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Conserved domains on  [gi|564401103|ref|XP_006257761|]
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interleukin-7 receptor subunit alpha isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FN3_7 super family cl39782
Fibronectin type III domain; This domain is found in Interleukin-7 receptor subunit alpha ...
 22-72 1.72e-19

Fibronectin type III domain; This domain is found in Interleukin-7 receptor subunit alpha (IL-7Ralpha), which together IL-7 form a complex crucial to several signalling cascades leading to the development and homeostasis of T and B cells. IL-7Ralpha carries a 219 residue ectodomain on the N-terminal region which is crucial for T and B-cell development. Mutations in the IL-7Ralpha ectodomain inhibits T and B cell development, resulting in patients with a form of severe combined immunodeficiency (SCID). The ectodomain folds into two fibronectin type III (FNIII) domains connected by a 310-helical linker. This entry comprises the first of the two FNIII domains, D1 while D2 domain is pfam00041. In the D1 domain of IL-7Ralpha, a disulfide bond (C22R-C37R) conserved among cytokine receptor class I (CRH I) family members bridges two beta strands.


The actual alignment was detected with superfamily member pfam18447:

Pssm-ID: 465772  Cd Length: 97  Bit Score: 82.79  E-value: 1.72e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564401103   22 LLGIDCLTLNKLREMYFIKTSKFLLIGNSSVCVKLGKMDVICKILDISTIV 72
Cdd:pfam18447  47 DLEVKCLNMEKLEDVYFIKTKKFLLIGNSDICVKLEMKRKTCKSLKITKIV 97
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 76-164 5.17e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


The actual alignment was detected with superfamily member pfam00041:

Pssm-ID: 473895 [Multi-domain]  Cd Length: 85  Bit Score: 38.55  E-value: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564401103   76 APSNLKVVYRKEaNDFLVTFNTSHSTKKYVTalKHDVAYRPERGESNWTHVYLFHTRTTILQRKLQPKAVYEIKVRSIPN 155
Cdd:pfam00041   2 APSNLTVTDVTS-TSLTVSWTPPPDGNGPIT--GYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                  ....*....
gi 564401103  156 HEYfkGFWS 164
Cdd:pfam00041  79 GGE--GPPS 85
 
Name Accession Description Interval E-value
FN3_7 pfam18447
Fibronectin type III domain; This domain is found in Interleukin-7 receptor subunit alpha ...
 22-72 1.72e-19

Fibronectin type III domain; This domain is found in Interleukin-7 receptor subunit alpha (IL-7Ralpha), which together IL-7 form a complex crucial to several signalling cascades leading to the development and homeostasis of T and B cells. IL-7Ralpha carries a 219 residue ectodomain on the N-terminal region which is crucial for T and B-cell development. Mutations in the IL-7Ralpha ectodomain inhibits T and B cell development, resulting in patients with a form of severe combined immunodeficiency (SCID). The ectodomain folds into two fibronectin type III (FNIII) domains connected by a 310-helical linker. This entry comprises the first of the two FNIII domains, D1 while D2 domain is pfam00041. In the D1 domain of IL-7Ralpha, a disulfide bond (C22R-C37R) conserved among cytokine receptor class I (CRH I) family members bridges two beta strands.


Pssm-ID: 465772  Cd Length: 97  Bit Score: 82.79  E-value: 1.72e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564401103   22 LLGIDCLTLNKLREMYFIKTSKFLLIGNSSVCVKLGKMDVICKILDISTIV 72
Cdd:pfam18447  47 DLEVKCLNMEKLEDVYFIKTKKFLLIGNSDICVKLEMKRKTCKSLKITKIV 97
fn3 pfam00041
Fibronectin type III domain;
76-164 5.17e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.55  E-value: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564401103   76 APSNLKVVYRKEaNDFLVTFNTSHSTKKYVTalKHDVAYRPERGESNWTHVYLFHTRTTILQRKLQPKAVYEIKVRSIPN 155
Cdd:pfam00041   2 APSNLTVTDVTS-TSLTVSWTPPPDGNGPIT--GYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                  ....*....
gi 564401103  156 HEYfkGFWS 164
Cdd:pfam00041  79 GGE--GPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 74-174 1.26e-03

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 37.86  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564401103  74 PEAPSNLKVVYRkEANDFLVTFNTSHSTKKYVTALKhdVAYRPErGESNWTHV-YLFHTRTTILQRKLQPKAVYEIKVRS 152
Cdd:cd00063    1 PSPPTNLRVTDV-TSTSVTLSWTPPEDDGGPITGYV--VEYREK-GSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRA 76

                         90       100
                 ....*....|....*....|..
gi 564401103 153 ipnheYFKGFWSEWSPSSTFET 174
Cdd:cd00063   77 -----VNGGGESPPSESVTVTT 93
 
Name Accession Description Interval E-value
FN3_7 pfam18447
Fibronectin type III domain; This domain is found in Interleukin-7 receptor subunit alpha ...
 22-72 1.72e-19

Fibronectin type III domain; This domain is found in Interleukin-7 receptor subunit alpha (IL-7Ralpha), which together IL-7 form a complex crucial to several signalling cascades leading to the development and homeostasis of T and B cells. IL-7Ralpha carries a 219 residue ectodomain on the N-terminal region which is crucial for T and B-cell development. Mutations in the IL-7Ralpha ectodomain inhibits T and B cell development, resulting in patients with a form of severe combined immunodeficiency (SCID). The ectodomain folds into two fibronectin type III (FNIII) domains connected by a 310-helical linker. This entry comprises the first of the two FNIII domains, D1 while D2 domain is pfam00041. In the D1 domain of IL-7Ralpha, a disulfide bond (C22R-C37R) conserved among cytokine receptor class I (CRH I) family members bridges two beta strands.


Pssm-ID: 465772  Cd Length: 97  Bit Score: 82.79  E-value: 1.72e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564401103   22 LLGIDCLTLNKLREMYFIKTSKFLLIGNSSVCVKLGKMDVICKILDISTIV 72
Cdd:pfam18447  47 DLEVKCLNMEKLEDVYFIKTKKFLLIGNSDICVKLEMKRKTCKSLKITKIV 97
fn3 pfam00041
Fibronectin type III domain;
76-164 5.17e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.55  E-value: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564401103   76 APSNLKVVYRKEaNDFLVTFNTSHSTKKYVTalKHDVAYRPERGESNWTHVYLFHTRTTILQRKLQPKAVYEIKVRSIPN 155
Cdd:pfam00041   2 APSNLTVTDVTS-TSLTVSWTPPPDGNGPIT--GYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                  ....*....
gi 564401103  156 HEYfkGFWS 164
Cdd:pfam00041  79 GGE--GPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 74-174 1.26e-03

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 37.86  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564401103  74 PEAPSNLKVVYRkEANDFLVTFNTSHSTKKYVTALKhdVAYRPErGESNWTHV-YLFHTRTTILQRKLQPKAVYEIKVRS 152
Cdd:cd00063    1 PSPPTNLRVTDV-TSTSVTLSWTPPEDDGGPITGYV--VEYREK-GSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRA 76

                         90       100
                 ....*....|....*....|..
gi 564401103 153 ipnheYFKGFWSEWSPSSTFET 174
Cdd:cd00063   77 -----VNGGGESPPSESVTVTT 93
 
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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