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Conserved domains on  [gi|27477074|ref|NP_061195|]
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interleukin-17 receptor B precursor [Homo sapiens]

Protein Classification

IL17R_fnIII_D2 and SEFIR domain-containing protein( domain architecture ID 11072049)

protein containing domains IL17R_fnIII_D1, IL17R_fnIII_D2, and SEFIR

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SEFIR pfam08357
SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are ...
 332-479 2.24e-61

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: 197.62  E-value: 2.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074   332 IKVLVVYPSEICFH-HTICYFTEFLQNHCRSEVILEKWQKKKIAEMGPVQWLATQKKAADKVVFLLSNDVNSVCDGTCGK 410
Cdd:pfam08357   1 RKVFIVYSSDSALHtEVVLKFAEFLQDYCGCEVALDLWELNEIAEIGPVAWLERQIQEADKVIIVCSKGAKAFCDKKADK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074   411 SEGSPSENSQ-DLFPLAFNLFCSDLRSQIHLHKYVVVYFREIDTKDDYNALSVCPKYHLMKDATAFCAEL 479
Cdd:pfam08357  81 RKGGVGTESQhDLFIPALSLILRDFKQSAALRKYLVVYFGYADKKDVPTILRVLPKYSLMDQLPQLLAEL 150
IL17R_fnIII_D1 super family cl24953
Interleukin-17 receptor, fibronectin-III-like domain 1; IL17R_fnIII_D1 is the first of two ...
 33-175 2.66e-21

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.


The actual alignment was detected with superfamily member pfam16556:

Pssm-ID: 435426  Cd Length: 154  Bit Score: 90.13  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074    33 EWMLQHDLIPGDLRDLRVEPVTTSVATGDYSILMNVSWVLRADASIRLLKATKICVTgKSNFQSYSCVRCNYTEAFQTQt 112
Cdd:pfam16556  14 SWLKPQNLTPSAPKDLQVSLDVRRDEDGDLVPVLVAEWKLQTDASILYLEGAELSVL-QLSTNERLCVRFEFLSKLLMR- 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477074   113 RPSGGKWTFSYIGFPVELNTVYFIGAHNIPNANMNEDGPSMSVNFTSPGCLDHIMKYKKKCVK 175
Cdd:pfam16556  92 SPHGERWRFSFDQFVVDPGQTYEVTVHHLPKPIPDGDPNHQSKNFTVPGCEDPLMKMTKPCVE 154
IL17R_fnIII_D2 super family cl24965
Interleukin 17 receptor D; IL17R_fnIII_D2 is the second extracellular fibronectin III-like ...
 176-268 2.72e-11

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.


The actual alignment was detected with superfamily member pfam16578:

Pssm-ID: 465185  Cd Length: 105  Bit Score: 60.09  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074   176 AGSLWDPNITACKKNEETVEVNFTTTPLGNRYMALIQ-------HSTIIGFSQVFEPHQKK-QTRASVVIPVTgDSEGA- 246
Cdd:pfam16578   1 SGSLWDPNITVETLEAHQLRVSFTLWNESTRYQILLTsfphtenQSCFEHVKDIPAPRQEEfHQRANVTLTLK-NSKWCc 79

                          90       100
                  ....*....|....*....|....
gi 27477074   247 --TVQLTPYFPTCGSDCIRHKGTV 268
Cdd:pfam16578  80 rhQVQIQPFFSSCLNDCLRHSVTV 103
 
Name Accession Description Interval E-value
SEFIR pfam08357
SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are ...
 332-479 2.24e-61

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: 197.62  E-value: 2.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074   332 IKVLVVYPSEICFH-HTICYFTEFLQNHCRSEVILEKWQKKKIAEMGPVQWLATQKKAADKVVFLLSNDVNSVCDGTCGK 410
Cdd:pfam08357   1 RKVFIVYSSDSALHtEVVLKFAEFLQDYCGCEVALDLWELNEIAEIGPVAWLERQIQEADKVIIVCSKGAKAFCDKKADK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074   411 SEGSPSENSQ-DLFPLAFNLFCSDLRSQIHLHKYVVVYFREIDTKDDYNALSVCPKYHLMKDATAFCAEL 479
Cdd:pfam08357  81 RKGGVGTESQhDLFIPALSLILRDFKQSAALRKYLVVYFGYADKKDVPTILRVLPKYSLMDQLPQLLAEL 150
IL17R_fnIII_D1 pfam16556
Interleukin-17 receptor, fibronectin-III-like domain 1; IL17R_fnIII_D1 is the first of two ...
 33-175 2.66e-21

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: 90.13  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074    33 EWMLQHDLIPGDLRDLRVEPVTTSVATGDYSILMNVSWVLRADASIRLLKATKICVTgKSNFQSYSCVRCNYTEAFQTQt 112
Cdd:pfam16556  14 SWLKPQNLTPSAPKDLQVSLDVRRDEDGDLVPVLVAEWKLQTDASILYLEGAELSVL-QLSTNERLCVRFEFLSKLLMR- 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477074   113 RPSGGKWTFSYIGFPVELNTVYFIGAHNIPNANMNEDGPSMSVNFTSPGCLDHIMKYKKKCVK 175
Cdd:pfam16556  92 SPHGERWRFSFDQFVVDPGQTYEVTVHHLPKPIPDGDPNHQSKNFTVPGCEDPLMKMTKPCVE 154
IL17R_fnIII_D2 pfam16578
Interleukin 17 receptor D; IL17R_fnIII_D2 is the second extracellular fibronectin III-like ...
 176-268 2.72e-11

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: 60.09  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074   176 AGSLWDPNITACKKNEETVEVNFTTTPLGNRYMALIQ-------HSTIIGFSQVFEPHQKK-QTRASVVIPVTgDSEGA- 246
Cdd:pfam16578   1 SGSLWDPNITVETLEAHQLRVSFTLWNESTRYQILLTsfphtenQSCFEHVKDIPAPRQEEfHQRANVTLTLK-NSKWCc 79

                          90       100
                  ....*....|....*....|....
gi 27477074   247 --TVQLTPYFPTCGSDCIRHKGTV 268
Cdd:pfam16578  80 rhQVQIQPFFSSCLNDCLRHSVTV 103
 
Name Accession Description Interval E-value
SEFIR pfam08357
SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are ...
 332-479 2.24e-61

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: 197.62  E-value: 2.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074   332 IKVLVVYPSEICFH-HTICYFTEFLQNHCRSEVILEKWQKKKIAEMGPVQWLATQKKAADKVVFLLSNDVNSVCDGTCGK 410
Cdd:pfam08357   1 RKVFIVYSSDSALHtEVVLKFAEFLQDYCGCEVALDLWELNEIAEIGPVAWLERQIQEADKVIIVCSKGAKAFCDKKADK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074   411 SEGSPSENSQ-DLFPLAFNLFCSDLRSQIHLHKYVVVYFREIDTKDDYNALSVCPKYHLMKDATAFCAEL 479
Cdd:pfam08357  81 RKGGVGTESQhDLFIPALSLILRDFKQSAALRKYLVVYFGYADKKDVPTILRVLPKYSLMDQLPQLLAEL 150
IL17R_fnIII_D1 pfam16556
Interleukin-17 receptor, fibronectin-III-like domain 1; IL17R_fnIII_D1 is the first of two ...
 33-175 2.66e-21

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: 90.13  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074    33 EWMLQHDLIPGDLRDLRVEPVTTSVATGDYSILMNVSWVLRADASIRLLKATKICVTgKSNFQSYSCVRCNYTEAFQTQt 112
Cdd:pfam16556  14 SWLKPQNLTPSAPKDLQVSLDVRRDEDGDLVPVLVAEWKLQTDASILYLEGAELSVL-QLSTNERLCVRFEFLSKLLMR- 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477074   113 RPSGGKWTFSYIGFPVELNTVYFIGAHNIPNANMNEDGPSMSVNFTSPGCLDHIMKYKKKCVK 175
Cdd:pfam16556  92 SPHGERWRFSFDQFVVDPGQTYEVTVHHLPKPIPDGDPNHQSKNFTVPGCEDPLMKMTKPCVE 154
IL17R_fnIII_D2 pfam16578
Interleukin 17 receptor D; IL17R_fnIII_D2 is the second extracellular fibronectin III-like ...
 176-268 2.72e-11

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: 60.09  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477074   176 AGSLWDPNITACKKNEETVEVNFTTTPLGNRYMALIQ-------HSTIIGFSQVFEPHQKK-QTRASVVIPVTgDSEGA- 246
Cdd:pfam16578   1 SGSLWDPNITVETLEAHQLRVSFTLWNESTRYQILLTsfphtenQSCFEHVKDIPAPRQEEfHQRANVTLTLK-NSKWCc 79

                          90       100
                  ....*....|....*....|....
gi 27477074   247 --TVQLTPYFPTCGSDCIRHKGTV 268
Cdd:pfam16578  80 rhQVQIQPFFSSCLNDCLRHSVTV 103
 
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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