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Conserved domains on  [gi|172045703|sp|Q2KI76|]
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RecName: Full=Selenoprotein S; Short=SelS

Protein Classification

DUF814 domain-containing protein( domain architecture ID 10536524)

DUF814 domain-containing protein similar to vertebrates coiled-coil domain-containing protein 25 and yeast protein JLP2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Selenoprotein_S pfam06936
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ...
 2-188 3.31e-114

Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.


:

Pssm-ID: 462043 [Multi-domain]  Cd Length: 192  Bit Score: 322.94  E-value: 3.31e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045703    2 ERDGDQLSARPTLETEGLRFLHVTVGSLLATYGWYIVFSCILLYVVFQKLSTRLRALRQRHLDQAAAALEPDIVVKRQEA 81
Cdd:pfam06936   5 EEPGVQLPARPALENEGLRFLQVTVGSLLSSYGWYLLFGCVLVYLLIQKLRKRRTALRQRSSDHSAATVDPDLVVKRQEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045703   82 LAAARLKMQEELNAQVEKHKEKLRQLEEEKRRQKIEMWDSMQEGKSYKGNTRKPQEE-DSPGPSTSSVIPKRKSDRKPLR 160
Cdd:pfam06936  85 LEASRLRMQEELDAQAEKFKEKQKQLEEEKRRQKIEMWESMQEGKSYKGNAKLAQEEtEETGPSASSAIPKPKPDKKPLR 164

                         170       180
                  ....*....|....*....|....*...
gi 172045703  161 GGGYNPLSGEGGGTCSWRPGRRGPSSGG 188
Cdd:pfam06936 165 GSGYNPLTGDGGGSCSWRPGRRGPSSGG 192
 
Name Accession Description Interval E-value
Selenoprotein_S pfam06936
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ...
 2-188 3.31e-114

Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.


Pssm-ID: 462043 [Multi-domain]  Cd Length: 192  Bit Score: 322.94  E-value: 3.31e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045703    2 ERDGDQLSARPTLETEGLRFLHVTVGSLLATYGWYIVFSCILLYVVFQKLSTRLRALRQRHLDQAAAALEPDIVVKRQEA 81
Cdd:pfam06936   5 EEPGVQLPARPALENEGLRFLQVTVGSLLSSYGWYLLFGCVLVYLLIQKLRKRRTALRQRSSDHSAATVDPDLVVKRQEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045703   82 LAAARLKMQEELNAQVEKHKEKLRQLEEEKRRQKIEMWDSMQEGKSYKGNTRKPQEE-DSPGPSTSSVIPKRKSDRKPLR 160
Cdd:pfam06936  85 LEASRLRMQEELDAQAEKFKEKQKQLEEEKRRQKIEMWESMQEGKSYKGNAKLAQEEtEETGPSASSAIPKPKPDKKPLR 164

                         170       180
                  ....*....|....*....|....*...
gi 172045703  161 GGGYNPLSGEGGGTCSWRPGRRGPSSGG 188
Cdd:pfam06936 165 GSGYNPLTGDGGGSCSWRPGRRGPSSGG 192
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 56-126 4.60e-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: 36.79  E-value: 4.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 172045703  56 RALRQRHLDQAAAALEPDIVVKRQEALAAARLKMQEELNAQVEKHKEKLRQLE---EEKRRQKIEMWDSMQEGK 126
Cdd:cd16269  191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKekmEEERENLLKEQERALESK 264
 
Name Accession Description Interval E-value
Selenoprotein_S pfam06936
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ...
 2-188 3.31e-114

Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.


Pssm-ID: 462043 [Multi-domain]  Cd Length: 192  Bit Score: 322.94  E-value: 3.31e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045703    2 ERDGDQLSARPTLETEGLRFLHVTVGSLLATYGWYIVFSCILLYVVFQKLSTRLRALRQRHLDQAAAALEPDIVVKRQEA 81
Cdd:pfam06936   5 EEPGVQLPARPALENEGLRFLQVTVGSLLSSYGWYLLFGCVLVYLLIQKLRKRRTALRQRSSDHSAATVDPDLVVKRQEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045703   82 LAAARLKMQEELNAQVEKHKEKLRQLEEEKRRQKIEMWDSMQEGKSYKGNTRKPQEE-DSPGPSTSSVIPKRKSDRKPLR 160
Cdd:pfam06936  85 LEASRLRMQEELDAQAEKFKEKQKQLEEEKRRQKIEMWESMQEGKSYKGNAKLAQEEtEETGPSASSAIPKPKPDKKPLR 164

                         170       180
                  ....*....|....*....|....*...
gi 172045703  161 GGGYNPLSGEGGGTCSWRPGRRGPSSGG 188
Cdd:pfam06936 165 GSGYNPLTGDGGGSCSWRPGRRGPSSGG 192
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 56-126 4.60e-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: 36.79  E-value: 4.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 172045703  56 RALRQRHLDQAAAALEPDIVVKRQEALAAARLKMQEELNAQVEKHKEKLRQLE---EEKRRQKIEMWDSMQEGK 126
Cdd:cd16269  191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKekmEEERENLLKEQERALESK 264
 
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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