370509662  211 NEGG 214
Cdd:cd05733     81 NELG 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 819-906 1.86e-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: 47.61  E-value: 1.86e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   819 PGAPSNLVISNISPRSATLQF-RPGYDGKTS-ISRWIVEGQvgaiGDEEEWVTLyeeENEPDAQMLEIPNLTPYTHYRFR 896
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWePPPDDGITGyIVGYRVEYR----EEGSEWKEV---NVTPSSTSYTLTGLKPGTEYEFR 73

                            90
                    ....*....|
gi 1370509662   897 MKQVNIVGPS 906
Cdd:smart00060   74 VRAVNGAGEG 83
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 135-224 1.87e-06

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: 47.93  E-value: 1.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESR---ISAEVEETVDIGCQAMGVPLPTLQWYKD--AISISRLQNPRYKVLAsggLRIQKLRPEDSGIFQCFA 209
Cdd:cd05856      1 PRFTQPAKMRrrvIARPVGSSVRLKCVASGNPRPDITWLKDnkPLTPPEIGENKKKKWT---LSLKNLKPEDSGKYTCHV 77

                           90
                   ....*....|....*
gi 1370509662  210 SNEGGEIQTHTYLDV 224
Cdd:cd05856     78 SNRAGEINATYKVDV 92
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 238-319 1.87e-06

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: 47.40  E-value: 1.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  238 TTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIPRFmlleSGGLQIAPVFIQDAGNYTCYAANTEGSlnASATL 317
Cdd:cd05731      5 TMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGRTKFENF----NKTLKIENVSEADSGEYQCTASNTMGS--ARHTI 78


                   ..
gi 1370509662  318 TV 319
Cdd:cd05731     79 SV 80
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 135-216 2.13e-06

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: 48.01  E-value: 2.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRISAE--VEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPRYKVLAsGGLRIQK-LRPEDSGIFQCFASN 211
Cdd:cd04967      2 PVFEEQPDDTIFPEdsDEKKVALNCRARANPVPSYRWLMNGTEIDLESDYRYSLVD-GTLVISNpSKAKDAGHYQCLATN 80


                   ....*
gi 1370509662  212 EGGEI 216
Cdd:cd04967     81 TVGSV 85
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 229-319 2.15e-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: 47.93  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRI-PRFMLLESGGLQIAPVF-----IQDAGNYTC 302
Cdd:cd07693      1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPrSHRIVLPSGSLFFLRVVhgrkgRSDEGVYVC 80

                           90
                   ....*....|....*...
gi 1370509662  303 YAANTEG-SLNASATLTV 319
Cdd:cd07693     81 VAHNSLGeAVSRNASLEV 98
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 239-319 2.78e-06

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: 47.18  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  239 TVTDGMTAILRCEVSGAPKPAITWKRENHILASGSvripRFMLLESGGLQIAPVF-IQDAGNYTCYAANTEGsLNASATL 317
Cdd:cd20958     11 TAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNH----RQRVFPNGTLVIENVQrSSDEGEYTCTARNQQG-QSASRSV 85


                   ..
gi 1370509662  318 TV 319
Cdd:cd20958     86 FV 87
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 326-413 3.34e-06

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: 47.00  E-value: 3.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  326 VHPPEDHVVIKGTTATLHCGATHDPRVSLRyvWKKDNVALtPSSTSRIVveKDGSLLISQTWSGDIGDYSCEIVSEGGND 405
Cdd:cd05725      1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVR--WRKEDGEL-PKGRYEIL--DDHSLKIRKVTAGDMGSYTCVAENMVGKI 75


                   ....*...
gi 1370509662  406 SRMARLEV 413
Cdd:cd05725     76 EASATLTV 83
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 420-507 3.39e-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: 47.02  E-value: 3.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  420 PQNLLVSPNSSHSHAVVlSWVRPFDGNSPILYYIVELSENNSPWKVHLSNVGPEMTG------VTVSGLTPARTYQFRVC 493
Cdd:pfam16656    1 PEQVHLSLTGDSTSMTV-SWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGtgyihrATLTGLEPGTTYYYRVG 79

                           90
                   ....*....|....
gi 1370509662  494 AVNEVGRGQYSAET 507
Cdd:pfam16656   80 DDNGGWSEVYSFTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 925-1020 3.65e-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: 47.11  E-value: 3.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  925 APTSVTVRTASETSLRLRWVPLPDSqyngNPESVGYRIKYWRSDLQSSAVAQVVSDRlEREFTIEELEEWMEYELQMQAF 1004
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDD----GGPITGYVVEYREKGSGDWKEVEVTPGS-ETSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....*.
gi 1370509662 1005 NAVGAGPWSEVVRGRT 1020
Cdd:cd00063     78 NGGGESPPSESVTVTT 93
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 153-214 4.06e-06

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: 46.02  E-value: 4.06e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370509662  153 VDIGCQAMGVPLPTLQWYKDAISISrlQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGG 214
Cdd:cd05746      1 VQIPCSAQGDPEPTITWNKDGVQVT--ESGKFHISPEGYLAIRDVGVADQGRYECVARNTIG 60
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 240-319 4.74e-06

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: 46.77  E-value: 4.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  240 VTDGMTAILRCEVSGAPKPAITWK------RENHILASGSVRIPRFML-LESgglqiapVFIQDAGNYTCYAANTEGSLN 312
Cdd:cd05857     16 VPAANTVKFRCPAAGNPTPTMRWLkngkefKQEHRIGGYKVRNQHWSLiMES-------VVPSDKGNYTCVVENEYGSIN 88


                   ....*..
gi 1370509662  313 ASATLTV 319
Cdd:cd05857     89 HTYHLDV 95
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 48-113 5.11e-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: 46.34  E-value: 5.11e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370509662    48 PGNRSVVAGSSeTTLECIASARPveDLSVTWKRNGV-------RITSGLHSFGRRLTISNPTSADTGPYVCEA 113
Cdd:smart00410    1 PPSVTVKEGES-VTLSCEASGSP--PPEVTWYKQGGkllaesgRFSVSRSGSTSTLTISNVTPEDSGTYTCAA 70
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 135-224 5.66e-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: 46.33  E-value: 5.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRisaEVEE--TVDIGCQAMGVPLPTLQW------YKDAISISRLQNPRYKVlasgGLRIQKLRPEDSGIFQ 206
Cdd:cd05744      1 PHFLQAPGDL---EVQEgrLCRFDCKVSGLPTPDLFWqlngkpVRPDSAHKMLVRENGRH----SLIIEPVTKRDAGIYT 73

                           90
                   ....*....|....*...
gi 1370509662  207 CFASNEGGEIQTHTYLDV 224
Cdd:cd05744     74 CIARNRAGENSFNAELVV 91
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 134-214 6.18e-06

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: 46.54  E-value: 6.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  134 PPYFTAEPESrISAEVEETVDIGCQAMGVPLPTLQW----------YKDAisisrLQNPRYKVLASGGLRIQKLRPEDSG 203
Cdd:cd20954      1 PPRWIVEPVD-ANVAAGQDVMLHCQADGFPTPTVTWkkatgstpgeYKDL-----LYDPNVRILPNGTLVFGHVQKENEG 74

                           90
                   ....*....|.
gi 1370509662  204 IFQCFASNEGG 214
Cdd:cd20954     75 HYLCEAKNGIG 85
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 135-224 6.20e-06

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: 46.30  E-value: 6.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRIS-AEVEETVDIGCQAMGVPLPTLQWYKDAISISrlQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEG 213
Cdd:cd04969      1 PDFELNPVKKKIlAAKGGDVIIECKPKASPKPTISWSKGTELLT--NSSRICILPDGSLKIKNVTKSDEGKYTCFAVNFF 78

                           90
                   ....*....|.
gi 1370509662  214 GEIQTHTYLDV 224
Cdd:cd04969     79 GKANSTGSLSV 89
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 157-217 6.35e-06

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: 46.40  E-value: 6.35e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370509662  157 CQAMGVPLPTLQWYKDAISISrlQNPRYKV---LASGG-----LRIQKLRPEDSGIFQCFASNEGGEIQ 217
Cdd:cd20956     23 CVASGNPLPQITWTLDGFPIP--ESPRFRVgdyVTSDGdvvsyVNISSVRVEDGGEYTCTATNDVGSVS 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 329-413 6.52e-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: 45.96  E-value: 6.52e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   329 PEDHVVIKGTTATLHCGATHDPRVSLRYVWKKDNVALTPSSTSRIVVEKDGSLLISQTWSGDIGDYSCEIVSEGGNDSRM 408
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 1370509662   409 ARLEV 413
Cdd:smart00410   81 TTLTV 85
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 229-317 6.56e-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: 46.47  E-value: 6.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVD---TTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRipRFMLLEsGGLQIA-PVFIQDAGNYTCYA 304
Cdd:cd05848      2 PVFVQEPDDaifPTDSDEKKVILNCEARGNPVPTYRWLRNGTEIDTESDY--RYSLID-GNLIISnPSEVKDSGRYQCLA 78

                           90
                   ....*....|....
gi 1370509662  305 ANTEGS-LNASATL 317
Cdd:cd05848     79 TNSIGSiLSREALL 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 229-319 6.66e-06

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: 46.39  E-value: 6.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQ----------RPVDTTVTdgmtaiLRCEVSGAPKPAITWKRENHILAS---GSVRIPRFMLLESgglQIAPvfiQ 295
Cdd:cd05856      1 PRFTQpakmrrrviaRPVGSSVR------LKCVASGNPRPDITWLKDNKPLTPpeiGENKKKKWTLSLK---NLKP---E 68

                           90       100
                   ....*....|....*....|....
gi 1370509662  296 DAGNYTCYAANTEGSLNASATLTV 319
Cdd:cd05856     69 DSGKYTCHVSNRAGEINATYKVDV 92
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 231-319 8.06e-06

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: 46.04  E-value: 8.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  231 FTQRPVDTTVTDGMTAILRCEVSGAPKPAITWkRENHILASGSVRIPRFMlLESGGLQIAPVFIQDAGNYTCYAANTEGS 310
Cdd:cd05867      2 WTRRPQSHLYGPGETARLDCQVEGIPTPNITW-SINGAPIEGTDPDPRRH-VSSGALILTDVQPSDTAVYQCEARNRHGN 79


                   ....*....
gi 1370509662  311 LNASATLTV 319
Cdd:cd05867     80 LLANAHVHV 88
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 234-319 8.88e-06

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: 45.90  E-value: 8.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  234 RPVDTTVTDGMTAILRCEVSGAPKPAITW---KRENHILASGSVRiprfmLLESGGLQIAPVFIQDAGNYTCYAANTEGS 310
Cdd:cd04978      5 EPPSLVLSPGETGELICEAEGNPQPTITWrlnGVPIEPAPEDMRR-----TVDGRTLIFSNLQPNDTAVYQCNASNVHGY 79


                   ....*....
gi 1370509662  311 LNASATLTV 319
Cdd:cd04978     80 LLANAFLHV 88
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 329-413 8.88e-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: 46.10  E-value: 8.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  329 PEDHVVIKGTTATLHCGATHDPRVSLryVWKKD--NVALTPS----STSRIVVEKDGSLLISQTWSGDIGDYSCEIVSEG 402
Cdd:cd05726      6 PRDQVVALGRTVTFQCETKGNPQPAI--FWQKEgsQNLLFPYqppqPSSRFSVSPTGDLTITNVQRSDVGYYICQALNVA 83

                           90
                   ....*....|.
gi 1370509662  403 GNDSRMARLEV 413
Cdd:cd05726     84 GSILAKAQLEV 94
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 135-216 9.22e-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: 46.09  E-value: 9.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRI--SAEVEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPRYKvLASGGLRIQKLRP-EDSGIFQCFASN 211
Cdd:cd05848      2 PVFVQEPDDAIfpTDSDEKKVILNCEARGNPVPTYRWLRNGTEIDTESDYRYS-LIDGNLIISNPSEvKDSGRYQCLATN 80


                   ....*
gi 1370509662  212 EGGEI 216
Cdd:cd05848     81 SIGSI 85
IgI_hNeurofascin_like cd05875
Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig ...
 155-214 9.60e-06

Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of human neurofascin (NF). NF 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 a cytoplasmic domain. NF has many alternatively spliced isoforms having different temporal expression patterns during development. NF participates in axon subcellular targeting and synapse formation, however little is known of the functions of the different isoforms. 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 lacks a C" strand.


Pssm-ID: 409459  Cd Length: 95  Bit Score: 46.12  E-value: 9.60e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370509662  155 IGCQAMGVPLPTLQWYKDAISISRLQNPRYKVLA-SGGLRIQ---KLRPED-SGIFQCFASNEGG 214
Cdd:cd05875     21 IECEAKGNPVPTFHWTRNGKFFNVAKDPRVSMRRrSGTLVIDfrgGGRPEDyEGEYQCFARNKFG 85
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 134-224 1.21e-05

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: 45.56  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  134 PPYFTAEPESRiSAEVEETVDIGCQAMGVPLPTLQW-YKDAISISRLQNP-----RYKVLASGGLRIQKLRPEDSGIFQC 207
Cdd:cd05734      1 PPRFVVQPNDQ-DGIYGKAVVLNCSADGYPPPTIVWkHSKGSGVPQFQHIvplngRIQLLSNGSLLIKHVLEEDSGYYLC 79

                           90
                   ....*....|....*...
gi 1370509662  208 FASNE-GGEIQTHTYLDV 224
Cdd:cd05734     80 KVSNDvGADISKSMYLTV 97
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 148-214 1.23e-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: 45.39  E-value: 1.23e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662  148 EVEETVDIGCQAMGVPLPTLQWYKDAISISRLQ-NPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGG 214
Cdd:cd05738     12 EKARTATMLCAASGNPDPEISWFKDFLPVDTATsNGRIKQLRSGALQIENSEESDQGKYECVATNSAG 79
IgI_1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; ...
 135-218 1.29e-05

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: 45.72  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRISAE--VEETVDIGCQAMGVPLPTLQWYKDAISISrLQNPRYKvLASGGLRIQKlrPE---DSGIFQCFA 209
Cdd:cd05849      2 PVFEEQPIDTIYPEesTEGKVSVNCRARANPFPIYKWRKNNLDID-LTNDRYS-MVGGNLVINN--PDkykDAGRYVCIV 77


                   ....*....
gi 1370509662  210 SNEGGEIQT 218
Cdd:cd05849     78 SNIYGKVRS 86
IgI_1_Contactin-2 cd05850
First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; ...
 135-216 1.50e-05

First immunoglobulin (Ig) domain of contactin-2; 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-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 in the developing chick retina, corresponding to the period of formation and maturation of AC processes. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409437 [Multi-domain]  Cd Length: 97  Bit Score: 45.30  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRISAE--VEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNE 212
Cdd:cd05850      3 PVFEEQPSSTLFPEgsAEEKVTLACRARASPPATYRWKMNGTELKMEPDSRYRLVAGNLVISNPVKAKDAGSYQCLASNR 82


                   ....
gi 1370509662  213 GGEI 216
Cdd:cd05850     83 RGTV 86
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 231-319 1.51e-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: 45.55  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  231 FTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRipRFMLLESGGLQIAPVFIQ-----DAGNYTCYAA 305
Cdd:cd05722      4 FLSEPSDIVAMRGGPVVLNCSAESDPPPKIEWKKDGVLLNLVSDE--RRQQLPNGSLLITSVVHSkhnkpDEGFYQCVAQ 81

                           90
                   ....*....|....*.
gi 1370509662  306 NTE-GS-LNASATLTV 319
Cdd:cd05722     82 NESlGSiVSRTARVTV 97
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 228-319 1.58e-05

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: 45.62  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  228 APVFTQRPVDTTVTDGMTAILRCEVSGAPKPAIT--WKRENHIL---ASGSVRIPRFMLLESGGLQIAPVFIQDAGNYTC 302
Cdd:cd04970      2 ATRITLAPSNADITVGENATLQCHASHDPTLDLTftWSFNGVPIdleKIEGHYRRRYGKDSNGDLEIVNAQLKHAGRYTC 81

                           90
                   ....*....|....*..
gi 1370509662  303 YAANTEGSLNASATLTV 319
Cdd:cd04970     82 TAQTVVDSDSASATLVV 98
fn3 pfam00041
Fibronectin type III domain;
925-1013 1.63e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.10  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  925 APTSVTVRTASETSLRLRWVPLPDsqynGNPESVGYRIKYWRSDLQSSAVAQVVSdRLEREFTIEELEEWMEYELQMQAF 1004
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD----GNGPITGYEVEYRPKNSGEPWNEITVP-GTTTSVTLTGLKPGTEYEVRVQAV 76


                   ....*....
gi 1370509662 1005 NAVGAGPWS 1013
Cdd:pfam00041   77 NGGGEGPPS 85
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 151-222 1.95e-05

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: 44.88  E-value: 1.95e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370509662  151 ETVDI--GCQAMGVPLPTLQWYKDAISIsrLQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGEIQTHTYL 222
Cdd:cd05723     11 ESMDIvfECEVTGKPTPTVKWVKNGDVV--IPSDYFKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQASAQL 82
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 233-320 1.98e-05

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: 44.92  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  233 QRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSvriPRFMLLESGG-LQIAPVFIQDAGNYTCYAANTEGSL 311
Cdd:cd05730      8 QSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGE---EKYSFNEDGSeMTILDVDKLDEAEYTCIAENKAGEQ 84


                   ....*....
gi 1370509662  312 NASATLTVW 320
Cdd:cd05730     85 EAEIHLKVF 93
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 141-214 2.11e-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: 2.11e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370509662  141 PESrISAEVEETVDIGCQAMGVPLPTLQWYKdaisISRLQNPRYKVLASGG-LRIQKLRPEDSGIFQCFASNEGG 214
Cdd:cd04968      8 PAD-TYALKGQTVTLECFALGNPVPQIKWRK----VDGSPSSQWEITTSEPvLEIPNVQFEDEGTYECEAENSRG 77
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 239-319 2.13e-05

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: 45.07  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  239 TVTDGMTAILRCEVSGAPKPAITW-KRENHILASGSVriPRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGSLNASATL 317
Cdd:cd20969     13 FVDEGHTVQFVCRADGDPPPAILWlSPRKHLVSAKSN--GRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHL 90


                   ..
gi 1370509662  318 TV 319
Cdd:cd20969     91 HV 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 621-706 2.44e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.53  E-value: 2.44e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   621 PPQNVQTEAVNSTTIQFLWNPPPQQFINGINQGYKLLAWPADAPEAVTVVTiapdfHGVHHGHITNLKKFTAYFTSVLCF 700
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVT-----PSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 1370509662   701 TTPGDG 706
Cdd:smart00060   78 NGAGEG 83
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 238-319 2.94e-05

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: 44.13  E-value: 2.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  238 TTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIPRFmlleSGGLQIAPVFIQDAGNYTCYAANTEGSLNASATL 317
Cdd:cd05876      5 LVALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQNH----NKTLQLLNVGESDDGEYVCLAENSLGSARHAYYV 80


                   ..
gi 1370509662  318 TV 319
Cdd:cd05876     81 TV 82
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 134-224 3.20e-05

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: 44.16  E-value: 3.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  134 PPYFTAEPESRISAEVEETVdIGCQAMGVPLPTLQWYKDAISISRLQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEG 213
Cdd:cd20976      1 APSFSSVPKDLEAVEGQDFV-AQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79

                           90
                   ....*....|.
gi 1370509662  214 GEIQTHTYLDV 224
Cdd:cd20976     80 GQVSCSAWVTV 90
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 151-216 3.40e-05

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: 44.02  E-value: 3.40e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370509662  151 ETVDIGCQAMGVPLPTLQWYKDAISISrlQNPRYKVLASGG---LRIQKLRPEDSGIFQCFASNEGGEI 216
Cdd:cd05743      2 ETVEFTCVATGVPTPIINWRLNWGHVP--DSARVSITSEGGygtLTIRDVKESDQGAYTCEAINTRGMV 68
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
 228-319 4.60e-05

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: 44.00  E-value: 4.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  228 APVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKR--------ENHILASGSVRIPRFMLLesgGLQIApvfiQDAGN 299
Cdd:cd20971      1 APHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRqgkeiiadGLKYRIQEFKGGYHQLII---ASVTD----DDATV 73

                           90       100
                   ....*....|....*....|
gi 1370509662  300 YTCYAANTEGSLNASATLTV 319
Cdd:cd20971     74 YQVRATNQGGSVSGTASLEV 93
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 340-403 4.97e-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: 43.09  E-value: 4.97e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370509662  340 ATLHCGATHDPRVSlrYVWKKDNVALTPSSTSRIVVEK-DGSLLISQTWSGDIGDYSCEIVSEGG 403
Cdd:cd00096      1 VTLTCSASGNPPPT--ITWYKNGKPLPPSSRDSRRSELgNGTLTISNVTLEDSGTYTCVASNSAG 63
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
 239-319 5.45e-05

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: 43.60  E-value: 5.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  239 TVTDGMTAILRCEVSGAPKPAiTWKRENHILasGSVRIPRFMLLESGGLQIAPVFIQDAGNYTCYAAN-TEGSLNASATL 317
Cdd:cd04979      7 SVKEGDTVILSCSVKSNNAPV-TWIHNGKKV--PRYRSPRLVLKTERGLLIRSAQEADAGVYECHSGErVLGSTLRSVTL 83


                   ..
gi 1370509662  318 TV 319
Cdd:cd04979     84 HV 85
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 229-319 5.49e-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: 5.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILA--SGSVRIPRfMLLESGGLQIAPVFIQDAGNYTCYAAN 306
Cdd:cd05893      1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpkSDHYTIQR-DLDGTCSLHTTASTLDDDGNYTIMAAN 79

                           90
                   ....*....|...
gi 1370509662  307 TEGSLNASATLTV 319
Cdd:cd05893     80 PQGRISCTGRLMV 92
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 228-319 5.98e-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: 43.70  E-value: 5.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  228 APVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKR-ENHILASGSVRIPRFMLLES---GGLQIAPVFIQDAGNYTCY 303
Cdd:cd20956      1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLdGFPIPESPRFRVGDYVTSDGdvvSYVNISSVRVEDGGEYTCT 80

                           90
                   ....*....|....*.
gi 1370509662  304 AANTEGSLNASATLTV 319
Cdd:cd20956     81 ATNDVGSVSHSARINV 96
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 135-219 6.57e-05

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: 43.69  E-value: 6.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRIsAEVEETVDIGCQAMGVPLPTLQWYKDAISI-SRLQNPRYK--VLASGGLRIQKLRP-----EDSGIFQ 206
Cdd:cd07693      1 PRIVEHPSDLI-VSKGDPATLNCKAEGRPTPTIQWLKNGQPLeTDKDDPRSHriVLPSGSLFFLRVVHgrkgrSDEGVYV 79

                           90
                   ....*....|...
gi 1370509662  207 CFASNEGGEIQTH 219
Cdd:cd07693     80 CVAHNSLGEAVSR 92
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 240-319 6.71e-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: 43.46  E-value: 6.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  240 VTDGMTAILRCEVSGAPKPAITWKRENHIL--ASGSVRIPRfmlLESGGLQIAPVFIQDAGNYTCYAANTEGS-LNASAT 316
Cdd:cd05738     11 VEKARTATMLCAASGNPDPEISWFKDFLPVdtATSNGRIKQ---LRSGALQIENSEESDQGKYECVATNSAGTrYSAPAN 87


                   ...
gi 1370509662  317 LTV 319
Cdd:cd05738     88 LYV 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 40-118 7.62e-05

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.95  E-value: 7.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   40 MAPTIVVPPGNRsvvagsseTTLECIASARPVeDLSVTWKRNGVRITSGL---HSFGRR----LTISNPTSADTGPYVCE 112
Cdd:pfam00047    2 APPTVTVLEGDS--------ATLTCSASTGSP-GPDVTWSKEGGTLIESLkvkHDNGRTtqssLLISNVTKEDAGTYTCV 72


                   ....*.
gi 1370509662  113 AALPGS 118
Cdd:pfam00047   73 VNNPGG 78
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 243-309 7.71e-05

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: 43.40  E-value: 7.71e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370509662  243 GMTAILRCEVSGAPKPAITWKRENHILASgsvRIPRFMLLESGG--LQIAPVFIQDAGNYTCYAANTEG 309
Cdd:cd05736     15 GVEASLRCHAEGIPLPRVQWLKNGMDINP---KLSKQLTLIANGseLHISNVRYEDTGAYTCIAKNEGG 80
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 41-135 7.79e-05

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: 43.69  E-value: 7.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   41 APTIVVPPGNRSVVAGSSeTTLECIASARPVEDLSVTWKRNGVRI---TSGLHsFGRR--------LTISNPTSADTGPY 109
Cdd:cd04970      2 ATRITLAPSNADITVGEN-ATLQCHASHDPTLDLTFTWSFNGVPIdleKIEGH-YRRRygkdsngdLEIVNAQLKHAGRY 79

                           90       100
                   ....*....|....*....|....*.
gi 1370509662  110 VCEAAlpgSAFEPARATAFLFIIEPP 135
Cdd:cd04970     80 TCTAQ---TVVDSDSASATLVVRGPP 102
Ig0_BSG1 cd20940
Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are ...
 149-212 8.06e-05

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


Pssm-ID: 409534  Cd Length: 116  Bit Score: 43.80  E-value: 8.06e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509662  149 VEETVDIGCQAMGVPLPTLQWY-------------KDAISISRLQ-NPRYKVLASGGLRIQKLRPEDSGIFQCFASNE 212
Cdd:cd20940     14 VGDSVELHCEAVGSPIPEIQWWfegqepneicsqlWDGARLDRVHiNATYHQHATSTISIDNLTEEDTGTYECRASND 91
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
 229-319 1.11e-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: 42.84  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIPRFMllESG--GLQIAPVFIQDAGNYTCYAAN 306
Cdd:cd20975      1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEA--EGGlcRLRILAAERGDAGFYTCKAVN 78

                           90
                   ....*....|...
gi 1370509662  307 TEGSLNASATLTV 319
Cdd:cd20975     79 EYGARQCEARLEV 91
Ig6_Contactin-2 cd05854
Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth ...
 41-135 1.13e-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: 43.11  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   41 APTIVVPPGNRSVVAGSSeTTLECIASARPVEDLSVTWKRNGV-----------RITSGLHSFGrRLTISNPTSADTGPY 109
Cdd:cd05854      2 ATKITLAPSSADINQGEN-LTLQCHASHDPTMDLTFTWSLDDFpidldkpnghyRRMEVKETIG-DLVIVNAQLSHAGTY 79

                           90       100
                   ....*....|....*....|....*.
gi 1370509662  110 VCEAAlpgSAFEPARATAFLFIIEPP 135
Cdd:cd05854     80 TCTAQ---TVVDSASASATLVVRGPP 102
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 235-318 1.28e-04

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: 42.79  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  235 PVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILAS--GSVRIPRFMLLESGG---------LQIAPVFIQDAGNYTCY 303
Cdd:cd04974      8 PANQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSkyGPDGLPYVTVLKVAGvnttgeentLTISNVTFDDAGEYICL 87

                           90
                   ....*....|....*
gi 1370509662  304 AANTEGSLNASATLT 318
Cdd:cd04974     88 AGNSIGLSFHSAWLT 102
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 137-224 2.23e-04

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: 41.84  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  137 FTAEPESrISAEVEETVDIGCQAMGVPLPTLQWYKD-AISISRLQNPRYKVLASGG-LRIQKLRPEDSGIFQCFASNEGG 214
Cdd:cd05763      2 FTKTPHD-ITIRAGSTARLECAATGHPTPQIAWQKDgGTDFPAARERRMHVMPEDDvFFIVDVKIEDTGVYSCTAQNSAG 80

                           90
                   ....*....|
gi 1370509662  215 EIQTHTYLDV 224
Cdd:cd05763     81 SISANATLTV 90
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 239-319 2.44e-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: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  239 TVTDGMTAILRCEVSGAPKPAITWKR--ENHILASGSV--RIPRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGSLNAS 314
Cdd:cd05732     12 TAVELEQITLTCEAEGDPIPEITWRRatRGISFEEGDLdgRIVVRGHARVSSLTLKDVQLTDAGRYDCEASNRIGGDQQS 91


                   ....*
gi 1370509662  315 ATLTV 319
Cdd:cd05732     92 MYLEV 96
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 323-413 2.53e-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: 42.15  E-value: 2.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  323 TSIVHPPEDHVVIKGTTATLHCGATHDPRVSLRYVWKKDNVALTPSSTS-----RIVVEKDGSLLISQTWSGDIGDYSCE 397
Cdd:cd04970      3 TRITLAPSNADITVGENATLQCHASHDPTLDLTFTWSFNGVPIDLEKIEghyrrRYGKDSNGDLEIVNAQLKHAGRYTCT 82

                           90
                   ....*....|....*.
gi 1370509662  398 IVSEGGNDSRMARLEV 413
Cdd:cd04970     83 AQTVVDSDSASATLVV 98
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 324-396 2.53e-04

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: 41.92  E-value: 2.53e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370509662  324 SIVHPPEDHVVIKGTTATLHCGATHDPRVSLryVWKKDNVALTP-SSTSRIVVEKDGSLLISQTWSGDIGDYSC 396
Cdd:cd05738      1 IIDMGPQLKVVEKARTATMLCAASGNPDPEI--SWFKDFLPVDTaTSNGRIKQLRSGALQIENSEESDQGKYEC 72
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 326-413 2.63e-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: 41.71  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  326 VHPPEDHVVIKGTTATLHC--GATHDPRVSlryvWKKDNVALTPSSTSRIVVEKDG--SLLISQTWSGDIGDYSCEIVSE 401
Cdd:cd05744      4 LQAPGDLEVQEGRLCRFDCkvSGLPTPDLF----WQLNGKPVRPDSAHKMLVRENGrhSLIIEPVTKRDAGIYTCIARNR 79

                           90
                   ....*....|..
gi 1370509662  402 GGNDSRMARLEV 413
Cdd:cd05744     80 AGENSFNAELVV 91
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 137-227 3.12e-04

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: 41.87  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  137 FTAEPESRISAEvEETVDIGCQAMGVPLPTLQWYKDA-----ISISRLQ-NPRYKVLASGGLRIQKLRPEDSGIFQCFAS 210
Cdd:cd05726      2 FVVKPRDQVVAL-GRTVTFQCETKGNPQPAIFWQKEGsqnllFPYQPPQpSSRFSVSPTGDLTITNVQRSDVGYYICQAL 80

                           90
                   ....*....|....*..
gi 1370509662  211 NEGGEIQTHTYLDVTNI 227
Cdd:cd05726     81 NVAGSILAKAQLEVTDV 97
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 146-214 3.37e-04

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: 41.34  E-value: 3.37e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370509662  146 SAEVEETVDIGCQAMGV-PLPTLQWYKDAISISRLQNPRYKVLASGG---LRIQKLRPEDSGIFQCFASNEGG 214
Cdd:cd05750     10 TVQEGSKLVLKCEATSEnPSPRYRWFKDGKELNRKRPKNIKIRNKKKnseLQINKAKLEDSGEYTCVVENILG 82
IgI_1_Dscam cd20955
First immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 135-216 3.68e-04

First 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 first 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: 409547  Cd Length: 99  Bit Score: 41.63  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  135 PYFTAEPESRISAEVEETVDIGCQAMGVPLPTLQWYK-DAISISRLQNPRyKVLASGGLRIQKLRPED------SGIFQC 207
Cdd:cd20955      2 PVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRsDGTAVGDVPGLR-QISSDGKLVFPPFRAEDyrqevhAQVYAC 80


                   ....*....
gi 1370509662  208 FASNEGGEI 216
Cdd:cd20955     81 LARNQFGSI 89
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 329-414 4.29e-04

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: 41.07  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  329 PEDHVVIKGTTATLHCGATHDPrvSLRYVWKKDNVALTPSSTSRI--VVEKDGSLLISQTWSGDIGDYSCEIVSEGGNDS 406
Cdd:cd05763      6 PHDITIRAGSTARLECAATGHP--TPQIAWQKDGGTDFPAARERRmhVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSIS 83


                   ....*...
gi 1370509662  407 RMARLEVI 414
Cdd:cd05763     84 ANATLTVL 91
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 42-113 4.59e-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: 40.94  E-value: 4.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   42 PTIVVPPGNRSVVAGSSeTTLECIASARPVEDlsVTWKRNGVRIT-----------SGLHSfgrrLTISNPTSADTGPYV 110
Cdd:cd05744      1 PHFLQAPGDLEVQEGRL-CRFDCKVSGLPTPD--LFWQLNGKPVRpdsahkmlvreNGRHS----LIIEPVTKRDAGIYT 73


                   ...
gi 1370509662  111 CEA 113
Cdd:cd05744     74 CIA 76
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
 227-319 5.00e-04

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: 41.12  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  227 IAPVFTQRPVDTTVTDGmTAILRCEVSGAPKPAITWKR--ENHILASGSV----RIPRFMLLESGGLQIAPVFIQDAGNY 300
Cdd:cd05870      1 VQPHIIQLKNETTVENG-AATLSCKAEGEPIPEITWKRasDGHTFSEGDKspdgRIEVKGQHGESSLHIKDVKLSDSGRY 79

                           90
                   ....*....|....*....
gi 1370509662  301 TCYAANTEGSLNASATLTV 319
Cdd:cd05870     80 DCEAASRIGGHQKSMYLDI 98
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 325-413 5.16e-04

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 40.94  E-value: 5.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  325 IVHPPEDHVVIKGTTATLHCGATHDPRVSLRyvWKKDNVALtPSSTSRIVVEKDGSLLISQTWSGDIGDYSCEIVSEGGN 404
Cdd:cd20952      2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTIS--WLKDGVPL-LGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78


                   ....*....
gi 1370509662  405 DSRMARLEV 413
Cdd:cd20952     79 ATWSAVLDV 87
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 141-221 6.15e-04

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 40.47  E-value: 6.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  141 PESRISAEVEETVDIGCQAMGVPLPTLQWYKDAISisrLQNPRYKVLASG-GLRIQKLRPEDSGIFQCFASNEGGEIQtH 219
Cdd:cd05731      1 SESSTMVLRGGVLLLECIAEGLPTPDIRWIKLGGE---LPKGRTKFENFNkTLKIENVSEADSGEYQCTASNTMGSAR-H 76


                   ..
gi 1370509662  220 TY 221
Cdd:cd05731     77 TI 78
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 243-309 6.62e-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: 40.17  E-value: 6.62e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370509662  243 GMTAILRCEVSGAPKPAITWkREN--HILASgsvriPRFMLLESGG---LQIAPVFIQDAGNYTCYAANTEG 309
Cdd:cd05743      1 GETVEFTCVATGVPTPIINW-RLNwgHVPDS-----ARVSITSEGGygtLTIRDVKESDQGAYTCEAINTRG 66
IgI_1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; ...
 229-318 6.99e-04

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: 40.71  E-value: 6.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  229 PVFTQRPVDTTV----TDGMTAiLRCEVSGAPKPAITWKRENHILASGSVRIPrfmlLESGGLQIA-PVFIQDAGNYTCY 303
Cdd:cd05849      2 PVFEEQPIDTIYpeesTEGKVS-VNCRARANPFPIYKWRKNNLDIDLTNDRYS----MVGGNLVINnPDKYKDAGRYVCI 76

                           90
                   ....*....|....*.
gi 1370509662  304 AANTEGSLNAS-ATLT 318
Cdd:cd05849     77 VSNIYGKVRSReATLS 92
IgI_2_Dscam cd20953
Second immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 134-215 7.02e-04

Second 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 second immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. 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: 409545  Cd Length: 95  Bit Score: 40.60  E-value: 7.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  134 PPYFTAEPESR-ISAEVEETVDIGCQAMGVPLPTLQWYKDAISISRLQ----NPRYKVLaSGGLRIQKLRPEDSGIFQCF 208
Cdd:cd20953      1 APKIPGLSKSQpLTVSSASSIALLCPAQGYPAPSFRWYKFIEGTTRKQavvlNDRVKQV-SGTLIIKDAVVEDSGKYLCV 79


                   ....*...
gi 1370509662  209 ASNE-GGE 215
Cdd:cd20953     80 VNNSvGGE 87
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
471-643 7.04e-04

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.55  E-value: 7.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  471 GPEMTGVTVSGLTPARTYQFRVCAVNEVGRGQYS-----------AETSRLMLPEEPPSAPPKNIVAS--------GRTN 531
Cdd:COG4733    472 TPEAGAVWAFGPDELETQLFRVVSIEENEDGTYTitavqhapekyAAIDAGAFDDVPPQWPPVNVTTSeslsvvaqGTAV 551

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  532 QSIMVQWQPPPETEHngvlrgYILRYRLAGlpGEYQQRNITSpevNYCLVTDLIIWTQYEIQVAAYNGAGLGVFSRAVTE 611
Cdd:COG4733    552 TTLTVSWDAPAGAVA------YEVEWRRDD--GNWVSVPRTS---GTSFEVPGIYAGDYEVRVRAINALGVSSAWAASSE 620

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1370509662  612 YTLQGVPTAPPQNVQTEAVNSTT-IQFLWNPPP 643
Cdd:COG4733    621 TTVTGKTAPPPAPTGLTATGGLGgITLSWSFPV 653
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
 248-319 7.41e-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: 40.73  E-value: 7.41e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370509662  248 LRCEVSGAPKPAITWKRENHILASGSVRIPRFMLLES----GGLQIAPVFIQDAGNYTCYAANTEGSLNASATLTV 319
Cdd:cd05869     22 LTCEASGDPIPSITWRTSTRNISSEEKTLDGHIVVRSharvSSLTLKYIQYTDAGEYLCTASNTIGQDSQSMYLEV 97
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 42-114 7.50e-04

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: 40.24  E-value: 7.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   42 PTIVVPPGNRSVVAGSSeTTLECIASARPVEdlSVTWKRNGVRITsglhsFGRR--------LTISN-PTSADTGPYVCE 112
Cdd:cd20958      1 PPFIRPMGNLTAVAGQT-LRLHCPVAGYPIS--SITWEKDGRRLP-----LNHRqrvfpngtLVIENvQRSSDEGEYTCT 72


                   ..
gi 1370509662  113 AA 114
Cdd:cd20958     73 AR 74
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 326-413 7.62e-04

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: 40.52  E-value: 7.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  326 VHPPEDHVVIKGTTATLHCGATHDPrvSLRYVWKKDNVALTpSSTSRIVVEKDGS----LLISQTWSGDIGDYSCEIVSE 401
Cdd:cd05892      4 IQKPQNKKVLEGDPVRLECQISAIP--PPQIFWKKNNEMLQ-YNTDRISLYQDNCgricLLIQNANKKDAGWYTVSAVNE 80

                           90
                   ....*....|..
gi 1370509662  402 GGNDSRMARLEV 413
Cdd:cd05892     81 AGVVSCNARLDV 92
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 134-224 8.22e-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: 40.30  E-value: 8.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  134 PPYFTA-EPESRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNE 212
Cdd:cd05730      1 PPTIRArQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENK 80

                           90
                   ....*....|..
gi 1370509662  213 GGEIQTHTYLDV 224
Cdd:cd05730     81 AGEQEAEIHLKV 92
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 151-220 8.73e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 39.69  E-value: 8.73e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  151 ETVDIGCQAMGVPLPTLQWYKDaisiSRLQNPRYKVLasgglrIQKLRPEDSGIFQCFASNEGGEIQTHT 220
Cdd:pfam13895   15 EPVTLTCSAPGNPPPSYTWYKD----GSAISSSPNFF------TLSVSAEDSGTYTCVARNGRGGKVSNP 74
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 147-224 9.19e-04

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third 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: 143259  Cd Length: 88  Bit Score: 40.00  E-value: 9.19e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370509662  147 AEVEETVDIGCQAMGVPLPTLQWYKdaisISRLQNPRYKVLASGG-LRIQKLRPEDSGIFQCFASNEGGEIQTHTYLDV 224
Cdd:cd05851     13 ALKGQNVTLECFALGNPVPVIRWRK----ILEPMPATAEISMSGAvLKIFNIQPEDEGTYECEAENIKGKDKHQARVYV 87
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 42-113 9.54e-04

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: 40.07  E-value: 9.54e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370509662   42 PTIVVPPGNRSVVAGSSETTLECIASARPVEdlSVTWKRNGVRIT--SGLHSFGR-RLTISNPTSADTGPYVCEA 113
Cdd:cd20978      1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQP--KITWLHNGKPLQgpMERATVEDgTLTIINVQPEDTGYYGCVA 73
IgC1_hNephrin_like cd05773
Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig ...
 157-235 1.20e-03

Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes.


Pssm-ID: 143250  Cd Length: 109  Bit Score: 40.30  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  157 CQAMGVPLPTLQWYKDAISISrLQNPRY--KVLASGGLRIQKL------RPEDSGIFQCFASNEGGEiqthtylDVTNIA 228
Cdd:cd05773     30 CQAQGVPRVQFRWAKNGVPLD-LGNPRYeeTTEHTGTVHTSILtiinvsAALDYALFTCTAHNSLGE-------DSLDIQ 101


                   ....*..
gi 1370509662  229 PVFTQRP 235
Cdd:cd05773    102 LVSTSRP 108
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 333-396 1.28e-03

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: 39.77  E-value: 1.28e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370509662  333 VVIKGTTATLHCGATHDPRVSLRYVWKKDNVAltpSSTSRIVVEKDGSLLISQTWSGDIGDYSC 396
Cdd:cd05764     11 RVLEGQRATLRCKARGDPEPAIHWISPEGKLI---SNSSRTLVYDNGTLDILITTVKDTGAFTC 71
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 325-413 1.30e-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: 39.84  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  325 IVHPPEDHVVIKGTTATLHCGATHDPRVSLRyvWKKDNVAL---TPSSTSRIVVEKDGSLLISQTWSG-----DIGDYSC 396
Cdd:cd07693      3 IVEHPSDLIVSKGDPATLNCKAEGRPTPTIQ--WLKNGQPLetdKDDPRSHRIVLPSGSLFFLRVVHGrkgrsDEGVYVC 80

                           90
                   ....*....|....*...
gi 1370509662  397 EIVSEGGND-SRMARLEV 413
Cdd:cd07693     81 VAHNSLGEAvSRNASLEV 98
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 151-215 1.59e-03

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: 39.38  E-value: 1.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370509662  151 ETVDIGCQAMGVPLPTLQW-YKDAISISrlQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGE 215
Cdd:cd05764     16 QRATLRCKARGDPEPAIHWiSPEGKLIS--NSSRTLVYDNGTLDILITTVKDTGAFTCIASNPAGE 79
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 134-215 1.62e-03

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: 39.47  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  134 PPYftAEPESRISAEVEETVDIGCQAMGVPLPTLQWYKDaisISRL-QNPRYKVLASGGLRIQKL-RPEDSGIFQCFASN 211
Cdd:cd20958      1 PPF--IRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKD---GRRLpLNHRQRVFPNGTLVIENVqRSSDEGEYTCTARN 75


                   ....
gi 1370509662  212 EGGE 215
Cdd:cd20958     76 QQGQ 79
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 329-413 1.72e-03

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: 39.55  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  329 PEDHVVIKGTTATLHCGATH--DPRVSlryvWKKDNVALTPSSTSRIVVEKDGS-LLISQTWSGDIGDYSCEIVSEGGND 405
Cdd:cd05736      7 PEFQAKEPGVEASLRCHAEGipLPRVQ----WLKNGMDINPKLSKQLTLIANGSeLHISNVRYEDTGAYTCIAKNEGGVD 82


                   ....*...
gi 1370509662  406 SRMARLEV 413
Cdd:cd05736     83 EDISSLFV 90
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 43-126 2.17e-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: 39.08  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   43 TIVVPPGNRSVVAGSSETTLECIASARPVEdLSVTWKRNGVRITSGLHSFGRRLTISNPTSADTGPYVCEAALPGSAFEp 122
Cdd:cd05754      2 QVTVEEPRSQEVRPGADVSFICRAKSKSPA-YTLVWTRVNGTLPSRAMDFNGILTIRNVQLSDAGTYVCTGSNMLDTDE- 79


                   ....
gi 1370509662  123 ARAT 126
Cdd:cd05754     80 ATAT 83
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 333-413 2.28e-03

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: 39.03  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  333 VVIKGTTATLHCGAT-HDPrvSLRYVWKKDNVALTPSSTSRIVV---EKDGSLLISQTWSGDIGDYSCEIVSEGGNDSRM 408
Cdd:cd05750     10 TVQEGSKLVLKCEATsENP--SPRYRWFKDGKELNRKRPKNIKIrnkKKNSELQINKAKLEDSGEYTCVVENILGKDTVT 87


                   ....*
gi 1370509662  409 ARLEV 413
Cdd:cd05750     88 GNVTV 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 235-319 2.37e-03

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 39.12  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  235 PVDTTVTDGMTAILRCEVSGAPKPAITW-KRENHILASGSVRIPrfmlLESG---GLQIAPVFIQDAGNYTCYAANTEGS 310
Cdd:cd05891      8 PDVVTIMEGKTLNLTCTVFGNPDPEVIWfKNDQDIELSEHYSVK----LEQGkyaSLTIKGVTSEDSGKYSINVKNKYGG 83


                   ....*....
gi 1370509662  311 LNASATLTV 319
Cdd:cd05891     84 ETVDVTVSV 92
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 329-405 2.50e-03

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: 39.01  E-value: 2.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  329 PEDHVVIKGTTATLHCGATHDPRVSLryVWKKDNVALTPS------STSRIVVEKDGSLLISQTWSGDIGDYSCEIVSEG 402
Cdd:cd05734      8 PNDQDGIYGKAVVLNCSADGYPPPTI--VWKHSKGSGVPQfqhivpLNGRIQLLSNGSLLIKHVLEEDSGYYLCKVSNDV 85


                   ...
gi 1370509662  403 GND 405
Cdd:cd05734     86 GAD 88
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 146-224 3.39e-03

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: 38.68  E-value: 3.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  146 SAEVEETVDIGCQAMGVPLPTLQWYKDAIS----ISRLQNPRYKVLAS--GGLRIQKLRPEDSGIFQCFASNEGGEIQTH 219
Cdd:cd05765     11 TVKVGETASFHCDVTGRPQPEITWEKQVPGkenlIMRPNHVRGNVVVTniGQLVIYNAQPQDAGLYTCTARNSGGLLRAN 90


                   ....*
gi 1370509662  220 TYLDV 224
Cdd:cd05765     91 FPLSV 95
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 157-224 3.40e-03

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


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 38.32  E-value: 3.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370509662  157 CQAMGVPLPTLQWYKDAISISrlQNPRYKVLASG----GLRIQKLRPEDSGIFQCFASNEGGEIQTHTYLDV 224
Cdd:cd20973     19 CKVEGYPDPEVKWMKDDNPIV--ESRRFQIDQDEdglcSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 62-119 3.73e-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: 38.16  E-value: 3.73e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370509662   62 LECIASARPVEDLSvtWKRNGVRITSG---LHSFGRRLTISNPTSADTGPYVCEAALP-GSA 119
Cdd:cd05731     15 LECIAEGLPTPDIR--WIKLGGELPKGrtkFENFNKTLKIENVSEADSGEYQCTASNTmGSA 74
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 358-413 4.00e-03

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: 38.21  E-value: 4.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370509662  358 WKKDNVALTPSStsRIVVEKDGSLLISQTWSGDIGDYSCEIVSEGGNDSRMARLEV 413
Cdd:cd04969     36 WSKGTELLTNSS--RICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 51-129 4.03e-03

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: 38.20  E-value: 4.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   51 RSVVAGSSET-TLECIASARPVEdlSVTWKRNGVRI-----TSGLHSFGRRLTISNPTSADTGPYVCEAALPGsafEPAR 124
Cdd:cd04978      7 PSLVLSPGETgELICEAEGNPQP--TITWRLNGVPIepapeDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVH---GYLL 81


                   ....*
gi 1370509662  125 ATAFL 129
Cdd:cd04978     82 ANAFL 86
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 328-407 4.46e-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: 37.94  E-value: 4.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  328 PPEDHVVIKGTTATLHCGATHDPrVSLRYVWKKDNVALTPSSTSRIVVEKDG--SLLISQTWSGDIGDYSCEIVSEGGND 405
Cdd:pfam00047    2 APPTVTVLEGDSATLTCSASTGS-PGPDVTWSKEGGTLIESLKVKHDNGRTTqsSLLISNVTKEDAGTYTCVVNNPGGSA 80


                   ..
gi 1370509662  406 SR 407
Cdd:pfam00047   81 TL 82
IgI_hCEACAM_2_4_6_like cd05740
Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion ...
 41-119 4.57e-03

Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains; The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.


Pssm-ID: 409402 [Multi-domain]  Cd Length: 89  Bit Score: 38.14  E-value: 4.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   41 APTIVVppGNRSVVAGSSETTLECIASArpvEDLSVTWKRNGV------RITsgLHSFGRRLTISNPTSADTGPYVCEAA 114
Cdd:cd05740      1 KPFISS--NNSNPVEDKDAVTLTCEPET---QNTSYLWWFNGQslpvtpRLT--LSNGNRTLTLLNVTREDAGAYQCEIS 73


                   ....*
gi 1370509662  115 LPGSA 119
Cdd:cd05740     74 NPVSA 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 925-1010 4.65e-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: 4.65e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662   925 APTSVTVRTASETSLRLRWVPLPDSQYNGnpESVGYRIKYWRSDLQSSAVAQVVSdrlEREFTIEELEEWMEYELQMQAF 1004
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITG--YIVGYRVEYREEGSEWKEVNVTPS---STSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 1370509662  1005 NAVGAG 1010
Cdd:smart00060   78 NGAGEG 83
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
 140-216 4.86e-03

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


Pssm-ID: 409417  Cd Length: 95  Bit Score: 38.37  E-value: 4.86e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370509662  140 EPESRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGEI 216
Cdd:cd05760      6 HPASAAEIQPSSRVTLRCHIDGHPRPTYQWFRDGTPLSDGQGNYSVSSKERTLTLRSAGPDDSGLYYCCAHNAFGSV 82
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 325-413 5.25e-03

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


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 37.99  E-value: 5.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  325 IVHPPEDHVVIKGTTATLHCGATHDPRVSLRyvWKKDNVALtpSSTSRIVVEKDGSLLISQTWSGDIGDYSCEIV-SEGG 403
Cdd:cd20968      2 ITRPPTNVTIIEGLKAVLPCTTMGNPKPSVS--WIKGDDLI--KENNRIAVLESGSLRIHNVQKEDAGQYRCVAKnSLGI 77

                           90
                   ....*....|
gi 1370509662  404 NDSRMARLEV 413
Cdd:cd20968     78 AYSKPVTIEV 87
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 235-317 6.74e-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: 37.54  E-value: 6.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  235 PVDTTVTDGMTAILRCE-VSGAPKPAITWKRENHILASgsvRIPRFMllesGGLQIAPVFIQDAGNYTCYAANTEGSLNA 313
Cdd:cd05754      8 PRSQEVRPGADVSFICRaKSKSPAYTLVWTRVNGTLPS---RAMDFN----GILTIRNVQLSDAGTYVCTGSNMLDTDEA 80


                   ....
gi 1370509662  314 SATL 317
Cdd:cd05754     81 TATL 84
IgI_1_Axl_like cd20966
First immunoglobulin (Ig)-like domain of Axl receptor tyrosine kinase (RTK), and similar ...
 231-302 7.11e-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: 38.14  E-value: 7.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  231 FTQRPVDTTVTDGMTAILRCE--VSGAPkPAITWKRENHILASGSVRIPRFMLLESG--------GLQIAPVFIQDAGNY 300
Cdd:cd20966      3 FVGNPGNITGARGLTGTLRCQlqVQGEP-PEVHWLRDGQILELADSTQTQVPLGEDEqddwivvsQLRITSLQLSDTGQY 81


                   ..
gi 1370509662  301 TC 302
Cdd:cd20966     82 QC 83
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 329-397 7.34e-03

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: 37.68  E-value: 7.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370509662  329 PEDHVVIKGTTATLHCGATHDPRVSLryVWKKdNVALTP------SSTSRIVVEKDGSLLISQTWSGDIGDYSCE 397
Cdd:cd20954      8 PVDANVAAGQDVMLHCQADGFPTPTV--TWKK-ATGSTPgeykdlLYDPNVRILPNGTLVFGHVQKENEGHYLCE 79
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 324-413 9.41e-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: 37.37  E-value: 9.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662  324 SIVHPPEDHVVIKGT-TATLHCGATHDPRVSLRyvWKKDNVALTPSSTSRIVveKDGSLLISQTWSGDIGDYSCEIVSEG 402
Cdd:cd20978      2 KFIQKPEKNVVVKGGqDVTLPCQVTGVPQPKIT--WLHNGKPLQGPMERATV--EDGTLTIINVQPEDTGYYGCVATNEI 77

                           90
                   ....*....|.
gi 1370509662  403 GNDSRMARLEV 413
Cdd:cd20978     78 GDIYTETLLHV 88
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
1411-1744 9.66e-03

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 41.08  E-value: 9.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1411 IIGESPASAPVEVFVGEAApamapqNVQVTPLTASQLEVTWDPPPPESqngniqGYKIyYWEADSQNETEKMKVlflPEP 1490
Cdd:COG4733    524 FDDVPPQWPPVNVTTSESL------SVVAQGTAVTTLTVSWDAPAGAV------AYEV-EWRRDDGNWVSVPRT---SGT 587

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1491 VVRLKNLTSHTkYLVSISAFNAAGDgpKSDPQQGRTHQ-----AAPGAP-SFLAFSEITSTTLNvsWGEPAAANgiLQGY 1564
Cdd:COG4733    588 SFEVPGIYAGD-YEVRVRAINALGV--SSAWAASSETTvtgktAPPPAPtGLTATGGLGGITLS--WSFPVDAD--TLRT 660

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1565 RVVYEPlAPVQGVSKVVTVEVRGNwqRWLKVrDLTKGVTYFFRVQARTiTYGPELQANITAGPAEGSPGSPRDVLVTKSA 1644
Cdd:COG4733    661 EIRYST-TGDWASATVAQALYPGN--TYTLA-GLKAGQTYYYRARAVD-RSGNVSAWWVSGQASADAAGILDAITGQILE 735

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509662 1645 SELT--LQWTEGHSGDTPTTGYVIEARPSDEGLWDMFVKDIPRSATSYTLSLDKLRQGVTYEFRVVAVNEAGYGEPSNPS 1722
Cdd:COG4733    736 TELGqeLDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIGAEARVAATVAESATAAAATGTAADAAGDASGGV 815

                          330       340
                   ....*....|....*....|..
gi 1370509662 1723 TAVSAQVEAPFYEEWWFLLVMA 1744
Cdd:COG4733    816 TAGTSGTTGAGDTAASTTRVAA 837
 
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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