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Conserved domains on  [gi|768037547|ref|XP_011529207|]
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X-linked interleukin-1 receptor accessory protein-like 2 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 22-113 1.27e-30

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: 114.73  E-value: 1.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  22 IRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELKYEGKLVRR 101
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                         90
                 ....*....|..
gi 768037547 102 TTELKVTALLTD 113
Cdd:cd05757   81 NVTRTISLTVTE 92
TIR super family cl23801
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 278-439 1.52e-24

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


The actual alignment was detected with superfamily member pfam01582:

Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 100.13  E-value: 1.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  278 YDAYLSYTKVDqdtldcdnpEEEQFALEVLPDVleKHYGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiLR 357
Cdd:pfam01582   1 YDVFLSFRGSD---------TREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNY-AS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  358 RGWSIFELESRLHNMLVSGeIKVILIECTELKGKVNCQE---VESLKRSIKLLS---LIKWKG----------SKSSKLN 421
Cdd:pfam01582  69 SGWCLDELVKILECALDLG-QKVIPIFYEVDPSDVRKQTgsfGKAFKKHKKVLTeekVLKWRGalnevaniwhSKSVSDE 147

                         170
                  ....*....|....*...
gi 768037547  422 SKFWKHLVYEMPIKKKEM 439
Cdd:pfam01582 148 SKFWKKIAYDISNKLNGT 165
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 126-223 2.87e-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: 48.27  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547   126 PSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMK-GEKFIeelaghIREGEIRLLKEHLgekevELALIFDSVVEADLAN 204
Cdd:smart00410   1 PPSVTVKEGESVTLSCEA----SGSPPPEVTWYKqGGKLL------AESGRFSVSRSGS-----TSTLTISNVTPEDSGT 65

                           90
                   ....*....|....*....
gi 768037547   205 YTCHVENRNGRKHASVLLR 223
Cdd:smart00410  66 YTCAATNSSGSASSGTTLT 84
 
Name Accession Description Interval E-value
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 22-113 1.27e-30

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: 114.73  E-value: 1.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  22 IRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELKYEGKLVRR 101
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                         90
                 ....*....|..
gi 768037547 102 TTELKVTALLTD 113
Cdd:cd05757   81 NVTRTISLTVTE 92
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 278-439 1.52e-24

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 100.13  E-value: 1.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  278 YDAYLSYTKVDqdtldcdnpEEEQFALEVLPDVleKHYGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiLR 357
Cdd:pfam01582   1 YDVFLSFRGSD---------TREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNY-AS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  358 RGWSIFELESRLHNMLVSGeIKVILIECTELKGKVNCQE---VESLKRSIKLLS---LIKWKG----------SKSSKLN 421
Cdd:pfam01582  69 SGWCLDELVKILECALDLG-QKVIPIFYEVDPSDVRKQTgsfGKAFKKHKKVLTeekVLKWRGalnevaniwhSKSVSDE 147

                         170
                  ....*....|....*...
gi 768037547  422 SKFWKHLVYEMPIKKKEM 439
Cdd:pfam01582 148 SKFWKKIAYDISNKLNGT 165
TIR smart00255
Toll - interleukin 1 - resistance;
277-435 5.55e-24

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 97.78  E-value: 5.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547   277 EYDAYLSYtkvdqdtldcdnPEEEQFALEVLPDVLEKHYGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiL 356
Cdd:smart00255   1 EYDVFISY------------SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNY-A 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547   357 RRGWSIFELESRLHNMLVSGEIKVILIECTELKgkvncQEVESLKRSIKLL---SLIKWKGSKSsklnSKFWKHLVYEMP 433
Cdd:smart00255  68 ESEWCLDELVAALENALEEGGLRVIPIFYEVIP-----SDVRKQPGKFRKVfkkNYLKWPEDEK----EQFWKKALYAVP 138


                   ..
gi 768037547   434 IK 435
Cdd:smart00255 139 SK 140
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 126-223 2.87e-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: 48.27  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547   126 PSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMK-GEKFIeelaghIREGEIRLLKEHLgekevELALIFDSVVEADLAN 204
Cdd:smart00410   1 PPSVTVKEGESVTLSCEA----SGSPPPEVTWYKqGGKLL------AESGRFSVSRSGS-----TSTLTISNVTPEDSGT 65

                           90
                   ....*....|....*....
gi 768037547   205 YTCHVENRNGRKHASVLLR 223
Cdd:smart00410  66 YTCAATNSSGSASSGTTLT 84
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 3-166 9.36e-06

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 47.70  E-value: 9.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547   3 VSMSLT-VAENESGLcynSRIRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKEckPKMWRSIIIQKGNALL-IQEV 80
Cdd:PHA02785 110 MSLNLTiVSVSESNI---DLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGH--RRLRNKRLKQRTPGIItIEDV 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  81 QEEDGGNYTCELKYegklVRRTTELKVTALLTDKPPKPLFPMENQ-PSVIDVQLGKPLNIPCKAFFGfSGESGPMIYWMK 159
Cdd:PHA02785 185 RKNDAGYYTCVLKY----IYGDKTYNVTRIVKLEVRDRIIPPTMQlPEGVVTSIGSNLTIACRVSLR-PPTTDADVFWIS 259


                 ....*..
gi 768037547 160 GEKFIEE 166
Cdd:PHA02785 260 NGMYYEE 266
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 47-107 1.50e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.15  E-value: 1.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768037547   47 SDQEPDVVWYKECKPkmwrsiIIQKGNaLLIQEVQEEDGGNYTCELKYE-GKLVRRTTELKV 107
Cdd:pfam13895  25 GNPPPSYTWYKDGSA------ISSSPN-FFTLSVSAEDSGTYTCVARNGrGGKVSNPVELTV 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 125-211 2.34e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  125 QPSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMKGEKFIEELAGHIREgeirllkehlgEKEVELALIFDSVVEADLAN 204
Cdd:pfam13927   7 SPSSVTVREGETVTLTCEA----TGSPPPTITWYKNGEPISSGSTRSRS-----------LSGSNSTLTISNVTRSDAGT 71


                  ....*..
gi 768037547  205 YTCHVEN 211
Cdd:pfam13927  72 YTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 35-107 3.14e-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: 42.49  E-value: 3.14e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768037547    35 EISCPdmddfKKSDQEPDVVWYKE-CKPKMWRSIIIQKGNA----LLIQEVQEEDGGNYTCELKYEGKLVRRTTELKV 107
Cdd:smart00410  13 TLSCE-----ASGSPPPEVTWYKQgGKLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 148-214 8.03e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 38.68  E-value: 8.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768037547 148 SGESGPMIYWMK-GEKFIEElagHiREGEIRLLKEHLgekevelALIFDSVVEADLANYTCHVENRNG 214
Cdd:cd05857   29 AGNPTPTMRWLKnGKEFKQE---H-RIGGYKVRNQHW-------SLIMESVVPSDKGNYTCVVENEYG 85
 
Name Accession Description Interval E-value
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 22-113 1.27e-30

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: 114.73  E-value: 1.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  22 IRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELKYEGKLVRR 101
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                         90
                 ....*....|..
gi 768037547 102 TTELKVTALLTD 113
Cdd:cd05757   81 NVTRTISLTVTE 92
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 278-439 1.52e-24

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 100.13  E-value: 1.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  278 YDAYLSYTKVDqdtldcdnpEEEQFALEVLPDVleKHYGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiLR 357
Cdd:pfam01582   1 YDVFLSFRGSD---------TREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNY-AS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  358 RGWSIFELESRLHNMLVSGeIKVILIECTELKGKVNCQE---VESLKRSIKLLS---LIKWKG----------SKSSKLN 421
Cdd:pfam01582  69 SGWCLDELVKILECALDLG-QKVIPIFYEVDPSDVRKQTgsfGKAFKKHKKVLTeekVLKWRGalnevaniwhSKSVSDE 147

                         170
                  ....*....|....*...
gi 768037547  422 SKFWKHLVYEMPIKKKEM 439
Cdd:pfam01582 148 SKFWKKIAYDISNKLNGT 165
TIR smart00255
Toll - interleukin 1 - resistance;
277-435 5.55e-24

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 97.78  E-value: 5.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547   277 EYDAYLSYtkvdqdtldcdnPEEEQFALEVLPDVLEKHYGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiL 356
Cdd:smart00255   1 EYDVFISY------------SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNY-A 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547   357 RRGWSIFELESRLHNMLVSGEIKVILIECTELKgkvncQEVESLKRSIKLL---SLIKWKGSKSsklnSKFWKHLVYEMP 433
Cdd:smart00255  68 ESEWCLDELVAALENALEEGGLRVIPIFYEVIP-----SDVRKQPGKFRKVfkkNYLKWPEDEK----EQFWKKALYAVP 138


                   ..
gi 768037547   434 IK 435
Cdd:smart00255 139 SK 140
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 24-107 1.34e-12

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: 63.64  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  24 YLEKSEVTKRKEISCPDMDDFKKSDQE-PDVVWYKECKPKMWRSIIIQ-KGNALLIQEVQEEDGGNYTCELKYE--GKL- 98
Cdd:cd20994    3 YKQKVPFTSGGRIVCPHLDFFKDENNNlPKVQWYKDCKPLLLDDKRFAgLESDLLIFNVTVQDQGNYTCHTSYTymGKQy 82

                         90
                 ....*....|
gi 768037547  99 -VRRTTELKV 107
Cdd:cd20994   83 nISRTISLIV 92
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 34-110 7.27e-10

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: 409585  Cd Length: 93  Bit Score: 56.06  E-value: 7.27e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768037547  34 KEISCPDMDDFKKSDQEPDVVWYKECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELKYE--GKLVRRTTELKVTAL 110
Cdd:cd20993   14 RTITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDRVPKGDKLVIHVMLEHYQGNYTCVVTYEtkGRTIKLTRTVNVKVV 92
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 281-389 2.40e-09

TIR domain; This is a family of Toll-like receptors.


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 55.40  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  281 YLSYTKVDQDtldcdnpeeeqFALEVLpDVLEKHyGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiLRRGW 360
Cdd:pfam13676   2 FISYAGEDRA-----------WAEWLA-DALEAA-GYRVWLDRWDIRPGDDWVEEIEEAIENSDRVLVVLSPNY-LESPW 67

                          90       100       110
                  ....*....|....*....|....*....|.
gi 768037547  361 SIFELESRLHnmLVSGEIKVI--LIECTELK 389
Cdd:pfam13676  68 CRAEWEAALA--DPEGRKRLIpvRLECDLEL 96
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 126-223 2.87e-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: 48.27  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547   126 PSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMK-GEKFIeelaghIREGEIRLLKEHLgekevELALIFDSVVEADLAN 204
Cdd:smart00410   1 PPSVTVKEGESVTLSCEA----SGSPPPEVTWYKqGGKLL------AESGRFSVSRSGS-----TSTLTISNVTPEDSGT 65

                           90
                   ....*....|....*....
gi 768037547   205 YTCHVENRNGRKHASVLLR 223
Cdd:smart00410  66 YTCAATNSSGSASSGTTLT 84
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 3-166 9.36e-06

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 47.70  E-value: 9.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547   3 VSMSLT-VAENESGLcynSRIRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKEckPKMWRSIIIQKGNALL-IQEV 80
Cdd:PHA02785 110 MSLNLTiVSVSESNI---DLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGH--RRLRNKRLKQRTPGIItIEDV 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  81 QEEDGGNYTCELKYegklVRRTTELKVTALLTDKPPKPLFPMENQ-PSVIDVQLGKPLNIPCKAFFGfSGESGPMIYWMK 159
Cdd:PHA02785 185 RKNDAGYYTCVLKY----IYGDKTYNVTRIVKLEVRDRIIPPTMQlPEGVVTSIGSNLTIACRVSLR-PPTTDADVFWIS 259


                 ....*..
gi 768037547 160 GEKFIEE 166
Cdd:PHA02785 260 NGMYYEE 266
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 47-107 1.50e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.15  E-value: 1.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768037547   47 SDQEPDVVWYKECKPkmwrsiIIQKGNaLLIQEVQEEDGGNYTCELKYE-GKLVRRTTELKV 107
Cdd:pfam13895  25 GNPPPSYTWYKDGSA------ISSSPN-FFTLSVSAEDSGTYTCVARNGrGGKVSNPVELTV 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 125-211 2.34e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  125 QPSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMKGEKFIEELAGHIREgeirllkehlgEKEVELALIFDSVVEADLAN 204
Cdd:pfam13927   7 SPSSVTVREGETVTLTCEA----TGSPPPTITWYKNGEPISSGSTRSRS-----------LSGSNSTLTISNVTRSDAGT 71


                  ....*..
gi 768037547  205 YTCHVEN 211
Cdd:pfam13927  72 YTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 35-107 3.14e-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: 42.49  E-value: 3.14e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768037547    35 EISCPdmddfKKSDQEPDVVWYKE-CKPKMWRSIIIQKGNA----LLIQEVQEEDGGNYTCELKYEGKLVRRTTELKV 107
Cdd:smart00410  13 TLSCE-----ASGSPPPEVTWYKQgGKLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 46-91 7.40e-05

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.16  E-value: 7.40e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 768037547  46 KSDQEPDVVWYKECKP---KMWRSIIIQKGNA-LLIQEVQEEDGGNYTCE 91
Cdd:cd00096    8 SGNPPPTITWYKNGKPlppSSRDSRRSELGNGtLTISNVTLEDSGTYTCV 57
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
 36-107 1.05e-04

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). 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 the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and 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.


Pssm-ID: 409478  Cd Length: 95  Bit Score: 41.28  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768037547  36 ISCPDMDDFKKSDQEPDVVWYKECK--PKMWRSIIIQKGNA-LLIQEVQEEDGGNYTCELK--YEGK--LVRRTTELKV 107
Cdd:cd05897   15 LVCPDLSEFTINRTDVEIQWYKDSLllDKDNEKFLSVKGSThLLIHDVSLNDSGYYTCKLTftHEGKkyNITRSIELRI 93
IgI_VEGFR cd04976
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); member ...
 51-92 2.68e-04

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: 40.28  E-value: 2.68e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 768037547  51 PDVVWYKECKPkMWRSIIIQKGNALLIQEVQEEDGGNYTCEL 92
Cdd:cd04976   33 PEVVWYKDGLP-LTEKARYLTRHSLIIKEVTEEDTGNYTILL 73
I-set pfam07679
Immunoglobulin I-set domain;
125-222 7.43e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 38.78  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  125 QPSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMKGEKfieelagHIREGEIRLLKEhlgeKEVELALIFDSVVEADLAN 204
Cdd:pfam07679   6 KPKDVEVQEGESARFTCTV----TGTPDPEVSWFKDGQ-------PLRSSDRFKVTY----EGGTYTLTISNVQPDDSGK 70

                          90
                  ....*....|....*...
gi 768037547  205 YTCHVENRNGRKHASVLL 222
Cdd:pfam07679  71 YTCVATNSAGEAEASAEL 88
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 148-214 8.03e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 38.68  E-value: 8.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768037547 148 SGESGPMIYWMK-GEKFIEElagHiREGEIRLLKEHLgekevelALIFDSVVEADLANYTCHVENRNG 214
Cdd:cd05857   29 AGNPTPTMRWLKnGKEFKQE---H-RIGGYKVRNQHW-------SLIMESVVPSDKGNYTCVVENEYG 85
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
 148-223 8.36e-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: 38.67  E-value: 8.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768037547 148 SGESGPMIYWMKGEKFIEELAGHIREgeirllkehlgEKEVELA-LIFDSVVEADLANYTCHVENRNGRKHASVLLR 223
Cdd:cd05894   20 SGEPAPTVTWSRGDKAFTATEGRVRV-----------ESYKDLSsFVIEGAEREDEGVYTITVTNPVGEDHASLFVK 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 137-219 1.42e-03

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: 37.31  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547 137 LNIPCKAffgfSGESGPMIYWMKGEKFIEELAGHIREgeirllkehlgEKEVELALIFDSVVEADLANYTCHVENRNGRK 216
Cdd:cd00096    1 VTLTCSA----SGNPPPTITWYKNGKPLPPSSRDSRR-----------SELGNGTLTISNVTLEDSGTYTCVASNSAGGS 65


                 ...
gi 768037547 217 HAS 219
Cdd:cd00096   66 ASA 68
IgI_VEGFR-2 cd05864
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); ...
 50-89 1.44e-03

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: 37.99  E-value: 1.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 768037547  50 EPDVVWYKECKPKMWRsIIIQKGNALLIQEVQEEDGGNYT 89
Cdd:cd05864   31 PPEIKWYKNGIPIESN-HTIKAGHVLTIMEVTEKDAGNYT 69
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 47-91 2.89e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.77  E-value: 2.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 768037547   47 SDQEPDVVWYK---ECKPKMWRSIIIQKGNALL-IQEVQEEDGGNYTCE 91
Cdd:pfam13927  27 GSPPPTITWYKngePISSGSTRSRSLSGSNSTLtISNVTRSDAGTYTCV 75
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 50-107 3.19e-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: 37.00  E-value: 3.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768037547  50 EPDVVWYKECKP---KMWRSIIIQKGNaLLIQEVQEEDGGNYTCELK-YEGKLVRRTTELKV 107
Cdd:cd05724   27 EPTVSWRKDGQPlnlDNERVRIVDDGN-LLIAEARKSDEGTYKCVATnMVGERESRAARLSV 87
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
 25-109 3.38e-03

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


Pssm-ID: 409368  Cd Length: 88  Bit Score: 37.05  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037547  25 LEKSEVTKRKE---ISCpdmddFKKSDQEPdVVWY---KECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELkyeGKL 98
Cdd:cd04979    2 SFKQISVKEGDtviLSC-----SVKSNNAP-VTWIhngKKVPRYRSPRLVLKTERGLLIRSAQEADAGVYECHS---GER 72

                         90
                 ....*....|.
gi 768037547  99 VRRTTELKVTA 109
Cdd:cd04979   73 VLGSTLRSVTL 83
I-set pfam07679
Immunoglobulin I-set domain;
48-107 4.80e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 36.47  E-value: 4.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768037547   48 DQEPDVVWYKECKP-KMWRSIIIQK--GNA-LLIQEVQEEDGGNYTCELKYEGKLVRRTTELKV 107
Cdd:pfam07679  27 TPDPEVSWFKDGQPlRSSDRFKVTYegGTYtLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_VEGFR-1 cd07702
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); ...
 51-89 5.92e-03

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: 36.39  E-value: 5.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 768037547  51 PDVVWYKECKPKMWRSI-IIQKGNALLIQEVQEEDGGNYT 89
Cdd:cd07702   33 PEVIWLKDGLPATEKCArYLTRGYSLIIKDVTEEDAGNYT 72
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 51-107 5.93e-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: 5.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768037547  51 PDVVWYKECKPKMWRSII-----IQKGNALLIQEVQEEDGGNYTCELKYEGKLVRRTTELKV 107
Cdd:cd05729   34 PNITWLKDGKEFKKEHRIggtkvEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
 
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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