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Conserved domains on  [gi|1034633593|ref|XP_016861998|]
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contactin-3 isoform X3 [Homo sapiens]

Protein Classification

Ig and FN3 domain-containing protein( domain architecture ID 10307510)

Ig and FN3 domain-containing protein similar to Homo sapiens contactins, which are comprised of six immunoglobulin (Ig)-like domains followed by four fibronectin type III (Fn3) domains anchored to the membrane by glycosylphosphatidylinositol, and to Robo (roundabout) receptors which typically contain five Ig-like domains and three FN3 domains

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 56-156 1.72e-51

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 cd05853:

Pssm-ID: 472250  Cd Length: 102  Bit Score: 172.12  E-value: 1.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  56 EPTRITLAPSNMDVSVGESVILPCQVQHDPLLDIIFTWYFNGALADFKKDGSHFEKVGGS-SSGDLMIRNIQLKHSGKYV 134
Cdd:cd05853     1 DPTRVMVPPSSMDVTVGESIVLPCQVSHDHSLDIVFTWSFNGHLIDFQKDGDHFERVGGQdSAGDLMIRSIQLKHAGKYV 80

                          90       100
                  ....*....|....*....|..
gi 1034633593 135 CMVQTGVDSVSSAADLIVRGSP 156
Cdd:cd05853    81 CMVQTSVDKLSAAADLIVRGPP 102
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 156-253 5.76e-19

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.77  E-value: 5.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 156 PGPPENVKVDEITDTTAQLSWKEGKDNHSPVISYSIQARTPFSVGWQTVTTVPevidGKTHTATVVELNPWVEYEFRVVA 235
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTP----GSETSYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*...
gi 1034633593 236 SNKIGGGEPSlPSEKVRT 253
Cdd:cd00063    77 VNGGGESPPS-ESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
137-564 2.80e-17

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 85.44  E-value: 2.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 137 VQTGVDSVSSAADLIVRGSPGPPENVKVDEITDTTAQLSWKEGKDNHSPVISYSIQARTPFSVGWQTVTTVPEVIDgKTH 216
Cdd:COG3401    11 AGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAA-APP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 217 TATVVELNPWVEYEFRVVASNKIGGGEPSLPSEKVRTEEAVPEVPPSEVNGGGGSRSELVITWDPVPEELQNGEGFGYVV 296
Cdd:COG3401    90 TATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 297 AFRPLGVTTWIQTVVTSPDTPRYVFRNESIVPYSPYEVKVGVYNNKGEGPFSPVTTVFSAEEEPTvAPSQVSANSLSSSE 376
Cdd:COG3401   170 VSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPS-APTGLTATADTPGS 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 377 IEVSWNTIPwklsNGHLLGYEVRYWNGGGKEESsskmKVA-GNETSARLRGLKSNLAYYTAVRAYNSAG-AGPFSATVNV 454
Cdd:COG3401   249 VTLSWDPVT----ESDATGYRVYRSNSGDGPFT----KVAtVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 455 TTKKTPPSQPPGNVVWNATDTKVLLNWEQVKamenESEVTGYKVFYRTSSQNNVQVLNTNKTSAELVLPIKED---YIIE 531
Cdd:COG3401   321 TTDLTPPAAPSGLTATAVGSSSITLSWTASS----DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPgttYYYK 396

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1034633593 532 VKATTDggDGTSSEQIRIPRITSMDARGSTSAI 564
Cdd:COG3401   397 VTAVDA--AGNESAPSEEVSATTASAASGESLT 427
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 13-54 3.67e-13

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 cd04969:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 89  Bit Score: 65.17  E-value: 3.67e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034633593  13 RISLLNDGGLKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd04969    48 RICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
 
Name Accession Description Interval E-value
Ig6_Contactin-4 cd05853
Sixth immunoglobulin (Ig) domain of contactin-4; The members here are composed of the sixth ...
 56-156 1.72e-51

Sixth immunoglobulin (Ig) domain of contactin-4; The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-4. 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 different contactins show different expression patterns in the central nervous system. Highest expression of contactin-4 is in testes, thyroid, small intestine, uterus, and brain. Contactin-4 plays a role in the response of neuroblastoma cells to differentiating agents, such as retinoids. The contactin 4 gene is associated with cerebellar degeneration in spinocerebellar ataxia type 16.


Pssm-ID: 409439  Cd Length: 102  Bit Score: 172.12  E-value: 1.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  56 EPTRITLAPSNMDVSVGESVILPCQVQHDPLLDIIFTWYFNGALADFKKDGSHFEKVGGS-SSGDLMIRNIQLKHSGKYV 134
Cdd:cd05853     1 DPTRVMVPPSSMDVTVGESIVLPCQVSHDHSLDIVFTWSFNGHLIDFQKDGDHFERVGGQdSAGDLMIRSIQLKHAGKYV 80

                          90       100
                  ....*....|....*....|..
gi 1034633593 135 CMVQTGVDSVSSAADLIVRGSP 156
Cdd:cd05853    81 CMVQTSVDKLSAAADLIVRGPP 102
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 156-253 5.76e-19

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.77  E-value: 5.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 156 PGPPENVKVDEITDTTAQLSWKEGKDNHSPVISYSIQARTPFSVGWQTVTTVPevidGKTHTATVVELNPWVEYEFRVVA 235
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTP----GSETSYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*...
gi 1034633593 236 SNKIGGGEPSlPSEKVRT 253
Cdd:cd00063    77 VNGGGESPPS-ESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
137-564 2.80e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 85.44  E-value: 2.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 137 VQTGVDSVSSAADLIVRGSPGPPENVKVDEITDTTAQLSWKEGKDNHSPVISYSIQARTPFSVGWQTVTTVPEVIDgKTH 216
Cdd:COG3401    11 AGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAA-APP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 217 TATVVELNPWVEYEFRVVASNKIGGGEPSLPSEKVRTEEAVPEVPPSEVNGGGGSRSELVITWDPVPEELQNGEGFGYVV 296
Cdd:COG3401    90 TATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 297 AFRPLGVTTWIQTVVTSPDTPRYVFRNESIVPYSPYEVKVGVYNNKGEGPFSPVTTVFSAEEEPTvAPSQVSANSLSSSE 376
Cdd:COG3401   170 VSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPS-APTGLTATADTPGS 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 377 IEVSWNTIPwklsNGHLLGYEVRYWNGGGKEESsskmKVA-GNETSARLRGLKSNLAYYTAVRAYNSAG-AGPFSATVNV 454
Cdd:COG3401   249 VTLSWDPVT----ESDATGYRVYRSNSGDGPFT----KVAtVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 455 TTKKTPPSQPPGNVVWNATDTKVLLNWEQVKamenESEVTGYKVFYRTSSQNNVQVLNTNKTSAELVLPIKED---YIIE 531
Cdd:COG3401   321 TTDLTPPAAPSGLTATAVGSSSITLSWTASS----DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPgttYYYK 396

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1034633593 532 VKATTDggDGTSSEQIRIPRITSMDARGSTSAI 564
Cdd:COG3401   397 VTAVDA--AGNESAPSEEVSATTASAASGESLT 427
fn3 pfam00041
Fibronectin type III domain;
157-245 8.24e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.83  E-value: 8.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 157 GPPENVKVDEITDTTAQLSWKEGKDNHSPVISYSIQARTPFSVGWQTVTTVPEVidgkTHTATVVELNPWVEYEFRVVAS 236
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGT----TTSVTLTGLKPGTEYEVRVQAV 76


                  ....*....
gi 1034633593 237 NKIGGGEPS 245
Cdd:pfam00041  77 NGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 156-242 2.62e-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: 65.33  E-value: 2.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  156 PGPPENVKVDEITDTTAQLSWKEGKDNH--SPVISYSIQARTPfSVGWQTVTTVPevidgKTHTATVVELNPWVEYEFRV 233
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREE-GSEWKEVNVTP-----SSTSYTLTGLKPGTEYEFRV 74


                   ....*....
gi 1034633593  234 VASNKIGGG 242
Cdd:smart00060  75 RAVNGAGEG 83
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 13-54 3.67e-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: 65.17  E-value: 3.67e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034633593  13 RISLLNDGGLKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd04969    48 RICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 363-456 1.29e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.97  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 363 APSQVSANSLSSSEIEVSWNtiPWKLSNGHLLGYEVRYWNGGGKEESSSKmKVAGNETSARLRGLKSNLAYYTAVRAYNS 442
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWT--PPEDDGGPITGYVVEYREKGSGDWKEVE-VTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 1034633593 443 AGAGPFSATVNVTT 456
Cdd:cd00063    80 GGESPPSESVTVTT 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 64-152 1.86e-11

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.21  E-value: 1.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593   64 PSNMDVSVGESVILPCQVQHDPllDIIFTWYFNGALADFKKDGSHFEKVGGSSSgdLMIRNIQLKHSGKYVCMVQTGVDS 143
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSP--PPEVTWYKQGGKLLAESGRFSVSRSGSTST--LTISNVTPEDSGTYTCAATNSSGS 76


                   ....*....
gi 1034633593  144 VSSAADLIV 152
Cdd:smart00410  77 ASSGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
363-449 4.09e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 4.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 363 APSQVSANSLSSSEIEVSWnTIPwKLSNGHLLGYEVRYWNGGGKEESSSKMkVAGNETSARLRGLKSNLAYYTAVRAYNS 442
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSW-TPP-PDGNGPITGYEVEYRPKNSGEPWNEIT-VPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                  ....*..
gi 1034633593 443 AGAGPFS 449
Cdd:pfam00041  79 GGEGPPS 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 59-137 9.87e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.96  E-value: 9.87e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633593  59 RITLAPSNMDVSVGESVILPCQVQHDPLLDIifTWYFNGALadfKKDGSHFEKVGGSSSGDLMIRNIQLKHSGKYVCMV 137
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPTI--TWYKNGEP---ISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 363-446 1.39e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.15  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  363 APSQVSANSLSSSEIEVSWNTIPWKLSNGHLLGYEVRYWNGGGKEEsssKMKVAGNETSARLRGLKSNLAYYTAVRAYNS 442
Cdd:smart00060   3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWK---EVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                   ....
gi 1034633593  443 AGAG 446
Cdd:smart00060  80 AGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 13-54 1.47e-07

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.04  E-value: 1.47e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034633593   13 RISLLNDGG---LKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:smart00410  41 RFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
8-54 7.64e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.56  E-value: 7.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633593   8 PTRRIRISllNDGG---LKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:pfam07679  43 SSDRFKVT--YEGGtytLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 10-97 2.71e-03

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 40.38  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  10 RRIRISLLND---GGLKIANVTKADAGTYTCMAENQFG-KANGTTHLVVTEpTRITLAPSNMD------VSVGESVILPC 79
Cdd:PHA02785  164 RRLRNKRLKQrtpGIITIEDVRKNDAGYYTCVLKYIYGdKTYNVTRIVKLE-VRDRIIPPTMQlpegvvTSIGSNLTIAC 242

                          90
                  ....*....|....*....
gi 1034633593  80 QVQ-HDPLLDIIFTWYFNG 97
Cdd:PHA02785  243 RVSlRPPTTDADVFWISNG 261
 
Name Accession Description Interval E-value
Ig6_Contactin-4 cd05853
Sixth immunoglobulin (Ig) domain of contactin-4; The members here are composed of the sixth ...
 56-156 1.72e-51

Sixth immunoglobulin (Ig) domain of contactin-4; The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-4. 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 different contactins show different expression patterns in the central nervous system. Highest expression of contactin-4 is in testes, thyroid, small intestine, uterus, and brain. Contactin-4 plays a role in the response of neuroblastoma cells to differentiating agents, such as retinoids. The contactin 4 gene is associated with cerebellar degeneration in spinocerebellar ataxia type 16.


Pssm-ID: 409439  Cd Length: 102  Bit Score: 172.12  E-value: 1.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  56 EPTRITLAPSNMDVSVGESVILPCQVQHDPLLDIIFTWYFNGALADFKKDGSHFEKVGGS-SSGDLMIRNIQLKHSGKYV 134
Cdd:cd05853     1 DPTRVMVPPSSMDVTVGESIVLPCQVSHDHSLDIVFTWSFNGHLIDFQKDGDHFERVGGQdSAGDLMIRSIQLKHAGKYV 80

                          90       100
                  ....*....|....*....|..
gi 1034633593 135 CMVQTGVDSVSSAADLIVRGSP 156
Cdd:cd05853    81 CMVQTSVDKLSAAADLIVRGPP 102
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 56-156 9.04e-46

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


Pssm-ID: 409359  Cd Length: 102  Bit Score: 156.56  E-value: 9.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  56 EPTRITLAPSNMDVSVGESVILPCQVQHDPLLDIIFTWYFNGALADFKKDGSHFEKVGG-SSSGDLMIRNIQLKHSGKYV 134
Cdd:cd04970     1 DATRITLAPSNADITVGENATLQCHASHDPTLDLTFTWSFNGVPIDLEKIEGHYRRRYGkDSNGDLEIVNAQLKHAGRYT 80

                          90       100
                  ....*....|....*....|..
gi 1034633593 135 CMVQTGVDSVSSAADLIVRGSP 156
Cdd:cd04970    81 CTAQTVVDSDSASATLVVRGPP 102
Ig6_Contactin-2 cd05854
Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth ...
 56-156 8.09e-34

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


Pssm-ID: 409440  Cd Length: 102  Bit Score: 124.00  E-value: 8.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  56 EPTRITLAPSNMDVSVGESVILPCQVQHDPLLDIIFTWYFNGALADFKKDGSHFEKVGGSSS-GDLMIRNIQLKHSGKYV 134
Cdd:cd05854     1 DATKITLAPSSADINQGENLTLQCHASHDPTMDLTFTWSLDDFPIDLDKPNGHYRRMEVKETiGDLVIVNAQLSHAGTYT 80

                          90       100
                  ....*....|....*....|..
gi 1034633593 135 CMVQTGVDSVSSAADLIVRGSP 156
Cdd:cd05854    81 CTAQTVVDSASASATLVVRGPP 102
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 156-253 5.76e-19

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 81.77  E-value: 5.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 156 PGPPENVKVDEITDTTAQLSWKEGKDNHSPVISYSIQARTPFSVGWQTVTTVPevidGKTHTATVVELNPWVEYEFRVVA 235
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTP----GSETSYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*...
gi 1034633593 236 SNKIGGGEPSlPSEKVRT 253
Cdd:cd00063    77 VNGGGESPPS-ESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
137-564 2.80e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 85.44  E-value: 2.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 137 VQTGVDSVSSAADLIVRGSPGPPENVKVDEITDTTAQLSWKEGKDNHSPVISYSIQARTPFSVGWQTVTTVPEVIDgKTH 216
Cdd:COG3401    11 AGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAA-APP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 217 TATVVELNPWVEYEFRVVASNKIGGGEPSLPSEKVRTEEAVPEVPPSEVNGGGGSRSELVITWDPVPEELQNGEGFGYVV 296
Cdd:COG3401    90 TATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 297 AFRPLGVTTWIQTVVTSPDTPRYVFRNESIVPYSPYEVKVGVYNNKGEGPFSPVTTVFSAEEEPTvAPSQVSANSLSSSE 376
Cdd:COG3401   170 VSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPS-APTGLTATADTPGS 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 377 IEVSWNTIPwklsNGHLLGYEVRYWNGGGKEESsskmKVA-GNETSARLRGLKSNLAYYTAVRAYNSAG-AGPFSATVNV 454
Cdd:COG3401   249 VTLSWDPVT----ESDATGYRVYRSNSGDGPFT----KVAtVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 455 TTKKTPPSQPPGNVVWNATDTKVLLNWEQVKamenESEVTGYKVFYRTSSQNNVQVLNTNKTSAELVLPIKED---YIIE 531
Cdd:COG3401   321 TTDLTPPAAPSGLTATAVGSSSITLSWTASS----DADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPgttYYYK 396

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1034633593 532 VKATTDggDGTSSEQIRIPRITSMDARGSTSAI 564
Cdd:COG3401   397 VTAVDA--AGNESAPSEEVSATTASAASGESLT 427
fn3 pfam00041
Fibronectin type III domain;
157-245 8.24e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.83  E-value: 8.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 157 GPPENVKVDEITDTTAQLSWKEGKDNHSPVISYSIQARTPFSVGWQTVTTVPEVidgkTHTATVVELNPWVEYEFRVVAS 236
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGT----TTSVTLTGLKPGTEYEVRVQAV 76


                  ....*....
gi 1034633593 237 NKIGGGEPS 245
Cdd:pfam00041  77 NGGGEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
186-537 1.32e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 73.50  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 186 VISYSIQARTPFSVGWQTVTTVPEVIDGKTHTATVVELNPWVEYEFRVVASNKIGGGEPSlPSEKVRTEEAVPEvPPSEV 265
Cdd:COG3401   162 SVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPS-NEVSVTTPTTPPS-APTGL 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 266 NGGGGSRSELVITWDPVPEElqngEGFGYVVAFRPLGVTTWiqTVVTSPDTPRYVFRNesIVPYSPYEVKVGVYNNKG-E 344
Cdd:COG3401   240 TATADTPGSVTLSWDPVTES----DATGYRVYRSNSGDGPF--TKVATVTTTSYTDTG--LTNGTTYYYRVTAVDAAGnE 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 345 GPFSPVTTVFSAEEEPTvAPSQVSANSLSSSEIEVSWNtipwKLSNGHLLGYEVRYWNGGGKeeSSSKMKVAGNETSARL 424
Cdd:COG3401   312 SAPSNVVSVTTDLTPPA-APSGLTATAVGSSSITLSWT----ASSDADVTGYNVYRSTSGGG--TYTKIAETVTTTSYTD 384

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 425 RGLKSNLAYYTAVRAYNSAG-AGPFSATVNVTTKKTPPSQPPGNVVWNAT---------DTKVLLNWEQVKAMENESEVT 494
Cdd:COG3401   385 TGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTASAASGESLTASVDAVPltdvagataAASAASNPGVSAAVLADGGDT 464

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1034633593 495 GYKVFYRTSSQNNVQVLNTNKTSAELVLPIKEDYIIEVKATTD 537
Cdd:COG3401   465 GNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTN 507
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 156-242 2.62e-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: 65.33  E-value: 2.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  156 PGPPENVKVDEITDTTAQLSWKEGKDNH--SPVISYSIQARTPfSVGWQTVTTVPevidgKTHTATVVELNPWVEYEFRV 233
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREE-GSEWKEVNVTP-----SSTSYTLTGLKPGTEYEFRV 74


                   ....*....
gi 1034633593  234 VASNKIGGG 242
Cdd:smart00060  75 RAVNGAGEG 83
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 13-54 3.67e-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: 65.17  E-value: 3.67e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034633593  13 RISLLNDGGLKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd04969    48 RICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 363-456 1.29e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.97  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 363 APSQVSANSLSSSEIEVSWNtiPWKLSNGHLLGYEVRYWNGGGKEESSSKmKVAGNETSARLRGLKSNLAYYTAVRAYNS 442
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWT--PPEDDGGPITGYVVEYREKGSGDWKEVE-VTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 1034633593 443 AGAGPFSATVNVTT 456
Cdd:cd00063    80 GGESPPSESVTVTT 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 64-152 1.86e-11

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 60.21  E-value: 1.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593   64 PSNMDVSVGESVILPCQVQHDPllDIIFTWYFNGALADFKKDGSHFEKVGGSSSgdLMIRNIQLKHSGKYVCMVQTGVDS 143
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSP--PPEVTWYKQGGKLLAESGRFSVSRSGSTST--LTISNVTPEDSGTYTCAATNSSGS 76


                   ....*....
gi 1034633593  144 VSSAADLIV 152
Cdd:smart00410  77 ASSGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
363-449 4.09e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.35  E-value: 4.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 363 APSQVSANSLSSSEIEVSWnTIPwKLSNGHLLGYEVRYWNGGGKEESSSKMkVAGNETSARLRGLKSNLAYYTAVRAYNS 442
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSW-TPP-PDGNGPITGYEVEYRPKNSGEPWNEIT-VPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                  ....*..
gi 1034633593 443 AGAGPFS 449
Cdd:pfam00041  79 GGEGPPS 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 59-137 9.87e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.96  E-value: 9.87e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633593  59 RITLAPSNMDVSVGESVILPCQVQHDPLLDIifTWYFNGALadfKKDGSHFEKVGGSSSGDLMIRNIQLKHSGKYVCMV 137
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPTI--TWYKNGEP---ISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
I-set pfam07679
Immunoglobulin I-set domain;
59-152 1.51e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 57.65  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  59 RITLAPSNMDVSVGESVILPCQVQHDPLLDIifTWYFNGalADFKKDGSH-FEKVGGSSSgdLMIRNIQLKHSGKYVCMV 137
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEV--SWFKDG--QPLRSSDRFkVTYEGGTYT--LTISNVQPDDSGKYTCVA 75

                          90
                  ....*....|....*
gi 1034633593 138 QTGVDSVSSAADLIV 152
Cdd:pfam07679  76 TNSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 261-353 2.06e-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: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 261 PPSEVNGGGGSRSELVITWDPVPEElqNGEGFGYVVAFRPLGVTTWIQTVVTSPDTPRYVFRNesIVPYSPYEVKVGVYN 340
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTG--LKPGTEYEFRVRAVN 78

                          90
                  ....*....|...
gi 1034633593 341 NKGEGPFSPVTTV 353
Cdd:cd00063    79 GGGESPPSESVTV 91
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 13-54 6.41e-10

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


Pssm-ID: 409438  Cd Length: 89  Bit Score: 56.16  E-value: 6.41e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034633593  13 RISLLNDGGLKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd05852    48 RISIWDDGSLEILNITKLDEGSYTCFAENNRGKANSTGVLSV 89
fn3 pfam00041
Fibronectin type III domain;
261-348 2.35e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 51.65  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 261 PPSEVNGGGGSRSELVITWDPVPEelQNGEGFGYVVAFRPLGVTTWIQTVVTSPDTPRYVFRNesIVPYSPYEVKVGVYN 340
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTG--LKPGTEYEVRVQAVN 77


                  ....*...
gi 1034633593 341 NKGEGPFS 348
Cdd:pfam00041  78 GGGEGPPS 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 75-147 3.13e-08

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: 50.79  E-value: 3.13e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034633593  75 VILPCQVQHDPLLDIifTWYFNGALADFKKDGSHFEKVGGSSsgdLMIRNIQLKHSGKYVCMVQTGVDSVSSA 147
Cdd:cd00096     1 VTLTCSASGNPPPTI--TWYKNGKPLPPSSRDSRRSELGNGT---LTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 8-54 5.20e-08

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: 50.47  E-value: 5.20e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1034633593   8 PTRRIRIslLNDGGLKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd05725    39 PKGRYEI--LDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 363-446 1.39e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.15  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  363 APSQVSANSLSSSEIEVSWNTIPWKLSNGHLLGYEVRYWNGGGKEEsssKMKVAGNETSARLRGLKSNLAYYTAVRAYNS 442
Cdd:smart00060   3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWK---EVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                   ....
gi 1034633593  443 AGAG 446
Cdd:smart00060  80 AGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 13-54 1.47e-07

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.04  E-value: 1.47e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034633593   13 RISLLNDGG---LKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:smart00410  41 RFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 13-46 4.12e-06

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


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 45.31  E-value: 4.12e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034633593  13 RISLLNDGGLKIANVTKADAGTYTCMAENQFGKA 46
Cdd:cd20968    45 RIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGIA 78
I-set pfam07679
Immunoglobulin I-set domain;
8-54 7.64e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.56  E-value: 7.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633593   8 PTRRIRISllNDGG---LKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:pfam07679  43 SSDRFKVT--YEGGtytLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 464-549 8.05e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 44.41  E-value: 8.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 464 PPGNV-VWNATDTKVLLNWEQVKamENESEVTGYKVFYRTSSQNNVQVLNT---NKTSAELV-LPIKEDYIIEVKATTDG 538
Cdd:cd00063     3 PPTNLrVTDVTSTSVTLSWTPPE--DDGGPITGYVVEYREKGSGDWKEVEVtpgSETSYTLTgLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|.
gi 1034633593 539 GDGTSSEQIRI 549
Cdd:cd00063    81 GESPPSESVTV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 5-44 9.28e-06

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.86  E-value: 9.28e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034633593   5 LQGPTRRIRISLLNDGGLKIANVTKADAGTYTCMAENQFG 44
Cdd:cd00096    24 LPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 461-541 1.06e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 43.76  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  461 PSQPPGNVVWNATDTKVLLNWEQVKAMENESEVTGYKVFYRTSSQNNVQVLNTNKTSAELVLPIKED--YIIEVKATTDG 538
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGteYEFRVRAVNGA 80


                   ...
gi 1034633593  539 GDG 541
Cdd:smart00060  81 GEG 83
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 62-146 1.11e-05

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 44.11  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  62 LAPSNMDVSVGESVILPCQVqHDPLLDIIFTWYFNGalaDFKKDGS-HFEKVGGSSSGDLMIRNIQLKHSGKYVCMVQTG 140
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSA-STGSPGPDVTWSKEG---GTLIESLkVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNP 76


                  ....*.
gi 1034633593 141 VDSVSS 146
Cdd:pfam00047  77 GGSATL 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 261-345 1.11e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 43.76  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  261 PPSEVNGGGGSRSELVITWDPVPEELQNGEGFGYVVAFRPLGvTTWiQTVVTSPDTPRYVFRNesIVPYSPYEVKVGVYN 340
Cdd:smart00060   3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEG-SEW-KEVNVTPSSTSYTLTG--LKPGTEYEFRVRAVN 78


                   ....*
gi 1034633593  341 NKGEG 345
Cdd:smart00060  79 GAGEG 83
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 3-54 1.18e-05

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 43.94  E-value: 1.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034633593   3 YNLQGPTRRIRISLLNDG-GLKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd05731    30 IKLGGELPKGRTKFENFNkTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
 62-135 1.27e-05

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


Pssm-ID: 409368  Cd Length: 88  Bit Score: 43.99  E-value: 1.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034633593  62 LAPSNMDVSVGESVILPCQV--QHDPLldiifTWYFNGAladfKKDGSHFEKVGGSSSGDLMIRNIQLKHSGKYVC 135
Cdd:cd04979     1 TSFKQISVKEGDTVILSCSVksNNAPV-----TWIHNGK----KVPRYRSPRLVLKTERGLLIRSAQEADAGVYEC 67
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 57-150 1.55e-05

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: 43.67  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  57 PTRITLAPSNMDVSVGESVILPCQVQHDPLLDIifTWYFNGaladfkKDGSHFEKVGGSSSGDLMIRNIQLKHSGKYVCM 136
Cdd:cd20957     1 PLSATIDPPVQTVDFGRTAVFNCSVTGNPIHTV--LWMKDG------KPLGHSSRVQILSEDVLVIPSVKREDKGMYQCF 72

                          90
                  ....*....|....
gi 1034633593 137 VQTGVDSVSSAADL 150
Cdd:cd20957    73 VRNDGDSAQATAEL 86
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 53-152 1.93e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 43.27  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  53 VVTEPTRitlaPSNMDVSVGESVILPCQVQHDPLLDIifTWYFNGALadfKKDGSHFEKVGGSSSgDLMIRNIQLKHSGK 132
Cdd:cd20970     2 VISTPQP----SFTVTAREGENATFMCRAEGSPEPEI--SWTRNGNL---IIEFNTRYIVRENGT-TLTIRNIRRSDMGI 71

                          90       100
                  ....*....|....*....|.
gi 1034633593 133 YVCMVQTGVD-SVSSAADLIV 152
Cdd:cd20970    72 YLCIASNGVPgSVEKRITLQV 92
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
 57-159 3.37e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.02  E-value: 3.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  57 PTRITLAPSNMDVSVGESVILPCQVQHDplLDIIFTWYfngalaDFKK---DGSHFEKVGGSSSGDLMIRNIQLKHSGKY 133
Cdd:cd05762     1 PPQIIQFPEDMKVRAGESVELFCKVTGT--QPITCTWM------KFRKqiqEGEGIKIENTENSSKLTITEGQQEHCGCY 72

                          90       100
                  ....*....|....*....|....*.
gi 1034633593 134 VCMVQTGVDSVSSAADLIVRGSPGPP 159
Cdd:cd05762    73 TLEVENKLGSRQAQVNLTVVDKPDPP 98
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 8-54 5.12e-05

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 42.10  E-value: 5.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1034633593   8 PTRRIRISLLNDGGLKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd20952    41 LGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
141-568 5.93e-05

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 46.09  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 141 VDSVSSAADLIVRGSPGPPENVKVDEITDTTAQLSWKEGkdnhSPVISYSIQARTPFSVGWQT--VTTVPEVIDGkTHTA 218
Cdd:COG4733   432 VTMEAGDRYLRVRLPDGTSVARTVQSVAGRTLTVSTAYS----ETPEAGAVWAFGPDELETQLfrVVSIEENEDG-TYTI 506

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 219 TVVELNPwvEYEFRVVAsnkiGGGEPSLPsekvrtEEAVPEVPPSE---VNGGGGSRSELVITWDPVPEElqngegFGYV 295
Cdd:COG4733   507 TAVQHAP--EKYAAIDA----GAFDDVPP------QWPPVNVTTSEslsVVAQGTAVTTLTVSWDAPAGA------VAYE 568

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 296 VAFRPlGVTTWIQTVVTSpdTPRYVFRNesiVPYSPYEVKVGVYNNKGE--GPFSPVTTVFSAEEEPTVAPSQVSANSLS 373
Cdd:COG4733   569 VEWRR-DDGNWVSVPRTS--GTSFEVPG---IYAGDYEVRVRAINALGVssAWAASSETTVTGKTAPPPAPTGLTATGGL 642

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 374 SSeIEVSWNTIPwklsNGHLLGYEVRYWNGGGKEeSSSKMKVAGNETSARLRGLKSNLAYYTAVRAYNSAG-AGPFSATV 452
Cdd:COG4733   643 GG-ITLSWSFPV----DADTLRTEIRYSTTGDWA-SATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGnVSAWWVSG 716

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 453 NVTTKKTPPSQPPGNVVWNATDTKVLLNWEQVKAMENESEVTGYKVFYRTSSQNNVQVLNTNKTSAElvlPIKEDYIIEV 532
Cdd:COG4733   717 QASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIGA---EARVAATVAE 793

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1034633593 533 KATTDGGDGTSSEQIRIPRITSMDARGSTSAISNVH 568
Cdd:COG4733   794 SATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTA 829
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 22-54 8.43e-05

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 41.73  E-value: 8.43e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1034633593  22 LKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd05750    60 LQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 5-54 1.17e-04

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


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 41.22  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034633593   5 LQGPTRRIrisLLNDGGLKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd20978    42 LQGPMERA---TVEDGTLTIINVQPEDTGYYGCVATNEIGDIYTETLLHV 88
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 16-54 1.36e-04

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


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 40.94  E-value: 1.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034633593  16 LLNDGG---LKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd05744    50 LVRENGrhsLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 64-152 1.66e-04

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


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 40.46  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  64 PSNMDVSVGESVILPCQVQHDPLLDIIftWYfngaladfKKDG----SHFEKVGGSSsgdLMIRNIQLKHSGKYVCMVQT 139
Cdd:cd05725     4 PQNQVVLVDDSAEFQCEVGGDPVPTVR--WR--------KEDGelpkGRYEILDDHS---LKIRKVTAGDMGSYTCVAEN 70

                          90
                  ....*....|...
gi 1034633593 140 GVDSVSSAADLIV 152
Cdd:cd05725    71 MVGKIEASATLTV 83
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 64-152 1.67e-04

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 40.46  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  64 PSNMDVSVGESVILPCQ--VQH-DPLLdiifTWYFNGALADFkkDGSHFEKVGGsssGDLMIRNIQLKHSGKYVCMVQTG 140
Cdd:cd05724     4 PSDTQVAVGEMAVLECSppRGHpEPTV----SWRKDGQPLNL--DNERVRIVDD---GNLLIAEARKSDEGTYKCVATNM 74

                          90
                  ....*....|...
gi 1034633593 141 V-DSVSSAADLIV 152
Cdd:cd05724    75 VgERESRAARLSV 87
IgI_VEGFR cd05862
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); ...
 60-152 1.92e-04

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (also known as Flt-1), VEGFR-2 (also known as KDR or Flk-1) and VEGFR-3 (also known as Flt-4). VEGF_A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF, VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-2 and -1 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth.


Pssm-ID: 409448  Cd Length: 102  Bit Score: 40.89  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  60 ITLAPSN-MDVSVGESVILPCQVQHDPLLDIIFTWYFNGALADFKKDGSHFEKVGGSS----SGDLMIRNIQLKHSGKYV 134
Cdd:cd05862     3 VQLSPPKpVELLVGEKLVLNCTARTELNVGVDFQWDYPGKKEQRRASVRRRRKQQSSEatefSSTLTIDNVTLSDKGLYT 82

                          90
                  ....*....|....*...
gi 1034633593 135 CMVQTGVDSVSSAADLIV 152
Cdd:cd05862    83 CAASSGPMFKKNSTSVIV 100
fn3 pfam00041
Fibronectin type III domain;
464-544 2.22e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.09  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593 464 PPGNV-VWNATDTKVLLNWEQVKamENESEVTGYKVFYRTSSQNNV---QVLNTNKTSAELV-LPIKEDYIIEVKATTDG 538
Cdd:pfam00041   2 APSNLtVTDVTSTSLTVSWTPPP--DGNGPITGYEVEYRPKNSGEPwneITVPGTTTSVTLTgLKPGTEYEVRVQAVNGG 79


                  ....*.
gi 1034633593 539 GDGTSS 544
Cdd:pfam00041  80 GEGPPS 85
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 13-54 2.37e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 40.30  E-value: 2.37e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034633593  13 RISLLNDGG-LKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd05730    50 KYSFNEDGSeMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 59-152 6.32e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 38.92  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  59 RITLAPSNMDVSVGESVILPCQVQHDPLLDiiFTWYfngaladfkKDGSHFekvggSSSGDLMIRNIQLKHSGKYVCMVQ 138
Cdd:pfam13895   1 KPVLTPSPTVVTEGEPVTLTCSAPGNPPPS--YTWY---------KDGSAI-----SSSPNFFTLSVSAEDSGTYTCVAR 64

                          90
                  ....*....|....*
gi 1034633593 139 TGVDS-VSSAADLIV 152
Cdd:pfam13895  65 NGRGGkVSNPVELTV 79
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
 66-146 8.37e-04

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


Pssm-ID: 409476  Cd Length: 93  Bit Score: 38.82  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  66 NMDVSVGESVILPCQ-VQHDPLLDiiFTWYFNGALADFKKDGSHFEKVGGSSSGDLMIRNIQLKHSGKYVCMV--QTGVD 142
Cdd:cd05895     8 SQEVAAGSKLVLRCEtSSEYPSLR--FKWFKNGKEINRKNKPENIKIQKKKKKSELRINKASLADSGEYMCKVssKLGND 85


                  ....
gi 1034633593 143 SVSS 146
Cdd:cd05895    86 SASA 89
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 4-44 8.89e-04

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 38.54  E-value: 8.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034633593   4 NLQGPTRRIrislLNDGGLKIANVTKADAGTYTCMAENQFG 44
Cdd:cd05724    40 NLDNERVRI----VDDGNLLIAEARKSDEGTYKCVATNMVG 76
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 64-140 9.26e-04

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 39.24  E-value: 9.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  64 PSNMDVSVGESVILPCQVQHDPLLDIIFtWYF----------------NGALADFKKDGSHFEKVGGSSSgDLMIRNIQL 127
Cdd:cd00099     5 PRSLSVQEGESVTLSCEVSSSFSSTYIY-WYRqkpgqgpefliylsssKGKTKGGVPGRFSGSRDGTSSF-SLTISNLQP 82

                          90
                  ....*....|...
gi 1034633593 128 KHSGKYVCMVQTG 140
Cdd:cd00099    83 EDSGTYYCAVSES 95
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 13-54 9.82e-04

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 38.32  E-value: 9.82e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1034633593  13 RISLLNDGGLKIANVTKA-DAGTYTCMAENQFG-KANGTTHLVV 54
Cdd:cd20958    46 RQRVFPNGTLVIENVQRSsDEGEYTCTARNQQGqSASRSVFVKV 89
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 60-152 1.10e-03

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 38.25  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  60 ITLAPSNMDVSVGESVILPCQVQHDPLLDIifTWYFNGALadFKKDGSHFEKVggsSSGDLMIRNIQLKHSGKYVCMVQT 139
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTI--SWLKDGVP--LLGKDERITTL---ENGSLQIKGAEKSDTGEYTCVALN 74

                          90
                  ....*....|...
gi 1034633593 140 GVDSVSSAADLIV 152
Cdd:cd20952    75 LSGEATWSAVLDV 87
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 20-54 1.17e-03

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


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 38.39  E-value: 1.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1034633593  20 GGLKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd20976    56 GELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 60-151 1.36e-03

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 38.59  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  60 ITLAPSNMDVSVGESVILPCQVQ----HDPLLDIifTW--------------YFNG----ALADFKKDGSHFekVGGSSS 117
Cdd:cd20960     3 ITSAQTEIKKVAGENVTLPCHHQlgleDQGTLDI--EWlllpsdkvekvvitYSGDrvynHYYPALKGRVAF--TSNDLS 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034633593 118 GD--LMIRNIQLKHSGKYVCMVQTGVDSVSSAADLI 151
Cdd:cd20960    79 GDasLNISNLKLSDTGTYQCKVKKAPGYAWSKITLI 114
IgI_VEGFR_like cd05742
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and ...
 65-152 1.98e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and similar proteins; member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and related proteins. The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4). VEGF-A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF; VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic, and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group also contains alpha-type platelet-derived growth factor receptor precursor (PDGFR)-alpha (CD140a), and PDGFR-beta (CD140b). PDGFRs alpha and beta have an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion that has protein tyrosine kinase activity.


Pssm-ID: 409404  Cd Length: 102  Bit Score: 37.90  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  65 SNMDVSVGESVILPCQVQHDPLLDIIFTWYF----NGALA----DFKKDGSHFEKVggssSGDLMIRNIQLKHSGKYVCM 136
Cdd:cd05742    10 EPTVLPQGETLVLNCTANVNLNEVVDFQWTYpsekEGKLAllkpDIKVDWSEPGEF----VSTLTIPEATLKDSGTYTCA 85

                          90
                  ....*....|....*.
gi 1034633593 137 VQTGVDSVSSAADLIV 152
Cdd:cd05742    86 ARSGVMKKEKQTSVSV 101
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 10-97 2.71e-03

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 40.38  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  10 RRIRISLLND---GGLKIANVTKADAGTYTCMAENQFG-KANGTTHLVVTEpTRITLAPSNMD------VSVGESVILPC 79
Cdd:PHA02785  164 RRLRNKRLKQrtpGIITIEDVRKNDAGYYTCVLKYIYGdKTYNVTRIVKLE-VRDRIIPPTMQlpegvvTSIGSNLTIAC 242

                          90
                  ....*....|....*....
gi 1034633593  80 QVQ-HDPLLDIIFTWYFNG 97
Cdd:PHA02785  243 RVSlRPPTTDADVFWISNG 261
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 11-41 3.21e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.77  E-value: 3.21e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034633593  11 RIRISLLNDGGLKIANVTKADAGTYTCMAEN 41
Cdd:pfam13927  48 RSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 66-146 3.42e-03

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 37.11  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  66 NMDVSVGESVILPCQ-VQHDPLLDiiFTWYFNGAlaDFKKDGSHFEKVGGS-SSGDLMIRNIQLKHSGKYVCMV--QTGV 141
Cdd:cd05750     8 SQTVQEGSKLVLKCEaTSENPSPR--YRWFKDGK--ELNRKRPKNIKIRNKkKNSELQINKAKLEDSGEYTCVVenILGK 83


                  ....*
gi 1034633593 142 DSVSS 146
Cdd:cd05750    84 DTVTG 88
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 18-55 4.37e-03

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 37.05  E-value: 4.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1034633593  18 NDGGLKIANVTKADAGTYTC-MAENQFGKANGTTHLVVT 55
Cdd:pfam07686  71 GDGSLTIQNLTLSDSGTYTCaVIPSGEGVFGKGTRLTVL 109
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 69-152 4.66e-03

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 36.67  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  69 VSVGESVILPCQVQHDPLLDIifTWYFNGALADFKKDGSHFEkvggssSGDLMIRNIQLKHSGKYVCMVQTGVDSVSSAA 148
Cdd:cd04969    14 AAKGGDVIIECKPKASPKPTI--SWSKGTELLTNSSRICILP------DGSLKIKNVTKSDEGKYTCFAVNFFGKANSTG 85


                  ....
gi 1034633593 149 DLIV 152
Cdd:cd04969    86 SLSV 89
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 20-54 4.82e-03

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: 36.75  E-value: 4.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1034633593  20 GGLKIAN---------VTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd05857    52 GGYKVRNqhwslimesVVPSDKGNYTCVVENEYGSINHTYHLDV 95
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 13-54 4.93e-03

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 36.30  E-value: 4.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034633593  13 RISLLNDGGLKIANVTKADAGTYTCMAENQFGKANGTTHLVV 54
Cdd:cd05764    47 RTLVYDNGTLDILITTVKDTGAFTCIASNPAGEATARVELHI 88
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
 19-57 5.18e-03

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


Pssm-ID: 409455  Cd Length: 92  Bit Score: 36.56  E-value: 5.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034633593  19 DGGLKIANVTKADAGTYTCMA-ENQFGKANGTTHLVVTEP 57
Cdd:cd05871    53 DRGLLLRSLQRSDAGVYTCQAvEHGFSQTLVKIRLHVIEP 92
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 64-137 5.96e-03

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 36.67  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  64 PSNMDVSVGESVILPCQVQHDPLLDII-FTWYF---------------NGALADFKKDGSHFEKVGGSSSGDLMIRNIQL 127
Cdd:pfam07686   3 PREVTVALGGSVTLPCTYSSSMSEASTsVYWYRqppgkgptfliayysNGSEEGVKKGRFSGRGDPSNGDGSLTIQNLTL 82

                          90
                  ....*....|
gi 1034633593 128 KHSGKYVCMV 137
Cdd:pfam07686  83 SDSGTYTCAV 92
Ig1_FcgammaR_like cd05752
First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
 72-152 8.62e-03

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409410 [Multi-domain]  Cd Length: 79  Bit Score: 35.42  E-value: 8.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633593  72 GESVILPCQVQHDPLLDIIFtWYFNGALadfkkdgshfekvGGSSSGDLMIRNIQLKHSGKYVCmvQTGVDSVSSAADLI 151
Cdd:cd05752    15 GEKVTLTCQGFYSPEQNSTQ-WYHNGTL-------------ISSTSSSYRIVAATVNDSGEYRC--QTQGSSLSDPVHLE 78


                  .
gi 1034633593 152 V 152
Cdd:cd05752    79 V 79
 
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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