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Conserved domains on  [gi|767998294|ref|XP_011524146|]
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netrin receptor DCC isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Neogenin_C pfam06583
Neogenin C-terminus; This family represents the C-terminus of eukaryotic neogenin precursor ...
 803-1100 1.03e-130

Neogenin C-terminus; This family represents the C-terminus of eukaryotic neogenin precursor proteins, which contains several potential phosphorylation sites. Neogenin is a member of the N-CAM family of cell adhesion molecules (and therefore contains multiple copies of pfam00047 and pfam00041) and is closely related to the DCC tumour suppressor gene product - these proteins may play an integral role in regulating differentiation programmes and/or cell migration events within many adult and embryonic tissues.


:

Pssm-ID: 461954 [Multi-domain]  Cd Length: 289  Bit Score: 398.90  E-value: 1.03e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   803 LRPPDLWIHHEEMEMKNIEKPSGTDPAGRDSPI-QSCQDLTPVSHSQSETQLGSKSTSHSGQDTEEAGSSmstlersLAA 881
Cdd:pfam06583    1 LKPPDLWIHHEQMELKNIEKSPSPNPSGTDSPIgQSSQDLPPVDHSQSESQIHQKSNSYSGNDSDEKSST-------LAG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   882 RRAPRAKLMIPMDAQSNNPAVVSAIPVPTLESAQ---YPGILPSPTCGYPHPQFTLrpvPFPTLSVDRGFGAGRSQSVSE 958
Cdd:pfam06583   74 RRGTRPKMMLPMDSQPSNQPVVSAIPIPSLDSSHqyaHPGILPSPTCGYLHNQFSL---PFPGTPVPRSDTAPSAESVEN 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   959 GPTTQQPPMLPPSQPEH----SSSEEAPSRTIPTACVRPTHPLRSFANPLLPPPMSaiepkvPYTPLLSQPGPTLPKTHV 1034
Cdd:pfam06583  151 TPLQSQLPYQPSSQSESgslsSAVEEEPNRSIPTAKVRPGHPLKSFSVPAPPPQSA------PSTPLQQQHRPTLSKSPV 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998294  1035 KTASLGLAGKARSPLlPVSVPTAPEVSEESHKPTEDSANVYEQDDLSEQMASLEGLMKQLNAITGS 1100
Cdd:pfam06583  225 KTASLGTAGKARSPL-PVSVPNAPDTSEETERLLEDAAPSYETDELSEEMANLEGLMKDLNAITAS 289
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 1-72 6.70e-43

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 cd05723:

Pssm-ID: 472250  Cd Length: 84  Bit Score: 150.81  E-value: 6.70e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998294    1 MDIEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05723    13 MDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
133-556 2.87e-23

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 105.85  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  133 NTTQPGSLQLTVGNLKPEAMYTFRVVAYNEWGPGESSQPIKVATQPELqvPGPVENLQAVSTSPTSILITWEPPayANGP 212
Cdd:COG3401   185 LTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP--PSAPTGLTATADTPGSVTLSWDPV--TESD 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  213 VQGYRLFCTEVSTGKEQNI-EVDGLSYKLEGLKKFTEYSLRFLAYNRYG-PGVSTDDITVVTLSDVPsAPPQNVSLEVVN 290
Cdd:COG3401   261 ATGYRVYRSNSGDGPFTKVaTVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPP-AAPSGLTATAVG 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  291 SRSIKVSWlpppSGTQNGFITGYKIrHRKTTRRGEMETL--EPNNLWYLFTGLEKGSQYSFQVSAMTVNGT-GPPSNWYT 367
Cdd:COG3401   340 SSSITLSW----TASSDADVTGYNV-YRSTSGGGTYTKIaeTVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVS 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  368 AETPENDLDES--QVPDQPSSLHVRPQTNCIIMSWTPPLNPNIVVRGYIIGYGV-GSPYAETVRVDSKQRYYSIERLESS 444
Cdd:COG3401   415 ATTASAASGESltASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVpFTTTSSTVTATTTDTTTANLSVTTG 494

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  445 SHYVISLKAFNNAGEGVPLYESATTRSITDPTDPVDYYPLLDDFPTSVPDLSTPMLPPVGVQAVAlthdavrvSWADNSV 524
Cdd:COG3401   495 SLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASS--------SVSGAGL 566

                         410       420       430
                  ....*....|....*....|....*....|..
gi 767998294  525 PKNQKTSEVRLYTVRWRTSFSASAKYKSEDTT 556
Cdd:COG3401   567 GSGNLYLITTLGGSLLTTTSTNTNDVAGVHGG 598
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 84-176 1.14e-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: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   84 PSAPRDVVPVLVSSRFVRLSWRPPAEAKGNIQTFTVFFSREGDNRERALNTTQPGSLQLTVGNLKPEAMYTFRVVAYNEW 163
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 767998294  164 GPGESSQPIKVAT 176
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 601-696 1.29e-13

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.52  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  601 SAPKDLTVitREGKPRAVIVSWQPPLEANGKITAYILFYTLDKNipiDDWI-METISGDRLTHQIMDLNLDTMYYFRIQA 679
Cdd:cd00063     2 SPPTNLRV--TDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKeVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*..
gi 767998294  680 RNSKGVGPLSDPILFRT 696
Cdd:cd00063    77 VNGGGESPPSESVTVTT 93
 
Name Accession Description Interval E-value
Neogenin_C pfam06583
Neogenin C-terminus; This family represents the C-terminus of eukaryotic neogenin precursor ...
 803-1100 1.03e-130

Neogenin C-terminus; This family represents the C-terminus of eukaryotic neogenin precursor proteins, which contains several potential phosphorylation sites. Neogenin is a member of the N-CAM family of cell adhesion molecules (and therefore contains multiple copies of pfam00047 and pfam00041) and is closely related to the DCC tumour suppressor gene product - these proteins may play an integral role in regulating differentiation programmes and/or cell migration events within many adult and embryonic tissues.


Pssm-ID: 461954 [Multi-domain]  Cd Length: 289  Bit Score: 398.90  E-value: 1.03e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   803 LRPPDLWIHHEEMEMKNIEKPSGTDPAGRDSPI-QSCQDLTPVSHSQSETQLGSKSTSHSGQDTEEAGSSmstlersLAA 881
Cdd:pfam06583    1 LKPPDLWIHHEQMELKNIEKSPSPNPSGTDSPIgQSSQDLPPVDHSQSESQIHQKSNSYSGNDSDEKSST-------LAG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   882 RRAPRAKLMIPMDAQSNNPAVVSAIPVPTLESAQ---YPGILPSPTCGYPHPQFTLrpvPFPTLSVDRGFGAGRSQSVSE 958
Cdd:pfam06583   74 RRGTRPKMMLPMDSQPSNQPVVSAIPIPSLDSSHqyaHPGILPSPTCGYLHNQFSL---PFPGTPVPRSDTAPSAESVEN 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   959 GPTTQQPPMLPPSQPEH----SSSEEAPSRTIPTACVRPTHPLRSFANPLLPPPMSaiepkvPYTPLLSQPGPTLPKTHV 1034
Cdd:pfam06583  151 TPLQSQLPYQPSSQSESgslsSAVEEEPNRSIPTAKVRPGHPLKSFSVPAPPPQSA------PSTPLQQQHRPTLSKSPV 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998294  1035 KTASLGLAGKARSPLlPVSVPTAPEVSEESHKPTEDSANVYEQDDLSEQMASLEGLMKQLNAITGS 1100
Cdd:pfam06583  225 KTASLGTAGKARSPL-PVSVPNAPDTSEETERLLEDAAPSYETDELSEEMANLEGLMKDLNAITAS 289
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 1-72 6.70e-43

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: 150.81  E-value: 6.70e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998294    1 MDIEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05723    13 MDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
133-556 2.87e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 105.85  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  133 NTTQPGSLQLTVGNLKPEAMYTFRVVAYNEWGPGESSQPIKVATQPELqvPGPVENLQAVSTSPTSILITWEPPayANGP 212
Cdd:COG3401   185 LTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP--PSAPTGLTATADTPGSVTLSWDPV--TESD 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  213 VQGYRLFCTEVSTGKEQNI-EVDGLSYKLEGLKKFTEYSLRFLAYNRYG-PGVSTDDITVVTLSDVPsAPPQNVSLEVVN 290
Cdd:COG3401   261 ATGYRVYRSNSGDGPFTKVaTVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPP-AAPSGLTATAVG 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  291 SRSIKVSWlpppSGTQNGFITGYKIrHRKTTRRGEMETL--EPNNLWYLFTGLEKGSQYSFQVSAMTVNGT-GPPSNWYT 367
Cdd:COG3401   340 SSSITLSW----TASSDADVTGYNV-YRSTSGGGTYTKIaeTVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVS 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  368 AETPENDLDES--QVPDQPSSLHVRPQTNCIIMSWTPPLNPNIVVRGYIIGYGV-GSPYAETVRVDSKQRYYSIERLESS 444
Cdd:COG3401   415 ATTASAASGESltASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVpFTTTSSTVTATTTDTTTANLSVTTG 494

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  445 SHYVISLKAFNNAGEGVPLYESATTRSITDPTDPVDYYPLLDDFPTSVPDLSTPMLPPVGVQAVAlthdavrvSWADNSV 524
Cdd:COG3401   495 SLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASS--------SVSGAGL 566

                         410       420       430
                  ....*....|....*....|....*....|..
gi 767998294  525 PKNQKTSEVRLYTVRWRTSFSASAKYKSEDTT 556
Cdd:COG3401   567 GSGNLYLITTLGGSLLTTTSTNTNDVAGVHGG 598
I-set pfam07679
Immunoglobulin I-set domain;
2-72 9.25e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 9.25e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998294     2 DIEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIV---GGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:pfam07679   17 SARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTyegGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 183-272 4.13e-18

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.23  E-value: 4.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  183 PGPVENLQAVSTSPTSILITWEPPAYANGPVQGYRLFCTEVSTGKEQNIEV---DGLSYKLEGLKKFTEYSLRFLAYNRY 259
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVtpgSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 767998294  260 GPGVSTDDITVVT 272
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 84-176 1.14e-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: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   84 PSAPRDVVPVLVSSRFVRLSWRPPAEAKGNIQTFTVFFSREGDNRERALNTTQPGSLQLTVGNLKPEAMYTFRVVAYNEW 163
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 767998294  164 GPGESSQPIKVAT 176
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 280-360 3.83e-15

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.49  E-value: 3.83e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    280 PPQNVSLEVVNSRSIKVSWLPPPSGTQNGFITGYKIRHRKTTRRGEMETLEPNNLWYLFTGLEKGSQYSFQVSAMTVNGT 359
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 767998294    360 G 360
Cdd:smart00060   83 G 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 2-72 1.92e-14

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.46  E-value: 1.92e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998294      2 DIEFECTVSGKPVPTVNWMKNGDV-VIPSDYFQIVGGSN---LRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:smart00410   11 SVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 601-696 1.29e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.52  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  601 SAPKDLTVitREGKPRAVIVSWQPPLEANGKITAYILFYTLDKNipiDDWI-METISGDRLTHQIMDLNLDTMYYFRIQA 679
Cdd:cd00063     2 SPPTNLRV--TDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKeVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*..
gi 767998294  680 RNSKGVGPLSDPILFRT 696
Cdd:cd00063    77 VNGGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
184-262 2.50e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.28  E-value: 2.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   184 GPVENLQAVSTSPTSILITWEPPAYANGPVQGYRLFCTEVSTGK-EQNIEVDG--LSYKLEGLKKFTEYSLRFLAYNRYG 260
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEpWNEITVPGttTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ..
gi 767998294   261 PG 262
Cdd:pfam00041   81 EG 82
fn3 pfam00041
Fibronectin type III domain;
601-689 3.74e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 3.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   601 SAPKDLTVITREgkPRAVIVSWQPPLEANGKITAYILFY-TLDKNipiDDWIMETISGDRLTHQIMDLNLDTMYYFRIQA 679
Cdd:pfam00041    1 SAPSNLTVTDVT--STSLTVSWTPPPDGNGPITGYEVEYrPKNSG---EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75

                           90
                   ....*....|
gi 767998294   680 RNSKGVGPLS 689
Cdd:pfam00041   76 VNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 84-166 2.61e-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: 60.71  E-value: 2.61e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294     84 PSAPRDVVPVLVSSRFVRLSWRPPAEAKGN--IQTFTVFFSREGDNRERAlnTTQPGSLQLTVGNLKPEAMYTFRVVAYN 161
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEV--NVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 767998294    162 EWGPG 166
Cdd:smart00060   79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 601-686 1.18e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.78  E-value: 1.18e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    601 SAPKDLTVITREgkPRAVIVSWQPPLEANGkiTAYILFYTLDKNIPIDDWIMETISGDRLTHQIMDLNLDTMYYFRIQAR 680
Cdd:smart00060    2 SPPSNLRVTDVT--STSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 767998294    681 NSKGVG 686
Cdd:smart00060   78 NGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
85-169 1.33e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    85 SAPRDVVPVLVSSRFVRLSWRPPAEAKGNIQTFTVFFSREGDNrERALNTTQPGSL-QLTVGNLKPEAMYTFRVVAYNEW 163
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSG-EPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 767998294   164 GPGESS 169
Cdd:pfam00041   80 GEGPPS 85
PHA03247 PHA03247
large tegument protein UL36; Provisional
 823-1071 5.64e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 5.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  823 PSGTDPAGRDSPIQSCQDLTPVSHSQSETQLGSKStshSGQDTEEAGSSMSTLERSLAARRAPRAKLMIPMDAQSNNPAV 902
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA---PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  903 VSAiPVPTLESAQYP-GILPSPTCGYPHPQFTLRPVPFPTLSVDRGFGAGrsQSVSEGPTTQQPPMLP--PSQPEHSS-S 978
Cdd:PHA03247 2811 VLA-PAAALPPAASPaGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG--GDVRRRPPSRSPAAKPaaPARPPVRRlA 2887

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  979 EEAPSRTIPTACVRPTHPLRSFANPLLPPPMSAIEPKVPYTPLLS-----QPGPTLPKTHVKTASLGLAGKARSPLLPVS 1053
Cdd:PHA03247 2888 RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPpppppRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967

                         250
                  ....*....|....*...
gi 767998294 1054 VPTAPEVSEESHKPTEDS 1071
Cdd:PHA03247 2968 VPGRVAVPRFRVPQPAPS 2985
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
480-684 6.05e-04

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.17  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  480 DYYPLLDdfpTSVPDLSTPMLPPVGVQAVALTHDavrvswadnsvpKNQKTSEVRLyTVRWRTS---FSASAKYKSED-- 554
Cdd:COG4733   514 EKYAAID---AGAFDDVPPQWPPVNVTTSESLSV------------VAQGTAVTTL-TVSWDAPagaVAYEVEWRRDDgn 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  555 ------TTSLSYTATGLKPNTmYEFSVM-VTKNRRSSTWSMTAHAT-TYEAAPTSAPKDLTVitrEGKPRAVIVSWQPPL 626
Cdd:COG4733   578 wvsvprTSGTSFEVPGIYAGD-YEVRVRaINALGVSSAWAASSETTvTGKTAPPPAPTGLTA---TGGLGGITLSWSFPV 653

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998294  627 EANgkITAYILFYTLDknipiDDW---IMETISGDRLTHQIMDLNLDTMYYFRIQARNSKG 684
Cdd:COG4733   654 DAD--TLRTEIRYSTT-----GDWasaTVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
 
Name Accession Description Interval E-value
Neogenin_C pfam06583
Neogenin C-terminus; This family represents the C-terminus of eukaryotic neogenin precursor ...
 803-1100 1.03e-130

Neogenin C-terminus; This family represents the C-terminus of eukaryotic neogenin precursor proteins, which contains several potential phosphorylation sites. Neogenin is a member of the N-CAM family of cell adhesion molecules (and therefore contains multiple copies of pfam00047 and pfam00041) and is closely related to the DCC tumour suppressor gene product - these proteins may play an integral role in regulating differentiation programmes and/or cell migration events within many adult and embryonic tissues.


Pssm-ID: 461954 [Multi-domain]  Cd Length: 289  Bit Score: 398.90  E-value: 1.03e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   803 LRPPDLWIHHEEMEMKNIEKPSGTDPAGRDSPI-QSCQDLTPVSHSQSETQLGSKSTSHSGQDTEEAGSSmstlersLAA 881
Cdd:pfam06583    1 LKPPDLWIHHEQMELKNIEKSPSPNPSGTDSPIgQSSQDLPPVDHSQSESQIHQKSNSYSGNDSDEKSST-------LAG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   882 RRAPRAKLMIPMDAQSNNPAVVSAIPVPTLESAQ---YPGILPSPTCGYPHPQFTLrpvPFPTLSVDRGFGAGRSQSVSE 958
Cdd:pfam06583   74 RRGTRPKMMLPMDSQPSNQPVVSAIPIPSLDSSHqyaHPGILPSPTCGYLHNQFSL---PFPGTPVPRSDTAPSAESVEN 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   959 GPTTQQPPMLPPSQPEH----SSSEEAPSRTIPTACVRPTHPLRSFANPLLPPPMSaiepkvPYTPLLSQPGPTLPKTHV 1034
Cdd:pfam06583  151 TPLQSQLPYQPSSQSESgslsSAVEEEPNRSIPTAKVRPGHPLKSFSVPAPPPQSA------PSTPLQQQHRPTLSKSPV 224

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998294  1035 KTASLGLAGKARSPLlPVSVPTAPEVSEESHKPTEDSANVYEQDDLSEQMASLEGLMKQLNAITGS 1100
Cdd:pfam06583  225 KTASLGTAGKARSPL-PVSVPNAPDTSEETERLLEDAAPSYETDELSEEMANLEGLMKDLNAITAS 289
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 1-72 6.70e-43

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: 150.81  E-value: 6.70e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998294    1 MDIEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05723    13 MDIVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
133-556 2.87e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 105.85  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  133 NTTQPGSLQLTVGNLKPEAMYTFRVVAYNEWGPGESSQPIKVATQPELqvPGPVENLQAVSTSPTSILITWEPPayANGP 212
Cdd:COG3401   185 LTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP--PSAPTGLTATADTPGSVTLSWDPV--TESD 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  213 VQGYRLFCTEVSTGKEQNI-EVDGLSYKLEGLKKFTEYSLRFLAYNRYG-PGVSTDDITVVTLSDVPsAPPQNVSLEVVN 290
Cdd:COG3401   261 ATGYRVYRSNSGDGPFTKVaTVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPP-AAPSGLTATAVG 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  291 SRSIKVSWlpppSGTQNGFITGYKIrHRKTTRRGEMETL--EPNNLWYLFTGLEKGSQYSFQVSAMTVNGT-GPPSNWYT 367
Cdd:COG3401   340 SSSITLSW----TASSDADVTGYNV-YRSTSGGGTYTKIaeTVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVS 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  368 AETPENDLDES--QVPDQPSSLHVRPQTNCIIMSWTPPLNPNIVVRGYIIGYGV-GSPYAETVRVDSKQRYYSIERLESS 444
Cdd:COG3401   415 ATTASAASGESltASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVpFTTTSSTVTATTTDTTTANLSVTTG 494

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  445 SHYVISLKAFNNAGEGVPLYESATTRSITDPTDPVDYYPLLDDFPTSVPDLSTPMLPPVGVQAVAlthdavrvSWADNSV 524
Cdd:COG3401   495 SLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASS--------SVSGAGL 566

                         410       420       430
                  ....*....|....*....|....*....|..
gi 767998294  525 PKNQKTSEVRLYTVRWRTSFSASAKYKSEDTT 556
Cdd:COG3401   567 GSGNLYLITTLGGSLLTTTSTNTNDVAGVHGG 598
I-set pfam07679
Immunoglobulin I-set domain;
2-72 9.25e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 81.92  E-value: 9.25e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998294     2 DIEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIV---GGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:pfam07679   17 SARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTyegGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
221-652 1.20e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 91.22  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  221 TEVSTGKEQNIEVDGLSYKLEGLKKFTEYSLRFLAYNRYGPGVSTDDITVVTLSDVPSaPPQNVSLEVVNSRSIKVSWLP 300
Cdd:COG3401   177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPS-APTGLTATADTPGSVTLSWDP 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  301 PPsgtqNGFITGYKIrHRKTTRRGEMETL-EPNNLWYLFTGLEKGSQYSFQVSAMTVNGT-GPPSNWYTAETpendldES 378
Cdd:COG3401   256 VT----ESDATGYRV-YRSNSGDGPFTKVaTVTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTT------DL 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  379 QVPDQPSSLHVRPQTNCIIM-SWTPPLNPNIVvrGYII--GYGVGSPYaETVRVDSKQRYYSIERLESSSHYVISLKAFN 455
Cdd:COG3401   325 TPPAAPSGLTATAVGSSSITlSWTASSDADVT--GYNVyrSTSGGGTY-TKIAETVTTTSYTDTGLTPGTTYYYKVTAVD 401

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  456 NAGEGVPLYESATTRSITDPTDPVDYYPLLDDFPTSVPD----LSTPMLPPVGVQAVALTHDAVRVSWADNSVPKNQKTS 531
Cdd:COG3401   402 AAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGataaASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATT 481

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  532 EVRLYTVRWRTSFSASAKYKSEDTTSLSYTATGLKPNTMYEFSVMVTkNRRSSTWSMTAHATTYEAAPTSAPKDLTVITR 611
Cdd:COG3401   482 TDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTP-NVTGASPVTVGASTGDVLITDLVSLTTSASSS 560

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 767998294  612 EGKPRAVIVSWQPPLEANGKITAYILFYTLDKNIPIDDWIM 652
Cdd:COG3401   561 VSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLL 601
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 183-272 4.13e-18

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 80.23  E-value: 4.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  183 PGPVENLQAVSTSPTSILITWEPPAYANGPVQGYRLFCTEVSTGKEQNIEV---DGLSYKLEGLKKFTEYSLRFLAYNRY 259
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVtpgSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 767998294  260 GPGVSTDDITVVT 272
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 84-176 1.14e-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: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   84 PSAPRDVVPVLVSSRFVRLSWRPPAEAKGNIQTFTVFFSREGDNRERALNTTQPGSLQLTVGNLKPEAMYTFRVVAYNEW 163
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 767998294  164 GPGESSQPIKVAT 176
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
52-454 3.52e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 86.59  E-value: 3.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   52 FYQCVAENEAGNAQTSAQLIVPKPAIPsssvlPSAPRDVVPVLVSSRFVRLSWRPPAEAkgNIQTFTVFFSREGDNRERA 131
Cdd:COG3401   206 YYRVAATDTGGESAPSNEVSVTTPTTP-----PSAPTGLTATADTPGSVTLSWDPVTES--DATGYRVYRSNSGDGPFTK 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  132 LNTTQpgSLQLTVGNLKPEAMYTFRVVAYNEWG-PGESSQPIKVATQPELqvPGPVENLQAVSTSPTSILITWEPPayAN 210
Cdd:COG3401   279 VATVT--TTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP--PAAPSGLTATAVGSSSITLSWTAS--SD 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  211 GPVQGYRLFCTEVSTGKEQNI--EVDGLSYKLEGLKKFTEYSLRFLAYNRYGP-GVSTDDITVVTLSDVPSAPPQNVSLE 287
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTKIaeTVTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDA 432

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  288 VVNSRSIKVSW-----LPPPSGTQNGFITGYKIRHRKTTRRGEMETLEPNNLWYLFTGLEKGSQYSFQVSAMTVNGTGPP 362
Cdd:COG3401   433 VPLTDVAGATAaasaaSNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVI 512

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  363 SNWYTAETPeNDLDESQVPDQPSSLHVRPQTNCIIMSWTPPLNPNIVVRGYIIGYGVGSPYAETVRVDSKQRYYSIERLE 442
Cdd:COG3401   513 GASAAAAVG-GAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTND 591

                         410
                  ....*....|..
gi 767998294  443 SSSHYVISLKAF 454
Cdd:COG3401   592 VAGVHGGTLLVL 603
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 280-370 2.69e-16

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 75.23  E-value: 2.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  280 PPQNVSLEVVNSRSIKVSWLPPPSGtqNGFITGYKIRHRKTTRRG--EMETLEPNNLWYLFTGLEKGSQYSFQVSAMTVN 357
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGSGDwkEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 767998294  358 GTGPPSNWYTAET 370
Cdd:cd00063    81 GESPPSESVTVTT 93
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 2-72 7.92e-16

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: 73.58  E-value: 7.92e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998294    2 DIEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20978    18 DVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDGTLTIINVQPEDTGYYGCVATNEIGDIYTETLLHV 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 280-360 3.83e-15

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 71.49  E-value: 3.83e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    280 PPQNVSLEVVNSRSIKVSWLPPPSGTQNGFITGYKIRHRKTTRRGEMETLEPNNLWYLFTGLEKGSQYSFQVSAMTVNGT 359
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 767998294    360 G 360
Cdd:smart00060   83 G 83
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 2-72 1.29e-14

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: 69.94  E-value: 1.29e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998294    2 DIEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSnLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05728    16 SLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGD-LRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 3-67 1.38e-14

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: 69.67  E-value: 1.38e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIV---GGSNLRILGVVKSDEGFYQCVAENEAGNAQTS 67
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRselGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 2-72 1.92e-14

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.46  E-value: 1.92e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998294      2 DIEFECTVSGKPVPTVNWMKNGDV-VIPSDYFQIVGGSN---LRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:smart00410   11 SVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 601-696 1.29e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.52  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  601 SAPKDLTVitREGKPRAVIVSWQPPLEANGKITAYILFYTLDKNipiDDWI-METISGDRLTHQIMDLNLDTMYYFRIQA 679
Cdd:cd00063     2 SPPTNLRV--TDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKeVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*..
gi 767998294  680 RNSKGVGPLSDPILFRT 696
Cdd:cd00063    77 VNGGGESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
247-692 1.54e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.04  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  247 TEYSLRFLAYNRYGPGVSTDDITVVTLSDVPSAPPQNVSLEVVNSRSIKVSWLPPPSGTQNGFITGYKIRHRKTTRRGEm 326
Cdd:COG3401     1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGV- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  327 eTLEPNNLWYLFTGLEKGSQYSFQVSAMTVNGTGPPSNWYTAETPEN-DLDESQVPDQPSSLHVRPQTNCIIMSWTPPLN 405
Cdd:COG3401    80 -AAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTAtTATAVAGGAATAGTYALGAGLYGVDGANASGT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  406 PNIVVRGYIIGYGVGSPYAETV-----RVDSKQRYYSIERLESSSHYVISLKAFNNAGEGVPlyesATTRSITDPTdpvd 480
Cdd:COG3401   159 TASSVAGAGVVVSPDTSATAAVattslTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAP----SNEVSVTTPT---- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  481 yypllddfptsvpdlsTPMLPPVGVQAVALTHDAVRVSWADNSVPknqktsEVRLYTVRWRTSfsASAKYKS-EDTTSLS 559
Cdd:COG3401   231 ----------------TPPSAPTGLTATADTPGSVTLSWDPVTES------DATGYRVYRSNS--GDGPFTKvATVTTTS 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  560 YTATGLKPNTMYEFSVM-VTKNRRSSTWSMTAHATTYEAAPTsAPKDLTVITREgkPRAVIVSWQPPleANGKITAYILF 638
Cdd:COG3401   287 YTDTGLTNGTTYYYRVTaVDAAGNESAPSNVVSVTTDLTPPA-APSGLTATAVG--SSSITLSWTAS--SDADVTGYNVY 361

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767998294  639 YTLDKNIPIDdWIMETISGdrLTHQIMDLNLDTMYYFRIQARNSKGV-GPLSDPI 692
Cdd:COG3401   362 RSTSGGGTYT-KIAETVTT--TSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEV 413
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 2-70 1.78e-13

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: 66.79  E-value: 1.78e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767998294    2 DIEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQL 70
Cdd:cd20957    18 TAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQATAEL 86
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 5-72 2.13e-13

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: 66.75  E-value: 2.13e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998294    5 FECTVSGKPVPTVNWMKNGDVVIPSD----YFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05744    20 FDCKVSGLPTPDLFWQLNGKPVRPDSahkmLVRENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
fn3 pfam00041
Fibronectin type III domain;
184-262 2.50e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.28  E-value: 2.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   184 GPVENLQAVSTSPTSILITWEPPAYANGPVQGYRLFCTEVSTGK-EQNIEVDG--LSYKLEGLKKFTEYSLRFLAYNRYG 260
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEpWNEITVPGttTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ..
gi 767998294   261 PG 262
Cdd:pfam00041   81 EG 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 183-262 2.61e-13

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: 66.48  E-value: 2.61e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    183 PGPVENLQAVSTSPTSILITWEPPAYAN--GPVQGYRL-FCTEVSTGKEQNIEVDGLSYKLEGLKKFTEYSLRFLAYNRY 259
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGitGYIVGYRVeYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 767998294    260 GPG 262
Cdd:smart00060   81 GEG 83
fn3 pfam00041
Fibronectin type III domain;
601-689 3.74e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 3.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   601 SAPKDLTVITREgkPRAVIVSWQPPLEANGKITAYILFY-TLDKNipiDDWIMETISGDRLTHQIMDLNLDTMYYFRIQA 679
Cdd:pfam00041    1 SAPSNLTVTDVT--STSLTVSWTPPPDGNGPITGYEVEYrPKNSG---EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75

                           90
                   ....*....|
gi 767998294   680 RNSKGVGPLS 689
Cdd:pfam00041   76 VNGGGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
280-363 7.69e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 7.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   280 PPQNVSLEVVNSRSIKVSWLPPPSGtqNGFITGYKIRHRKTTRRGEM--ETLEPNNLWYLFTGLEKGSQYSFQVSAMTVN 357
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDG--NGPITGYEVEYRPKNSGEPWneITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 767998294   358 GTGPPS 363
Cdd:pfam00041   80 GEGPPS 85
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 1-72 9.73e-13

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: 64.79  E-value: 9.73e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998294    1 MDIEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd04969    18 GDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 1-72 1.16e-12

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: 64.75  E-value: 1.16e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998294    1 MDIEFECTVSGKPVPTVNWMKNGDVV----IPSDY-FQIVGG-SNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20951    16 SDAKLRVEVQGKPDPEVKWYKNGVPIdpssIPGKYkIESEYGvHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASVVV 93
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 3-72 6.43e-12

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: 62.41  E-value: 6.43e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    3 IEFECTVSGKPVPTVNWMKNgDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05725    15 AEFQCEVGGDPVPTVRWRKE-DGELPKGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 1-59 2.54e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 60.66  E-value: 2.54e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998294     1 MDIEFECTVSGKPVPTVNWMKNGDVVIP---SDYFQIVGGSNLRILGVVKSDEGFYQCVAEN 59
Cdd:pfam13927   17 ETVTLTCEATGSPPPTITWYKNGEPISSgstRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 84-166 2.61e-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: 60.71  E-value: 2.61e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294     84 PSAPRDVVPVLVSSRFVRLSWRPPAEAKGN--IQTFTVFFSREGDNRERAlnTTQPGSLQLTVGNLKPEAMYTFRVVAYN 161
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEV--NVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 767998294    162 EWGPG 166
Cdd:smart00060   79 GAGEG 83
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 5-72 5.68e-11

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: 59.90  E-value: 5.68e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998294    5 FECTVSGKPVPTVNWMKNGDVVIPSDYFQIV----GGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20973    17 FDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqdedGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 601-686 1.18e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.78  E-value: 1.18e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    601 SAPKDLTVITREgkPRAVIVSWQPPLEANGkiTAYILFYTLDKNIPIDDWIMETISGDRLTHQIMDLNLDTMYYFRIQAR 680
Cdd:smart00060    2 SPPSNLRVTDVT--STSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 767998294    681 NSKGVG 686
Cdd:smart00060   78 NGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 501-594 4.87e-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: 57.51  E-value: 4.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  501 PPVGVQAVALTHDAVRVSWadnsVPKNQKTSEVRLYTVRWR-TSFSASAKYKSEDTTSLSYTATGLKPNTMYEFSVMVTK 579
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSW----TPPEDDGGPITGYVVEYReKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....*
gi 767998294  580 NRRSSTWSMTAHATT 594
Cdd:cd00063    79 GGGESPPSESVTVTT 93
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 2-72 6.98e-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: 56.87  E-value: 6.98e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998294    2 DIEFECTVSGKPVPTVNWMKNG-DVVIPSDYFQI-VGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20976    18 DFVAQCSARGKPVPRITWIRNAqPLQYAADRSTCeAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 381-460 1.14e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 56.08  E-value: 1.14e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    381 PDQPSSLHVRPQT-NCIIMSWTPPLNPNIV--VRGYIIGYGVGSPYAETVRVDSKQRYYSIERLESSSHYVISLKAFNNA 457
Cdd:smart00060    1 PSPPSNLRVTDVTsTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 767998294    458 GEG 460
Cdd:smart00060   81 GEG 83
fn3 pfam00041
Fibronectin type III domain;
85-169 1.33e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    85 SAPRDVVPVLVSSRFVRLSWRPPAEAKGNIQTFTVFFSREGDNrERALNTTQPGSL-QLTVGNLKPEAMYTFRVVAYNEW 163
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSG-EPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 767998294   164 GPGESS 169
Cdd:pfam00041   80 GEGPPS 85
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 3-72 1.79e-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: 54.94  E-value: 1.79e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05745     5 VDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 6-72 2.33e-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: 55.10  E-value: 2.33e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    6 ECTVS-GKPVPTVNWMKNGDVVIPSD-YFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTS-AQLIV 72
Cdd:cd05724    18 ECSPPrGHPEPTVSWRKDGQPLNLDNeRVRIVDDGNLLIAEARKSDEGTYKCVATNMVGERESRaARLSV 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 7-72 5.67e-09

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: 54.04  E-value: 5.67e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998294    7 CTVSGKPVPTVNWMKNGDVVIPSD--YFQIVGGSnLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20952    21 CQATGEPVPTISWLKDGVPLLGKDerITTLENGS-LQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 3-62 6.70e-09

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: 54.28  E-value: 6.70e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVG---GSNLRILGVVKSDEGFYQCVAENEAG 62
Cdd:cd05747    21 ARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSteyKSTFEISKVQMSDEGNYTVVVENSEG 83
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 1-72 7.84e-09

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: 53.57  E-value: 7.84e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998294    1 MDIEFECTVSGKPVPTVNWMK-NGDvvIPSDYFQIVG-GSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05731    11 GVLLLECIAEGLPTPDIRWIKlGGE--LPKGRTKFENfNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 3-70 1.17e-08

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: 52.57  E-value: 1.17e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQL 70
Cdd:cd05746     1 VQIPCSAQGDPEPTITWNKDGVQVTESGKFHISPEGYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 381-469 1.41e-08

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: 53.27  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  381 PDQPSSLHVRPQT-NCIIMSWTPPLNPNIVVRGYIIGY-GVGSPYAETVRV-DSKQRYYSIERLESSSHYVISLKAFNNA 457
Cdd:cd00063     1 PSPPTNLRVTDVTsTSVTLSWTPPEDDGGPITGYVVEYrEKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 767998294  458 GEGVPLYESATT 469
Cdd:cd00063    81 GESPPSESVTVT 92
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 3-72 4.71e-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: 51.78  E-value: 4.71e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVIPSDYfqiVGGSNLR-------ILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05857    22 VKFRCPAAGNPTPTMRWLKNGKEFKQEHR---IGGYKVRnqhwsliMESVVPSDKGNYTCVVENEYGSINHTYHLDV 95
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 7-64 7.42e-08

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: 51.09  E-value: 7.42e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767998294    7 CTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNA 64
Cdd:cd20968    21 CTTMGNPKPSVSWIKGDDLIKENNRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGIA 78
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 7-72 7.70e-08

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: 51.09  E-value: 7.70e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998294    7 CTVSGKPVPTVNWMKNGDVVIPSD--YFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05730    25 CDADGFPEPTMTWTKDGEPIESGEekYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 3-72 8.19e-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: 50.97  E-value: 8.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSN--LRILGVVKSDEGFYQCVAENEA-GNAQTSAQLIV 72
Cdd:cd20970    20 ATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGttLTIRNIRRSDMGIYLCIASNGVpGSVEKRITLQV 92
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 7-72 2.30e-07

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: 49.95  E-value: 2.30e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767998294    7 CTVSGKPVPTVNWMKNGDVVIP--SDYFQIVG-GSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05736    22 CHAEGIPLPRVQWLKNGMDINPklSKQLTLIAnGSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFV 90
fn3 pfam00041
Fibronectin type III domain;
382-462 2.72e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 49.34  E-value: 2.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   382 DQPSSLHVRPQT-NCIIMSWTPPLNPNIVVRGYIIGYGV--GSPYAETVRVDSKQRYYSIERLESSSHYVISLKAFNNAG 458
Cdd:pfam00041    1 SAPSNLTVTDVTsTSLTVSWTPPPDGNGPITGYEVEYRPknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 767998294   459 EGVP 462
Cdd:pfam00041   81 EGPP 84
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 5-64 2.97e-07

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: 49.47  E-value: 2.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998294    5 FECTVSGKPVPTVNWMKNGD-------------VVIPSD---YFQIVGGSNlrilgvVKSDEGFYQCVAENEAGNA 64
Cdd:cd07693    20 LNCKAEGRPTPTIQWLKNGQpletdkddprshrIVLPSGslfFLRVVHGRK------GRSDEGVYVCVAHNSLGEA 89
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 3-72 3.18e-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: 49.12  E-value: 3.18e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKS---DEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20972    19 VRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAfeeDTGRYSCLATNSVGSDTTSAEIFV 91
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 6-72 3.65e-07

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: 49.23  E-value: 3.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767998294    6 ECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05852    23 ECKPKAAPKPKFSWSKGTELLVNNSRISIWDDGSLEILNITKLDEGSYTCFAENNRGKANSTGVLSV 89
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 3-72 3.82e-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: 49.08  E-value: 3.82e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    3 IEFECTVSGKPVPTVNWMKNgDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd04968    19 VTLECFALGNPVPQIKWRKV-DGSPSSQWEITTSEPVLEIPNVQFEDEGTYECEAENSRGKDTVQGRIIV 87
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 6-65 3.88e-07

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


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 48.75  E-value: 3.88e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    6 ECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQ 65
Cdd:cd05876    16 ECIAEGLPTPTVKWLRPSGPLPPDRVKYQNHNKTLQLLNVGESDDGEYVCLAENSLGSAR 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 501-584 4.17e-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: 48.76  E-value: 4.17e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    501 PPVGVQAVALTHDAVRVSWadNSVPKNQKTSEVRLYTVRWRTSFSASAKYkSEDTTSLSYTATGLKPNTMYEFSVMVTKN 580
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSW--EPPPDDGITGYIVGYRVEYREEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 767998294    581 RRSS 584
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 ...
 7-60 4.75e-07

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: 49.01  E-value: 4.75e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998294    7 CTVSGKPVPTVNWMKNG---DVVIPSDYFQIVGGSnLRILGVV-----KSDEGFYQCVAENE 60
Cdd:cd05722    23 CSAESDPPPKIEWKKDGvllNLVSDERRQQLPNGS-LLITSVVhskhnKPDEGFYQCVAQNE 83
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 4-72 5.57e-07

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: 48.60  E-value: 5.57e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998294    4 EFECTVSGKPVPTVNWMKNGDVV--IPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd04978    18 ELICEAEGNPQPTITWRLNGVPIepAPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHGYLLANAFLHV 88
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 3-72 7.53e-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: 48.50  E-value: 7.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVIPSDY--FQI---VGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20974    18 ATFEAHVSGKPVPEVSWFRDGQVISTSTLpgVQIsfsDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAELLV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 9-72 8.71e-07

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


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 47.58  E-value: 8.71e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767998294    9 VSGKPVPTVNWMKNGDVVIPSDYFQIVGGSN---LRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05748    16 IKGRPTPTVTWSKDGQPLKETGRVQIETTASstsLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
 2-72 1.09e-06

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: 47.85  E-value: 1.09e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998294    2 DIEFECTVSGKPVPTVNWMKNGDVVIPsDYFQIV-----GGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20975    17 DVIMSIRVQGEPKPVVSWLRNRQPVRP-DQRRFAeeaegGLCRLRILAAERGDAGFYTCKAVNEYGARQCEARLEV 91
fn3 pfam00041
Fibronectin type III domain;
501-575 3.52e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 3.52e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998294   501 PPVGVQAVALTHDAVRVSWAdnsvPKNQKTSEVRLYTVRWRTSFSASA-KYKSEDTTSLSYTATGLKPNTMYEFSV 575
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWT----PPPDGNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRV 73
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 7-72 3.86e-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: 3.86e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998294    7 CTVSGKPVPTVNWMKNGDVVIPSDYFQIvgGSNLRILGVVKS----------DEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20956    23 CVASGNPLPQITWTLDGFPIPESPRFRV--GDYVTSDGDVVSyvnissvrveDGGEYTCTATNDVGSVSHSARINV 96
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
277-709 3.96e-06

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 51.10  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  277 PSAPPQNV----SLEVVNS----RSIKVSWLPPPSGTqngfitGYKIRHRK--TTRRGEMETLEPNnlwYLFTGLEKGsQ 346
Cdd:COG4733   529 PQWPPVNVttseSLSVVAQgtavTTLTVSWDAPAGAV------AYEVEWRRddGNWVSVPRTSGTS---FEVPGIYAG-D 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  347 YSFQVSAmtVNGTGPPSNWYTAETPENDLDESqVPDQPSSLHVRPQTNCIIMSWTPPLNPNivVRGYIIGYGVGSPY--A 424
Cdd:COG4733   599 YEVRVRA--INALGVSSAWAASSETTVTGKTA-PPPAPTGLTATGGLGGITLSWSFPVDAD--TLRTEIRYSTTGDWasA 673

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  425 ETVRVDSKQRYYSIERLESSSHYVISLKAFNNAGEGVPLYESATT--------RSITDPTDPVDYYPLLDDF--PTSVPD 494
Cdd:COG4733   674 TVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVSAWWVSGQAsadaagilDAITGQILETELGQELDAIiqNATVAE 753

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  495 LSTPMLPPVGVQAVALTHDAVRVSWADNSVPKNQKTSEVRLYTVRWRTS-FSASAKYKSEDTTSLSYTATGLKPNTMYEF 573
Cdd:COG4733   754 VVAATVTDVTAQIDTAVLFAGVATAAAIGAEARVAATVAESATAAAATGtAADAAGDASGGVTAGTSGTTGAGDTAASTT 833

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  574 SVMVTKNRRSSTWSMTAHATTYEAAPTSAPKDLTVITREGKPRAVIVSWQPPLEANGKITAYILFYTLDKNIPIDDWIME 653
Cdd:COG4733   834 RVAAAVVLAGVVVYGDAIIESGNTGDIVATGDIASAAAGAVATTVSGTTAADVSAVADSTAASLTAIVIAATTIIDAIGD 913

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767998294  654 TISGDRlthQIMDLNLDTMYYFRIQARNSKGVGPLSDPILFRTLKVEHPDKMANDQ 709
Cdd:COG4733   914 GTTREP---AGDIGASGGAQGFAVTIVGSFDGAGAVATVDAGQSVVDGVGTAVEAA 966
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 2-72 3.99e-06

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: 46.17  E-value: 3.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998294    2 DIEFECTVSGKPVPTVNWMKNGDVvIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05851    18 NVTLECFALGNPVPVIRWRKILEP-MPATAEISMSGAVLKIFNIQPEDEGTYECEAENIKGKDKHQARVYV 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
 823-1071 5.64e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 5.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  823 PSGTDPAGRDSPIQSCQDLTPVSHSQSETQLGSKStshSGQDTEEAGSSMSTLERSLAARRAPRAKLMIPMDAQSNNPAV 902
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA---PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  903 VSAiPVPTLESAQYP-GILPSPTCGYPHPQFTLRPVPFPTLSVDRGFGAGrsQSVSEGPTTQQPPMLP--PSQPEHSS-S 978
Cdd:PHA03247 2811 VLA-PAAALPPAASPaGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG--GDVRRRPPSRSPAAKPaaPARPPVRRlA 2887

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  979 EEAPSRTIPTACVRPTHPLRSFANPLLPPPMSAIEPKVPYTPLLS-----QPGPTLPKTHVKTASLGLAGKARSPLLPVS 1053
Cdd:PHA03247 2888 RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPpppppRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967

                         250
                  ....*....|....*...
gi 767998294 1054 VPTAPEVSEESHKPTEDS 1071
Cdd:PHA03247 2968 VPGRVAVPRFRVPQPAPS 2985
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 2-62 5.89e-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: 45.77  E-value: 5.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    2 DIEFECTVSGKPVPTVNWMKN-GDvvIPSDYFQIVGGSNLRILG--------VVKSDEGFYQCVAENEAG 62
Cdd:cd20954    18 DVMLHCQADGFPTPTVTWKKAtGS--TPGEYKDLLYDPNVRILPngtlvfghVQKENEGHYLCEAKNGIG 85
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 4-72 6.15e-06

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: 45.69  E-value: 6.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    4 EFECTVSGKPVPTVNWMKNGDVVIPS------------DYFQIVggsNLRIlgvvkSDEGFYQCVAENEAGNAQTSAQLI 71
Cdd:cd05763    18 RLECAATGHPTPQIAWQKDGGTDFPAarerrmhvmpedDVFFIV---DVKI-----EDTGVYSCTAQNSAGSISANATLT 89


                  .
gi 767998294   72 V 72
Cdd:cd05763    90 V 90
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 2-72 6.27e-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: 45.64  E-value: 6.27e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998294    2 DIEFECTVSGKPVPTVNWMKNGDVvIPSDYFQIVGgSN--LRILGVVK-SDEGFYQCVAENEAGN-AQTSAQLIV 72
Cdd:cd20958    17 TLRLHCPVAGYPISSITWEKDGRR-LPLNHRQRVF-PNgtLVIENVQRsSDEGEYTCTARNQQGQsASRSVFVKV 89
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
 2-64 6.64e-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: 45.47  E-value: 6.64e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767998294    2 DIEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRIL------GVVKSDEGFYQCVAENEAGNA 64
Cdd:cd05733    18 NITIKCEAKGNPQPTFRWTKDGKFFDPAKDPRVSMRRRSGTLvidnhnGGPEDYQGEYQCYASNELGTA 86
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 6-72 1.11e-05

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: 45.09  E-value: 1.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998294    6 ECTVSGKPVPTVNWMKNGDVVIPSDYFQIV----GGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20990    21 DCKVSGLPTPDLSWQLDGKPIRPDSAHKMLvrenGVHSLIIEPVTSRDAGIYTCIATNRAGQNSFNLELVV 91
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 3-72 1.81e-05

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: 44.56  E-value: 1.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVI--------PSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05726    17 VTFQCETKGNPQPAIFWQKEGSQNLlfpyqppqPSSRFSVSPTGDLTITNVQRSDVGYYICQALNVAGSILAKAQLEV 94
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 3-62 1.86e-05

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


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 44.52  E-value: 1.86e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSN----LRILGVVKSDEGFYQCVAENEAG 62
Cdd:cd05729    22 VRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEkgwsLIIERAIPRDKGKYTCIVENEYG 85
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 1-72 3.55e-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: 3.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767998294    1 MDIEFECTVSGKPVPTVNWMKNGDVVIP-SDYFQIV----GGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05893    16 MPVTFTCRVAGNPKPKIYWFKDGKQISPkSDHYTIQrdldGTCSLHTTASTLDDDGNYTIMAANPQGRISCTGRLMV 92
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 3-62 3.58e-05

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: 43.78  E-value: 3.58e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998294    3 IEFECTVSGKPVPTVNWMKNG-DVVIPSDY-FQIVGGSNLRILGVVKSDEGFYQCVAENEAG 62
Cdd:cd05848    22 VILNCEARGNPVPTYRWLRNGtEIDTESDYrYSLIDGNLIISNPSEVKDSGRYQCLATNSIG 83
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 3-70 3.87e-05

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 43.34  E-value: 3.87e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998294     3 IEFECTVS-GKPVPTVNWMKNGDVVIPSDYFQI----VGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQL 70
Cdd:pfam00047   14 ATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHdngrTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLSTSL 86
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 3-62 6.85e-05

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


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 43.00  E-value: 6.85e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998294    3 IEFECTVSGKPVPTVNW-MKNGDVVIPSDY-FQIVGGsNLRILGVVKS-DEGFYQCVAENEAG 62
Cdd:cd04967    22 VALNCRARANPVPSYRWlMNGTEIDLESDYrYSLVDG-TLVISNPSKAkDAGHYQCLATNTVG 83
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 3-72 7.41e-05

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: 42.45  E-value: 7.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVIP-----SDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05892    18 VRLECQISAIPPPQIFWKKNNEMLQYntdriSLYQDNCGRICLLIQNANKKDAGWYTVSAVNEAGVVSCNARLDV 92
IgI_1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; ...
 3-67 1.00e-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: 42.25  E-value: 1.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767998294    3 IEFECTVSGKPVPTVNW-MKNGDVVIPSDYFQIVGGsNLRILGVVKS-DEGFYQCVAENEAGNAQTS 67
Cdd:cd05849    22 VSVNCRARANPFPIYKWrKNNLDIDLTNDRYSMVGG-NLVINNPDKYkDAGRYVCIVSNIYGKVRSR 87
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 3-72 1.02e-04

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: 42.38  E-value: 1.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVVIPS---DYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20969    20 VQFVCRADGDPPPAILWLSPRKHLVSAksnGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 502-594 1.59e-04

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: 41.63  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   502 PVGVQaVALTHDA--VRVSWADNSVPKNqktSEVRLYTVRWRTSFSASAK------YKSEDTTSLSYTATGLKPNTMYEF 573
Cdd:pfam16656    1 PEQVH-LSLTGDStsMTVSWVTPSAVTS---PVVQYGTSSSALTSTATATsstyttGDGGTGYIHRATLTGLEPGTTYYY 76

                           90       100
                   ....*....|....*....|.
gi 767998294   574 SVMVTknrrSSTWSMTAHATT 594
Cdd:pfam16656   77 RVGDD----NGGWSEVYSFTT 93
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 8-72 1.99e-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: 1.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    8 TVSGKPVPTVNWMKNGDVV--IPSDYFQIVGG---SNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05750    23 ATSENPSPRYRWFKDGKELnrKRPKNIKIRNKkknSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 7-62 2.58e-04

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: 41.05  E-value: 2.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    7 CTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGS----NLRILGVVKSDEGFYQCVAENEAG 62
Cdd:cd05891    23 CTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQgkyaSLTIKGVTSEDSGKYSINVKNKYG 82
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 7-72 2.87e-04

Sixth 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 sixth 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: 409551  Cd Length: 94  Bit Score: 40.94  E-value: 2.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998294    7 CTVSGKPVP-TVNWMKNGDVvIPSDY---FQIVG--GSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20959    24 CGVPGGDLPlNIRWTLDGQP-ISDDLgitVSRLGrrSSILSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
 3-72 2.92e-04

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: 40.92  E-value: 2.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998294    3 IEFECTVSGKPVPTVNWMKNGDVViPSDYFQIV-----GGSNLRILGV-VKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd20971    19 ATLVCKVTGHPKPIVKWYRQGKEI-IADGLKYRiqefkGGYHQLIIASvTDDDATVYQVRATNQGGSVSGTASLEV 93
Interfer-bind pfam09294
Interferon-alpha/beta receptor, fibronectin type III; Members of this family adopt a secondary ...
 280-371 4.95e-04

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


Pssm-ID: 462746  Cd Length: 103  Bit Score: 40.40  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   280 PPQnVSLEVVNsRSIKVSWLPPPSGTQNGFIT-------GYKIRHRKTTRRGEMETLEPNNLWYLFTGLEKGSQYSFQVS 352
Cdd:pfam09294    5 PPE-VELEVEG-GSLNVTVKDPETREGKNLSLrdlygslQYRVSYWKNSSNGEKKNTTSTNSFVVLSDLEPGTTYCVSVQ 82

                           90       100
                   ....*....|....*....|.
gi 767998294   353 A--MTVNGTGPPSNWYTAETP 371
Cdd:pfam09294   83 AfsPLDNKSSQRSPPQCIRTT 103
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
480-684 6.05e-04

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.17  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  480 DYYPLLDdfpTSVPDLSTPMLPPVGVQAVALTHDavrvswadnsvpKNQKTSEVRLyTVRWRTS---FSASAKYKSED-- 554
Cdd:COG4733   514 EKYAAID---AGAFDDVPPQWPPVNVTTSESLSV------------VAQGTAVTTL-TVSWDAPagaVAYEVEWRRDDgn 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  555 ------TTSLSYTATGLKPNTmYEFSVM-VTKNRRSSTWSMTAHAT-TYEAAPTSAPKDLTVitrEGKPRAVIVSWQPPL 626
Cdd:COG4733   578 wvsvprTSGTSFEVPGIYAGD-YEVRVRaINALGVSSAWAASSETTvTGKTAPPPAPTGLTA---TGGLGGITLSWSFPV 653

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998294  627 EANgkITAYILFYTLDknipiDDW---IMETISGDRLTHQIMDLNLDTMYYFRIQARNSKG 684
Cdd:COG4733   654 DAD--TLRTEIRYSTT-----GDWasaTVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 797-1020 7.27e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.91  E-value: 7.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  797 KGSQKDLRPPDlwihhEEMEMKNIEKPSGTDPAGrdspiqscqdLTPVSHSQSETQLGSKSTSHSGQDTEEAGSSMSTLE 876
Cdd:PTZ00449  490 KKSKKKLAPIE-----EEDSDKHDEPPEGPEASG----------LPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKE 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  877 RSLAARRAPraklmipmdAQSNNPavvSAIPVPTlESAQYPGILPSPTcGYPHPQFTLRPVpfptlsvdrgfgagrsqsV 956
Cdd:PTZ00449  555 GEVGKKPGP---------AKEHKP---SKIPTLS-KKPEFPKDPKHPK-DPEEPKKPKRPR------------------S 602

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767998294  957 SEGPTTQQPPMLP-----PSQPEHSSSEEAPSRTIPTAcvRPTHPLRSFANPLLPPPMSAIEPKVPYTP 1020
Cdd:PTZ00449  603 AQRPTRPKSPKLPelldiPKSPKRPESPKSPKRPPPPQ--RPSSPERPEGPKIIKSPKPPKSPKPPFDP 669
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
153-374 1.26e-03

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 43.01  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  153 YTFRVVAYNE--WGPGESS--QPIKVATQPELQVPGPVENLQAVSTSPTSILITWEPPAYANG-PVQGYRlfctevSTGK 227
Cdd:COG4733   504 YTITAVQHAPekYAAIDAGafDDVPPQWPPVNVTTSESLSVVAQGTAVTTLTVSWDAPAGAVAyEVEWRR------DDGN 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  228 EQNI-EVDGLSYKLEGLKKfTEYSLRFLAYNRYG---PGVSTDDITVVTLSDVPSAPpqnVSLEVVNS-RSIKVSWLPPP 302
Cdd:COG4733   578 WVSVpRTSGTSFEVPGIYA-GDYEVRVRAINALGvssAWAASSETTVTGKTAPPPAP---TGLTATGGlGGITLSWSFPV 653

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998294  303 sgtqNGFITGYKIRHRKTTRRGEME---TLEPNNLWYLfTGLEKGSQYSFQVSAmtVNGTGPPSNWYTAETPEND 374
Cdd:COG4733   654 ----DADTLRTEIRYSTTGDWASATvaqALYPGNTYTL-AGLKAGQTYYYRARA--VDRSGNVSAWWVSGQASAD 721
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 820-1079 1.29e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   820 IEKPSGTDPAGRDSPIQSCQ------DLTPVSHSQSETQLGSKSTSHSGQDTEE-----AGSSM-----------STLER 877
Cdd:pfam03154  289 MQHPVPPQPFPLTPQSSQSQvppgpsPAAPGQSQQRIHTPPSQSQLQSQQPPREqplppAPLSMphikpppttpiPQLPN 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   878 SLAARRAPRAKLMIPMDAQSNNPAVVSAIPVPTLESAQYPGILPSPTCGYPHPQ-FTLRPVPFPTLSVDRGFGAGRSQSV 956
Cdd:pfam03154  369 PQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQqLPPPPAQPPVLTQSQSLPPPAASHP 448

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   957 SEGPTTQQPPMLPpsQPEHSSSEEAPSRTIPTACVRPThplRSFANPLLPPPMSAiePKVPYTPLLSQPGPTLPKTHVKT 1036
Cdd:pfam03154  449 PTSGLHQVPSQSP--FPQHPFVPGGPPPITPPSGPPTS---TSSAMPGIQPPSSA--SVSSSGPVPAAVSCPLPPVQIKE 521

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 767998294  1037 ASLGLAGKARSPLLPVSVPTAPEVSEESHKPTEDSANVYEQDD 1079
Cdd:pfam03154  522 EALDEAEEPESPPPPPRSPSPEPTVVNTPSHASQSARFYKHLD 564
IgI_NrCAM cd05874
Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); ...
 2-67 1.44e-03

Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule). NrCAM 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. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 409458  Cd Length: 95  Bit Score: 39.20  E-value: 1.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998294    2 DIEFECTVSGKPVPTVNWMKNGDVV-IPSDYFQIV----GGSNLRILGVVKSD--EGFYQCVAENEAGNAQTS 67
Cdd:cd05874    18 NIVIQCEAKGKPPPSFSWTRNGTHFdIDKDPKVTMkpntGTLVINIMNGEKAEayEGVYQCTARNERGAAVSN 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 823-1069 1.73e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  823 PSGTDPAGRDSPIQScqdltPVSHSQSETQLGSKSTSHSGQDTEE-AGSSMSTLERSLAARRAPRAKlmIPMDAQSNNPA 901
Cdd:PHA03247 2616 PLPPDTHAPDPPPPS-----PSPAANEPDPHPPPTVPPPERPRDDpAPGRVSRPRRARRLGRAAQAS--SPPQRPRRRAA 2688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  902 VVSAIPVPTLESAQYPGILPSPTcgyPHPQFTLRPVPFPTLSVDRGFGAgrsqsvseGPTTQQPPMLPPSQPEHSSSEEA 981
Cdd:PHA03247 2689 RPTVGSLTSLADPPPPPPTPEPA---PHALVSATPLPPGPAAARQASPA--------LPAAPAPPAVPAGPATPGGPARP 2757

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  982 PSRTIPTACVRPTHPLRSFANP---LLPPPMSAIEPKVPYTPLLSQPGPTLPKTHVKTASLGLAGKARSPLLP--VSVPT 1056
Cdd:PHA03247 2758 ARPPTTAGPPAPAPPAAPAAGPprrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPptSAQPT 2837

                         250
                  ....*....|...
gi 767998294 1057 APEVSEESHKPTE 1069
Cdd:PHA03247 2838 APPPPPGPPPPSL 2850
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 281-370 1.82e-03

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: 38.54  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   281 PQNVSLEVVN-SRSIKVSWLPPPSGTQNGFITGYKIRHRKTTRRGEMETLEPNNLW------YLFTGLEKGSQYSFQVSA 353
Cdd:pfam16656    1 PEQVHLSLTGdSTSMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTYTTGDGGtgyihrATLTGLEPGTTYYYRVGD 80

                           90
                   ....*....|....*..
gi 767998294   354 mtvnGTGPPSNWYTAET 370
Cdd:pfam16656   81 ----DNGGWSEVYSFTT 93
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The ...
 7-62 1.87e-03

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The members here are composed of the fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM 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. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 409454  Cd Length: 89  Bit Score: 38.42  E-value: 1.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767998294    7 CTVSGKPVPTVNWMKNG--DVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAG 62
Cdd:cd05868    21 CRANGNPKPSISWLTNGvpIEIAPTDPSRKVDGDTIIFSKVQERSSAVYQCNASNEYG 78
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 7-72 2.01e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 38.14  E-value: 2.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767998294     7 CTVSGKPVPTVNWMKNGDVVIPSdyfqivggSNLRILGVVKSDEGFYQCVAENEAGNAQT-SAQLIV 72
Cdd:pfam13895   21 CSAPGNPPPSYTWYKDGSAISSS--------PNFFTLSVSAEDSGTYTCVARNGRGGKVSnPVELTV 79
PHA03247 PHA03247
large tegument protein UL36; Provisional
 823-1083 2.28e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  823 PSGTDPAGRDSPIQSCQDLTPVSHSQSETQLGSKSTSHSGQDTEEAGSSMSTLERslAARRAPRAKLMIPMDAQSNNPAV 902
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQR--PRRRAARPTVGSLTSLADPPPPP 2705

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  903 VSAIPVPTLESAQYPGILPSPTCGYPHPQFTLRPVPFPTLS---VDRGFGAGRSQSVSEGPTTQQPPMLPPSQPEHS--- 976
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAgpaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRltr 2785

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  977 --------SSEEAPS------RTIPTACVRPTHPLRSFANPLLPPPMSAIEPKVPYTPLLSQPGPTLPKTHVKTASLGLA 1042
Cdd:PHA03247 2786 pavaslseSRESLPSpwdpadPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRR 2865

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767998294 1043 GKARSPLLPVSVPTAPEVSEESHKPTEDSANVYEQDDLSEQ 1083
Cdd:PHA03247 2866 PPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPE 2906
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
 3-72 2.44e-03

Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the 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: 409398  Cd Length: 101  Bit Score: 38.62  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    3 IEFECTVSG-KPVpTVNWMKNGDVVIPSDYFQIVGG---------SNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05735    21 KEMSCTAHGeKPI-IVRWEKEDTIINPSEMSRYLVTtkevgdeviSTLQILPTVREDSGFFSCHAINSYGEDRGIIQLTV 99
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 7-62 2.91e-03

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 37.96  E-value: 2.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    7 CTVSGKPVPTVNWMKNGDVVIPSDYF--QIVGGS--NLRILGVVKSDEGFYQCVAENEAG 62
Cdd:cd05737    23 CNVWGDPPPEVSWLKNDQALAFLDHCnlKVEAGRtvYFTINGVSSEDSGKYGLVVKNKYG 82
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 7-72 4.08e-03

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: 37.68  E-value: 4.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294    7 CTVSGKPVPTVNWMKNG---DVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTS-AQLIV 72
Cdd:cd05738    21 CAASGNPDPEISWFKDFlpvDTATSNGRIKQLRSGALQIENSEESDQGKYECVATNSAGTRYSApANLYV 90
PHA03379 PHA03379
EBNA-3A; Provisional
 818-1074 4.32e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.20  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  818 KNIEKPSGTDPAGRDSPIQSCQDLTPVSHSQSetqlgsksTSHSGQDTEEAGSSMSTLERSLAARRApraklMIPMDAQS 897
Cdd:PHA03379  403 EALEKASEPTYGTPRPPVEKPRPEVPQSLETA--------TSHGSAQVPEPPPVHDLEPGPLHDQHS-----MAPCPVAQ 469

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  898 NNPAvvsaiPVPTLESA-QYPGILPSPTCGyphpqftLRPVPFPTLSVDRGFGAGRSQSVSEGPTTQQP-PMLPPSQPEH 975
Cdd:PHA03379  470 LPPG-----PLQDLEPGdQLPGVVQDGRPA-------CAPVPAPAGPIVRPWEASLSQVPGVAFAPVMPqPMPVEPVPVP 537

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294  976 SSSEEAPSRTIPT--ACVRPTHP--LRSFANPLLPPPMSAIEPKVPY-TPLLSQPGPTLPKTHVKTASLGLAG---KARS 1047
Cdd:PHA03379  538 TVALERPVCPAPPliAMQGPGETsgIVRVRERWRPAPWTPNPPRSPSqMSVRDRLARLRAEAQPYQASVEVQPpqlTQVS 617

                         250       260
                  ....*....|....*....|....*..
gi 767998294 1048 PLLPVSVPTAPEVSEESHKPTEDSANV 1074
Cdd:PHA03379  618 PQQPMEYPLEPEQQMFPGSPFSQVADV 644
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 820-1027 4.85e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   820 IEKPSGTDPAGRDSPIQSCQ--DLTPVSHSQSETQLGSKSTSHSGQDTEEAGSSMSTLER--SLAARRAPRAKLMIPMDA 895
Cdd:pfam03154  174 LQAQSGAASPPSPPPPGTTQaaTAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQtpTLHPQRLPSPHPPLQPMT 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998294   896 QSNNPAVVSAIPVPT-LESAQYPGILPSPTCGYPHPQFTLRPVPFPTLSVDRGFGAGRSQSVSEGPTTQQPPMLPPSQPE 974
Cdd:pfam03154  254 QPPPPSQVSPQPLPQpSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQ 333

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767998294   975 HSSSEEAPSRTIPTACVRPTH--PLRSFANPLLPPPMSAIEPkvpytPLLSQPGP 1027
Cdd:pfam03154  334 LQSQQPPREQPLPPAPLSMPHikPPPTTPIPQLPNPQSHKHP-----PHLSGPSP 383
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
 7-72 9.69e-03

Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F (also known as LAR), type IIa; member of the I-set of IgSF domains; The members here are composed of the third 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. Included in this group is Drosophila LAR (DLAR).


Pssm-ID: 409401  Cd Length: 82  Bit Score: 36.42  E-value: 9.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998294    7 CTVSGKPVPTVNWMKNGDVVIPSDYFQiVGGSNLRILGVVKSDEgfYQCVAENEAGNAQTSAQLIV 72
Cdd:cd05739    19 CVAVGAPMPYVKWMKGGEELTKEDEMP-VGRNVLELTNIYESAN--YTCVAISSLGMIEATAQVTV 81
 
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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