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Conserved domains on  [gi|1388591307|ref|NP_001350145|]
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vascular endothelial growth factor receptor 2 isoform 2 precursor [Mus musculus]

Protein Classification

immunoglobulin domain-containing protein( domain architecture ID 10310347)

immunoglobulin (Ig) domain-containing protein adopts a fold comprised of a sandwich of two beta sheets and may function in cell adhesion and pattern recognition; similar to Drosophila melanogaster DIP/Dpr cell recognition proteins, which are members of the Wirin family of IgSF proteins with neuronal wiring functions, and human IgLON proteins, a family of cell adhesion molecules

CATH:  2.60.40.10
PubMed:  9541533|3289571|7932691|10436082
SCOP:  3000071

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 ...
 331-419 1.06e-39

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 cd05864:

Pssm-ID: 472250  Cd Length: 89  Bit Score: 140.45  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 331 FIAFGSGMKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDELTIMEVTERDAGNYTVILTNPISMEK 410
Cdd:cd05864     1 FIALGSGMESLVEAKVGERVRIPVKYLGYPPPEIKWYKNGIPIESNHTIKAGHVLTIMEVTEKDAGNYTVVLTNPISKEK 80


                  ....*....
gi 1388591307 411 QSHMVSLVV 419
Cdd:cd05864    81 QRHTFSLVV 89
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 226-327 1.42e-39

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 cd05862:

Pssm-ID: 472250  Cd Length: 102  Bit Score: 140.66  E-value: 1.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 226 YDVILSPPHEIELSAGEKLVLNCTARTELNVGLDFTWHSPPSKSHHKKIVNRDVKPFPGTvAKMFLSTLTIESVTKSDQG 305
Cdd:cd05862     1 YDVQLSPPKPVELLVGEKLVLNCTARTELNVGVDFQWDYPGKKEQRRASVRRRRKQQSSE-ATEFSSTLTIDNVTLSDKG 79

                          90       100
                  ....*....|....*....|..
gi 1388591307 306 EYTCVASSGRMIKRNRTFVRVH 327
Cdd:cd05862    80 LYTCAASSGPMFKKNSTSVIVH 101
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 549-642 2.20e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.94  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 549 PEITVQPAAQ-PTEQESVSLLCTADRNTFENLTWYKLGSQATSVHMGESltpvcknldalwklngtmFSNSTNDILIVaf 627
Cdd:pfam13927   2 PVITVSPSSVtVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSR------------------SLSGSNSTLTI-- 61

                          90
                  ....*....|....*
gi 1388591307 628 QNASLQDQGDYVCSA 642
Cdd:pfam13927  62 SNVTRSDAGTYTCVA 76
 
Name Accession Description Interval E-value
IgI_VEGFR-2 cd05864
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); ...
 331-419 1.06e-39

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2). 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. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-2 (KDR/Flk-1) is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A; 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. VEGF-A also interacts with VEGFR-1, which it binds more strongly than VEGFR-2. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. 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: 409450  Cd Length: 89  Bit Score: 140.45  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 331 FIAFGSGMKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDELTIMEVTERDAGNYTVILTNPISMEK 410
Cdd:cd05864     1 FIALGSGMESLVEAKVGERVRIPVKYLGYPPPEIKWYKNGIPIESNHTIKAGHVLTIMEVTEKDAGNYTVVLTNPISKEK 80


                  ....*....
gi 1388591307 411 QSHMVSLVV 419
Cdd:cd05864    81 QRHTFSLVV 89
IgI_VEGFR cd05862
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); ...
 226-327 1.42e-39

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: 140.66  E-value: 1.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 226 YDVILSPPHEIELSAGEKLVLNCTARTELNVGLDFTWHSPPSKSHHKKIVNRDVKPFPGTvAKMFLSTLTIESVTKSDQG 305
Cdd:cd05862     1 YDVQLSPPKPVELLVGEKLVLNCTARTELNVGVDFQWDYPGKKEQRRASVRRRRKQQSSE-ATEFSSTLTIDNVTLSDKG 79

                          90       100
                  ....*....|....*....|..
gi 1388591307 306 EYTCVASSGRMIKRNRTFVRVH 327
Cdd:cd05862    80 LYTCAASSGPMFKKNSTSVIVH 101
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 339-404 8.21e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 55.65  E-value: 8.21e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591307 339 KSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDE-----LTIMEVTERDAGNYTVILTN 404
Cdd:pfam13927   8 PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSgsnstLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 233-326 1.49e-08

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: 52.12  E-value: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307  233 PHEIELSAGEKLVLNCTARTELNVglDFTWH----SPPSKSHHKKIVNRDvkpfpgtvakmFLSTLTIESVTKSDQGEYT 308
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPP--EVTWYkqggKLLAESGRFSVSRSG-----------STSTLTISNVTPEDSGTYT 67

                           90
                   ....*....|....*...
gi 1388591307  309 CVASSGRMIKRNRTFVRV 326
Cdd:smart00410  68 CAATNSSGSASSGTTLTV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 231-312 6.43e-08

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: 50.66  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 231 SPPHEIELSAGEKLVLNCTARTeLNVGLDFTWH----SPPSKSHHKKIVNRdvkpfpgtvakMFLSTLTIESVTKSDQGE 306
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAST-GSPGPDVTWSkeggTLIESLKVKHDNGR-----------TTQSSLLISNVTKEDAGT 68


                  ....*.
gi 1388591307 307 YTCVAS 312
Cdd:pfam00047  69 YTCVVN 74
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 142-401 1.86e-07

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 53.48  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 142 ENKNKTVVIPCrgsiSNLNvSLCARYP------EKRFVPDGNRISWDSEIGFTLPSYMISYAGMVFCEAKinDETYQSIM 215
Cdd:PHA02785   38 ELENEPVILPC----PQIN-TLSSGYNildilwEKRGADNDRIIPIDNGSNMLILNPTQSDSGIYICITK--NETYCDMM 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 216 YI---VVVVGYRIYDVILSPPHEIELSAGEKLVLNCTARTELNVGLDFTWhsppskSHHKKIVNRDVKPFPGTVakmfls 292
Cdd:PHA02785  111 SLnltIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNVNADIIW------SGHRRLRNKRLKQRTPGI------ 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 293 tLTIESVTKSDQGEYTCVAssgRMIKRNRTF-----VRVHTKP-FIAFGSGMKSLVEATVGSQVRIPVKYLSYPA---PD 363
Cdd:PHA02785  179 -ITIEDVRKNDAGYYTCVL---KYIYGDKTYnvtriVKLEVRDrIIPPTMQLPEGVVTSIGSNLTIACRVSLRPPttdAD 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591307 364 IKWYRNGRPIESN--------------YTM----IVGDELTIMEVTERDAGNYTVI 401
Cdd:PHA02785  255 VFWISNGMYYEEDdedgdgrisvankiYTTdkrrVITSRLNINPVKEEDATTFTCM 310
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 342-419 2.24e-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: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307  342 VEATVGSQVRIPVKYLSYPAPDIKWYRNGR--PIESNYTMIVGD----ELTIMEVTERDAGNYTVILTNPISMEKQShmV 415
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGklLAESGRFSVSRSgstsTLTISNVTPEDSGTYTCAATNSSGSASSG--T 81


                   ....
gi 1388591307  416 SLVV 419
Cdd:smart00410  82 TLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 549-642 2.20e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.94  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 549 PEITVQPAAQ-PTEQESVSLLCTADRNTFENLTWYKLGSQATSVHMGESltpvcknldalwklngtmFSNSTNDILIVaf 627
Cdd:pfam13927   2 PVITVSPSSVtVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSR------------------SLSGSNSTLTI-- 61

                          90
                  ....*....|....*
gi 1388591307 628 QNASLQDQGDYVCSA 642
Cdd:pfam13927  62 SNVTRSDAGTYTCVA 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 563-649 2.46e-03

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: 37.48  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307  563 ESVSLLCTADRNTFENLTWYKLGsqatsvhmgesLTPVCKNLDALWKLNGTMFSnstndiLIvaFQNASLQDQGDYVCSA 642
Cdd:smart00410  10 ESVTLSCEASGSPPPEVTWYKQG-----------GKLLAESGRFSVSRSGSTST------LT--ISNVTPEDSGTYTCAA 70


                   ....*..
gi 1388591307  643 QDKKTKK 649
Cdd:smart00410  71 TNSSGSA 77
 
Name Accession Description Interval E-value
IgI_VEGFR-2 cd05864
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); ...
 331-419 1.06e-39

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2). 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. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-2 (KDR/Flk-1) is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A; 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. VEGF-A also interacts with VEGFR-1, which it binds more strongly than VEGFR-2. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. 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: 409450  Cd Length: 89  Bit Score: 140.45  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 331 FIAFGSGMKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDELTIMEVTERDAGNYTVILTNPISMEK 410
Cdd:cd05864     1 FIALGSGMESLVEAKVGERVRIPVKYLGYPPPEIKWYKNGIPIESNHTIKAGHVLTIMEVTEKDAGNYTVVLTNPISKEK 80


                  ....*....
gi 1388591307 411 QSHMVSLVV 419
Cdd:cd05864    81 QRHTFSLVV 89
IgI_VEGFR cd05862
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); ...
 226-327 1.42e-39

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: 140.66  E-value: 1.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 226 YDVILSPPHEIELSAGEKLVLNCTARTELNVGLDFTWHSPPSKSHHKKIVNRDVKPFPGTvAKMFLSTLTIESVTKSDQG 305
Cdd:cd05862     1 YDVQLSPPKPVELLVGEKLVLNCTARTELNVGVDFQWDYPGKKEQRRASVRRRRKQQSSE-ATEFSSTLTIDNVTLSDKG 79

                          90       100
                  ....*....|....*....|..
gi 1388591307 306 EYTCVASSGRMIKRNRTFVRVH 327
Cdd:cd05862    80 LYTCAASSGPMFKKNSTSVIVH 101
IgI_VEGFR cd04976
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); member ...
 331-419 2.22e-34

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR). 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). VEGFRs bind VEGFs with high affinity at 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 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: 409365  Cd Length: 90  Bit Score: 125.79  E-value: 2.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 331 FIAFGSGMKSLVEATVGSQ-VRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDELTIMEVTERDAGNYTVILTNPISME 409
Cdd:cd04976     1 FITVKHRKQQVLEATAGKRsVRLPMKVKAYPPPEVVWYKDGLPLTEKARYLTRHSLIIKEVTEEDTGNYTILLSNKQSNV 80

                          90
                  ....*....|
gi 1388591307 410 KQSHMVSLVV 419
Cdd:cd04976    81 FKNLTATLVV 90
IgI_VEGFR_like cd05742
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and ...
 226-327 3.63e-29

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: 111.48  E-value: 3.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 226 YDVILSPP-HEIELSAGEKLVLNCTARTELNVGLDFTWHSPPSKSHHKKIVNRDVKpFPGTVAKMFLSTLTIESVTKSDQ 304
Cdd:cd05742     1 SDLELSPNaEPTVLPQGETLVLNCTANVNLNEVVDFQWTYPSEKEGKLALLKPDIK-VDWSEPGEFVSTLTIPEATLKDS 79

                          90       100
                  ....*....|....*....|...
gi 1388591307 305 GEYTCVASSGRMIKRNRTFVRVH 327
Cdd:cd05742    80 GTYTCAARSGVMKKEKQTSVSVH 102
IgI_VEGFR-3 cd05863
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3); ...
 330-411 2.29e-14

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3). 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. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-3 (Flt-4) binds two members of the VEGF family (VEGF-C and VEGF-D) and is involved in tumor angiogenesis and growth. 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: 409449  Cd Length: 88  Bit Score: 68.81  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 330 PFIAFGSGMKSLVEATVGSQ-VRIPVKYLSYPAPDIKWYRNGRPIESNYTmivGDELTIMEVTERDAGNYTVILTN-PIS 407
Cdd:cd05863     1 PFISVEWRKGPVIEATAGDElVKLPVKVAAYPPPEFQWYKDGKLISGKHS---PHSLQIKDVTEASAGTYTLVLWNsAAG 77


                  ....
gi 1388591307 408 MEKQ 411
Cdd:cd05863    78 LEKR 81
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 339-404 8.21e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 55.65  E-value: 8.21e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591307 339 KSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDE-----LTIMEVTERDAGNYTVILTN 404
Cdd:pfam13927   8 PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSgsnstLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
342-419 1.90e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.96  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 342 VEATVGSQVRIPVKYLSYPAPDIKWYRNGRPI-ESNYTMIVGDE----LTIMEVTERDAGNYTVILTNPIsmEKQSHMVS 416
Cdd:pfam07679  10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQPLrSSDRFKVTYEGgtytLTISNVQPDDSGKYTCVATNSA--GEAEASAE 87


                  ...
gi 1388591307 417 LVV 419
Cdd:pfam07679  88 LTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 233-326 1.49e-08

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: 52.12  E-value: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307  233 PHEIELSAGEKLVLNCTARTELNVglDFTWH----SPPSKSHHKKIVNRDvkpfpgtvakmFLSTLTIESVTKSDQGEYT 308
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPP--EVTWYkqggKLLAESGRFSVSRSG-----------STSTLTISNVTPEDSGTYT 67

                           90
                   ....*....|....*...
gi 1388591307  309 CVASSGRMIKRNRTFVRV 326
Cdd:smart00410  68 CAATNSSGSASSGTTLTV 85
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 342-411 1.62e-08

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


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 52.51  E-value: 1.62e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591307 342 VEATVGSQVRIPVKYLSYPAPDIKWYRNG-RPIESNYTMIV---GDELTIMEVTERDAGNYTVILTN--PISMEKQ 411
Cdd:cd20970    12 VTAREGENATFMCRAEGSPEPEISWTRNGnLIIEFNTRYIVrenGTTLTIRNIRRSDMGIYLCIASNgvPGSVEKR 87
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 231-312 6.43e-08

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: 50.66  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 231 SPPHEIELSAGEKLVLNCTARTeLNVGLDFTWH----SPPSKSHHKKIVNRdvkpfpgtvakMFLSTLTIESVTKSDQGE 306
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAST-GSPGPDVTWSkeggTLIESLKVKHDNGR-----------TTQSSLLISNVTKEDAGT 68


                  ....*.
gi 1388591307 307 YTCVAS 312
Cdd:pfam00047  69 YTCVVN 74
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 350-412 8.72e-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: 49.64  E-value: 8.72e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591307 350 VRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDE-----LTIMEVTERDAGNYTVILTNPISMEKQS 412
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSElgngtLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 339-404 9.56e-08

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


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 49.88  E-value: 9.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591307 339 KSLVEATV--GSQVRIPVKYLSYPAPDIKWYRNGRPI-ESNYTMIVGDE-----LTIMEVTERDAGNYTVILTN 404
Cdd:cd20973     2 QTLRDKEVveGSAARFDCKVEGYPDPEVKWMKDDNPIvESRRFQIDQDEdglcsLIISDVCGDDSGKYTCKAVN 75
Ig4_PDGFR cd05859
Fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR); The ...
 331-421 1.02e-07

Fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR); The members here are composed of the fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR; also known as cluster of differentiation (CD) 140a) alpha and beta. PDGF is a potent mitogen for connective tissue cells. PDGF-stimulated processes are mediated by three different PDGFs (PDGF-A,PDGF-B, and PDGF-C). PDGFR alpha binds to all three PDGFs, whereas the PDGFR beta binds only to PDGF-B. PDGF alpha is organized as an extracellular component having five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. In mice, PDGFR alpha and PDGFR beta are essential for normal development.


Pssm-ID: 409445  Cd Length: 101  Bit Score: 50.25  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 331 FIAFGSGMKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGD-----------ELTIMEVTERDAGNYT 399
Cdd:cd05859     2 FIALKPTFGQLEFANLHEVKEFVVEVEAYPPPQIRWLKDNRTLIENLTEITTStrnvqetryvsKLKLIRAKEEDSGLYT 81

                          90       100
                  ....*....|....*....|..
gi 1388591307 400 VILTNpiSMEKQSHMVSLVVNV 421
Cdd:cd05859    82 ALAQN--EDAVKSYTFALQIQV 101
I-set pfam07679
Immunoglobulin I-set domain;
228-312 1.07e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 49.95  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 228 VILSPPHEIELSAGEKLVLNCTARtelnvG---LDFTWH---SPPSKSHHKKIVNRDVKpfpgtvakmflSTLTIESVTK 301
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVT-----GtpdPEVSWFkdgQPLRSSDRFKVTYEGGT-----------YTLTISNVQP 65

                          90
                  ....*....|.
gi 1388591307 302 SDQGEYTCVAS 312
Cdd:pfam07679  66 DDSGKYTCVAT 76
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 343-412 1.77e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 49.50  E-value: 1.77e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591307 343 EATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDE-----LTIMEVTERDAGNYTVILTNPISMEKQS 412
Cdd:cd20972    12 EVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEgdlhsLIIAEAFEEDTGRYSCLATNSVGSDTTS 86
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 346-419 1.83e-07

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


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 49.13  E-value: 1.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591307 346 VGSQVRIPVKYLSYPAPDIKWYRNGRPIESN--YTMIVGDE---LTIMEVTERDAGNYTVILTNPiSMEKQSHmVSLVV 419
Cdd:cd05748     6 AGESLRLDIPIKGRPTPTVTWSKDGQPLKETgrVQIETTASstsLVIKNAKRSDSGKYTLTLKNS-AGEKSAT-INVKV 82
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 142-401 1.86e-07

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 53.48  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 142 ENKNKTVVIPCrgsiSNLNvSLCARYP------EKRFVPDGNRISWDSEIGFTLPSYMISYAGMVFCEAKinDETYQSIM 215
Cdd:PHA02785   38 ELENEPVILPC----PQIN-TLSSGYNildilwEKRGADNDRIIPIDNGSNMLILNPTQSDSGIYICITK--NETYCDMM 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 216 YI---VVVVGYRIYDVILSPPHEIELSAGEKLVLNCTARTELNVGLDFTWhsppskSHHKKIVNRDVKPFPGTVakmfls 292
Cdd:PHA02785  111 SLnltIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNVNADIIW------SGHRRLRNKRLKQRTPGI------ 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 293 tLTIESVTKSDQGEYTCVAssgRMIKRNRTF-----VRVHTKP-FIAFGSGMKSLVEATVGSQVRIPVKYLSYPA---PD 363
Cdd:PHA02785  179 -ITIEDVRKNDAGYYTCVL---KYIYGDKTYnvtriVKLEVRDrIIPPTMQLPEGVVTSIGSNLTIACRVSLRPPttdAD 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591307 364 IKWYRNGRPIESN--------------YTM----IVGDELTIMEVTERDAGNYTVI 401
Cdd:PHA02785  255 VFWISNGMYYEEDdedgdgrisvankiYTTdkrrVITSRLNINPVKEEDATTFTCM 310
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 342-419 2.24e-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: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307  342 VEATVGSQVRIPVKYLSYPAPDIKWYRNGR--PIESNYTMIVGD----ELTIMEVTERDAGNYTVILTNPISMEKQShmV 415
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGklLAESGRFSVSRSgstsTLTISNVTPEDSGTYTCAATNSSGSASSG--T 81


                   ....
gi 1388591307  416 SLVV 419
Cdd:smart00410  82 TLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 228-312 2.41e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 48.72  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 228 VILSPPHEIELSAGEKLVLNCTArtELNVGLDFTWHSPPSKSHHKKIVNRDVKPFPgtvakmflSTLTIESVTKSDQGEY 307
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEA--TGSPPPTITWYKNGEPISSGSTRSRSLSGSN--------STLTISNVTRSDAGTY 72


                  ....*
gi 1388591307 308 TCVAS 312
Cdd:pfam13927  73 TCVAS 77
IgI_VEGFR-1 cd07702
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); ...
 331-402 7.05e-07

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1). 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. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-1 binds VEGF-A strongly; 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-1 may play an inhibitory role in the function of VEGFR-2 by binding VEGF-A and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis and may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. 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: 409499  Cd Length: 92  Bit Score: 47.56  E-value: 7.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591307 331 FIAFGSGMKSLVEATVGSQ-VRIPVKYLSYPAPDIKWYRNGRPI--ESNYTMIVGDELTIMEVTERDAGNYTVIL 402
Cdd:cd07702     1 FITVKHRKQQVLETFAGQKsYRLSMKVKAFPSPEVIWLKDGLPAteKCARYLTRGYSLIIKDVTEEDAGNYTILL 75
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 347-404 5.41e-06

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 45.09  E-value: 5.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591307 347 GSQVRIPVKYLSYPAPDIKWYRNGRPI--ESNYTMIVGD----ELTIMEVTERDAGNYTVILTN 404
Cdd:cd20990    15 GKLCRMDCKVSGLPTPDLSWQLDGKPIrpDSAHKMLVREngvhSLIIEPVTSRDAGIYTCIATN 78
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 343-404 7.25e-06

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


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.79  E-value: 7.25e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591307 343 EATVGSQVRIPVKYLSYPAPDIKWYRNGRPI--ESNYTMIVGD----ELTIMEVTERDAGNYTVILTN 404
Cdd:cd05744    11 EVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVrpDSAHKMLVREngrhSLIIEPVTKRDAGIYTCIARN 78
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 359-404 8.54e-06

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


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 44.54  E-value: 8.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1388591307 359 YPAPDIKWYRNGRPIESNYTMIV----GDELTIMEVTERDAGNYTVILTN 404
Cdd:cd05730    30 FPEPTMTWTKDGEPIESGEEKYSfnedGSEMTILDVDKLDEAEYTCIAEN 79
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 362-403 1.24e-05

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409415  Cd Length: 92  Bit Score: 44.24  E-value: 1.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1388591307 362 PDIKWYRNGRPIE--SNYTMiVGDELTIMEVTERDAGNYTVILT 403
Cdd:cd05757    30 PPIQWYKDCKPLQgdKRFIP-KGSKLLIQNVTEEDAGNYTCKFT 72
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 334-404 1.44e-05

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: 43.92  E-value: 1.44e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591307 334 FGSGMKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNY-TMIVGD-ELTIMEVTERDAGNYTVILTN 404
Cdd:cd20978     3 FIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMeRATVEDgTLTIINVQPEDTGYYGCVATN 75
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 232-327 1.64e-05

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: 44.37  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 232 PPHEIELSAGEKLVLNCTART-ELNVGLDFTWH-SPPSKSHHKKIV----NRDVKPFPGTVAKMFLS-----TLTIESVT 300
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSSsMSEASTSVYWYrQPPGKGPTFLIAyysnGSEEGVKKGRFSGRGDPsngdgSLTIQNLT 81

                          90       100
                  ....*....|....*....|....*...
gi 1388591307 301 KSDQGEYTC-VASSGRMIKRNRTFVRVH 327
Cdd:pfam07686  82 LSDSGTYTCaVIPSGEGVFGKGTRLTVL 109
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 549-642 2.20e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.94  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 549 PEITVQPAAQ-PTEQESVSLLCTADRNTFENLTWYKLGSQATSVHMGESltpvcknldalwklngtmFSNSTNDILIVaf 627
Cdd:pfam13927   2 PVITVSPSSVtVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSR------------------SLSGSNSTLTI-- 61

                          90
                  ....*....|....*
gi 1388591307 628 QNASLQDQGDYVCSA 642
Cdd:pfam13927  62 SNVTRSDAGTYTCVA 76
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 345-419 5.39e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.00  E-value: 5.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591307 345 TVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYtmivgdELTIMEVTERDAGNYTVILTNPISMeKQSHMVSLVV 419
Cdd:pfam13895  12 TEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSP------NFFTLSVSAEDSGTYTCVARNGRGG-KVSNPVELTV 79
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 232-339 1.34e-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: 41.55  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 232 PPHEIELSAGEKLVLNCTARTELNVGlDFTW-HSPPSKSHH--------KKIVNRDVKP-FPGTVAKMFLSTLTIESVTK 301
Cdd:cd00099     4 SPRSLSVQEGESVTLSCEVSSSFSST-YIYWyRQKPGQGPEfliylsssKGKTKGGVPGrFSGSRDGTSSFSLTISNLQP 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1388591307 302 SDQGEYTCVASSGRMikrnrtfvrvhTKPFIaFGSGMK 339
Cdd:cd00099    83 EDSGTYYCAVSESGG-----------TDKLT-FGSGTR 108
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 244-323 1.58e-04

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 40.39  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 244 LVLNCTARTELNVglDFTWHSPPSKSHHKKIVNRDVKPFPGTvakmflstLTIESVTKSDQGEYTCVASSGRMIKRNRTF 323
Cdd:cd00096     1 VTLTCSASGNPPP--TITWYKNGKPLPPSSRDSRRSELGNGT--------LTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 228-313 1.86e-04

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 40.56  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 228 VILSPPHEIELSAGEKLVLNCTARTE-LNVgldFTWhsppskshhkkivNRDVKPFPGTVAKMFL---STLTIESVTKSD 303
Cdd:cd20952     1 IILQGPQNQTVAVGGTVVLNCQATGEpVPT---ISW-------------LKDGVPLLGKDERITTlenGSLQIKGAEKSD 64

                          90
                  ....*....|
gi 1388591307 304 QGEYTCVASS 313
Cdd:cd20952    65 TGEYTCVALN 74
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 360-419 1.91e-04

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 40.47  E-value: 1.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591307 360 PAPDIKWYR------NGRPIESNYtmivGDELTIMEVTERDAGNYTVILTNPisMEKQSHMVSLVV 419
Cdd:cd05731    23 PTPDIRWIKlggelpKGRTKFENF----NKTLKIENVSEADSGEYQCTASNT--MGSARHTISVTV 82
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 338-408 2.77e-04

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: 40.26  E-value: 2.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591307 338 MKSLVEATVGSQVRIPVKY-LSYPAPDIKWYRNG-RPIES-----NYTMIVGDELTIMEVTERDAGNYTVILTNPISM 408
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGgTLIESlkvkhDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 237-313 4.15e-04

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 39.80  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 237 ELSAGEKLVLNCTARTElNVGLDFTWHS-----PPSKSHHKKIVNRDVKpfpgtvakmflSTLTIESVTKSDQGEYTCVA 311
Cdd:cd05750    10 TVQEGSKLVLKCEATSE-NPSPRYRWFKdgkelNRKRPKNIKIRNKKKN-----------SELQINKAKLEDSGEYTCVV 77


                  ..
gi 1388591307 312 SS 313
Cdd:cd05750    78 EN 79
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 360-417 4.29e-04

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: 39.93  E-value: 4.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591307 360 PAPDIKWYRNGRPIESNYTMIVGD----ELTIMEVTERDAGNYTVILTNPISMEKQSHMVSL 417
Cdd:cd20976    29 PVPRITWIRNAQPLQYAADRSTCEagvgELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 293-326 6.21e-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: 39.09  E-value: 6.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1388591307 293 TLTIESVTK-SDQGEYTCVASSGR-MIKRNRTFVRV 326
Cdd:cd20958    54 TLVIENVQRsSDEGEYTCTARNQQgQSASRSVFVKV 89
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 344-421 6.91e-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: 39.09  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 344 ATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDE--LTIMEVT-ERDAGNYTVILTNPismEKQSHMVSLVVN 420
Cdd:cd20958    12 AVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVFPNgtLVIENVQrSSDEGEYTCTARNQ---QGQSASRSVFVK 88


                  .
gi 1388591307 421 V 421
Cdd:cd20958    89 V 89
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 338-404 6.93e-04

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 38.98  E-value: 6.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591307 338 MKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPI-ESNYTMIVGD-ELTIMEVTERDAGNYTVILTN 404
Cdd:cd04969     8 VKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLtNSSRICILPDgSLKIKNVTKSDEGKYTCFAVN 76
IgI_1_FGFR cd04973
First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 364-421 9.00e-04

First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for all FGFs.


Pssm-ID: 409362  Cd Length: 94  Bit Score: 39.11  E-value: 9.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591307 364 IKWYRNGRPI-ESNYTMIVGDELTIMEVTERDAGNYTVILTNPIsmekQSHMVSLVVNV 421
Cdd:cd04973    40 INWTKDGVQLgENNRTRITGEEVQIKDAVPRDSGLYACVTSSPS----GSDTTYFSVNV 94
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 347-419 1.02e-03

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 38.94  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 347 GSQVRIPVKYLSYPAPDIKWYRNGRPI-----------ESNYTMivgDELTIMEVTERDAGNYTVILTNPISMEKQShmV 415
Cdd:cd20951    15 KSDAKLRVEVQGKPDPEVKWYKNGVPIdpssipgkykiESEYGV---HVLHIRRVTVEDSAVYSAVAKNIHGEASSS--A 89


                  ....
gi 1388591307 416 SLVV 419
Cdd:cd20951    90 SVVV 93
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 340-400 1.22e-03

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 38.47  E-value: 1.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591307 340 SLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIE------SNYTmIVGDELTIMEVTERDAGNYTV 400
Cdd:cd20949     7 YVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISasvadmSKYR-ILADGLLINKVTQDDTGEYTC 72
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 359-419 1.55e-03

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 38.15  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591307 359 YPAPDIKWYRNGRPI---ESNYTMIVGDELTIMEVTERDAGNYTVILTNPISmEKQSHMVSLVV 419
Cdd:cd05724    25 HPEPTVSWRKDGQPLnldNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVG-ERESRAARLSV 87
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 360-404 1.60e-03

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


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 38.31  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1388591307 360 PAPDIKWYRNGRPIESNYTMIVGDELT----------IMEVTERDAGNYTVILTN 404
Cdd:cd20956    29 PLPQITWTLDGFPIPESPRFRVGDYVTsdgdvvsyvnISSVRVEDGGEYTCTATN 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 563-649 2.46e-03

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: 37.48  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307  563 ESVSLLCTADRNTFENLTWYKLGsqatsvhmgesLTPVCKNLDALWKLNGTMFSnstndiLIvaFQNASLQDQGDYVCSA 642
Cdd:smart00410  10 ESVTLSCEASGSPPPEVTWYKQG-----------GKLLAESGRFSVSRSGSTST------LT--ISNVTPEDSGTYTCAA 70


                   ....*..
gi 1388591307  643 QDKKTKK 649
Cdd:smart00410  71 TNSSGSA 77
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 343-404 3.00e-03

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


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 37.19  E-value: 3.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591307 343 EATVGSQVRIPVKYLSYPAPDIKWYRNGRPIES-NYTMIVGDELTIMEVTERDAGNYTVILTN 404
Cdd:cd05728    10 EADIGSSLRWECKASGNPRPAYRWLKNGQPLASeNRIEVEAGDLRITKLSLSDSGMYQCVAEN 72
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 330-404 4.41e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 36.76  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591307 330 PFIAFGSGMKSLV-EATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYtmiVGDE------LTIMEVTERDAGNYTVIL 402
Cdd:cd05856     1 PRFTQPAKMRRRViARPVGSSVRLKCVASGNPRPDITWLKDNKPLTPPE---IGENkkkkwtLSLKNLKPEDSGKYTCHV 77


                  ..
gi 1388591307 403 TN 404
Cdd:cd05856    78 SN 79
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 290-326 6.42e-03

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 36.23  E-value: 6.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1388591307 290 FLSTLTIESVTKSDQGEYTCVASSGRMIKRNRTFVRV 326
Cdd:cd05731    46 FNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 338-404 7.93e-03

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


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 36.43  E-value: 7.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591307 338 MKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGD------ELTIMEVTERDAGNYTVILTN 404
Cdd:cd05729    10 EEREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKveekgwSLIIERAIPRDKGKYTCIVEN 82
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 360-417 8.70e-03

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 36.04  E-value: 8.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591307 360 PAPDIKWYRNGRPIESNYTMIVGDE------LTIMEVTERDAGNYTVILTNPISMEKQSHMVSL 417
Cdd:cd05891    29 PDPEVIWFKNDQDIELSEHYSVKLEqgkyasLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 362-399 8.89e-03

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409586  Cd Length: 94  Bit Score: 36.29  E-value: 8.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1388591307 362 PDIKWYRNGRPIESNYTMIVG--DELTIMEVTERDAGNYT 399
Cdd:cd20994    31 PKVQWYKDCKPLLLDDKRFAGleSDLLIFNVTVQDQGNYT 70
 
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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