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Conserved domains on  [gi|320546064|ref|NP_001189135|]
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uncharacterized protein Dmel_CG17732 [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GBP_C super family cl46256
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 473-569 2.25e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


The actual alignment was detected with superfamily member cd16269:

Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546064 473 KLPASQQQHEAIfQQQQQAGKdnlQQLRVLYQRIKNRERNQLHHLSKSMKKVLDERlicERQHAEEKRLFQLKM-EQFKK 551
Cdd:cd16269  199 EIEAERAKAEAA-EQERKLLE---EQQRELEQKLEDQERSYEEHLRQLKEKMEEER---ENLLKEQERALESKLkEQEAL 271

                         90
                 ....*....|....*...
gi 320546064 552 VEEKFKLDREQLQHQLRS 569
Cdd:cd16269  272 LEEGFKEQAELLQEEIRS 289
 
Name Accession Description Interval E-value
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 473-569 2.25e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546064 473 KLPASQQQHEAIfQQQQQAGKdnlQQLRVLYQRIKNRERNQLHHLSKSMKKVLDERlicERQHAEEKRLFQLKM-EQFKK 551
Cdd:cd16269  199 EIEAERAKAEAA-EQERKLLE---EQQRELEQKLEDQERSYEEHLRQLKEKMEEER---ENLLKEQERALESKLkEQEAL 271

                         90
                 ....*....|....*...
gi 320546064 552 VEEKFKLDREQLQHQLRS 569
Cdd:cd16269  272 LEEGFKEQAELLQEEIRS 289
 
Name Accession Description Interval E-value
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 473-569 2.25e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546064 473 KLPASQQQHEAIfQQQQQAGKdnlQQLRVLYQRIKNRERNQLHHLSKSMKKVLDERlicERQHAEEKRLFQLKM-EQFKK 551
Cdd:cd16269  199 EIEAERAKAEAA-EQERKLLE---EQQRELEQKLEDQERSYEEHLRQLKEKMEEER---ENLLKEQERALESKLkEQEAL 271

                         90
                 ....*....|....*...
gi 320546064 552 VEEKFKLDREQLQHQLRS 569
Cdd:cd16269  272 LEEGFKEQAELLQEEIRS 289
 
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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