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Conserved domains on  [gi|1021312266|ref|NP_001310433|]
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oncostatin-M-specific receptor subunit beta isoform 2 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LIFR_D2 super family cl39403
Leukemia inhibitory factor receptor D2 domain; This is the D2 domain in cytokine-binding ...
 30-138 1.12e-23

Leukemia inhibitory factor receptor D2 domain; This is the D2 domain in cytokine-binding module 1 (CBM1) found in Leukemia inhibitory factor receptor (LIFR) and OSM receptors (OSMR). LIFR has an extracellular region with a modular structure containing two cytokine-binding modules (CBM) separated by an Ig-like domain and followed by three membrane-proximal fibronectin type-III (FNIII) domains. The D2 domain in CBM1 shows structural similarity to the corresponding CBM domains of both gp130 and IL-6Ralpha because it contains conserved structural features like the WSXWS motif. The WSXWS motif in cytokine receptors is a molecular switch involved in receptor activation.


The actual alignment was detected with superfamily member pfam17971:

Pssm-ID: 375455  Cd Length: 114  Bit Score: 94.05  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312266  30 LPLTPVSLKVSTNSTRQSLHLQWTVHNLPYHQELKMVFQIQISRIETSNVIWVGNYSTTVKW-NQVLHWSWESELPLECA 108
Cdd:pfam17971   5 IPDTPQILNLTADFSTSTLHLKWNDKGSAFPYHSNVIWEIKVLRKEKMEIVTLVTYNTTLNGkDTVHHWNWTSDMPLECT 84

                          90       100       110
                  ....*....|....*....|....*....|
gi 1021312266 109 THFVRIKSLVDDAKFPEPNFWSNWSSWEEV 138
Cdd:pfam17971  85 SHSVRIRCYIDDVHFSGPKEWSEWSPLKNI 114
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 233-288 1.09e-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.


The actual alignment was detected with superfamily member pfam09067:

Pssm-ID: 473895  Cd Length: 104  Bit Score: 38.17  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1021312266 233 VSKVLEEPKDFSCETEDFKTLHCTWDPGTDTALGwskqpsQSYTLFESFSGEK-KLC 288
Cdd:pfam09067   4 ALLLPEKPEDIKCFSREKEDFTCFWEEEEDGGLP------TTYSFSYAYENETvKEC 54
 
Name Accession Description Interval E-value
LIFR_D2 pfam17971
Leukemia inhibitory factor receptor D2 domain; This is the D2 domain in cytokine-binding ...
 30-138 1.12e-23

Leukemia inhibitory factor receptor D2 domain; This is the D2 domain in cytokine-binding module 1 (CBM1) found in Leukemia inhibitory factor receptor (LIFR) and OSM receptors (OSMR). LIFR has an extracellular region with a modular structure containing two cytokine-binding modules (CBM) separated by an Ig-like domain and followed by three membrane-proximal fibronectin type-III (FNIII) domains. The D2 domain in CBM1 shows structural similarity to the corresponding CBM domains of both gp130 and IL-6Ralpha because it contains conserved structural features like the WSXWS motif. The WSXWS motif in cytokine receptors is a molecular switch involved in receptor activation.


Pssm-ID: 375455  Cd Length: 114  Bit Score: 94.05  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312266  30 LPLTPVSLKVSTNSTRQSLHLQWTVHNLPYHQELKMVFQIQISRIETSNVIWVGNYSTTVKW-NQVLHWSWESELPLECA 108
Cdd:pfam17971   5 IPDTPQILNLTADFSTSTLHLKWNDKGSAFPYHSNVIWEIKVLRKEKMEIVTLVTYNTTLNGkDTVHHWNWTSDMPLECT 84

                          90       100       110
                  ....*....|....*....|....*....|
gi 1021312266 109 THFVRIKSLVDDAKFPEPNFWSNWSSWEEV 138
Cdd:pfam17971  85 SHSVRIRCYIDDVHFSGPKEWSEWSPLKNI 114
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 233-288 1.09e-03

Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin (EPO), with subsequent initiation of the downstream chain of events associated with binding of EPO to the receptor, including EPO-induced erythroblast proliferation and differentiation through induction of the JAK2/STAT5 signaling cascade. The domain adopts a secondary structure composed of a short amino-terminal helix, followed by two beta-sandwich regions.


Pssm-ID: 401127  Cd Length: 104  Bit Score: 38.17  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1021312266 233 VSKVLEEPKDFSCETEDFKTLHCTWDPGTDTALGwskqpsQSYTLFESFSGEK-KLC 288
Cdd:pfam09067   4 ALLLPEKPEDIKCFSREKEDFTCFWEEEEDGGLP------TTYSFSYAYENETvKEC 54
 
Name Accession Description Interval E-value
LIFR_D2 pfam17971
Leukemia inhibitory factor receptor D2 domain; This is the D2 domain in cytokine-binding ...
 30-138 1.12e-23

Leukemia inhibitory factor receptor D2 domain; This is the D2 domain in cytokine-binding module 1 (CBM1) found in Leukemia inhibitory factor receptor (LIFR) and OSM receptors (OSMR). LIFR has an extracellular region with a modular structure containing two cytokine-binding modules (CBM) separated by an Ig-like domain and followed by three membrane-proximal fibronectin type-III (FNIII) domains. The D2 domain in CBM1 shows structural similarity to the corresponding CBM domains of both gp130 and IL-6Ralpha because it contains conserved structural features like the WSXWS motif. The WSXWS motif in cytokine receptors is a molecular switch involved in receptor activation.


Pssm-ID: 375455  Cd Length: 114  Bit Score: 94.05  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312266  30 LPLTPVSLKVSTNSTRQSLHLQWTVHNLPYHQELKMVFQIQISRIETSNVIWVGNYSTTVKW-NQVLHWSWESELPLECA 108
Cdd:pfam17971   5 IPDTPQILNLTADFSTSTLHLKWNDKGSAFPYHSNVIWEIKVLRKEKMEIVTLVTYNTTLNGkDTVHHWNWTSDMPLECT 84

                          90       100       110
                  ....*....|....*....|....*....|
gi 1021312266 109 THFVRIKSLVDDAKFPEPNFWSNWSSWEEV 138
Cdd:pfam17971  85 SHSVRIRCYIDDVHFSGPKEWSEWSPLKNI 114
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 233-288 1.09e-03

Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin (EPO), with subsequent initiation of the downstream chain of events associated with binding of EPO to the receptor, including EPO-induced erythroblast proliferation and differentiation through induction of the JAK2/STAT5 signaling cascade. The domain adopts a secondary structure composed of a short amino-terminal helix, followed by two beta-sandwich regions.


Pssm-ID: 401127  Cd Length: 104  Bit Score: 38.17  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1021312266 233 VSKVLEEPKDFSCETEDFKTLHCTWDPGTDTALGwskqpsQSYTLFESFSGEK-KLC 288
Cdd:pfam09067   4 ALLLPEKPEDIKCFSREKEDFTCFWEEEEDGGLP------TTYSFSYAYENETvKEC 54
 
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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