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Conserved domains on  [gi|1958782067|ref|XP_038967781|]
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vasoactive intestinal polypeptide receptor 2 isoform X5 [Rattus norvegicus]

Protein Classification

HormR domain-containing protein( domain architecture ID 10634995)

HormR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HormR smart00008
Domain present in hormone receptors;
47-117 1.41e-20

Domain present in hormone receptors;


:

Pssm-ID: 214468  Cd Length: 70  Bit Score: 82.56  E-value: 1.41e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782067   47 NHRACSGVWDNITCWRPADIGETVTVPCPKVFSNFYSRPGnISKNCTSDG-WSETFPDFiDACGYNDPEDES 117
Cdd:smart00008   1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFSYKTG-ASRNCTENGgWSPPFPNY-SNCTSNDYEELK 70
 
Name Accession Description Interval E-value
HormR smart00008
Domain present in hormone receptors;
47-117 1.41e-20

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 82.56  E-value: 1.41e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782067   47 NHRACSGVWDNITCWRPADIGETVTVPCPKVFSNFYSRPGnISKNCTSDG-WSETFPDFiDACGYNDPEDES 117
Cdd:smart00008   1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFSYKTG-ASRNCTENGgWSPPFPNY-SNCTSNDYEELK 70
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
 48-111 1.04e-19

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 80.11  E-value: 1.04e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782067  48 HRACSGVWDNITCWRPADIGETVTVPCPKVFSNFYSRpGNISKNCTSDG-WSETFPDFIDACGYN 111
Cdd:pfam02793   1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFSGFDPR-GNASRNCTEDGtWSEHPPSNYSNCTSN 64
 
Name Accession Description Interval E-value
HormR smart00008
Domain present in hormone receptors;
47-117 1.41e-20

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 82.56  E-value: 1.41e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782067   47 NHRACSGVWDNITCWRPADIGETVTVPCPKVFSNFYSRPGnISKNCTSDG-WSETFPDFiDACGYNDPEDES 117
Cdd:smart00008   1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFSYKTG-ASRNCTENGgWSPPFPNY-SNCTSNDYEELK 70
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
 48-111 1.04e-19

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 80.11  E-value: 1.04e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782067  48 HRACSGVWDNITCWRPADIGETVTVPCPKVFSNFYSRpGNISKNCTSDG-WSETFPDFIDACGYN 111
Cdd:pfam02793   1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFSGFDPR-GNASRNCTEDGtWSEHPPSNYSNCTSN 64
 
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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