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Conserved domains on  [gi|23238208|ref|NP_055154|]
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interleukin-17 receptor A isoform 1 precursor [Homo sapiens]

Protein Classification

SEFIR domain-containing protein( domain architecture ID 11243961)

SEFIR domain-containing protein may function as signaling components of Toll/IL-1R-similar pathways and the SEFIR domain mediates physical protein-protein interactions between pathway components

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IL17R_fnIII_D1 pfam16556
Interleukin-17 receptor, fibronectin-III-like domain 1; IL17R_fnIII_D1 is the first of two ...
 48-198 5.73e-101

Interleukin-17 receptor, fibronectin-III-like domain 1; IL17R_fnIII_D1 is the first of two fibronectin 3-like domains on interleukin-17 receptor proteins A and B. The tow fnIII domains are linked and together bind two molecules of IL-17 at one of its receptor-binding interfaces. This allows the other interface to bind to another receptor, thus allowing the IL-17 family of homodimeric cytokines to coordinate two different receptors.


:

Pssm-ID: 435426  Cd Length: 154  Bit Score: 310.08  E-value: 5.73e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208    48 LNCTVKNSTCLDDSWIHPRNLTPSSPKDLQIQLHFAHTQQGDLFPVAHIEWTLQTDASILYLEGAELSVLQLNTNERLCV 127
Cdd:pfam16556   1 LNCTVRNSTCLDDSWLKPQNLTPSAPKDLQVSLDVRRDEDGDLVPVLVAEWKLQTDASILYLEGAELSVLQLSTNERLCV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23238208   128 RFEFLSKL---RHHHRRWRFTFSHFVVDPDQEYEVTVHHLPKPIPDGDPNHQSKNFLVPDCEHARMKVTTPCMS 198
Cdd:pfam16556  81 RFEFLSKLlmrSPHGERWRFSFDQFVVDPGQTYEVTVHHLPKPIPDGDPNHQSKNFTVPGCEDPLMKMTKPCVE 154
IL17R_fnIII_D2 pfam16578
Interleukin 17 receptor D; IL17R_fnIII_D2 is the second extracellular fibronectin III-like ...
 199-303 3.51e-75

Interleukin 17 receptor D; IL17R_fnIII_D2 is the second extracellular fibronectin III-like domain on interleukin17-receptor-D molecules. The exact ligands of IL17R-D are not known.


:

Pssm-ID: 465185  Cd Length: 105  Bit Score: 239.98  E-value: 3.51e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208   199 SGSLWDPNITVETLEAHQLRVSFTLWNESTHYQILLTSFPHMENHSCFEHMHHIPAPRPEEFHQRSNVTLTLRNLKGCCR 278
Cdd:pfam16578   1 SGSLWDPNITVETLEAHQLRVSFTLWNESTRYQILLTSFPHTENQSCFEHVKDIPAPRQEEFHQRANVTLTLKNSKWCCR 80

                          90       100
                  ....*....|....*....|....*
gi 23238208   279 HQVQIQPFFSSCLNDCLRHSATVSC 303
Cdd:pfam16578  81 HQVQIQPFFSSCLNDCLRHSVTVPC 105
SEFIR pfam08357
SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are ...
 378-536 5.52e-49

SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are feedback inhibitors of FGF signalling and are also thought to be receptors. Due to its similarity to the TIR domain (pfam01582), the SEFIR region is thought to be involved in homotypic interactions with other SEFIR/TIR-domain-containing proteins. Thus, SEFs and IL17Rs may be involved in TOLL/IL1R-like signalling pathways.


:

Pssm-ID: 254756  Cd Length: 150  Bit Score: 169.88  E-value: 5.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208   378 RKVWIIYSADHPLYVDVVLKFAQFLLTACGTEVALDLLEEQAISEAGVMTWVGRQKQEmvesNSKIIVLCSRGTRAKWQA 457
Cdd:pfam08357   1 RKVFIVYSSDSALHTEVVLKFAEFLQDYCGCEVALDLWELNEIAEIGPVAWLERQIQE----ADKVIIVCSKGAKAFCDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208   458 LLGRGAP-VRLRCDHgkpvgDLFTAAMNMILPDFKRPACFGTYVVCYFSEvSCDGDVPDLFGAAPRYPLMDRFEEVYFRI 536
Cdd:pfam08357  77 KADKRKGgVGTESQH-----DLFIPALSLILRDFKQSAALRKYLVVYFGY-ADKKDVPTILRVLPKYSLMDQLPQLLAEL 150
 
Name Accession Description Interval E-value
IL17R_fnIII_D1 pfam16556
Interleukin-17 receptor, fibronectin-III-like domain 1; IL17R_fnIII_D1 is the first of two ...
 48-198 5.73e-101

Interleukin-17 receptor, fibronectin-III-like domain 1; IL17R_fnIII_D1 is the first of two fibronectin 3-like domains on interleukin-17 receptor proteins A and B. The tow fnIII domains are linked and together bind two molecules of IL-17 at one of its receptor-binding interfaces. This allows the other interface to bind to another receptor, thus allowing the IL-17 family of homodimeric cytokines to coordinate two different receptors.


Pssm-ID: 435426  Cd Length: 154  Bit Score: 310.08  E-value: 5.73e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208    48 LNCTVKNSTCLDDSWIHPRNLTPSSPKDLQIQLHFAHTQQGDLFPVAHIEWTLQTDASILYLEGAELSVLQLNTNERLCV 127
Cdd:pfam16556   1 LNCTVRNSTCLDDSWLKPQNLTPSAPKDLQVSLDVRRDEDGDLVPVLVAEWKLQTDASILYLEGAELSVLQLSTNERLCV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23238208   128 RFEFLSKL---RHHHRRWRFTFSHFVVDPDQEYEVTVHHLPKPIPDGDPNHQSKNFLVPDCEHARMKVTTPCMS 198
Cdd:pfam16556  81 RFEFLSKLlmrSPHGERWRFSFDQFVVDPGQTYEVTVHHLPKPIPDGDPNHQSKNFTVPGCEDPLMKMTKPCVE 154
IL17R_fnIII_D2 pfam16578
Interleukin 17 receptor D; IL17R_fnIII_D2 is the second extracellular fibronectin III-like ...
 199-303 3.51e-75

Interleukin 17 receptor D; IL17R_fnIII_D2 is the second extracellular fibronectin III-like domain on interleukin17-receptor-D molecules. The exact ligands of IL17R-D are not known.


Pssm-ID: 465185  Cd Length: 105  Bit Score: 239.98  E-value: 3.51e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208   199 SGSLWDPNITVETLEAHQLRVSFTLWNESTHYQILLTSFPHMENHSCFEHMHHIPAPRPEEFHQRSNVTLTLRNLKGCCR 278
Cdd:pfam16578   1 SGSLWDPNITVETLEAHQLRVSFTLWNESTRYQILLTSFPHTENQSCFEHVKDIPAPRQEEFHQRANVTLTLKNSKWCCR 80

                          90       100
                  ....*....|....*....|....*
gi 23238208   279 HQVQIQPFFSSCLNDCLRHSATVSC 303
Cdd:pfam16578  81 HQVQIQPFFSSCLNDCLRHSVTVPC 105
SEFIR pfam08357
SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are ...
 378-536 5.52e-49

SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are feedback inhibitors of FGF signalling and are also thought to be receptors. Due to its similarity to the TIR domain (pfam01582), the SEFIR region is thought to be involved in homotypic interactions with other SEFIR/TIR-domain-containing proteins. Thus, SEFs and IL17Rs may be involved in TOLL/IL1R-like signalling pathways.


Pssm-ID: 254756  Cd Length: 150  Bit Score: 169.88  E-value: 5.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208   378 RKVWIIYSADHPLYVDVVLKFAQFLLTACGTEVALDLLEEQAISEAGVMTWVGRQKQEmvesNSKIIVLCSRGTRAKWQA 457
Cdd:pfam08357   1 RKVFIVYSSDSALHTEVVLKFAEFLQDYCGCEVALDLWELNEIAEIGPVAWLERQIQE----ADKVIIVCSKGAKAFCDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208   458 LLGRGAP-VRLRCDHgkpvgDLFTAAMNMILPDFKRPACFGTYVVCYFSEvSCDGDVPDLFGAAPRYPLMDRFEEVYFRI 536
Cdd:pfam08357  77 KADKRKGgVGTESQH-----DLFIPALSLILRDFKQSAALRKYLVVYFGY-ADKKDVPTILRVLPKYSLMDQLPQLLAEL 150
 
Name Accession Description Interval E-value
IL17R_fnIII_D1 pfam16556
Interleukin-17 receptor, fibronectin-III-like domain 1; IL17R_fnIII_D1 is the first of two ...
 48-198 5.73e-101

Interleukin-17 receptor, fibronectin-III-like domain 1; IL17R_fnIII_D1 is the first of two fibronectin 3-like domains on interleukin-17 receptor proteins A and B. The tow fnIII domains are linked and together bind two molecules of IL-17 at one of its receptor-binding interfaces. This allows the other interface to bind to another receptor, thus allowing the IL-17 family of homodimeric cytokines to coordinate two different receptors.


Pssm-ID: 435426  Cd Length: 154  Bit Score: 310.08  E-value: 5.73e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208    48 LNCTVKNSTCLDDSWIHPRNLTPSSPKDLQIQLHFAHTQQGDLFPVAHIEWTLQTDASILYLEGAELSVLQLNTNERLCV 127
Cdd:pfam16556   1 LNCTVRNSTCLDDSWLKPQNLTPSAPKDLQVSLDVRRDEDGDLVPVLVAEWKLQTDASILYLEGAELSVLQLSTNERLCV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23238208   128 RFEFLSKL---RHHHRRWRFTFSHFVVDPDQEYEVTVHHLPKPIPDGDPNHQSKNFLVPDCEHARMKVTTPCMS 198
Cdd:pfam16556  81 RFEFLSKLlmrSPHGERWRFSFDQFVVDPGQTYEVTVHHLPKPIPDGDPNHQSKNFTVPGCEDPLMKMTKPCVE 154
IL17R_fnIII_D2 pfam16578
Interleukin 17 receptor D; IL17R_fnIII_D2 is the second extracellular fibronectin III-like ...
 199-303 3.51e-75

Interleukin 17 receptor D; IL17R_fnIII_D2 is the second extracellular fibronectin III-like domain on interleukin17-receptor-D molecules. The exact ligands of IL17R-D are not known.


Pssm-ID: 465185  Cd Length: 105  Bit Score: 239.98  E-value: 3.51e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208   199 SGSLWDPNITVETLEAHQLRVSFTLWNESTHYQILLTSFPHMENHSCFEHMHHIPAPRPEEFHQRSNVTLTLRNLKGCCR 278
Cdd:pfam16578   1 SGSLWDPNITVETLEAHQLRVSFTLWNESTRYQILLTSFPHTENQSCFEHVKDIPAPRQEEFHQRANVTLTLKNSKWCCR 80

                          90       100
                  ....*....|....*....|....*
gi 23238208   279 HQVQIQPFFSSCLNDCLRHSATVSC 303
Cdd:pfam16578  81 HQVQIQPFFSSCLNDCLRHSVTVPC 105
SEFIR pfam08357
SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are ...
 378-536 5.52e-49

SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are feedback inhibitors of FGF signalling and are also thought to be receptors. Due to its similarity to the TIR domain (pfam01582), the SEFIR region is thought to be involved in homotypic interactions with other SEFIR/TIR-domain-containing proteins. Thus, SEFs and IL17Rs may be involved in TOLL/IL1R-like signalling pathways.


Pssm-ID: 254756  Cd Length: 150  Bit Score: 169.88  E-value: 5.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208   378 RKVWIIYSADHPLYVDVVLKFAQFLLTACGTEVALDLLEEQAISEAGVMTWVGRQKQEmvesNSKIIVLCSRGTRAKWQA 457
Cdd:pfam08357   1 RKVFIVYSSDSALHTEVVLKFAEFLQDYCGCEVALDLWELNEIAEIGPVAWLERQIQE----ADKVIIVCSKGAKAFCDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23238208   458 LLGRGAP-VRLRCDHgkpvgDLFTAAMNMILPDFKRPACFGTYVVCYFSEvSCDGDVPDLFGAAPRYPLMDRFEEVYFRI 536
Cdd:pfam08357  77 KADKRKGgVGTESQH-----DLFIPALSLILRDFKQSAALRKYLVVYFGY-ADKKDVPTILRVLPKYSLMDQLPQLLAEL 150
 
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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