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Conserved domains on  [gi|229892302|ref|NP_001153503|]
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vascular endothelial growth factor receptor 1 isoform 4 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgI_VEGFR-1 cd07702
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); ...
 333-424 6.34e-56

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: 182.38  E-value: 6.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 333 FITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQS 412
Cdd:cd07702    1 FITVKHRKQQVLETFAGQKSYRLSMKVKAFPSPEVIWLKDGLPATEKCARYLTRGYSLIIKDVTEEDAGNYTILLSIKQS 80

                         90
                 ....*....|..
gi 229892302 413 NVFKNLTATLIV 424
Cdd:cd07702   81 NLFKNLTATLIV 92
IgI_VEGFR cd05862
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); ...
 230-330 9.66e-50

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: 166.46  E-value: 9.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 230 IDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKN-KRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGL 308
Cdd:cd05862    1 YDVQLSPPKPVELLVGEKLVLNCTARTELNVGVDFQWDYPGKKEqRRASVRRRRKQQSSEATEFSSTLTIDNVTLSDKGL 80

                         90       100
                 ....*....|....*....|..
gi 229892302 309 YTCRVRSGPSFKSVNTSVHIYD 330
Cdd:cd05862   81 YTCAASSGPMFKKNSTSVIVHE 102
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 143-219 2.18e-05

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: 42.88  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302   143 PEIIHMTEGRELVIPCRVTS-PNITVTLKKFPLDTLIPDGkRIIWDSRKG---FIISNATYKEIGLLTCEATVNGHLYKT 218
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGsPPPEVTWYKQGGKLLAESG-RFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSASS 79


                   .
gi 229892302   219 N 219
Cdd:smart00410  80 G 80
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 427-467 5.09e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.09  E-value: 5.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 229892302  427 KPQIyekavSSFPDPALYPLGSRQILTCTAYGIPQPTIKWF 467
Cdd:pfam13927   1 KPVI-----TVSPSSVTVREGETVTLTCEATGSPPPTITWY 36
 
Name Accession Description Interval E-value
IgI_VEGFR-1 cd07702
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); ...
 333-424 6.34e-56

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: 182.38  E-value: 6.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 333 FITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQS 412
Cdd:cd07702    1 FITVKHRKQQVLETFAGQKSYRLSMKVKAFPSPEVIWLKDGLPATEKCARYLTRGYSLIIKDVTEEDAGNYTILLSIKQS 80

                         90
                 ....*....|..
gi 229892302 413 NVFKNLTATLIV 424
Cdd:cd07702   81 NLFKNLTATLIV 92
IgI_VEGFR cd05862
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); ...
 230-330 9.66e-50

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: 166.46  E-value: 9.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 230 IDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKN-KRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGL 308
Cdd:cd05862    1 YDVQLSPPKPVELLVGEKLVLNCTARTELNVGVDFQWDYPGKKEqRRASVRRRRKQQSSEATEFSSTLTIDNVTLSDKGL 80

                         90       100
                 ....*....|....*....|..
gi 229892302 309 YTCRVRSGPSFKSVNTSVHIYD 330
Cdd:cd05862   81 YTCAASSGPMFKKNSTSVIVHE 102
I-set pfam07679
Immunoglobulin I-set domain;
354-426 1.02e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 52.64  E-value: 1.02e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229892302  354 RLSMKVKAFPSPEVVWLKDGLPATEkSARYLTR----GYSLIIKDVTEEDAGNYTillsIKQSNVFKNLTATLIVNV 426
Cdd:pfam07679  19 RFTCTVTGTPDPEVSWFKDGQPLRS-SDRFKVTyeggTYTLTISNVQPDDSGKYT----CVATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 237-328 6.49e-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: 50.20  E-value: 6.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302   237 PRPVKLLRGHTLVLNCTATTplNTRVQMTWSYPDEKNKRASVRRRIDQSNSHanifySVLTIDKMQNKDKGLYTCRVRSG 316
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASG--SPPPEVTWYKQGGKLLAESGRFSVSRSGST-----STLTISNVTPEDSGTYTCAATNS 73

                           90
                   ....*....|..
gi 229892302   317 PSFKSVNTSVHI 328
Cdd:smart00410  74 SGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 354-424 1.12e-06

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.73  E-value: 1.12e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229892302   354 RLSMKVKAFPSPEVVWLKDGLPATEKSARYL----TRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKnlTATLIV 424
Cdd:smart00410  13 TLSCEASGSPPPEVTWYKQGGKLLAESGRFSvsrsGSTSTLTISNVTPEDSGTYTCAATNSSGSASS--GTTLTV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 235-326 1.17e-06

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: 46.42  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302  235 STPRPVKLLRGHTLVLNCTATTPlNTRVQMTWSYPDEKNKRASVRRRIDQSNSHanifySVLTIDKMQNKDKGLYTCRVR 314
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTG-SPGPDVTWSKEGGTLIESLKVKHDNGRTTQ-----SSLLISNVTKEDAGTYTCVVN 74

                          90
                  ....*....|..
gi 229892302  315 SGPSFKSVNTSV 326
Cdd:pfam00047  75 NPGGSATLSTSL 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 143-219 2.18e-05

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: 42.88  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302   143 PEIIHMTEGRELVIPCRVTS-PNITVTLKKFPLDTLIPDGkRIIWDSRKG---FIISNATYKEIGLLTCEATVNGHLYKT 218
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGsPPPEVTWYKQGGKLLAESG-RFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSASS 79


                   .
gi 229892302   219 N 219
Cdd:smart00410  80 G 80
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 427-467 5.09e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.09  E-value: 5.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 229892302  427 KPQIyekavSSFPDPALYPLGSRQILTCTAYGIPQPTIKWF 467
Cdd:pfam13927   1 KPVI-----TVSPSSVTVREGETVTLTCEATGSPPPTITWY 36
 
Name Accession Description Interval E-value
IgI_VEGFR-1 cd07702
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); ...
 333-424 6.34e-56

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: 182.38  E-value: 6.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 333 FITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQS 412
Cdd:cd07702    1 FITVKHRKQQVLETFAGQKSYRLSMKVKAFPSPEVIWLKDGLPATEKCARYLTRGYSLIIKDVTEEDAGNYTILLSIKQS 80

                         90
                 ....*....|..
gi 229892302 413 NVFKNLTATLIV 424
Cdd:cd07702   81 NLFKNLTATLIV 92
IgI_VEGFR cd05862
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); ...
 230-330 9.66e-50

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: 166.46  E-value: 9.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 230 IDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKN-KRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGL 308
Cdd:cd05862    1 YDVQLSPPKPVELLVGEKLVLNCTARTELNVGVDFQWDYPGKKEqRRASVRRRRKQQSSEATEFSSTLTIDNVTLSDKGL 80

                         90       100
                 ....*....|....*....|..
gi 229892302 309 YTCRVRSGPSFKSVNTSVHIYD 330
Cdd:cd05862   81 YTCAASSGPMFKKNSTSVIVHE 102
IgI_VEGFR_like cd05742
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and ...
 230-329 3.27e-43

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: 149.23  E-value: 3.27e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 230 IDVQISTP-RPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKN-KRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKG 307
Cdd:cd05742    1 SDLELSPNaEPTVLPQGETLVLNCTANVNLNEVVDFQWTYPSEKEgKLALLKPDIKVDWSEPGEFVSTLTIPEATLKDSG 80

                         90       100
                 ....*....|....*....|..
gi 229892302 308 LYTCRVRSGPSFKSVNTSVHIY 329
Cdd:cd05742   81 TYTCAARSGVMKKEKQTSVSVH 102
IgI_VEGFR cd04976
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); member ...
 333-424 3.31e-42

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: 145.82  E-value: 3.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 333 FITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKsARYLTRgYSLIIKDVTEEDAGNYTILLSIKQS 412
Cdd:cd04976    1 FITVKHRKQQVLEATAGKRSVRLPMKVKAYPPPEVVWYKDGLPLTEK-ARYLTR-HSLIIKEVTEEDTGNYTILLSNKQS 78

                         90
                 ....*....|..
gi 229892302 413 NVFKNLTATLIV 424
Cdd:cd04976   79 NVFKNLTATLVV 90
IgI_VEGFR-3 cd05863
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3); ...
 333-424 1.28e-17

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: 77.67  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 333 FITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARyltrgYSLIIKDVTEEDAGNYTILLSIKQS 412
Cdd:cd05863    2 FISVEWRKGPVIEATAGDELVKLPVKVAAYPPPEFQWYKDGKLISGKHSP-----HSLQIKDVTEASAGTYTLVLWNSAA 76

                         90
                 ....*....|..
gi 229892302 413 NVFKNLTATLIV 424
Cdd:cd05863   77 GLEKRISLELIV 88
IgI_VEGFR-2 cd05864
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); ...
 333-424 3.59e-12

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: 62.25  E-value: 3.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 333 FITVKHRKQQVLETVAGKRSyRLSMKVKAFPSPEVVWLKDGLPATEKSARYltRGYSLIIKDVTEEDAGNYTILLSIKQS 412
Cdd:cd05864    1 FIALGSGMESLVEAKVGERV-RIPVKYLGYPPPEIKWYKNGIPIESNHTIK--AGHVLTIMEVTEKDAGNYTVVLTNPIS 77

                         90
                 ....*....|..
gi 229892302 413 NVFKNLTATLIV 424
Cdd:cd05864   78 KEKQRHTFSLVV 89
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 339-406 6.57e-11

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: 58.66  E-value: 6.57e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 229892302 339 RKQQVLETVAGkRSYRLSMKVKAFPSPEVVWLKDGLPATEKSA--RYLTRG--YSLIIKDVTEEDAGNYTIL 406
Cdd:cd05744    5 QAPGDLEVQEG-RLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAhkMLVRENgrHSLIIEPVTKRDAGIYTCI 75
I-set pfam07679
Immunoglobulin I-set domain;
354-426 1.02e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 52.64  E-value: 1.02e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229892302  354 RLSMKVKAFPSPEVVWLKDGLPATEkSARYLTR----GYSLIIKDVTEEDAGNYTillsIKQSNVFKNLTATLIVNV 426
Cdd:pfam07679  19 RFTCTVTGTPDPEVSWFKDGQPLRS-SDRFKVTyeggTYTLTISNVQPDDSGKYT----CVATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 237-328 6.49e-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: 50.20  E-value: 6.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302   237 PRPVKLLRGHTLVLNCTATTplNTRVQMTWSYPDEKNKRASVRRRIDQSNSHanifySVLTIDKMQNKDKGLYTCRVRSG 316
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASG--SPPPEVTWYKQGGKLLAESGRFSVSRSGST-----STLTISNVTPEDSGTYTCAATNS 73

                           90
                   ....*....|..
gi 229892302   317 PSFKSVNTSVHI 328
Cdd:smart00410  74 SGSASSGTTLTV 85
Ig4_PDGFR cd05859
Fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR); The ...
 333-426 3.68e-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: 48.32  E-value: 3.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 333 FITVKHRKQQvLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLP------------ATEKSARYLTRgysLIIKDVTEEDA 400
Cdd:cd05859    2 FIALKPTFGQ-LEFANLHEVKEFVVEVEAYPPPQIRWLKDNRTlienlteittstRNVQETRYVSK---LKLIRAKEEDS 77

                         90       100
                 ....*....|....*....|....*.
gi 229892302 401 GNYTILlsIKQSNVFKNLTATLIVNV 426
Cdd:cd05859   78 GLYTAL--AQNEDAVKSYTFALQIQV 101
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 348-426 3.98e-07

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


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 47.58  E-value: 3.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 348 AGkRSYRLSMKVKAFPSPEVVWLKDGLPATEkSARYLTRGY----SLIIKDVTEEDAGNYTILLsikqSNVFKNLTATLI 423
Cdd:cd05748    6 AG-ESLRLDIPIKGRPTPTVTWSKDGQPLKE-TGRVQIETTasstSLVIKNAKRSDSGKYTLTL----KNSAGEKSATIN 79


                 ...
gi 229892302 424 VNV 426
Cdd:cd05748   80 VKV 82
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 358-404 8.79e-07

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 46.55  E-value: 8.79e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 229892302 358 KVKAFPSPEVVWLKDG---LPATEKSARYLTRGYSLIIKDVTEEDAGNYT 404
Cdd:cd00096    6 SASGNPPPTITWYKNGkplPPSSRDSRRSELGNGTLTISNVTLEDSGTYT 55
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 354-424 1.12e-06

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.73  E-value: 1.12e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229892302   354 RLSMKVKAFPSPEVVWLKDGLPATEKSARYL----TRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKnlTATLIV 424
Cdd:smart00410  13 TLSCEASGSPPPEVTWYKQGGKLLAESGRFSvsrsGSTSTLTISNVTPEDSGTYTCAATNSSGSASS--GTTLTV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 235-326 1.17e-06

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: 46.42  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302  235 STPRPVKLLRGHTLVLNCTATTPlNTRVQMTWSYPDEKNKRASVRRRIDQSNSHanifySVLTIDKMQNKDKGLYTCRVR 314
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTG-SPGPDVTWSKEGGTLIESLKVKHDNGRTTQ-----SSLLISNVTKEDAGTYTCVVN 74

                          90
                  ....*....|..
gi 229892302  315 SGPSFKSVNTSV 326
Cdd:pfam00047  75 NPGGSATLSTSL 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 334-404 1.33e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.02  E-value: 1.33e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229892302  334 ITVKHRKQQVLEtvagKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTR---GYSLIIKDVTEEDAGNYT 404
Cdd:pfam13927   4 ITVSPSSVTVRE----GETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLsgsNSTLTISNVTRSDAGTYT 73
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 354-404 1.34e-06

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


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 46.41  E-value: 1.34e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 229892302 354 RLSMKVKAFPSPEVVWLKDGLPATEksARYLTRGY------SLIIKDVTEEDAGNYT 404
Cdd:cd20973   16 RFDCKVEGYPDPEVKWMKDDNPIVE--SRRFQIDQdedglcSLIISDVCGDDSGKYT 70
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 334-427 1.77e-06

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: 46.26  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 334 ITVKHRKQQVLEtvagKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSA----RYLTRGY--SLIIKDVTEEDAGNYtill 407
Cdd:cd20951    3 FIIRLQSHTVWE----KSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIpgkyKIESEYGvhVLHIRRVTVEDSAVY---- 74

                         90       100
                 ....*....|....*....|
gi 229892302 408 SIKQSNVFKNLTATLIVNVK 427
Cdd:cd20951   75 SAVAKNIHGEASSSASVVVE 94
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 364-427 2.40e-06

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: 45.78  E-value: 2.40e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229892302 364 SPEVVWLKDGLPATEKSaRYLTRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKNLTATLIVNVK 427
Cdd:cd05757   29 LPPIQWYKDCKPLQGDK-RFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQYNVTRTISLTVT 91
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 335-404 2.98e-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: 45.69  E-value: 2.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 229892302 335 TVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTR--GYSLIIKDVTEEDAGNYT 404
Cdd:cd05730    3 TIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNedGSEMTILDVDKLDEAEYT 74
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 234-314 3.27e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.25  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302  234 ISTPRPVKLLRGHTLVLNCTATTplNTRVQMTWSYPDEKNKRASVRRRIDQSNShanifySVLTIDKMQNKDKGLYTCRV 313
Cdd:pfam13927   5 TVSPSSVTVREGETVTLTCEATG--SPPPTITWYKNGEPISSGSTRSRSLSGSN------STLTISNVTRSDAGTYTCVA 76


                  .
gi 229892302  314 R 314
Cdd:pfam13927  77 S 77
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 360-403 7.61e-06

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: 44.31  E-value: 7.61e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 229892302 360 KAFPSPEVVWLKDGLPATEKSARYLTR-GYSLIIKDVTEEDAGNY 403
Cdd:cd05724   23 RGHPEPTVSWRKDGQPLNLDNERVRIVdDGNLLIAEARKSDEGTY 67
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 346-406 1.70e-05

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


Pssm-ID: 409582  Cd Length: 91  Bit Score: 43.55  E-value: 1.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229892302 346 TVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSA-RYLTRG---YSLIIKDVTEEDAGNYTIL 406
Cdd:cd20990   11 TVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAhKMLVREngvHSLIIEPVTSRDAGIYTCI 75
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 143-219 2.18e-05

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: 42.88  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302   143 PEIIHMTEGRELVIPCRVTS-PNITVTLKKFPLDTLIPDGkRIIWDSRKG---FIISNATYKEIGLLTCEATVNGHLYKT 218
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGsPPPEVTWYKQGGKLLAESG-RFSVSRSGStstLTISNVTPEDSGTYTCAATNSSGSASS 79


                   .
gi 229892302   219 N 219
Cdd:smart00410  80 G 80
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 346-418 6.44e-05

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: 41.93  E-value: 6.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 346 TVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSA---RYLTRGYSLIIKDVTEEDAGNYTI----LLSIKQSNVFKNL 418
Cdd:cd20949   10 TVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVAdmsKYRILADGLLINKVTQDDTGEYTCrayqVNSIASDMQERTV 89
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 346-426 6.46e-05

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 41.82  E-value: 6.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 346 TVAGKRSYRLSMKVKAFPSPEVVWLKDGlPATEKSARYLT-----RGYSLIIKDVTEEDAGNYTILLsikqSNVFKNLTA 420
Cdd:cd05891   12 TIMEGKTLNLTCTVFGNPDPEVIWFKND-QDIELSEHYSVkleqgKYASLTIKGVTSEDSGKYSINV----KNKYGGETV 86


                 ....*.
gi 229892302 421 TLIVNV 426
Cdd:cd05891   87 DVTVSV 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 337-426 6.95e-05

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: 41.77  E-value: 6.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 337 KHRKQQVLETVAGkrSYRLSMKVKAFPSPEVVWLKDGLPAT-EKSARYLTRGYSLIIKDVTEEDAGNYTILLsikqSNVF 415
Cdd:cd05856    8 KMRRRVIARPVGS--SVRLKCVASGNPRPDITWLKDNKPLTpPEIGENKKKKWTLSLKNLKPEDSGKYTCHV----SNRA 81

                         90
                 ....*....|.
gi 229892302 416 KNLTATLIVNV 426
Cdd:cd05856   82 GEINATYKVDV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 344-426 1.36e-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: 40.70  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 344 LETVAGKrSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYS--LIIKDVTEEDAGNYTILlsikQSNVFKNLTAT 421
Cdd:cd20976   11 LEAVEGQ-DFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGVgeLHIQDVLPEDHGTYTCL----AKNAAGQVSCS 85


                 ....*
gi 229892302 422 LIVNV 426
Cdd:cd20976   86 AWVTV 90
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
 347-405 1.89e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 40.21  E-value: 1.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229892302 347 VAGKRsYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGY----SLIIKDVTEEDAGNYTI 405
Cdd:cd05894    8 VAGNK-LRLDVPISGEPAPTVTWSRGDKAFTATEGRVRVESYkdlsSFVIEGAEREDEGVYTI 69
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 339-424 2.44e-04

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 40.14  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 339 RKQQVLETVAGKRSYRLSM--KVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILlsikQSNVF- 415
Cdd:cd04969    4 ELNPVKKKILAAKGGDVIIecKPKASPKPTISWSKGTELLTNSSRICILPDGSLKIKNVTKSDEGKYTCF----AVNFFg 79

                         90
                 ....*....|
gi 229892302 416 -KNLTATLIV 424
Cdd:cd04969   80 kANSTGSLSV 89
I-set pfam07679
Immunoglobulin I-set domain;
234-313 3.67e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.55  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302  234 ISTPRPVKLLRGHTLVLNCTAT---TPlntrvQMTWSYPDEKnKRASVRRRIDQSNSHanifySVLTIDKMQNKDKGLYT 310
Cdd:pfam07679   4 TQKPKDVEVQEGESARFTCTVTgtpDP-----EVSWFKDGQP-LRSSDRFKVTYEGGT-----YTLTISNVQPDDSGKYT 72


                  ...
gi 229892302  311 CRV 313
Cdd:pfam07679  73 CVA 75
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 248-314 4.83e-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: 38.85  E-value: 4.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229892302 248 LVLNCTATTplNTRVQMTWSYPDEKNKRASVRRRIDQSNShanifySVLTIDKMQNKDKGLYTCRVR 314
Cdd:cd00096    1 VTLTCSASG--NPPPTITWYKNGKPLPPSSRDSRRSELGN------GTLTISNVTLEDSGTYTCVAS 59
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 352-408 4.96e-04

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


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 39.51  E-value: 4.96e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 229892302 352 SYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTR----GYSLIIKDVTEEDAGNYTILLS 408
Cdd:cd05729   21 KVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKveekGWSLIIERAIPRDKGKYTCIVE 81
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 427-467 5.09e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.09  E-value: 5.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 229892302  427 KPQIyekavSSFPDPALYPLGSRQILTCTAYGIPQPTIKWF 467
Cdd:pfam13927   1 KPVI-----TVSPSSVTVREGETVTLTCEATGSPPPTITWY 36
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 359-404 5.34e-04

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


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 39.17  E-value: 5.34e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 229892302 359 VKAFPSPEVVWLKDGLPATEKSARYLT---RGYSLIIKDVTEEDAGNYT 404
Cdd:cd05736   24 AEGIPLPRVQWLKNGMDINPKLSKQLTliaNGSELHISNVRYEDTGAYT 72
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 358-404 6.98e-04

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


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 38.91  E-value: 6.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 229892302 358 KVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYT 404
Cdd:cd20978   24 QVTGVPQPKITWLHNGKPLQGPMERATVEDGTLTIINVQPEDTGYYG 70
IGv smart00406
Immunoglobulin V-Type;
247-311 8.92e-04

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 38.13  E-value: 8.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302   247 TLVLNCTATTPLNTRVQMTW---------------SYPDEKNKRASVRRRIDQSNSHA-NIFYsvLTIDKMQNKDKGLYT 310
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWvrqppgkglewlgyiGSNGSSYYQESYKGRFTISKDTSkNDVS--LTISNLRVEDTGTYY 78


                   .
gi 229892302   311 C 311
Cdd:smart00406  79 C 79
IgI_PDGFR-alphabeta cd05861
Immunoglobulin (Ig)-like domain of platelet-derived growth factor (PDGF) receptors (R), alpha ...
 230-327 1.16e-03

Immunoglobulin (Ig)-like domain of platelet-derived growth factor (PDGF) receptors (R), alpha and beta; member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of platelet-derived growth factor (PDGF) receptors (R), alpha (also known as cluster of differentiation (CD) 140a), and beta (also known as CD140b). 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). PDGFRalpha binds to all three PDGFs, whereas the PDGFRbeta binds only to PDGF-B. PDGFRs alpha and beta have similar organization: an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. In mice, PDGFRalpha and PDGFRbeta are essential for normal development.


Pssm-ID: 409447  Cd Length: 99  Bit Score: 38.35  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302 230 IDVQISTPRPVkLLRGHTLVLNCTATTplNTRVQMTWSYPDEKNKRASvrRRIDQSNSHANIFYSVLTIDKMQNKDKGLY 309
Cdd:cd05861    3 INVEMEAVKTV-VRQGETITLMCIVIG--NEVVDLEWTYPGKESGRGI--EPVEEFKVPPYHLVYTLTIPSATLEDSGTY 77

                         90       100
                 ....*....|....*....|..
gi 229892302 310 TCRVRSG----PSFKSVNTSVH 327
Cdd:cd05861   78 ECAVTEAtndhQDEKKINITVH 99
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 365-414 1.52e-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: 37.83  E-value: 1.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 229892302 365 PEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSI----KQSNV 414
Cdd:cd20994   31 PKVQWYKDCKPLLLDDKRFAGLESDLLIFNVTVQDQGNYTCHTSYtymgKQYNI 84
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 345-408 1.81e-03

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


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 37.56  E-value: 1.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229892302 345 ETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRG---YSLIIKDVTEEDAGNYTILLS 408
Cdd:cd20972   11 QEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEgdlHSLIIAEAFEEDTGRYSCLAT 77
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 354-426 2.87e-03

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


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 37.18  E-value: 2.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229892302 354 RLSMKVKAFPSPEVVWLKDGLP--ATEKSARYLTRGYSLIIKDVTEEDagnyTILLSIKQSNVFKNLTATLIVNV 426
Cdd:cd05867   18 RLDCQVEGIPTPNITWSINGAPieGTDPDPRRHVSSGALILTDVQPSD----TAVYQCEARNRHGNLLANAHVHV 88
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 354-405 3.44e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 37.06  E-value: 3.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 229892302 354 RLSMKVKAFPSPEVVWLKDGLPATEKSARYL----TRGY-SLIIKDVTEEDAGNYTI 405
Cdd:cd05892   19 RLECQISAIPPPQIFWKKNNEMLQYNTDRISlyqdNCGRiCLLIQNANKKDAGWYTV 75
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 236-327 7.16e-03

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 36.28  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229892302  236 TPRPVKLLRGHTLVLNCTATTPLNTRVQ-MTWSY-------------------PDEKNKRASVRRRIDQSNSHanifysv 295
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSSSMSEASTsVYWYRqppgkgptfliayysngseEGVKKGRFSGRGDPSNGDGS------- 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 229892302  296 LTIDKMQNKDKGLYTCRVRSGP---SFKSVNTSVH 327
Cdd:pfam07686  75 LTIQNLTLSDSGTYTCAVIPSGegvFGKGTRLTVL 109
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 363-404 8.22e-03

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 35.63  E-value: 8.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 229892302  363 PSPEVVWLKDG----LPATEKSARYLTRGYSLIIKDVTEEDAGNYT 404
Cdd:pfam00047  25 PGPDVTWSKEGgtliESLKVKHDNGRTTQSSLLISNVTKEDAGTYT 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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